PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
15695803-3	2005	The 1.4 angstrom crystal structure of the extracellular C-type lectin-like domain of human Lox-1 reveals a heart-shaped homodimer with a ridge of six basic amino acids extending diagonally across the apolar top of Lox-1, a central hydrophobic tunnel that extends through the entire molecule, and an electrostatically neutral patch of 12 charged residues that resides next to the tunnel at each opening.	Amino Acids, Basic	150-167	oxidized low density lipoprotein receptor 1	Homo sapiens	91-96
15707981-5	2005	Thus, it is deduced that spermidine and basic amino acids have almost the same affinity for Gap1p.	Amino Acids, Basic	40-57	amino acid permease GAP1	Saccharomyces cerevisiae S288C	92-97
15576628-0	2005	Deorphanization of GPRC6A: a promiscuous L-alpha-amino acid receptor with preference for basic amino acids.	Amino Acids, Basic	89-106	G protein-coupled receptor class C group 6 member A	Homo sapiens	19-25
15649405-3	2005	Amino acid sequence analysis showed that cleavage sites are located between two basic amino acids at Arg93-Arg94, resulting in the production of preproIMD(95-147), namely IMD(1-53).	Amino Acids, Basic	80-97	adrenomedullin 2	Rattus norvegicus	151-154
15582732-1	2005	INTRODUCTION: The primary structure of human chromogranin B (CgB) contains 15 pairs of basic amino acids, which are potential cleavage sites for specific endogenous proteases, but also other sites in the molecule can be subjected to cleavage.	Amino Acids, Basic	87-104	chromogranin B	Homo sapiens	45-59
15582732-1	2005	INTRODUCTION: The primary structure of human chromogranin B (CgB) contains 15 pairs of basic amino acids, which are potential cleavage sites for specific endogenous proteases, but also other sites in the molecule can be subjected to cleavage.	Amino Acids, Basic	87-104	chromogranin B	Homo sapiens	61-64
16003952-7	2005	Our findings here allow to speculate that basic amino acid residues on the C-terminal and molecular regions near catalytic site regions such as Calcium binding loop or beta-wing region may be involved in the binding of this PLA2 to the molecular receptor to induce the neurotoxic effect.	Amino Acids, Basic	42-58	phospholipase A2 group IIA	Gallus gallus	224-228
15638545-7	2005	Results from MOPAC and the molecular mechanics method (MM2) demonstrated that electrostatic interactions can take place between sulfonic and carboxyl groups of gamma-PGA-S and basic amino acid residues in FGF-2.	Amino Acids, Basic	176-192	fibroblast growth factor 2	Homo sapiens	205-210
15673927-5	2005	We propose that, because of the Phe508 deletion and polypeptide misfolding: (1) a forward-directing signal recognized by the sec24 component of the COPII complex that mediates ER exit is eliminated; (2) a basic amino acid signal recognized by the COPI machinery involved in Golgi to ER retrieval becomes activated; and (3) a tyrosine-based sorting signal that targets to the lysosomes likewise becomes activated.	Amino Acids, Basic	205-221	SEC24 homolog B, COPII coat complex component	Homo sapiens	125-130
15809202-1	2005	Analysis of published data reveals that the introduction of more basic amino acid residues in the flexible N-terminal region of the human tumour necrosis factor alpha (TNF) molecule indicates a weak but consistent trend towards increased in vitro cytotoxicity, especially when the effect of N-terminal length is taken into account.	Amino Acids, Basic	65-81	tumor necrosis factor	Homo sapiens	168-171
15541730-8	2005	P13 is rich in basic amino acids and in silico modeling of the EGFR in conjunction with our results suggests a novel role for the juxtamembrane domain (JM) of EGFR in mediating intracellular dimerization and thus receptor kinase activation and function.	Amino Acids, Basic	15-32	H3 histone pseudogene 6	Homo sapiens	0-3
15541730-8	2005	P13 is rich in basic amino acids and in silico modeling of the EGFR in conjunction with our results suggests a novel role for the juxtamembrane domain (JM) of EGFR in mediating intracellular dimerization and thus receptor kinase activation and function.	Amino Acids, Basic	15-32	epidermal growth factor receptor	Homo sapiens	159-163
15901925-2	2005	Its principle is based on the ability of the protein dye sulforhodamine B to bind electrostatically and pH dependent on protein basic amino acid residues of trichloroacetic acid-fixed cells.	Amino Acids, Basic	128-144	chaperonin containing TCP1 subunit 4	Homo sapiens	57-73
15498774-7	2004	Results from several deletion and point mutants using green fluorescent protein reporter show that SAF-1 contains two independent nuclear localization signals; one is composed of a stretch of basic amino acids, and the other is a bipartite signal located within the core DNA-binding domain.	Amino Acids, Basic	192-209	MYC associated zinc finger protein	Homo sapiens	99-104
16113502-7	2005	Another C-terminal-deficient mutant G(1-462) (termed CT1) was deprived of the whole cytoplasmic domain except for a basic amino acid left at the C-terminus, but was transported to the cell surface, where it showed pH-dependent cell fusion activity and almost full antigenicity to most of the anti-G mAbs with the exception of very weak antigenicity to mAb #1-30-44.	Amino Acids, Basic	116-132	cardiotrophin 1	Homo sapiens	53-56
15730807-9	2004	A consensus motif at the positions 8, 11, 18, and 25 in V3 loop was identified as follows: a sequence as "8-TXXS/GXXXXXXR/QXXXXXXE/D-25" will predict the usage of CCR5 coreceptor; a sequence replacing these positions with basic amino acids (except position 25) will very likely predict the usage of CXCR4 coreceptor.	Amino Acids, Basic	222-239	C-C motif chemokine receptor 5	Homo sapiens	163-167
15730807-9	2004	A consensus motif at the positions 8, 11, 18, and 25 in V3 loop was identified as follows: a sequence as "8-TXXS/GXXXXXXR/QXXXXXXE/D-25" will predict the usage of CCR5 coreceptor; a sequence replacing these positions with basic amino acids (except position 25) will very likely predict the usage of CXCR4 coreceptor.	Amino Acids, Basic	222-239	C-X-C motif chemokine receptor 4	Homo sapiens	299-304
15730807-10	2004	CONCLUSION: The biological characteristics of HIV isolates are linked to env V3 loop sequence variability: introducing basic amino acids (or translating from acidic amino acids into neutral amino acids) at the positions 8, 11, 18, and 25 in V3 loop will change viral strain"s biological phenotype from NSI/CCR5 to SI/CXCR4.	Amino Acids, Basic	119-136	C-C motif chemokine receptor 5	Homo sapiens	306-310
15730807-10	2004	CONCLUSION: The biological characteristics of HIV isolates are linked to env V3 loop sequence variability: introducing basic amino acids (or translating from acidic amino acids into neutral amino acids) at the positions 8, 11, 18, and 25 in V3 loop will change viral strain"s biological phenotype from NSI/CCR5 to SI/CXCR4.	Amino Acids, Basic	119-136	C-X-C motif chemokine receptor 4	Homo sapiens	317-322
15682870-2	2004	These genetically distinct proteins, CgA, CgB, SgII and the less well known secretogranins III-VII are collectively referred to as "granins" and characterised by numerous pairs of basic amino acids as potential cleavage sites for processing by the co-stored prohormone converting enzymes PC 1/3 and PC2.	Amino Acids, Basic	180-197	chromogranin B	Homo sapiens	42-45
15682870-2	2004	These genetically distinct proteins, CgA, CgB, SgII and the less well known secretogranins III-VII are collectively referred to as "granins" and characterised by numerous pairs of basic amino acids as potential cleavage sites for processing by the co-stored prohormone converting enzymes PC 1/3 and PC2.	Amino Acids, Basic	180-197	secretogranin II	Homo sapiens	47-51
15383602-1	2004	Carboxypeptidase R (CPR) is a heat-labile enzyme found in serum in addition to stable carboxypeptidase N. CPR cleaves the C-terminal basic amino acids, arginine and lysine, from inflammatory peptides such as complement C3a and C5a, bradykinin, and enkephalin.	Amino Acids, Basic	133-150	carboxypeptidase B2 (plasma)	Mus musculus	0-18
15568682-8	2004	The only common element found in most conformations of the active peptides was a helical character of fragment 8-13, which allowed the side chains of basic amino acid residues to be exposed to the outside of the molecule and probably to interact with the ORL1 receptor.	Amino Acids, Basic	150-166	opioid related nociceptin receptor 1	Homo sapiens	255-259
15464838-0	2004	A C-terminal basic amino acid motif of Zaire ebolavirus VP35 is essential for type I interferon antagonism and displays high identity with the RNA-binding domain of another interferon antagonist, the NS1 protein of influenza A virus.	Amino Acids, Basic	13-29	polymerase complex protein	Zaire ebolavirus	56-60
15464838-2	2004	To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production.	Amino Acids, Basic	142-158	polymerase complex protein	Zaire ebolavirus	26-30
15464838-2	2004	To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production.	Amino Acids, Basic	142-158	polymerase complex protein	Zaire ebolavirus	104-108
15464838-2	2004	To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production.	Amino Acids, Basic	142-158	interferon induced protein with tetratricopeptide repeats 1	Homo sapiens	195-200
15464838-2	2004	To identify the domain of VP35 responsible for interferon antagonism, we generated mutations within the VP35 gene and found that a C-terminal basic amino acid motif is required for inhibition of ISG56 reporter gene expression as well as IFN-beta production.	Amino Acids, Basic	142-158	interferon beta 1	Homo sapiens	237-245
15383602-1	2004	Carboxypeptidase R (CPR) is a heat-labile enzyme found in serum in addition to stable carboxypeptidase N. CPR cleaves the C-terminal basic amino acids, arginine and lysine, from inflammatory peptides such as complement C3a and C5a, bradykinin, and enkephalin.	Amino Acids, Basic	133-150	carboxypeptidase B2 (plasma)	Mus musculus	20-23
15383602-1	2004	Carboxypeptidase R (CPR) is a heat-labile enzyme found in serum in addition to stable carboxypeptidase N. CPR cleaves the C-terminal basic amino acids, arginine and lysine, from inflammatory peptides such as complement C3a and C5a, bradykinin, and enkephalin.	Amino Acids, Basic	133-150	carboxypeptidase B2 (plasma)	Mus musculus	106-109
15383602-1	2004	Carboxypeptidase R (CPR) is a heat-labile enzyme found in serum in addition to stable carboxypeptidase N. CPR cleaves the C-terminal basic amino acids, arginine and lysine, from inflammatory peptides such as complement C3a and C5a, bradykinin, and enkephalin.	Amino Acids, Basic	133-150	hemolytic complement	Mus musculus	227-230
15556297-2	2004	PAPA-1 comprises 345 amino acids with a basic amino-acid cluster.	Amino Acids, Basic	40-56	INO80 complex subunit B	Homo sapiens	0-6
15197186-8	2004	The amino acid sequence within this insert shows a high basic amino acid content in all of the kinases of the NDR family known to interact with MOB proteins.	Amino Acids, Basic	56-72	serine/threonine kinase 38	Homo sapiens	110-113
15197186-8	2004	The amino acid sequence within this insert shows a high basic amino acid content in all of the kinases of the NDR family known to interact with MOB proteins.	Amino Acids, Basic	56-72	sphingomyelin synthase 1	Homo sapiens	144-147
15252129-3	2004	Here we show that nuclear NIK also occurs in nucleoli and that this localization is mediated by a stretch of basic amino acids in the N-terminal part of the protein (R(143)-K-K-R-K-K-K(149)).	Amino Acids, Basic	109-126	mitogen-activated protein kinase kinase kinase 14	Homo sapiens	26-29
15222765-4	2004	RB38 contains four 70 amino acid repeats with a high percentage of basic amino acids, as well as an amino-terminal extension predicted to act as a chloroplast import sequence.	Amino Acids, Basic	67-84	uncharacterized protein	Chlamydomonas reinhardtii	0-4
15111623-0	2004	Structural model of MD-2 and functional role of its basic amino acid clusters involved in cellular lipopolysaccharide recognition.	Amino Acids, Basic	52-68	lymphocyte antigen 96	Homo sapiens	20-24
15178693-3	2004	Here we identify two basic amino acid residues within the L-selectin tail that are required for binding to ezrin-radixinmoesin (ERM) proteins: arginine 357 and lysine 362.	Amino Acids, Basic	21-37	selectin L	Homo sapiens	58-68
15148321-5	2004	Here, we have identified four basic amino acid residues (Lys-312, Lys-316, Lys-401, and Arg-409) in the basic surface of the Smad7 MH2 domain that play important roles in interaction with type I receptors.	Amino Acids, Basic	30-46	SMAD family member 7 L homeolog	Xenopus laevis	125-130
15148321-6	2004	Mutations of the four basic amino acid residues to acidic residues (K312E, K316E, K401E, and R409E) abolished the interaction of Smad7 with TGF-beta type I receptors, inhibition of Smad2 phosphorylation and transcriptional responses induced by TGF-beta, and induction of target genes of endogenous activin/Nodal signals in Xenopus early embryos.	Amino Acids, Basic	22-38	SMAD family member 7 L homeolog	Xenopus laevis	129-134
15148321-6	2004	Mutations of the four basic amino acid residues to acidic residues (K312E, K316E, K401E, and R409E) abolished the interaction of Smad7 with TGF-beta type I receptors, inhibition of Smad2 phosphorylation and transcriptional responses induced by TGF-beta, and induction of target genes of endogenous activin/Nodal signals in Xenopus early embryos.	Amino Acids, Basic	22-38	SMAD family member 2 S homeolog	Xenopus laevis	181-186
15218525-7	2004	This suggests that the amino-terminal basic amino-acid motif of mature BMP4 controls long-range activity for dorsoventral patterning of the vertebrate neural tube.	Amino Acids, Basic	38-54	bone morphogenetic protein 4	Mus musculus	71-75
15044392-3	2004	In the present study we construct and characterize one gC-1 mutant virus, in which two basic amino acids (114K and 117R) in a putative O-glycosylation sequon were changed to alanine.	Amino Acids, Basic	87-104	solute carrier family 25 member 22	Homo sapiens	55-59
15063792-2	2004	We previously identified the minimum nuclear localization signal (NLS) of AhR(13-39): it is composed of two basic amino acid segments, AhR(13-16:RKRR) and AhR(37-39:KRH).	Amino Acids, Basic	108-124	aryl hydrocarbon receptor	Homo sapiens	74-77
15184403-5	2004	The domains of LTBP-1 necessary for activation include the TGF-beta propeptide-binding domain and a basic amino acid sequence (hinge domain) with ECM targeting properties.	Amino Acids, Basic	100-116	latent transforming growth factor beta binding protein 1	Homo sapiens	15-21
14976207-5	2004	Secondary structure predictions suggest that a region contained within amino acids 546-565 of GRK5 forms an amphipathic helix, with the key features of the predicted helix being a hydrophobic patch of amino acids on one face of the helix, hydrophilic amino acids on the opposite face, and a number of basic amino acids surrounding the hydrophobic patch.	Amino Acids, Basic	301-318	G protein-coupled receptor kinase 5	Homo sapiens	94-98
15218525-4	2004	We created a GAL4/UAS bigenic mouse system to overexpress BMP4 or a mutant form of BMP4 (mutBMP4), which lacks a subset of amino-terminal basic amino acids that limits its range of action, in the dorsal neural tube.	Amino Acids, Basic	138-155	bone morphogenetic protein 4	Mus musculus	83-87
15087119-7	2004	In addition, to identify the nuclear localization signal of TBX5, we searched for cluster of basic amino acids.	Amino Acids, Basic	93-110	T-box transcription factor 5	Homo sapiens	60-64
14711814-4	2004	Nuclear import of the full-length ADAR1 is predominantly regulated by a nuclear localization signal at the C terminus (NLS-c), which consists of a bipartite basic amino acid motif plus the last 39 residues of ADAR1.	Amino Acids, Basic	157-173	adenosine deaminase, RNA-specific	Mus musculus	34-39
14715715-2	2004	These animals have a point mutation in carboxypeptidase E (CPE), an exopeptidase that removes C-terminal basic amino acids from peptide intermediates.	Amino Acids, Basic	105-122	carboxypeptidase E	Mus musculus	39-57
14715715-2	2004	These animals have a point mutation in carboxypeptidase E (CPE), an exopeptidase that removes C-terminal basic amino acids from peptide intermediates.	Amino Acids, Basic	105-122	carboxypeptidase E	Mus musculus	59-62
14749043-1	2004	INTRODUCTION: The primary structure of human chromogranin A (CgA) not only contains 10 pairs of basic amino acids, which are potential cleavage sites for specific endogenous proteases, but also other sites in the molecule can be subjected to cleavage.	Amino Acids, Basic	96-113	chromogranin A	Homo sapiens	45-59
14749043-1	2004	INTRODUCTION: The primary structure of human chromogranin A (CgA) not only contains 10 pairs of basic amino acids, which are potential cleavage sites for specific endogenous proteases, but also other sites in the molecule can be subjected to cleavage.	Amino Acids, Basic	96-113	chromogranin A	Homo sapiens	61-64
14660799-5	2003	This arginine transport defect in btn1-delta is complemented by expression of either BTN1 or the human CLN3 gene and strongly suggests a function for transport of, or regulation of the transport of, basic amino acids into the vacuole or lysosome for yeast Btn1p, and human CLN3 protein, respectively.	Amino Acids, Basic	199-216	CLN3 lysosomal/endosomal transmembrane protein, battenin	Homo sapiens	103-107
14699168-2	2004	P2X receptors comprise a family of ATP-gated ion channels with the basic amino acids Lys-68, Arg-292, and Lys-309 (P2X(1) receptor numbering) contributing to agonist potency.	Amino Acids, Basic	67-84	purinergic receptor P2X 1	Homo sapiens	115-130
14560312-2	2004	The gene encodes a zinc-finger transcription factor, which contains two regions with basic amino acids LRRRRG (NLS1) and RRRTRKR (NLS2) that resemble potential nuclear localization signals (NLSs).	Amino Acids, Basic	85-102	major facilitator superfamily domain containing 2A	Homo sapiens	111-115
14697214-9	2004	Thus, the NLS consisting of a cluster of basic amino acids with Pro and Tyr at the C-terminal end is novel and well conserved in the SIM proteins during evolution.	Amino Acids, Basic	41-58	SIM bHLH transcription factor 2	Homo sapiens	133-136
12962541-9	2004	The computed simulations detailing the docking of Pi1 peptides on to the Kv1.2 channels support an unexpected key role of specific basic amino acid residues, which form a basic ring (Arg-5, Arg-12, Arg-28 and Lys-31 residues), in toxin binding.	Amino Acids, Basic	131-147	Pancreas inflammation QTL 1	Rattus norvegicus	50-53
14514689-9	2003	Surprisingly, as well as residues adjacent to Switch I, in Switch II, and in helix alpha5, it appears that the C-terminal stretch of basic amino acids in Rac is required for a high affinity interaction with HR1b.	Amino Acids, Basic	133-150	Rac family small GTPase 1	Homo sapiens	154-157
14664719-4	2003	This can be surmounted by engineering the paired basic amino acid processing sites within proinsulin to sites that would be recognized by the ubiquitously expressed protease, furin.	Amino Acids, Basic	49-65	furin (paired basic amino acid cleaving enzyme)	Rattus norvegicus	175-180
14600268-8	2003	The existence of targeting information within the N-terminal motifs was confirmed by mutagenesis of residues corresponding to three conserved basic amino acids in hippocalcin and NCS-1 at positions 3, 7 and 9.	Amino Acids, Basic	142-159	neuronal calcium sensor 1	Homo sapiens	179-184
12888571-6	2003	Site-directed mutagenesis of active site residues demonstrated that replacement of a hydrophobic residue by a basic amino acid enabled the meprin alpha protease to cleave gastrin.	Amino Acids, Basic	110-126	gastrin	Homo sapiens	171-178
14645582-4	2003	For this purpose, we substituted alanines for two basic amino acids within NS1 (R38 and K41) that were previously found to be required for RNA binding.	Amino Acids, Basic	50-67	influenza virus NS1A binding protein	Homo sapiens	75-78
15127951-3	2003	On Leu-enkephalin, dynorphin (1-6), dynorphin (1-13), alpha-neoendorphin, and Lys-bradykinin, it showed a preferential aminopeptidase activity by cleaving off hydrophobic or basic amino acids.	Amino Acids, Basic	174-191	prodynorphin	Homo sapiens	3-17
15127951-3	2003	On Leu-enkephalin, dynorphin (1-6), dynorphin (1-13), alpha-neoendorphin, and Lys-bradykinin, it showed a preferential aminopeptidase activity by cleaving off hydrophobic or basic amino acids.	Amino Acids, Basic	174-191	kininogen 1	Homo sapiens	82-92
12960019-0	2003	Two basic amino acids C-terminal of the proximal box specify functional binding of the vitamin D receptor to its rat osteocalcin deoxyribonucleic acid-responsive element.	Amino Acids, Basic	4-21	vitamin D receptor	Rattus norvegicus	87-105
12960019-0	2003	Two basic amino acids C-terminal of the proximal box specify functional binding of the vitamin D receptor to its rat osteocalcin deoxyribonucleic acid-responsive element.	Amino Acids, Basic	4-21	bone gamma-carboxyglutamate protein	Rattus norvegicus	117-128
12960019-4	2003	Gel mobility shift and 1,25-dihydroxyvitamin D3-stimulated transcription assays verified that an hVDR-GR DBD chimera is functional on the rat osteocalcin VDRE with only the conservative change of lys-49 to arg, and of the negatively charged glu-53 to a basic amino acid (lys or arg).	Amino Acids, Basic	253-269	vitamin D receptor	Homo sapiens	97-101
12960019-4	2003	Gel mobility shift and 1,25-dihydroxyvitamin D3-stimulated transcription assays verified that an hVDR-GR DBD chimera is functional on the rat osteocalcin VDRE with only the conservative change of lys-49 to arg, and of the negatively charged glu-53 to a basic amino acid (lys or arg).	Amino Acids, Basic	253-269	bone gamma-carboxyglutamate protein	Rattus norvegicus	142-153
14688232-6	2003	When a basic amino acid residue was introduced at the cleavage site of Edg-1/S1P1, the molecular weight of the glycosylated protein was greater in the mutant compared to the wild type, due to the bound oligosaccharide.	Amino Acids, Basic	7-23	sphingosine-1-phosphate receptor 1	Homo sapiens	71-76
14688232-6	2003	When a basic amino acid residue was introduced at the cleavage site of Edg-1/S1P1, the molecular weight of the glycosylated protein was greater in the mutant compared to the wild type, due to the bound oligosaccharide.	Amino Acids, Basic	7-23	sphingosine-1-phosphate receptor 1	Homo sapiens	77-81
12939146-4	2003	HP-RNase has basic amino acids at positions where RNase A shows instead neutral residues.	Amino Acids, Basic	13-30	ribonuclease A family member 1, pancreatic	Homo sapiens	0-8
12939146-4	2003	HP-RNase has basic amino acids at positions where RNase A shows instead neutral residues.	Amino Acids, Basic	13-30	ribonuclease A family member 1, pancreatic	Homo sapiens	50-57
12921785-4	2003	The deduced sequence of mature bovine TFPI-2 revealed a short acidic amino-terminal region, three tandem Kunitz-type domains, and a carboxy-terminal tail highly enriched in basic amino acids.	Amino Acids, Basic	173-190	tissue factor pathway inhibitor 2	Bos taurus	38-44
12941609-5	2003	The carboxyl terminus of Mybbp1a, which contains seven short basic amino acid repeat sequences, is responsible for both nuclear and nucleolar localization, and this activity can be transferred to a heterologous protein.	Amino Acids, Basic	61-77	MYB binding protein 1a	Homo sapiens	25-32
12944468-4	2003	Here we show that the two basic amino acid groups in the p53 bipartite NLS function collaboratively to import p53.	Amino Acids, Basic	26-42	tumor protein p53	Homo sapiens	57-60
12944468-4	2003	Here we show that the two basic amino acid groups in the p53 bipartite NLS function collaboratively to import p53.	Amino Acids, Basic	26-42	tumor protein p53	Homo sapiens	110-113
12893261-4	2003	Several distinct domains are discernable in the ORF of pNO40, including a ribosomal protein S1 RNA binding region, a CCHC type zinc finger, and clusters of basic amino acid representing potential nucleolar targeting signal.	Amino Acids, Basic	156-172	zinc finger CCHC-type containing 17	Homo sapiens	55-60
12801587-2	2003	Enzymes such as the prohormone convertases and carboxypeptidase E are highly specific for these basic amino acid-containing sites.	Amino Acids, Basic	96-112	carboxypeptidase E	Homo sapiens	47-65
12662153-10	2003	Our data revealed further the critical role of the last two basic amino acid residues (e.g. Lys(82)-Arg(83) for the mouse PC1/3 sequence) of the prodomain in imparting a strong anti-convertase activity.	Amino Acids, Basic	60-76	proprotein convertase subtilisin/kexin type 1	Mus musculus	122-127
12684504-2	2003	The primary region of apoE responsible for receptor binding has been limited to a cluster of basic amino acids between residues 134 and 150, located in the fourth helix of the N-terminal domain globular helix bundle structure.	Amino Acids, Basic	93-110	apolipoprotein E	Homo sapiens	22-26
12665517-8	2003	Cleavage of model peptide substrates occurred on the C-terminal side of basic amino acids, and Km for this reaction was approximately 200-fold greater than that for gp120 cleavage, indicating Ab specialization for the gp120 substrate.	Amino Acids, Basic	72-89	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	165-170
12637530-5	2003	We determined that mutation of basic amino acids located within the beta1-beta2 and beta3-beta4 loops of the PH domain resulted in impaired phospholipid binding in vitro, yet full guanine nucleotide exchange activity in vitro was retained for RhoA and Cdc42.	Amino Acids, Basic	31-48	ras homolog family member A	Mus musculus	243-247
12637530-5	2003	We determined that mutation of basic amino acids located within the beta1-beta2 and beta3-beta4 loops of the PH domain resulted in impaired phospholipid binding in vitro, yet full guanine nucleotide exchange activity in vitro was retained for RhoA and Cdc42.	Amino Acids, Basic	31-48	cell division cycle 42	Mus musculus	252-257
12802008-6	2003	PTPRQ does not have either of the basic amino acids in the catalytic domain that are important for the PIPase activity of PTEN or the sequence motifs that are characteristic of type II phosphatidylinositol 5-phosphatases.	Amino Acids, Basic	34-51	protein tyrosine phosphatase receptor type Q	Homo sapiens	0-5
12665517-8	2003	Cleavage of model peptide substrates occurred on the C-terminal side of basic amino acids, and Km for this reaction was approximately 200-fold greater than that for gp120 cleavage, indicating Ab specialization for the gp120 substrate.	Amino Acids, Basic	72-89	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	218-223
12641447-4	2003	By utilizing residue-specific chemical modification and site-directed mutagenesis techniques, we revealed that the acidic amino acid residues on PEDF (Asp(255), Asp(257), and Asp(299)) are critical to collagen binding, and three clustered basic amino acid residues (Arg(145), Lys(146), and Arg(148)) are necessary for heparin binding.	Amino Acids, Basic	239-255	serpin family F member 1	Homo sapiens	145-149
12825692-4	2003	PtaAGP6 resembles tomato LeAGP-1 and Arabidopsis AtAGP17-19 in that they all possess a subdomain composed of basic amino acids.	Amino Acids, Basic	109-126	arabinogalactan protein 17	Arabidopsis thaliana	49-56
12646039-12	2003	N-terminally truncated RHA2a also directed nuclear localization, apparently dependent on basic amino acids in the RING-H2 domain.	Amino Acids, Basic	89-106	RING-H2 finger A2A	Arabidopsis thaliana	23-28
12631327-1	2003	We describe the identification and functional characterization of two Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also known as Arg11p.	Amino Acids, Basic	96-112	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	129-136
12634901-7	2003	The vgf gene encodes a polypeptide rich in paired basic amino acids; this polypeptide is differentially processed in neuronal and neuroendocrine cells and is released via the regulated secretory pathway.	Amino Acids, Basic	50-67	VGF nerve growth factor inducible	Rattus norvegicus	4-7
12631327-1	2003	We describe the identification and functional characterization of two Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also known as Arg11p.	Amino Acids, Basic	96-112	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	141-148
12631327-1	2003	We describe the identification and functional characterization of two Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also known as Arg11p.	Amino Acids, Basic	96-112	Ort1p	Saccharomyces cerevisiae S288C	205-210
12631327-1	2003	We describe the identification and functional characterization of two Arabidopsis mitochondrial basic amino acid carriers (BAC), AtmBAC1 and AtmBAC2, which are related to the yeast ornithine (Orn) carrier Ort1p, also known as Arg11p.	Amino Acids, Basic	96-112	Ort1p	Saccharomyces cerevisiae S288C	226-232
12675515-3	2003	By applying phage display technology, we have identified a putative uPA-binding consensus sequence BXXSSXXB (where B represents a basic amino acid and X represents any amino acid), which has no apparent sequence correlation to uPAR.	Amino Acids, Basic	130-146	plasminogen activator, urokinase	Homo sapiens	68-71
12517962-3	2003	The tapasin dependence of HLA class I alleles bearing different residues at position 114 decreases in the order of acidity, with high tapasin dependence for acidic amino acids (aspartic acid and glutamic acid), moderate dependence for neutral amino acids (asparagine and glutamine), and low dependence for basic amino acids (histidine and arginine).	Amino Acids, Basic	306-323	TAP binding protein	Homo sapiens	4-11
12609044-5	2003	Mutation of the conserved basic amino acids in this motif, or the deletion of N-terminal 64 amino acids containing this motif significantly compromised or abolished the ability of NtMEK2DD to activate SIPK/WIPK in vivo.	Amino Acids, Basic	26-43	mitogen-activated protein kinase kinase 5-like	Nicotiana tabacum	180-186
12914653-5	2003	Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE in being a carboxypeptidase that preferentially removes carboxy-terminal hydrophobic or basic amino acids; it appears to be important in cardiac function.	Amino Acids, Basic	172-189	angiotensin I converting enzyme	Homo sapiens	13-16
12515824-3	2003	Mitochondrial targeting of Bcl-x(L) requires the COOH-terminal transmembrane (TM) domain flanked at both ends by at least two basic amino acids.	Amino Acids, Basic	126-143	BCL2 like 1	Homo sapiens	27-35
12914653-5	2003	Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE in being a carboxypeptidase that preferentially removes carboxy-terminal hydrophobic or basic amino acids; it appears to be important in cardiac function.	Amino Acids, Basic	172-189	angiotensin converting enzyme 2	Homo sapiens	26-30
12914653-5	2003	Recently, an ACE homolog, ACE2, has been identified in humans that differs from ACE in being a carboxypeptidase that preferentially removes carboxy-terminal hydrophobic or basic amino acids; it appears to be important in cardiac function.	Amino Acids, Basic	172-189	angiotensin I converting enzyme	Homo sapiens	26-29
12491096-4	2002	A major characteristic of many spherical RNA viruses appears to be the positioning of A-type double helical segments of 7-9 basepairs at icosahedral symmetry axes, probably interacting via its phosphates with basic amino acid residues of the coat protein in a sequence-independent manner.	Amino Acids, Basic	209-225	golgi phosphoprotein 3	Homo sapiens	242-254
12553726-4	2002	Deletions at both termini and point mutations of different basic amino acids especially within the extended C-terminal tail of human S100A9 were introduced.	Amino Acids, Basic	59-76	S100 calcium binding protein A9	Homo sapiens	133-139
12408990-4	2002	Using surface plasmon resonance biosensor analysis, we also provided direct evidence of the influence of basic amino acids in the interaction between V3 and the amino terminal domain of CCR5.	Amino Acids, Basic	105-122	C-C motif chemokine receptor 5	Homo sapiens	186-190
12472693-6	2002	Examination of the amino acid sequence of NPK1 showed that at the carboxyl-terminal region in the regulatory domain, which contains the binding site of NACK1, NPK1 contained a cluster of basic amino acids that resemble a bipartite nuclear localization signal (NLS).	Amino Acids, Basic	187-204	mitogen-activated protein kinase kinase kinase NPK1	Nicotiana tabacum	42-46
12472693-6	2002	Examination of the amino acid sequence of NPK1 showed that at the carboxyl-terminal region in the regulatory domain, which contains the binding site of NACK1, NPK1 contained a cluster of basic amino acids that resemble a bipartite nuclear localization signal (NLS).	Amino Acids, Basic	187-204	kinesin-like protein NACK1	Nicotiana tabacum	152-157
12472693-6	2002	Examination of the amino acid sequence of NPK1 showed that at the carboxyl-terminal region in the regulatory domain, which contains the binding site of NACK1, NPK1 contained a cluster of basic amino acids that resemble a bipartite nuclear localization signal (NLS).	Amino Acids, Basic	187-204	mitogen-activated protein kinase kinase kinase NPK1	Nicotiana tabacum	159-163
12223482-4	2002	In the search for Pex16p topogenic sequence, basic amino acids clustered sequence, RKELRKKLPVSLSQQK, at positions 66-81 and the first transmembrane segment locating far downstream, nearly by 40 amino acids, of this basic region were defined to be essential for integration into peroxisome membranes.	Amino Acids, Basic	45-62	peroxisomal biogenesis factor 16	Homo sapiens	18-24
12241547-0	2002	An analysis of target preferences of Escherichia coli outer-membrane endoprotease OmpT for use in therapeutic peptide production: efficient cleavage of substrates with basic amino acids at the P4 and P6 positions.	Amino Acids, Basic	168-185	outer membrane protease	Escherichia coli	82-86
12429519-4	2002	Vpr contains a carboxy-terminal basic amino acid rich segment stretch that is homologous to domains that mediate the energy- and receptor-independent cellular uptake of polypeptides by a process termed protein transduction.	Amino Acids, Basic	32-48	Vpr	Human immunodeficiency virus 1	0-3
12241547-1	2002	The Escherichia coli outer-membrane endoprotease OmpT mainly cleaves peptide bonds between consecutive basic amino acids.	Amino Acids, Basic	103-120	outer membrane protease	Escherichia coli	49-53
12296828-0	2002	Carboxyl-terminal basic amino acids in the X domain are essential for the nuclear import of phospholipase C delta1.	Amino Acids, Basic	18-35	phospholipase C delta 1	Canis lupus familiaris	92-114
12531031-8	2002	Alignment of the N-terminal sequence of human and mouse NTH1 showed that mNTH1 lacks a basic amino acid cluster corresponding to one of the NLS sequences found in hNTH1.	Amino Acids, Basic	87-103	nth (endonuclease III)-like 1 (E.coli)	Mus musculus	73-78
12021356-11	2002	These basic amino acids on pRB define a discrete interaction point with E7.	Amino Acids, Basic	6-23	RB transcriptional corepressor 1	Homo sapiens	27-30
12186856-7	2002	Although Etf1 does not contain a known 3-phosphoinositide-binding domain (i.e., FYVE or Phox), we find that Etf1 interacts with PtdIns(3)P and that this interaction requires a basic amino acid motif (KKPAKK) within the cytosolic region of the protein.	Amino Acids, Basic	176-192	eukaryotic translation termination factor 1	Homo sapiens	108-112
11932252-11	2002	Our studies indicate that the basic amino acids present in the tail play an important role in cleavage, and this mechanism is specific to aggrecan.	Amino Acids, Basic	30-47	aggrecan	Homo sapiens	138-146
12047381-3	2002	Recently, a neural counterpart of hnRNP I has been identified that contains a putative NLS with two strings of basic amino acids separated by a spacer of 30 residues.	Amino Acids, Basic	111-128	polypyrimidine tract binding protein 1	Homo sapiens	34-41
12070165-5	2002	In vitro studies have identified five clusters of basic amino acids in delipidated apoB48 that bind negatively charged glycosaminoglycans.	Amino Acids, Basic	50-67	apolipoprotein B	Homo sapiens	83-89
12066187-6	2002	The interaction between atherogenic lipoproteins and proteoglycans involves an ionic interaction between basic amino acids in apoB100 and negatively charged sulphate groups on the proteoglycans.	Amino Acids, Basic	105-122	apolipoprotein B	Mus musculus	126-133
11914920-5	2002	These data suggest a protein segment rich in basic amino acids to be important for the binding to Prm1- and Prm2-mRNA.	Amino Acids, Basic	45-62	protamine 1	Homo sapiens	98-102
11893746-5	2002	Sequence analysis of the cloned murine CMP-Neu5Ac synthetase identified three clusters of basic amino acids (BC1-BC3) that might function as nuclear localization signals (NLS).	Amino Acids, Basic	90-107	brain cytoplasmic RNA 1	Mus musculus	109-116
11960773-2	2002	It is presumed that progastrin is cleaved at pairs of basic amino acids by a prohormone convertase to form a glycine-extended intermediate (G-Gly) that serves as a substrate for peptidyl-glycine alpha-amidating monooxygenase (PAM), resulting in COOH-terminally amidated gastrin.	Amino Acids, Basic	54-71	gastrin	Canis lupus familiaris	23-30
11971977-0	2002	Mutational analysis of all conserved basic amino acids in RAG-1 reveals catalytic, step arrest, and joining-deficient mutants in the V(D)J recombinase.	Amino Acids, Basic	37-54	recombination activating 1	Homo sapiens	58-63
11969400-8	2002	Basic amino acids within the N-terminal arm of Nhp6Ap are required for high-affinity binding to the cisplatin adduct as well as to unmodified DNA.	Amino Acids, Basic	0-17	high-mobility group nucleosome-binding protein	Saccharomyces cerevisiae S288C	47-53
11782474-3	2002	Two regions in the FOXC1 forkhead domain, one rich in basic amino acid residues, and a second, highly conserved among all FOX proteins, were necessary for nuclear localization of the FOXC1 protein.	Amino Acids, Basic	54-70	forkhead box C1	Homo sapiens	19-24
11782474-3	2002	Two regions in the FOXC1 forkhead domain, one rich in basic amino acid residues, and a second, highly conserved among all FOX proteins, were necessary for nuclear localization of the FOXC1 protein.	Amino Acids, Basic	54-70	forkhead box C1	Homo sapiens	183-188
11914920-5	2002	These data suggest a protein segment rich in basic amino acids to be important for the binding to Prm1- and Prm2-mRNA.	Amino Acids, Basic	45-62	protamine 2	Homo sapiens	108-112
11948238-1	2002	Inhibitor-of-differentiation 2 (Id2) belongs to a family of transcriptional modulators that are characterized by a helix loop helix region but lack the basic amino acid domain.	Amino Acids, Basic	152-168	inhibitor of DNA binding 2	Mus musculus	0-30
11948238-1	2002	Inhibitor-of-differentiation 2 (Id2) belongs to a family of transcriptional modulators that are characterized by a helix loop helix region but lack the basic amino acid domain.	Amino Acids, Basic	152-168	inhibitor of DNA binding 2	Mus musculus	32-35
11866094-1	2002	Though OmpT has been reported to mainly cleave the peptide bond between consecutive basic amino acids, we identified more precise substrate specificity by using a series of modified substrates, termed PRX fusion proteins, consisting of 184 residues.	Amino Acids, Basic	84-101	outer membrane protease	Escherichia coli	7-11
11799183-2	2002	The VP1 N terminus contains a number of groups of basic amino acids which resemble classical nuclear localization sequences, including a conserved sequence near the N terminus comprised of four basic amino acids, which in a peptide can act to transport other proteins into the cell nucleus.	Amino Acids, Basic	50-67	VP1	Canine parvovirus	4-7
11799183-2	2002	The VP1 N terminus contains a number of groups of basic amino acids which resemble classical nuclear localization sequences, including a conserved sequence near the N terminus comprised of four basic amino acids, which in a peptide can act to transport other proteins into the cell nucleus.	Amino Acids, Basic	194-211	VP1	Canine parvovirus	4-7
11706008-10	2002	Alanine mutations of membrane-proximal basic amino acid residues in the cytoplasmic domain of L-selectin identified arginine 357 as a critical residue for both ezrin and moesin interaction.	Amino Acids, Basic	39-55	selectin L	Homo sapiens	94-104
11706008-10	2002	Alanine mutations of membrane-proximal basic amino acid residues in the cytoplasmic domain of L-selectin identified arginine 357 as a critical residue for both ezrin and moesin interaction.	Amino Acids, Basic	39-55	ezrin	Homo sapiens	160-165
11706008-10	2002	Alanine mutations of membrane-proximal basic amino acid residues in the cytoplasmic domain of L-selectin identified arginine 357 as a critical residue for both ezrin and moesin interaction.	Amino Acids, Basic	39-55	moesin	Homo sapiens	170-176
11866094-3	2002	OmpT under denaturing conditions (in the presence of 4 M urea) cleaved not only between two consecutive basic amino acids but also at the carboxyl side of Arg140 except for the Arg140-Asp141, -Glu141, and -Pro141 pairs.	Amino Acids, Basic	104-121	outer membrane protease	Escherichia coli	0-4
11546762-4	2001	Systematic mutagenesis of the GAP-43 and PSD-95 palmitoylation motifs indicates that the spacing of the palmitoylated cysteines and the presence of nearby basic amino acids determine polarized targeting by these two motifs.	Amino Acids, Basic	155-172	growth associated protein 43	Homo sapiens	30-36
11809829-6	2002	We also demonstrate that Nullo is a myristoylprotein and that the myristate group acts in conjunction with a cluster of basic amino acids to target Nullo to the plasma membrane.	Amino Acids, Basic	120-137	nullo	Drosophila melanogaster	25-30
11809829-6	2002	We also demonstrate that Nullo is a myristoylprotein and that the myristate group acts in conjunction with a cluster of basic amino acids to target Nullo to the plasma membrane.	Amino Acids, Basic	120-137	nullo	Drosophila melanogaster	148-153
11878899-0	2001	Membrane activity of the southern cowpea mosaic virus coat protein: the role of basic amino acids, helix-forming potential, and lipid composition.	Amino Acids, Basic	80-97	golgi phosphoprotein 3	Homo sapiens	54-66
11730482-2	2001	A pentapeptide, Gly-Arg-Arg-Arg-Arg, corresponding to a region of the N-terminal portion of human Lf rich in basic amino acids, was synthesized and its intracellular localization was investigated.	Amino Acids, Basic	109-126	HLF transcription factor, PAR bZIP family member	Homo sapiens	98-100
11546762-4	2001	Systematic mutagenesis of the GAP-43 and PSD-95 palmitoylation motifs indicates that the spacing of the palmitoylated cysteines and the presence of nearby basic amino acids determine polarized targeting by these two motifs.	Amino Acids, Basic	155-172	discs large MAGUK scaffold protein 4	Homo sapiens	41-47
11342582-3	2001	Three basic amino acids in the carboxyl terminal region of LpL were mutated, yielding an active enzyme with reduced heparin binding.	Amino Acids, Basic	6-23	lipoprotein lipase	Mus musculus	59-62
11382778-0	2001	High affinity binding of receptor-associated protein to heparin and low density lipoprotein receptor-related protein requires similar basic amino acid sequence motifs.	Amino Acids, Basic	134-150	LDL receptor related protein associated protein 1	Homo sapiens	25-52
11382778-0	2001	High affinity binding of receptor-associated protein to heparin and low density lipoprotein receptor-related protein requires similar basic amino acid sequence motifs.	Amino Acids, Basic	134-150	LDL receptor related protein 1	Homo sapiens	80-116
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Amino Acids, Basic	100-117	LDL receptor related protein associated protein 1	Homo sapiens	52-55
11382778-5	2001	Several motifs were found to mediate the binding of RAP to heparin, and each contained a cluster of basic amino acids; among them, an intact R(282)VSR(285)SR(287)EK(289) motif is required for high affinity binding of RAP to heparin, whereas two other motifs, R(203)LR(205)R(206) and R(314)ISR(317)AR(319), also contribute to this interaction.	Amino Acids, Basic	100-117	LDL receptor related protein associated protein 1	Homo sapiens	217-220
11746662-7	2001	Results show that (1) the hair-forming activity of LSP1 is localized to the basic C-terminal half of the molecule, which contains all of the F-actin binding domains; (2) both the caldesmon-like domains and the villin headpiece-like domains are required for the hair-forming activity of LSP1; (3) basic amino acids in the villin headpiece regions are crucial for the hair-forming activity of LSP1 molecule.	Amino Acids, Basic	296-313	lymphocyte specific protein 1	Homo sapiens	51-55
11453649-3	2001	Here we have identified a novel domain rich in basic amino acids at the extreme C-terminus of Hsf1.	Amino Acids, Basic	47-64	stress-responsive transcription factor HSF1	Saccharomyces cerevisiae S288C	94-98
11323437-9	2001	Using chimeric SHP proteins and mutagenesis studies, the nuclear localization signal of SHP-1 was identified within the C-terminal domain of SHP-1 and found to consist of a short cluster of basic amino acids (KRK).	Amino Acids, Basic	190-207	protein tyrosine phosphatase non-receptor type 6	Homo sapiens	88-93
11384227-2	2001	Basic amino acid residues in the V3 loop of HIV Env allow efficient coreceptor utilization of X4.	Amino Acids, Basic	0-16	endogenous retrovirus group K member 20	Homo sapiens	48-51
11279119-0	2001	Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor alpha-Subunit.	Amino Acids, Basic	9-25	caspase recruitment domain family member 16	Homo sapiens	53-56
11279119-0	2001	Adjacent basic amino acid residues recognized by the COP I complex and ubiquitination govern endoplasmic reticulum to cell surface trafficking of the nicotinic acetylcholine receptor alpha-Subunit.	Amino Acids, Basic	9-25	cholinergic receptor nicotinic alpha 1 subunit	Homo sapiens	150-196
11343794-0	2001	Synthesis and hydrolysis by cathepsin B of fluorogenic substrates with the general structure benzoyl-X-ARG-MCA containing non-natural basic amino acids at position X.	Amino Acids, Basic	134-151	cathepsin B	Homo sapiens	28-39
11311142-9	2001	It is concluded that basic amino acids in a restricted C-terminal region of rPLD(1) are important for binding of RhoA and its activation of PLD activity.	Amino Acids, Basic	21-38	phospholipase D1	Rattus norvegicus	76-83
11311142-9	2001	It is concluded that basic amino acids in a restricted C-terminal region of rPLD(1) are important for binding of RhoA and its activation of PLD activity.	Amino Acids, Basic	21-38	ras homolog family member A	Rattus norvegicus	113-117
11316783-0	2001	Mutagenesis of basic amino acids in the carboxyl-terminal region of insulin-like growth factor binding protein-5 affects acid-labile subunit binding.	Amino Acids, Basic	15-32	insulin like growth factor binding protein 5	Homo sapiens	68-112
11322758-4	2001	Primary sequence analysis of ErbB-3 identified a basic amino acid cluster (466)KHNRPRR(472) localized to the proximal, cysteine-rich extracellular ligand binding domain of the receptor, with charge density and distribution compatible with, but different to, known linear heparin binding motifs.	Amino Acids, Basic	49-65	erb-b2 receptor tyrosine kinase 3	Homo sapiens	29-35
11423119-0	2001	Requirements of basic amino acid residues within the lectin-like domain of LOX-1 for the binding of oxidized low-density lipoprotein.	Amino Acids, Basic	16-32	oxidized low density lipoprotein receptor 1	Homo sapiens	75-80
11278650-1	2001	Basic amino acid residues differentially contribute to CX3CR1 binding, signaling, and cell adhesion.	Amino Acids, Basic	0-16	C-X3-C motif chemokine receptor 1	Homo sapiens	55-61
11145957-4	2001	The N- and C-terminal cleavage sites where pro-IAPP is processed by prohormone convertases contain a series of basic amino acid residues that we hypothesized may interact with heparan sulfate proteoglycans.	Amino Acids, Basic	111-127	islet amyloid polypeptide	Homo sapiens	47-51
11328610-0	2001	A cluster of basic amino acid residues in calcineurin b participates in the binding of calcineurin to phosphatidylserine vesicles.	Amino Acids, Basic	13-29	protein phosphatase 3 regulatory subunit B, alpha	Homo sapiens	42-55
11383885-1	2001	Prohormone convertases PC1 and PC2 are endoproteases involved in prohormone cleavage at pairs of basic amino acids.	Amino Acids, Basic	97-114	proprotein convertase subtilisin/kexin type 1	Rattus norvegicus	23-26
11383885-1	2001	Prohormone convertases PC1 and PC2 are endoproteases involved in prohormone cleavage at pairs of basic amino acids.	Amino Acids, Basic	97-114	proprotein convertase subtilisin/kexin type 2	Rattus norvegicus	31-34
11171125-8	2001	These results therefore add to our understanding of the nature of the interaction between MIP-1alpha and proteoglycans and suggests that the basic amino acids might not be the sole regulators of proteoglycan binding.	Amino Acids, Basic	141-158	C-C motif chemokine ligand 3	Homo sapiens	90-100
11259764-2	2001	Its precursor protein, prepro-OFQ/N (ppOFQ/N) contains several series of amino acids bounded by pairs of basic amino acids, raising the possibility that additional functional neuropeptides could be generated by proteolytic posttranslational processing.	Amino Acids, Basic	105-122	prepronociceptin	Mus musculus	30-35
11172713-3	2001	Site-directed mutagenesis targeting each conserved basic amino acid in RAG2 revealed several separation-of-function mutants that address these questions.	Amino Acids, Basic	51-67	recombination activating 2	Homo sapiens	71-75
28095235-1	2001	To explain the insurmountable/long-lasting binding of biphenyltetrazole-containing AT1-receptor antagonists such as candesartan, to the human angiotensin II type 1-receptor, a model is proposed in which the basic amino acids Lys199 and Arg 167 of the receptor interact respectively with the carboxylate and the tetrazole group of the antagonists.	Amino Acids, Basic	207-224	angiotensin II receptor type 1	Homo sapiens	142-172
11013258-6	2001	This is the first demonstration that, to activate the VPAC(1) receptor, the Asp(3) side chain of VIP must penetrate within the transmembrane domain, in close proximity to two highly conserved basic amino acids from transmembrane 2.	Amino Acids, Basic	192-209	vasoactive intestinal peptide receptor 1	Homo sapiens	54-70
11013258-6	2001	This is the first demonstration that, to activate the VPAC(1) receptor, the Asp(3) side chain of VIP must penetrate within the transmembrane domain, in close proximity to two highly conserved basic amino acids from transmembrane 2.	Amino Acids, Basic	192-209	vasoactive intestinal peptide	Homo sapiens	97-100
11235919-0	2001	A tale of two charges: distinct roles for an acidic and a basic amino acid in the structure and function of cytochrome c.	Amino Acids, Basic	58-74	cytochrome c, somatic	Equus caballus	108-120
10961991-6	2000	The sequence surrounding this lysine conforms to a consensus SUMO-1 modification site b(X)XXhKXE, where b is a basic amino acid.	Amino Acids, Basic	111-127	small ubiquitin like modifier 1	Homo sapiens	61-67
11148456-11	2001	This is related to the interactions between negative charges of sulfate groups of proteoglycans and positive charges of basic amino acids in N-terminal side of B2M.	Amino Acids, Basic	120-137	beta-2-microglobulin	Homo sapiens	160-163
10991942-3	2000	The loop between the H helix and C2 sheet of kallistatin containing clusters of basic amino acid residues has been identified as a heparin-binding site.	Amino Acids, Basic	80-96	serpin family A member 4	Homo sapiens	45-56
11029577-4	2000	Amyloid-beta peptide (Abeta) has a cluster of basic amino acids at the N-terminus (residues 13-16, His-His-Gln-Lys), which are considered critical for glycosaminoglycan interactions.	Amino Acids, Basic	46-63	amyloid beta precursor protein	Homo sapiens	22-27
11027265-4	2000	Fluorescence microscopy studies using green fluorescent protein (GFP)-fusion proteins indicate that both yeast SmB and SmD1 basic amino acid stretches exhibit nuclear localization properties.	Amino Acids, Basic	124-140	mRNA splicing protein SMD1	Saccharomyces cerevisiae S288C	119-123
10931201-3	2000	We have cloned a cDNA encoding a novel Pim-1 binding protein, PAP-1, comprising 213 amino acids with a basic amino-acid cluster near the C-terminus.	Amino Acids, Basic	103-119	Pim-1 proto-oncogene, serine/threonine kinase	Homo sapiens	39-44
10950986-2	2000	ORF1 is predicted to encode a replication-associated protein (Rep) essential for replication of viral DNA, while ORF2 contains a conserved basic amino acid sequence at the N terminus resembling that of the major structural protein of chicken anaemia virus.	Amino Acids, Basic	139-155	capsid protein	Porcine circovirus 2	113-117
11881039-2	2000	To investigate the involved basic amino-acids of the human AT1-receptor, wild-type and mutant receptors were transiently transfected in CHO-K1 cells and characterised by [3H]candesartan binding.	Amino Acids, Basic	28-45	angiotensin II receptor type 1	Homo sapiens	59-62
10925289-9	2000	Site-directed mutagenesis of the basic amino acids in the KRYK (VI) or KYEK (VII) sequences to acidic amino acids create mutants that bind F-actin with lower affinity than full-length wild-type LSP1.	Amino Acids, Basic	33-50	lymphocyte specific protein 1	Homo sapiens	194-198
10931201-3	2000	We have cloned a cDNA encoding a novel Pim-1 binding protein, PAP-1, comprising 213 amino acids with a basic amino-acid cluster near the C-terminus.	Amino Acids, Basic	103-119	RP9 pre-mRNA splicing factor	Homo sapiens	62-67
10777485-10	2000	Therefore, for the substrate recognition by ry(+)LAT1, the positive charge on basic amino acid side chains or that conferred by inorganic monovalent cations such as Na(+) and H(+), which are cotransported with neutral amino acids, is presumed to be required.	Amino Acids, Basic	78-94	solute carrier family 7 member 5 L homeolog	Xenopus laevis	49-53
10899939-8	2000	The cellular distribution is altered by treatment with taxol, nocodazole, and cytochalasin D. The tubulin binding domain was located at the N terminus of GABARAP by using synthetic peptides and deletion constructs and is marked by a specific arrangement of basic amino acids.	Amino Acids, Basic	257-274	GABA type A receptor-associated protein	Homo sapiens	154-161
10899939-12	2000	The structural arrangement of the basic amino acids present in the tubulin binding domain of GABARAP may aid in recognition of the potential of tubulin binding activity in other known proteins.	Amino Acids, Basic	34-51	GABA type A receptor-associated protein	Homo sapiens	93-100
10801814-3	2000	MUK-binding inhibitory protein (MBIP) contains two tandemly orientated leucine-zipper-like motifs with a cluster of basic amino acids located between the two motifs.	Amino Acids, Basic	116-133	MAP3K12 binding inhibitory protein 1	Homo sapiens	0-30
10801814-3	2000	MUK-binding inhibitory protein (MBIP) contains two tandemly orientated leucine-zipper-like motifs with a cluster of basic amino acids located between the two motifs.	Amino Acids, Basic	116-133	MAP3K12 binding inhibitory protein 1	Homo sapiens	32-36
10777485-3	2000	ry(+)LAT1-mediated transport of basic amino acids was Na(+)-independent, whereas that of neutral amino acids, although not completely, was dependent on Na(+), as is typical of system y(+)L-mediated transport.	Amino Acids, Basic	32-49	solute carrier family 7 member 5 L homeolog	Xenopus laevis	5-9
10777485-11	2000	We further demonstrate that ry(+)LAT1, due to its peculiar cation dependence, mediates a heteroexchange, wherein the influx of substrate amino acids is accompanied by the efflux of basic amino acids.	Amino Acids, Basic	181-198	solute carrier family 7 member 5 L homeolog	Xenopus laevis	33-37
10873651-5	2000	Computational analysis revealed that Klp1 has a leucine-zipper-like structure, a Leu-X-X-Leu-Leu motif, and a putative nuclear localization signal in the basic amino acid rich region.	Amino Acids, Basic	154-170	N-acetyltransferase 14 (putative)	Homo sapiens	37-41
10830477-4	2000	Substitution of Asp76 to Ser or Thr and deletion of Ser78, corresponding to the mammalian aspartic proteinases, cathepsin D and pepsin, caused drastic decreases in the activities towards substrates containing a basic amino acid residue at 1.	Amino Acids, Basic	211-227	cathepsin D	Homo sapiens	112-123
10888599-5	2000	Here, we show that FXR2P contains in its C-terminal part, a stretch of basic amino acids "RPQRRNRSRRRRFR" that resemble the nucleolar-targeting signal (NoS) of the viral protein Rev.	Amino Acids, Basic	71-88	FMR1 autosomal homolog 2	Homo sapiens	19-24
10900462-5	2000	This family of PCs is currently comprised of fewer than a dozen members, known as furin/paired basic amino-acid-cleaving enzyme (PACE), PC1/PC3, PC2, PC4, PACE4, PC5/PC6, and PC7/PC8/lymphoma proprotein convertase.	Amino Acids, Basic	95-111	furin (paired basic amino acid cleaving enzyme)	Mus musculus	82-87
10762650-3	2000	The BLM protein is homologous to DNA helicase and has two basic amino acid clusters in its C-terminal region.	Amino Acids, Basic	58-74	BLM RecQ like helicase	Homo sapiens	4-7
10762650-4	2000	Previously, we reported that the distal arm of these basic amino acids clusters in the BLM protein functioned as the nuclear localization signal (NLS) of the protein.	Amino Acids, Basic	53-70	BLM RecQ like helicase	Homo sapiens	87-90
10762650-5	2000	In this study, we generated plasmid constructs for expression of enhanced green fluorescent protein (EGFP) fused with various BLM protein variants having a mutation with deletions or substitutions in the basic amino acid and analyzed the subcellular localization of the expressed proteins.	Amino Acids, Basic	204-220	BLM RecQ like helicase	Homo sapiens	126-129
10762650-6	2000	The EGFP-fused protein containing the basic amino acid cluster region proximal to the C-terminus of BLM helicase was localized exclusively in the nucleus.	Amino Acids, Basic	38-54	BLM RecQ like helicase	Homo sapiens	100-103
10762650-9	2000	Mouse BLM protein which also migrate to the nucleus has two basic amino acid clusters in the C-terminus and the basic amino acids (Lys1346-Pro1347-Lys1348-Arg1349-Arg1350) proximal to the C-terminus are conserved between mouse and human.	Amino Acids, Basic	60-76	Bloom syndrome, RecQ like helicase	Mus musculus	6-9
10762650-9	2000	Mouse BLM protein which also migrate to the nucleus has two basic amino acid clusters in the C-terminus and the basic amino acids (Lys1346-Pro1347-Lys1348-Arg1349-Arg1350) proximal to the C-terminus are conserved between mouse and human.	Amino Acids, Basic	112-129	Bloom syndrome, RecQ like helicase	Mus musculus	6-9
10882540-6	2000	The predicted VGF sequence is rich in paired basic amino acid residues that are potential sites for proteolytic processing, and VGF undergoes regulated release from dense core secretory vesicles.	Amino Acids, Basic	45-61	VGF nerve growth factor inducible	Rattus norvegicus	14-17
10799289-3	2000	Here we show that a polypeptide encompassing the C-terminal cluster of basic amino acids of netrin-1 (i) adopts an alpha-helical conformation in water-trifluoroethanol mixtures according to circular dichroism experiments and (ii) binds electrostatically to heparin with high affinity under physiological ionic conditions (K(D) = 15 nM for the binding to immobilized heparin according to surface plasmon resonance, K(D) = 50 nM in solution as determined with isothermal titration calorimetry).	Amino Acids, Basic	71-88	netrin 1	Homo sapiens	92-100
10799289-4	2000	These data indicate that the cluster of basic amino acids at the C-terminus of netrin-1 forms an alpha-helical structural element which can contribute to the glycosaminoglycan-binding activity of this neurotrophic guidance molecule.	Amino Acids, Basic	40-57	netrin 1	Homo sapiens	79-87
10707958-3	2000	Alteration of either of these basic amino acids to alanine also compromised hVDR transcriptional activity.	Amino Acids, Basic	30-47	vitamin D receptor	Homo sapiens	76-80
10671548-1	2000	CD98 is a type II transmembrane protein involved in neutral and basic amino acid transport and in cell fusion events.	Amino Acids, Basic	64-80	solute carrier family 3 member 2	Homo sapiens	0-4
10657249-1	2000	Several integrin alpha subunits undergo post-translational endoproteolytic processing at pairs of basic amino acids that is mediated by the proprotein convertase furin.	Amino Acids, Basic	98-115	furin, paired basic amino acid cleaving enzyme	Homo sapiens	162-167
10652159-6	2000	B-cell binding correlated with basic amino acids in the VH-CDR3.	Amino Acids, Basic	31-48	CDR3	Homo sapiens	59-63
10652159-8	2000	These anti-ssDNA reactive monoclonal antibodies had basic amino acids in the VH-CDR3, strongly supporting the suggested role of arginine in DNA binding.	Amino Acids, Basic	52-69	CDR3	Homo sapiens	80-84
11996121-2	2000	Krr1p contains a motif of clustered basic amino acids highly conserved in the evolutionarly distant species from yeast to human.	Amino Acids, Basic	36-53	ribosome biosynthesis protein KRR1	Saccharomyces cerevisiae S288C	0-5
10580115-6	1999	From mouse testes, two forms of Bv8 mRNA have been characterized, of which one contains an additional exon which codes for 21 mostly basic amino acids.	Amino Acids, Basic	133-150	prokineticin 2	Mus musculus	32-35
10753724-5	2000	By use of a series of artificially generated mutants, the RNA-binding domain of p23 was mapped between positions 50-86, a region containing several basic amino acids and a putative zinc-finger domain.	Amino Acids, Basic	148-165	prostaglandin E synthase 3	Homo sapiens	80-83
10523755-1	1999	The presence of pairs of basic amino acids within the orphanin FQ/Nociceptin (OFQ/N) sequence has raised the possibility that truncated versions of the peptide might be physiologically important.	Amino Acids, Basic	25-42	prepronociceptin	Mus musculus	54-76
10523755-1	1999	The presence of pairs of basic amino acids within the orphanin FQ/Nociceptin (OFQ/N) sequence has raised the possibility that truncated versions of the peptide might be physiologically important.	Amino Acids, Basic	25-42	prepronociceptin	Mus musculus	78-83
10545103-4	1999	This interacting motif contains critical basic amino acid residues that are required for stimulation of PLD activity by phosphoinositides.	Amino Acids, Basic	41-57	phospholipase D	Saccharomyces cerevisiae S288C	104-107
10562541-3	1999	We demonstrate that transmembrane segment 6 of CFTR, which contains three basic amino acids, is extremely unstable in the lipid bilayer upon membrane insertion in vitro and in vivo.	Amino Acids, Basic	74-91	CF transmembrane conductance regulator	Homo sapiens	47-51
10491208-1	1999	The N-terminal end of thyroid transcription factor-1 (TTF-1) homeodomain is composed of a stretch of five basic amino-acids that is conserved in both POU- and NK2-class homeodomains and constitutes a functional nuclear localization signal.	Amino Acids, Basic	106-123	NK2 homeobox 1	Homo sapiens	22-52
10491208-1	1999	The N-terminal end of thyroid transcription factor-1 (TTF-1) homeodomain is composed of a stretch of five basic amino-acids that is conserved in both POU- and NK2-class homeodomains and constitutes a functional nuclear localization signal.	Amino Acids, Basic	106-123	NK2 homeobox 1	Homo sapiens	54-59
10393815-4	1999	Various FGF2 mutants originated by deletion or substitution of basic amino acid residues in the amino terminus or in the carboxyl terminus of FGF2 retained the capacity to induce a long-lasting activation of ERK1/2 in BAE cells.	Amino Acids, Basic	63-79	fibroblast growth factor 2	Bos taurus	8-12
12903814-5	1999	When the two basic amino acids (K) at position 178 and 189 of TFIIB were substituted by neutral amino acids (L), the binding of TFIIB K178L and K189L to HBX was siginificantly reduced.	Amino Acids, Basic	13-30	general transcription factor IIB	Homo sapiens	62-67
12903814-5	1999	When the two basic amino acids (K) at position 178 and 189 of TFIIB were substituted by neutral amino acids (L), the binding of TFIIB K178L and K189L to HBX was siginificantly reduced.	Amino Acids, Basic	13-30	general transcription factor IIB	Homo sapiens	128-133
12903814-6	1999	When the the basic amino acids were substituted by the acidic amino acids (E), the binding of TFIIB K178E and K189E to HBX were almost lost.	Amino Acids, Basic	13-30	general transcription factor IIB	Homo sapiens	94-99
10573124-7	1999	In addition, certain basic amino acid residues conserved between mammalian SRP14 and Srp14p are essential for RNA binding in both proteins.	Amino Acids, Basic	21-37	signal recognition particle 14	Homo sapiens	75-80
10573124-7	1999	In addition, certain basic amino acid residues conserved between mammalian SRP14 and Srp14p are essential for RNA binding in both proteins.	Amino Acids, Basic	21-37	signal recognition particle 14	Homo sapiens	85-91
10508788-8	1999	P38gamma residue phosphoryl-Thr183 forms hydrogen bonds with five basic amino acids, and these interactions induce an interdomain rotation.	Amino Acids, Basic	66-83	mitogen-activated protein kinase 12	Homo sapiens	0-8
10535306-6	1999	Single point mutations of basic amino acids within the basic region of CREB2 identified the sequence KKLKK (amino acids 280 to 284) as important for nuclear targeting.	Amino Acids, Basic	26-43	activating transcription factor 4	Homo sapiens	71-76
10413594-11	1999	The amino acids in the nonbasic intervening region of Ku70 might be important for full NLS activity not only to provide sufficient length between the two separated clusters of basic amino acids but also to have an adequate amino acid sequence.	Amino Acids, Basic	176-193	X-ray repair cross complementing 6	Homo sapiens	54-58
10413594-12	1999	All of the basic amino acid residues in the basic subregions were conserved among mammalian and avian homologues, confirming their importance in the nuclear translocation of Ku70.	Amino Acids, Basic	11-27	X-ray repair cross complementing 6	Homo sapiens	174-178
10393815-4	1999	Various FGF2 mutants originated by deletion or substitution of basic amino acid residues in the amino terminus or in the carboxyl terminus of FGF2 retained the capacity to induce a long-lasting activation of ERK1/2 in BAE cells.	Amino Acids, Basic	63-79	mitogen-activated protein kinase 3	Bos taurus	208-214
10393104-1	1999	Kex2 in the yeast Saccharomyces cerevisiae is a transmembrane, Ca2+-dependent serine protease of the subtilisin-like pro-protein convertase (SPC) family with specificity for cleavage after paired basic amino acids.	Amino Acids, Basic	196-213	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Amino Acids, Basic	45-62	insulin-like growth factor binding protein 5	Rattus norvegicus	66-73
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Amino Acids, Basic	45-62	insulin-like growth factor 1	Rattus norvegicus	144-149
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Amino Acids, Basic	45-62	insulin-like growth factor binding protein 5	Rattus norvegicus	257-264
10425523-7	1999	We therefore propose that heparin binding to basic amino acids in IGFBP-5 between 201-218 may physically occlude subsequent interaction between IGF-I and Gly203/Gln209, and that this may explain previous work of others showing reduced affinity of ECM bound IGFBP-5 for IGF-I.	Amino Acids, Basic	45-62	insulin-like growth factor 1	Rattus norvegicus	269-274
10497893-0	1999	Mutational analysis of Raf-1 cysteine rich domain: requirement for a cluster of basic aminoacids for interaction with phosphatidylserine.	Amino Acids, Basic	80-96	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	23-28
10444088-8	1999	A range of amino acids inhibited citrulline uptake, suggesting that RcAAP3 may be a broad substrate permease that can transport neutral and basic amino acids with a lower affinity for acidic amino acids.	Amino Acids, Basic	140-157	amino acid permease 3	Ricinus communis	68-74
10393104-1	1999	Kex2 in the yeast Saccharomyces cerevisiae is a transmembrane, Ca2+-dependent serine protease of the subtilisin-like pro-protein convertase (SPC) family with specificity for cleavage after paired basic amino acids.	Amino Acids, Basic	196-213	surfactant protein C	Homo sapiens	141-144
10430019-2	1999	The protein, called Tsg118, has a predicted molecular mass of 59.4 kDa and a high content of basic amino acids.	Amino Acids, Basic	93-110	lysine rich nucleolar protein 1	Homo sapiens	20-26
10420092-5	1999	The African lungfish POMC encodes a tetrapod-like gamma-MSH sequence that is flanked by sets of paired basic amino acid proteolytic cleavage sites.	Amino Acids, Basic	103-119	proopiomelanocortin S homeolog	Xenopus laevis	21-25
10336644-3	1999	Using inhibitors of angiotensin I-converting enzyme (ACE) and CP, we show that both these enzymes in mouse serum can remove the basic amino acids from the C-terminus of CCK5-GRR and LH-RH-GKR, but only CP is responsible for converting diarginyl insulin to insulin.	Amino Acids, Basic	128-145	angiotensin I converting enzyme	Homo sapiens	20-51
10336644-3	1999	Using inhibitors of angiotensin I-converting enzyme (ACE) and CP, we show that both these enzymes in mouse serum can remove the basic amino acids from the C-terminus of CCK5-GRR and LH-RH-GKR, but only CP is responsible for converting diarginyl insulin to insulin.	Amino Acids, Basic	128-145	angiotensin I converting enzyme	Homo sapiens	53-56
10382669-2	1999	We show here that granzyme B can be redesigned by a single amino acid substitution in one wall of the specificity pocket, arginine-226 to glutamate, to hydrolyze preferentially thioester substrates following basic amino acids.	Amino Acids, Basic	208-225	granzyme B	Mus musculus	18-28
10383055-1	1999	Pleiotrophin (HB-GAM), an extracellular matrix-associated protein with a high content of basic amino acid residues, is expressed in the central nervous system during late pre- and early post-natal development and promotes neurite outgrowth in vitro.	Amino Acids, Basic	89-105	pleiotrophin	Rattus norvegicus	0-12
10383055-1	1999	Pleiotrophin (HB-GAM), an extracellular matrix-associated protein with a high content of basic amino acid residues, is expressed in the central nervous system during late pre- and early post-natal development and promotes neurite outgrowth in vitro.	Amino Acids, Basic	89-105	pleiotrophin	Rattus norvegicus	14-20
10328871-4	1999	These interactions were inhibited by synthetic peptides mimicking the sequences of the basic amino acid cluster located at the C-terminal end of mouse and human IFN-gamma, or by poly-L-lysine, suggesting that ionic interactions between the positively-charged C-terminus and negatively charged groups in GAGs were involved.	Amino Acids, Basic	87-103	interferon gamma	Homo sapiens	161-170
10341419-10	1999	The KEX1 disruption strain may be a useful tool for the expression of other proteins with a C-terminal basic amino acid.	Amino Acids, Basic	103-119	serine-type carboxypeptidase	Saccharomyces cerevisiae S288C	4-8
10196205-1	1999	Protease inhibitor 10 (PI-10), an intracellular ovalbumin-serpin, contains a series of basic amino acids in the loop between helices C and D that exhibit homology to known nuclear targeting signals.	Amino Acids, Basic	87-104	serpin family B member 10	Homo sapiens	0-28
9795050-5	1998	In vitro release experiments indicated that an initial lysozyme release rate from the microspheres was mainly controlled by ionic interaction between basic amino acid residues in lysozyme and free carboxylate groups in PLGA polymer chain ends, which was probed by incubating the microspheres in a series of media having different NaCl concentrations.	Amino Acids, Basic	150-166	lysozyme	Homo sapiens	55-63
10069410-10	1999	rpL7 fragments rich in basic amino acids could be identified as epitopes recognized by the TCR of three cell lines.	Amino Acids, Basic	23-40	ribosomal protein L7	Homo sapiens	0-4
10780449-5	1999	Also, it was shown that the mutations in the basic amino acid residues abolish the repression and inhibition of spore formation by Rme1p in vivo.	Amino Acids, Basic	45-61	Rme1p	Saccharomyces cerevisiae S288C	131-136
9830050-1	1998	Nearly identical proteins (denoted NAA-Tr, rBAT, D2, NBAT), cloned from mammalian kidneys, induce a largely sodium-independent high-affinity transport system for cystine, basic amino acids, and some neutral amino acids in Xenopus oocytes (system b0,+-like).	Amino Acids, Basic	171-188	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	43-47
9830050-1	1998	Nearly identical proteins (denoted NAA-Tr, rBAT, D2, NBAT), cloned from mammalian kidneys, induce a largely sodium-independent high-affinity transport system for cystine, basic amino acids, and some neutral amino acids in Xenopus oocytes (system b0,+-like).	Amino Acids, Basic	171-188	solute carrier family 3 member 1	Homo sapiens	53-57
9819387-6	1998	In contrast, deletion of the C1 domain or an adjacent cluster of basic amino acids eliminated the transforming activity of mRasGRP.	Amino Acids, Basic	65-82	RAS guanyl releasing protein 1	Mus musculus	123-130
10198291-3	1999	This site contains a basic amino acid recognition sequence (R-G-R-K-R-R) for proprotein convertases of the furin/PACE family.	Amino Acids, Basic	21-37	furin, paired basic amino acid cleaving enzyme	Homo sapiens	107-112
10198291-3	1999	This site contains a basic amino acid recognition sequence (R-G-R-K-R-R) for proprotein convertases of the furin/PACE family.	Amino Acids, Basic	21-37	furin, paired basic amino acid cleaving enzyme	Homo sapiens	113-117
10191286-5	1999	Using in vitro RNA editing assay, we found that basic amino acid clusters at the amino-terminal region R15R16R17 and R33K34, are essential for apoB mRNA editing.	Amino Acids, Basic	48-64	apolipoprotein B	Homo sapiens	143-147
9813010-7	1998	The mutant cyt b5, in which the acidic amino acid in its carboxyl-terminal end was replaced by basic amino acid, could be transported to the mitochondria.	Amino Acids, Basic	95-111	cytochrome b5 type A	Homo sapiens	11-17
9795050-5	1998	In vitro release experiments indicated that an initial lysozyme release rate from the microspheres was mainly controlled by ionic interaction between basic amino acid residues in lysozyme and free carboxylate groups in PLGA polymer chain ends, which was probed by incubating the microspheres in a series of media having different NaCl concentrations.	Amino Acids, Basic	150-166	lysozyme	Homo sapiens	179-187
9786917-1	1998	The transcription factor ATF-2 (also called CRE-BP1), whose DNA-binding domain consists of a basic amino acid cluster and a leucine zipper (b-ZIP) region, binds to the cAMP response element as a homodimer or as a heterodimer with c-Jun.	Amino Acids, Basic	93-109	activating transcription factor 2	Homo sapiens	25-30
9765428-7	1998	Mutational analysis revealed that both myristoylation and an N-terminal cluster of basic amino acids were required for virion incorporation and for plasma membrane targeting of Nef.	Amino Acids, Basic	83-100	S100 calcium binding protein B	Homo sapiens	177-180
9786917-1	1998	The transcription factor ATF-2 (also called CRE-BP1), whose DNA-binding domain consists of a basic amino acid cluster and a leucine zipper (b-ZIP) region, binds to the cAMP response element as a homodimer or as a heterodimer with c-Jun.	Amino Acids, Basic	93-109	activating transcription factor 2	Homo sapiens	44-51
9740326-6	1998	These findings support the hypothesis that polysulphate binding sites on proacrosin are formed by a restricted number of basic amino acids on the surface of the protein, presenting a specific orientation that is complementary to negatively charged sulphate groups on zona glycoproteins.	Amino Acids, Basic	121-138	acrosin	Homo sapiens	73-83
9790687-2	1998	BNP was tentatively identified as a heparin-binding protein on the basis of its cyclic structure and the high frequency of the basic amino acid residues, lysine and arginine.	Amino Acids, Basic	127-143	natriuretic peptide B	Homo sapiens	0-3
9784842-7	1998	The basic amino acid cluster in this region may be contribute to the binding of HBp17 to heparin or heparan sulfate proteoglycan on the cell surface and extracellular matrix.	Amino Acids, Basic	4-20	fibroblast growth factor binding protein 1	Homo sapiens	80-85
9725901-12	1998	The findings suggest that specific basic amino acids at positions 207 and 214 mediate the binding of IGFBP-5 to pSMC/ECM.	Amino Acids, Basic	35-52	insulin like growth factor binding protein 5	Homo sapiens	101-108
9488702-3	1998	We substituted Ala, Lys, His, Asp, and Asn mutations for Arg to evaluate the role of a basic amino acid at position 197 in SP-A action.	Amino Acids, Basic	87-103	surfactant protein A1	Rattus norvegicus	123-127
9642296-10	1998	However, potato TOM7 has a N-terminal extension, which is very rich in basic amino acids.	Amino Acids, Basic	71-88	Tom7p	Saccharomyces cerevisiae S288C	16-20
9637922-4	1998	We have mapped the ezrin-binding site to two clusters of basic amino acids in a membrane-proximal 9 amino-acid region within the CD44 cytoplasmic domain.	Amino Acids, Basic	57-74	CD44 molecule (Indian blood group)	Homo sapiens	129-133
9681993-1	1998	A region of basic amino acids spanning residues 639-656 in the human 5-lipoxygenase sequence resembles a consensus bipartite nuclear localizing sequence.	Amino Acids, Basic	12-29	arachidonate 5-lipoxygenase	Homo sapiens	69-83
9668120-0	1998	A basic amino acid in the cytoplasmic domain of Alzheimer"s beta-amyloid precursor protein (APP) is essential for cleavage of APP at the alpha-site.	Amino Acids, Basic	2-18	amyloid beta precursor protein	Homo sapiens	60-90
9655916-0	1998	Differential requirements for basic amino acids in transcription factor IIIA-5S gene interaction.	Amino Acids, Basic	30-47	general transcription factor 3A L homeolog	Xenopus laevis	51-76
9655916-1	1998	Basic amino acids Arg, Lys, and His in the Cys2His2 zinc fingers of transcription factor IIIA (TFIIIA) potentially have important roles in factor binding to the extended internal control region (ICR) of the 5S ribosomal gene.	Amino Acids, Basic	0-17	general transcription factor 3A L homeolog	Xenopus laevis	68-93
9655916-1	1998	Basic amino acids Arg, Lys, and His in the Cys2His2 zinc fingers of transcription factor IIIA (TFIIIA) potentially have important roles in factor binding to the extended internal control region (ICR) of the 5S ribosomal gene.	Amino Acids, Basic	0-17	general transcription factor 3A L homeolog	Xenopus laevis	95-101
9632111-1	1998	The human vitamin D receptor (hVDR) possesses a unique array of five basic amino acids positioned between the two DNA-binding zinc fingers that is similar to well-characterized nuclear localization sequences in other proteins.	Amino Acids, Basic	69-86	vitamin D receptor	Homo sapiens	10-28
9632111-1	1998	The human vitamin D receptor (hVDR) possesses a unique array of five basic amino acids positioned between the two DNA-binding zinc fingers that is similar to well-characterized nuclear localization sequences in other proteins.	Amino Acids, Basic	69-86	vitamin D receptor	Homo sapiens	30-34
9637699-3	1998	In vitro studies have identified eight clusters of basic amino acids in delipidated apo-B100, the protein moiety of LDL, that bind the negatively charged proteoglycans.	Amino Acids, Basic	51-68	apolipoprotein B	Homo sapiens	84-92
9603966-5	1998	Scanning the surface of this region identified three basic amino acids Lys249, Arg307, and Lys311 flanking a small crevice on the p66 thumb subdomain outside the primer-template binding cleft.	Amino Acids, Basic	53-70	DNA polymerase delta 3, accessory subunit	Homo sapiens	130-133
9657386-0	1998	Substrate-dependent activation requirements and kinetic properties of protein kinase C. Protein kinase C (PKC) requires basic amino acids around the phosphorylated Ser or Thr.	Amino Acids, Basic	120-137	protein kinase C alpha	Homo sapiens	106-109
9604002-1	1998	The removal of N-terminally located clusters of basic amino acids (N-tail) or C-terminally located clusters of basic amino acids (C-tail) from the midkine (MK) molecule severely reduced its neurite-promoting activity.	Amino Acids, Basic	111-128	midkine	Homo sapiens	147-154
9604002-1	1998	The removal of N-terminally located clusters of basic amino acids (N-tail) or C-terminally located clusters of basic amino acids (C-tail) from the midkine (MK) molecule severely reduced its neurite-promoting activity.	Amino Acids, Basic	111-128	midkine	Homo sapiens	156-158
9632883-1	1998	Viral transcription factor Tat is a small nuclear protein containing a large number of basic amino acids.	Amino Acids, Basic	87-104	tyrosine aminotransferase	Homo sapiens	27-30
9461550-8	1998	Like Fe65, Fe65L1 and Fe65L2 genes encode two different protein isoforms, derived from the alternative splicing of a very small exon of only six nucleotides, which results, within the N-terminal PID/PTB domain, in the presence or absence of two acidic/basic amino acids.	Amino Acids, Basic	252-269	amyloid beta precursor protein binding family B member 1	Rattus norvegicus	5-9
9604002-0	1998	Clusters of basic amino acids in midkine: roles in neurite-promoting activity and plasminogen activator-enhancing activity.	Amino Acids, Basic	12-29	midkine	Homo sapiens	33-40
9461491-6	1998	We demonstrate in vitro a novel activity of ACE that removes pairs of basic amino acid residues from a locustamyotropin peptide extended at the C-terminus with either Gly-Lys-Arg or Gly-Arg-Arg, corresponding to a consensus recognition sequence for endoproteolysis of prohormone proteins by prohormone convertases.	Amino Acids, Basic	70-86	angiotensin I converting enzyme	Homo sapiens	44-47
9461550-8	1998	Like Fe65, Fe65L1 and Fe65L2 genes encode two different protein isoforms, derived from the alternative splicing of a very small exon of only six nucleotides, which results, within the N-terminal PID/PTB domain, in the presence or absence of two acidic/basic amino acids.	Amino Acids, Basic	252-269	amyloid beta precursor protein binding family B member 3	Rattus norvegicus	22-28
9341152-2	1997	Cleavage occurs carboxyl-terminally of basic amino acid motifs, such as RX(K/R)R, RXXR, and (R/K)R. As already available for the other known mammalian members of this enzyme family, we here define structural and functional features of human lymphoma proprotein convertase (LPC).	Amino Acids, Basic	39-55	proprotein convertase subtilisin/kexin type 7	Homo sapiens	241-271
9452465-13	1998	In both wild-type and mutant islets, proinsulin I was processed more rapidly to insulin, reflecting the preference of both PC2 and PC3 for substrates having a basic amino acid positioned four residues upstream of the cleavage site.	Amino Acids, Basic	159-175	insulin II	Mus musculus	37-47
9452465-13	1998	In both wild-type and mutant islets, proinsulin I was processed more rapidly to insulin, reflecting the preference of both PC2 and PC3 for substrates having a basic amino acid positioned four residues upstream of the cleavage site.	Amino Acids, Basic	159-175	proprotein convertase subtilisin/kexin type 2	Mus musculus	123-126
9452465-13	1998	In both wild-type and mutant islets, proinsulin I was processed more rapidly to insulin, reflecting the preference of both PC2 and PC3 for substrates having a basic amino acid positioned four residues upstream of the cleavage site.	Amino Acids, Basic	159-175	proprotein convertase subtilisin/kexin type 1	Mus musculus	131-134
9445004-8	1998	The functional domains, including the two cysteines at positions 114 and 133, a serine phosphorylation site at position 144, and the C-terminal basic amino acids essential for vif protein function, were highly conserved in most of the sequences.	Amino Acids, Basic	144-161	Vif	Human immunodeficiency virus 1	176-179
9417098-0	1998	Replacements of single basic amino acids in the pleckstrin homology domain of phospholipase C-delta1 alter the ligand binding, phospholipase activity, and interaction with the plasma membrane.	Amino Acids, Basic	23-40	phospholipase C delta 1	Homo sapiens	78-100
9417098-9	1998	To investigate the role of these basic residues, we have performed site-directed mutagenesis replacing each of the basic amino acid in the N-terminal 60 residues of PLC-delta1 (Lys24, Lys30, Lys32, Arg37, Arg38, Arg40, Lys43, Lys49, Arg56, Lys57, and Arg60) with a neutral or an acidic amino acid.	Amino Acids, Basic	115-131	phospholipase C delta 1	Homo sapiens	165-175
9427758-4	1998	While wild-type HNF3 protein does not compact DNA extending from the nucleosome, as does linker histone, site-directed mutants of HNF3 can compact nucleosomal DNA if they contain basic amino acids at positions previously shown to be essential for nucleosomal DNA compaction by linker histones.	Amino Acids, Basic	179-196	forkhead box M1	Homo sapiens	130-134
9747901-1	1998	The presence of pairs of basic amino acids within the sequence of orphanin FQ/nociceptin (OFQ/N) peptide, the endogenous ligand for the ORL1/KOR-3 receptor, has raised the possibility that processing might generate pharmacologically important truncated peptides, including OFQ/N(1-11).	Amino Acids, Basic	25-42	prepronociceptin	Mus musculus	66-88
9747901-1	1998	The presence of pairs of basic amino acids within the sequence of orphanin FQ/nociceptin (OFQ/N) peptide, the endogenous ligand for the ORL1/KOR-3 receptor, has raised the possibility that processing might generate pharmacologically important truncated peptides, including OFQ/N(1-11).	Amino Acids, Basic	25-42	prepronociceptin	Mus musculus	90-95
9747901-1	1998	The presence of pairs of basic amino acids within the sequence of orphanin FQ/nociceptin (OFQ/N) peptide, the endogenous ligand for the ORL1/KOR-3 receptor, has raised the possibility that processing might generate pharmacologically important truncated peptides, including OFQ/N(1-11).	Amino Acids, Basic	25-42	opioid receptor-like 1	Mus musculus	136-140
9747901-1	1998	The presence of pairs of basic amino acids within the sequence of orphanin FQ/nociceptin (OFQ/N) peptide, the endogenous ligand for the ORL1/KOR-3 receptor, has raised the possibility that processing might generate pharmacologically important truncated peptides, including OFQ/N(1-11).	Amino Acids, Basic	25-42	prepronociceptin	Mus musculus	273-278
9405039-5	1997	With these peptides, the recognition sequence for gamma-PAK has been shown to contain two basic amino acids in the -2 and -3 positions, as represented by (K/R)RXS, in which the -2 position is an arginine, the -3 position is an arginine or a lysine, and X can be an acidic, basic, or neutral amino acid.	Amino Acids, Basic	90-107	p21 (RAC1) activated kinase 2	Homo sapiens	50-59
9405039-9	1997	The substrate requirements of protein kinases that recognize basic amino acids on the N-terminal side of the phosphorylatable residue such as cAMP-dependent protein kinase (PKA) and Ca2+/phospholipid-dependent protein kinase (PKC) have been compared with gamma-PAK using the same peptides.	Amino Acids, Basic	61-78	p21 (RAC1) activated kinase 2	Homo sapiens	255-264
9398246-2	1997	In this study, we have mutated two putative G protein-coupling regions of CXCR2 and characterized the effects of these mutations on ligand-activated signal transductions: aspartic acid 89 in the second transmembrane domain and the HRAMR sequence (BBXXB motif, found in the third intracellular loop where B indicates a basic amino acid and X represents any amino acid).	Amino Acids, Basic	318-334	C-X-C motif chemokine receptor 2	Homo sapiens	74-79
9362504-5	1997	Nuclear localization of glypican beta-galactosidase or Fc fusion proteins in transfected 293 cells and C6 glioma cells was greatly reduced or abolished after mutation of the basic amino acids or deletion of the sequence containing the nuclear localization signal, and no nuclear staining was seen in the case of heparan sulfate and chondroitin sulfate proteoglycans that do not possess a nuclear localization signal, such as syndecan-3 or decorin (which is closely related in structure to biglycan).	Amino Acids, Basic	174-191	glypican 1	Homo sapiens	24-32
9362504-5	1997	Nuclear localization of glypican beta-galactosidase or Fc fusion proteins in transfected 293 cells and C6 glioma cells was greatly reduced or abolished after mutation of the basic amino acids or deletion of the sequence containing the nuclear localization signal, and no nuclear staining was seen in the case of heparan sulfate and chondroitin sulfate proteoglycans that do not possess a nuclear localization signal, such as syndecan-3 or decorin (which is closely related in structure to biglycan).	Amino Acids, Basic	174-191	galactosidase beta 1	Homo sapiens	33-51
9362294-1	1997	The submandibular rat 1 protein (SMR1) is selectively processed at pairs of basic amino acid residues in a tissue- and sex-specific manner.	Amino Acids, Basic	76-92	submaxillary gland androgen regulated protein 3B	Rattus norvegicus	4-31
9362294-1	1997	The submandibular rat 1 protein (SMR1) is selectively processed at pairs of basic amino acid residues in a tissue- and sex-specific manner.	Amino Acids, Basic	76-92	submaxillary gland androgen regulated protein 3B	Rattus norvegicus	33-37
9299339-9	1997	Furthermore, the loop region between beta2 and beta3 of the Sxl RBD1 has an exceptional cluster of aromatic amino acid residues, in place of the normal basic amino acid cluster.	Amino Acids, Basic	152-168	beta-Tubulin at 85D	Drosophila melanogaster	37-52
9299339-9	1997	Furthermore, the loop region between beta2 and beta3 of the Sxl RBD1 has an exceptional cluster of aromatic amino acid residues, in place of the normal basic amino acid cluster.	Amino Acids, Basic	152-168	Sex lethal	Drosophila melanogaster	60-63
9299339-9	1997	Furthermore, the loop region between beta2 and beta3 of the Sxl RBD1 has an exceptional cluster of aromatic amino acid residues, in place of the normal basic amino acid cluster.	Amino Acids, Basic	152-168	l(3)62Bi	Drosophila melanogaster	64-68
9210463-7	1997	Point mutations engineered at the Arg-rich motif of HIV-1 Nef revealed that basic amino acid residues are essential for RNA-binding activity.	Amino Acids, Basic	76-92	Nef	Human immunodeficiency virus 1	58-61
9346931-8	1997	The implications of the present results are discussed regarding (a) the apparent dual function of certain basic amino acid residues in the HMG domain of SRY in both DNA binding and in nuclear localization and (b) the possible control of SOX9 in early gonadal differentiation at the level of nuclear translocation.	Amino Acids, Basic	106-122	sex determining region Y	Homo sapiens	153-156
9346305-8	1997	Neutralization of basic amino acids in the PCI molecule by glutamic acid, which prevented in a dose-dependent way the inhibitory effect of heparin, did not have any effect on the tissue-kallikrein-PCI interaction.	Amino Acids, Basic	18-35	serpin family A member 5	Homo sapiens	43-46
9346305-9	1997	Therefore, direct involvement of basic amino acid residues present in the heparin-binding site of PCI in the tissue-kallikrein-PCI interaction can be excluded.	Amino Acids, Basic	33-49	serpin family A member 5	Homo sapiens	98-101
9328258-4	1997	Molecular genetic analysis disclosed a missense mutation in the connexin32 gene in codon 15 (Arg15Trp) which predicts the replacement of a basic amino acid to a non-polar amino acid in the first cytoplasmic loop of the protein.	Amino Acids, Basic	139-155	gap junction protein beta 1	Homo sapiens	64-74
9268357-3	1997	Human RB possesses a bipartite nuclear localization sequence (NLS) consisting of two clusters of basic amino acids within amino acids 860-877, also present in mouse and Xenopus homologs, which resembles that of nucleoplasmin.	Amino Acids, Basic	97-114	RB transcriptional corepressor 1	Homo sapiens	6-8
9238027-6	1997	Analysis of the deduced amino acid sequences showed the presence of a region enriched in basic amino acids in zebrafish apoE similar to the lipoprotein receptor-binding region of human apoE.	Amino Acids, Basic	89-106	apolipoprotein Ea	Danio rerio	120-124
9238027-6	1997	Analysis of the deduced amino acid sequences showed the presence of a region enriched in basic amino acids in zebrafish apoE similar to the lipoprotein receptor-binding region of human apoE.	Amino Acids, Basic	89-106	apolipoprotein E	Homo sapiens	185-189
9378725-1	1997	PACE4 (paired basic amino acid cleaving enzyme) is a member of a family of the mammalian kexin-like proprotein convertases containing a subtilisin-like catalytic domain.	Amino Acids, Basic	14-30	proprotein convertase subtilisin/kexin type 6	Homo sapiens	0-5
9234712-6	1997	Deletion analysis localized a region of the N terminus critical for this effect to amino acids 216 to 238, and further mutagenesis demonstrated that a small basic amino acid motif (BIIa) in this region is essential for enhancing the activity of RAG1.	Amino Acids, Basic	157-173	recombination activating 1	Mus musculus	245-249
9224594-3	1997	Members of the CREB/ATF family share in common a cluster of basic amino acids at the N-terminus of their bZIP element.	Amino Acids, Basic	60-77	cAMP responsive element binding protein 1	Homo sapiens	15-19
9263127-6	1997	Our results show that the enzyme activity of purified tryptase TL2 is inhibited not only by variants with basic amino acids, but also those with hydrophobic residues in the reactive-site region.	Amino Acids, Basic	106-123	TNF superfamily member 10	Homo sapiens	63-66
9306415-4	1997	A specific hydrophobic/basic amino acid cluster in the rat nNOS sequence, Lys732LysLeu, critical for its CaM binding was also identified.	Amino Acids, Basic	23-39	nitric oxide synthase 1	Rattus norvegicus	59-63
9306415-4	1997	A specific hydrophobic/basic amino acid cluster in the rat nNOS sequence, Lys732LysLeu, critical for its CaM binding was also identified.	Amino Acids, Basic	23-39	calmodulin 1	Rattus norvegicus	105-108
9218427-6	1997	Comparison of the amino acid sequences of the TGF-beta isoforms strongly implicates the basic amino acid residue at position 26 of each monomer as being a vital binding determinant.	Amino Acids, Basic	88-104	transforming growth factor beta 1	Homo sapiens	46-54
9230112-0	1997	The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies.	Amino Acids, Basic	15-32	vitronectin	Homo sapiens	36-47
9230112-0	1997	The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies.	Amino Acids, Basic	15-32	serpin family E member 1	Homo sapiens	78-111
9230112-0	1997	The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies.	Amino Acids, Basic	15-32	coagulation factor II, thrombin	Homo sapiens	127-135
9230112-0	1997	The cluster of basic amino acids in vitronectin contributes to its binding of plasminogen activator inhibitor-1: evidence from thrombin-, elastase- and plasmin-cleaved vitronectins and anti-peptide antibodies.	Amino Acids, Basic	15-32	plasminogen	Homo sapiens	78-85
9230112-1	1997	Derivatives of vitronectin obtained by specific cleavage at its cluster of basic amino acids with thrombin, elastase and plasmin are shown to have a decreased ability to bind plasminogen activator inhibitor-1 (PAI-1).	Amino Acids, Basic	75-92	vitronectin	Homo sapiens	15-26
9230112-1	1997	Derivatives of vitronectin obtained by specific cleavage at its cluster of basic amino acids with thrombin, elastase and plasmin are shown to have a decreased ability to bind plasminogen activator inhibitor-1 (PAI-1).	Amino Acids, Basic	75-92	coagulation factor II, thrombin	Homo sapiens	98-106
9230112-1	1997	Derivatives of vitronectin obtained by specific cleavage at its cluster of basic amino acids with thrombin, elastase and plasmin are shown to have a decreased ability to bind plasminogen activator inhibitor-1 (PAI-1).	Amino Acids, Basic	75-92	serpin family E member 1	Homo sapiens	175-208
9223427-2	1997	The three dimensional structure of MK clarified by NMR spectroscopy indicates that several basic amino acids are exposed on the surface of the C-terminal half domain, which retains heparin-binding and neurite-promoting activity.	Amino Acids, Basic	91-108	midkine	Homo sapiens	35-37
9202242-10	1997	Two mutants that contained neutral substitutions for specific basic amino acids within the glycosaminoglycan binding domain had reduced binding to PAI-1.	Amino Acids, Basic	62-79	serpin family E member 1	Homo sapiens	147-152
9247068-3	1997	Biochemical and immunological approaches have shown that in the hypothalamus, pro-TRH is extensively cleaved at pairs of basic amino acids.	Amino Acids, Basic	121-138	thyrotropin releasing hormone	Rattus norvegicus	78-85
9182552-1	1997	We have previously described the expression of the human proprotein convertase furin or paired basic amino acid-cleaving enzyme, in mice transgenic for paired basic amino acid-cleaving enzyme and human Protein C (HPC).	Amino Acids, Basic	95-111	protein C, inactivator of coagulation factors Va and VIIIa	Homo sapiens	202-211
9182552-1	1997	We have previously described the expression of the human proprotein convertase furin or paired basic amino acid-cleaving enzyme, in mice transgenic for paired basic amino acid-cleaving enzyme and human Protein C (HPC).	Amino Acids, Basic	159-175	furin, paired basic amino acid cleaving enzyme	Homo sapiens	79-84
9285100-6	1997	Motif analysis suggested that eIF-5A resembles a bimodular RNA-binding protein in that it contains a stretch of basic amino acids clustered at the N-terminal region and a leucine-rich stretch at the C-terminal region.	Amino Acids, Basic	112-129	eukaryotic translation initiation factor 5A	Homo sapiens	30-36
9097924-6	1997	In addition, a particular sequence motif enriched in basic amino acids in the CDR3 may be required to supplement the reactivity mediated by the V(H) region of the MoAb molecule.	Amino Acids, Basic	53-70	CDR3	Homo sapiens	78-82
9099699-7	1997	In summary, CPZ is a novel metallocarboxypeptidase that is active toward substrates with C-terminal basic amino acids.	Amino Acids, Basic	100-117	carboxypeptidase Z	Homo sapiens	12-15
9188504-3	1997	A region of the Tat protein centered on a cluster of basic amino acids has been assigned to this translocation activity.	Amino Acids, Basic	53-70	tyrosine aminotransferase	Homo sapiens	16-19
9038363-4	1997	A specific hydrophobic/basic amino acid cluster in the rat nNOS sequence, Lys732 Lys Leu, that was critical for its CaM binding was also identified in this study.	Amino Acids, Basic	23-39	nitric oxide synthase 1	Rattus norvegicus	59-63
9087432-1	1997	LCR-F1 is a mammalian bZIP transcription factor containing a basic amino acid domain highly homologous to a domain in the Drosophila Cap "N" Collar and Caenorhabditis elegans SKN-1 proteins.	Amino Acids, Basic	61-77	NFE2 like bZIP transcription factor 1	Homo sapiens	0-6
9067536-7	1997	These results appear to demonstrate that IFN-gamma is sequestered at the surface of endothelial cells by electrostatic interaction between specific basic amino acid residues and sulphated domains on HS, the most abundant endothelial GAG.	Amino Acids, Basic	148-164	interferon gamma	Homo sapiens	41-50
9017204-0	1997	Bilayer interactions of indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids.	Amino Acids, Basic	100-117	cathelicidin-4	Bos taurus	24-35
9157850-3	1997	The values of rate constants of the digestions of the most easily hydrolyzable bonds (those formed by the pairs of the basic amino acid residues) in proinsulin were found to be of the same order as those formed by the separate lysine residues (Lys7) and those formed by the four basic amino acid residues of the C-terminal cluster of melittin.	Amino Acids, Basic	119-135	insulin	Homo sapiens	149-159
9157850-3	1997	The values of rate constants of the digestions of the most easily hydrolyzable bonds (those formed by the pairs of the basic amino acid residues) in proinsulin were found to be of the same order as those formed by the separate lysine residues (Lys7) and those formed by the four basic amino acid residues of the C-terminal cluster of melittin.	Amino Acids, Basic	279-295	insulin	Homo sapiens	149-159
9030777-7	1997	We also identify Ser362 as the major PKC phosphorylation site in vitronectin, and confirm this localization by means of synthetic peptides derived from the cluster of basic amino acids in vitronectin surrounding Ser362.	Amino Acids, Basic	167-184	vitronectin	Homo sapiens	188-199
8995387-4	1997	All isozymes, except PKC mu, selected peptides with basic amino acids at positions -6, -4, and -2.	Amino Acids, Basic	52-69	protein kinase D1	Homo sapiens	21-27
9094218-6	1997	Additional proteolytic cleavages at basic amino acids N-terminal of Gln133 occurred during the later stages of the culture resulting in a heterogeneous IFN-gamma polypeptide with "ragged" C-termini.	Amino Acids, Basic	36-53	interferon gamma	Homo sapiens	152-161
8702889-0	1996	The role of carboxyl-terminal basic amino acids in Gqalpha-dependent activation, particulate association, and nuclear localization of phospholipase C-beta1.	Amino Acids, Basic	30-47	phospholipase C beta 1	Rattus norvegicus	134-155
8945635-3	1996	The characteristic three KPI domains with short spacer sequences and a basic amino acid stretch in the carboxyl-terminal region present in human PP5/TFPI-2 were well conserved in mouse PP5/TFPI-2.	Amino Acids, Basic	71-87	tissue factor pathway inhibitor 2	Homo sapiens	145-155
8945635-3	1996	The characteristic three KPI domains with short spacer sequences and a basic amino acid stretch in the carboxyl-terminal region present in human PP5/TFPI-2 were well conserved in mouse PP5/TFPI-2.	Amino Acids, Basic	71-87	tissue factor pathway inhibitor 2	Mus musculus	185-195
8901832-6	1996	The activation of human prorenin by PC5 depended on a pair of basic amino acids at positions 42 and 43 of the prorenin prosegment and occurred only in cells containing dense core secretory granules.	Amino Acids, Basic	62-79	proprotein convertase subtilisin/kexin type 5	Homo sapiens	36-39
8986654-2	1996	An association of BBMI with anionic phospholipids has been shown to be mediated by a carboxy-terminal domain which is rich in basic amino acids.	Amino Acids, Basic	126-143	myosin IA	Homo sapiens	18-22
8830661-3	1996	This cDNA encodes a 574 amino acid protein which exhibits 46-48% sequence identity with mammalian SgII and contains 11 pairs of basic amino acids.	Amino Acids, Basic	128-145	secretogranin II	Homo sapiens	98-102
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	G protein-coupled receptor kinase 5	Homo sapiens	19-23
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	gelsolin	Homo sapiens	107-115
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	G protein-coupled receptor kinase 4	Homo sapiens	160-164
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	G protein-coupled receptor kinase 4	Homo sapiens	176-180
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	G protein-coupled receptor kinase 5	Homo sapiens	182-186
8798768-8	1996	This region of the GRK5, which has a similar distribution of basic amino acids to the PIP2 binding site of gelsolin, is highly conserved between members of the GRK4 subfamily (GRK4, GRK5, and GRK6).	Amino Acids, Basic	61-78	G protein-coupled receptor kinase 6	Homo sapiens	192-196
8916141-1	1996	Prohormone convertase 1/3 (PC1/3; also termed PC1 or PC3) and PC2 are enzymes that activate prohormones by cleaving the pairs of basic amino acids.	Amino Acids, Basic	129-146	proprotein convertase subtilisin/kexin type 1	Homo sapiens	0-25
8916141-1	1996	Prohormone convertase 1/3 (PC1/3; also termed PC1 or PC3) and PC2 are enzymes that activate prohormones by cleaving the pairs of basic amino acids.	Amino Acids, Basic	129-146	proprotein convertase subtilisin/kexin type 1	Homo sapiens	27-32
8916141-1	1996	Prohormone convertase 1/3 (PC1/3; also termed PC1 or PC3) and PC2 are enzymes that activate prohormones by cleaving the pairs of basic amino acids.	Amino Acids, Basic	129-146	proprotein convertase subtilisin/kexin type 1	Homo sapiens	27-30
8916141-1	1996	Prohormone convertase 1/3 (PC1/3; also termed PC1 or PC3) and PC2 are enzymes that activate prohormones by cleaving the pairs of basic amino acids.	Amino Acids, Basic	129-146	proprotein convertase subtilisin/kexin type 1	Homo sapiens	53-56
8916141-1	1996	Prohormone convertase 1/3 (PC1/3; also termed PC1 or PC3) and PC2 are enzymes that activate prohormones by cleaving the pairs of basic amino acids.	Amino Acids, Basic	129-146	proprotein convertase subtilisin/kexin type 2	Homo sapiens	62-65
8830774-0	1996	Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions.	Amino Acids, Basic	0-16	plectin	Rattus norvegicus	102-109
8830774-0	1996	Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions.	Amino Acids, Basic	0-16	vimentin	Rattus norvegicus	110-118
8830774-4	1996	Site directed mutagenesis revealed a specific cluster of four basic amino acid residues (arg4277-arg4280) residing within the NLS sequence motif to be essential for IF binding.	Amino Acids, Basic	62-78	glial fibrillary acidic protein	Rattus norvegicus	165-167
9037147-4	1997	SB401 cDNA, which possesses a long stretch of AT-rich 5"-untranslated leader sequence, encodes a glutamic acid-rich protein (GARP) which is hydrophilic throughout and contains six imperfect repeated motifs of the sequence V-V-E-K-K-N/E-E with the di-basic amino acid residue pair (K-K) as the core within the repeats.	Amino Acids, Basic	250-266	glutamic acid-rich protein	Solanum tuberosum	97-123
9037147-4	1997	SB401 cDNA, which possesses a long stretch of AT-rich 5"-untranslated leader sequence, encodes a glutamic acid-rich protein (GARP) which is hydrophilic throughout and contains six imperfect repeated motifs of the sequence V-V-E-K-K-N/E-E with the di-basic amino acid residue pair (K-K) as the core within the repeats.	Amino Acids, Basic	250-266	glutamic acid-rich protein	Solanum tuberosum	125-129
8986770-4	1996	Although I-POU lacks two basic amino acid residues in the POU-homeodomain found in tI-POU and Brn-3.0, these three POU-IV class proteins exhibit very similar DNA-binding specificity.	Amino Acids, Basic	25-41	abnormal chemosensory jump 6	Drosophila melanogaster	9-14
8988514-5	1996	To examine somatostatin processing in the canine gut we noted that synthesis of SS-14 and somatostatin octacosapeptide (SS-28) involves endoproteolytic cleavage of prosomatostatin (proSS) at both paired and single basic amino-acid residues, respectively.	Amino Acids, Basic	214-230	somatostatin	Canis lupus familiaris	164-179
8988514-5	1996	To examine somatostatin processing in the canine gut we noted that synthesis of SS-14 and somatostatin octacosapeptide (SS-28) involves endoproteolytic cleavage of prosomatostatin (proSS) at both paired and single basic amino-acid residues, respectively.	Amino Acids, Basic	214-230	somatostatin	Canis lupus familiaris	181-186
8870652-10	1996	G13 contains a bZIP motif, a region rich in basic amino acids adjacent to a coiled-coil leucine zipper domain, common to this class of proteins that is known to be involved in dimerization and DNA binding.	Amino Acids, Basic	44-61	activating transcription factor 6 beta	Homo sapiens	0-3
8710930-4	1996	The predicted amino acid sequence of the OFQ precursor contains a putative signal peptide and one copy of the OFQ sequence flanked by pairs of basic amino acid residues.	Amino Acids, Basic	143-159	prepronociceptin	Rattus norvegicus	41-44
8650173-5	1996	This activity is as much as 3 to 5 times stronger than VP16 at activating transcription and requires a large stretch of amino acids that contain glutamine-glycine rich and serine-threonine-basic amino acid rich regions.	Amino Acids, Basic	189-205	host cell factor C1	Homo sapiens	55-59
8874758-1	1996	The prohormone convertases PC1/PC3 and PC2 are endoproteases involved in prohormone cleavage at pairs of basic amino acids.	Amino Acids, Basic	105-122	proprotein convertase subtilisin/kexin type 1	Rattus norvegicus	27-30
8874758-1	1996	The prohormone convertases PC1/PC3 and PC2 are endoproteases involved in prohormone cleavage at pairs of basic amino acids.	Amino Acids, Basic	105-122	proprotein convertase subtilisin/kexin type 1	Rattus norvegicus	31-34
8874758-1	1996	The prohormone convertases PC1/PC3 and PC2 are endoproteases involved in prohormone cleavage at pairs of basic amino acids.	Amino Acids, Basic	105-122	proprotein convertase subtilisin/kexin type 2	Rattus norvegicus	39-42
8710372-6	1996	First, site directed mutagenesis was used to identify a basic amino acid sequence motif within Wnt-1 protein that is required for this protein to accumulate on the cell surface.	Amino Acids, Basic	56-72	wingless-type MMTV integration site family, member 1	Mus musculus	95-100
8661935-0	1996	An intracellular aminopeptidase from Streptomyces rimosus that prefers basic amino acids.	Amino Acids, Basic	71-88	DF17_RS36920	Streptomyces rimosus	17-31
8662813-3	1996	Synthetic peptides were prepared that were homologous with two regions of basic amino acids within IGFBP-5 (Arg201-Arg218 and Ala131-Thr141).	Amino Acids, Basic	74-91	insulin like growth factor binding protein 5	Homo sapiens	99-106
8816979-9	1996	DRB1*0402 differs from DRB1*0404 by only two acidic residues at positions 70 and 71 within the peptide binding groove, instead of amide and basic amino acids.	Amino Acids, Basic	140-157	major histocompatibility complex, class II, DR beta 1	Homo sapiens	0-4
8679688-8	1996	By contrast, the basic polypeptides poly(L-arginine) and poly(L-lysine) potently inhibited sPLA2 activity, indicating the important role of basic amino acids in the inhibitory effect evoked by protamine.	Amino Acids, Basic	140-157	phospholipase A2 group IIA	Homo sapiens	91-96
8797807-8	1996	Based on these data, these 17 amino acids (Gln1012-Ala1028), essential for signaling of GC activation by STa, have an abundance of basic amino acids which might be functionally influenced by phosphorylation of Ser1029.	Amino Acids, Basic	131-148	GCY	Homo sapiens	105-108
8626450-5	1996	The binding region of CD3 epsilon is located within the N-terminal 12 amino acids containing the motif of a basic amino acid cluster.	Amino Acids, Basic	108-124	CD3 epsilon subunit of T-cell receptor complex	Homo sapiens	22-33
8626396-2	1996	In the present study, mutagenesis was used to analyze the effect of substitutions for basic amino acids in the Arg201-Arg218 region of IGFBP-5 on heparin-binding and the heparin-induced affinity shift.	Amino Acids, Basic	86-103	insulin like growth factor binding protein 5	Homo sapiens	135-142
8654390-6	1996	MTB-Zf possesses other structural features characteristic of transcription factors, including a long stretch of acidic amino acids (amino acids 67 - 95), a proline-rich region (positions 733-849), a region rich in basic amino acids (positions 1161-1247), and a leucine repeat-like region (positions 486-514).	Amino Acids, Basic	214-231	PR/SET domain 2	Homo sapiens	0-6
8632015-3	1996	Deduced from the nucleotide sequences of cDNA, DREF is a polypeptide of 701 amino acid residues with a molecular weight of 80,096, which contains three characteristic regions, rich in basic amino acids, proline, and acidic amino acids, respectively.	Amino Acids, Basic	184-201	DNA replication-related element factor	Drosophila melanogaster	47-51
8632015-4	1996	Deletion analysis of bacterially expressed DREF fused with glutathione S-transferase (GST-DREF) indicated that a part of the N-terminal basic amino acid region (16-115 amino acids) is responsible for the specific binding to DRE.	Amino Acids, Basic	136-152	DNA replication-related element factor	Drosophila melanogaster	43-47
8632015-4	1996	Deletion analysis of bacterially expressed DREF fused with glutathione S-transferase (GST-DREF) indicated that a part of the N-terminal basic amino acid region (16-115 amino acids) is responsible for the specific binding to DRE.	Amino Acids, Basic	136-152	Glutathione S transferase S1	Drosophila melanogaster	59-84
8632015-4	1996	Deletion analysis of bacterially expressed DREF fused with glutathione S-transferase (GST-DREF) indicated that a part of the N-terminal basic amino acid region (16-115 amino acids) is responsible for the specific binding to DRE.	Amino Acids, Basic	136-152	DNA replication-related element factor	Drosophila melanogaster	90-94
7592764-2	1995	The contribution of individual basic amino acids within three putative "consensus sequences" for heparin binding of fibroblast growth factor-1 have been examined by site-directed mutagenesis.	Amino Acids, Basic	31-48	fibroblast growth factor 1	Homo sapiens	116-142
8822205-3	1996	Reverse transcription-PCR showed that PIGF-2, a subtype of PIGF-1 that bears a basic amino acid-rich domain, is more abundant than PIGF-1 and thus is the major subtype in human placenta.	Amino Acids, Basic	79-95	phosphatidylinositol glycan anchor biosynthesis class F	Homo sapiens	38-42
8822205-3	1996	Reverse transcription-PCR showed that PIGF-2, a subtype of PIGF-1 that bears a basic amino acid-rich domain, is more abundant than PIGF-1 and thus is the major subtype in human placenta.	Amino Acids, Basic	79-95	phosphatidylinositol glycan anchor biosynthesis class F	Homo sapiens	59-63
8822205-3	1996	Reverse transcription-PCR showed that PIGF-2, a subtype of PIGF-1 that bears a basic amino acid-rich domain, is more abundant than PIGF-1 and thus is the major subtype in human placenta.	Amino Acids, Basic	79-95	phosphatidylinositol glycan anchor biosynthesis class F	Homo sapiens	59-63
8719703-3	1996	As with other species, cat proenkephalin-A contains four conserved copies of (Met5)-enkephalin, and one of (Leu5)-enkephalin, flanked by processing sites of paired basic amino acids.	Amino Acids, Basic	164-181	proenkephalin	Homo sapiens	27-42
8567680-12	1996	The predicted amino acid sequence of the protein fulfilled the minimal criteria for binding to hyaluronic acid, i.e. two basic amino acids flanking a seven-amino acid stretch, as reported for other hyaluronic acid affinity of the recombinant P-32 protein was confirmed by biotinylated hyaluronic acid binding assay.	Amino Acids, Basic	121-138	complement C1q binding protein	Homo sapiens	242-246
8599890-0	1996	A charged segment mainly composed of basic amino acids forms an autoepitope of CENP-A.	Amino Acids, Basic	37-54	centromere protein A	Homo sapiens	79-85
8664898-6	1996	Substitution of a basic amino acid for asparagine at residue 47, conserved in all known murine Pax and human PAX genes, appears to have a more drastic effect on the phenotype than missense, frameshift and deletion mutations of PAX3 that cause Waardenburg syndrome type 1.	Amino Acids, Basic	18-34	paxillin	Mus musculus	95-98
8664898-6	1996	Substitution of a basic amino acid for asparagine at residue 47, conserved in all known murine Pax and human PAX genes, appears to have a more drastic effect on the phenotype than missense, frameshift and deletion mutations of PAX3 that cause Waardenburg syndrome type 1.	Amino Acids, Basic	18-34	paxillin	Mus musculus	109-112
8825523-1	1996	The rBAT protein, when expressed in Xenopus oocytes, was previously shown to reproduce the selectivity of the Na(+)-independent neutral and basic amino acid transport system called bo,+.	Amino Acids, Basic	140-156	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	4-8
8825523-2	1996	More recently, the capacity of rBAT to generate a transmembrane current was demonstrated when addition of neutral amino acids stimulated the efflux of cations (presumably basic amino acids) in rBAT-injected oocytes.	Amino Acids, Basic	171-188	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	31-35
8825523-2	1996	More recently, the capacity of rBAT to generate a transmembrane current was demonstrated when addition of neutral amino acids stimulated the efflux of cations (presumably basic amino acids) in rBAT-injected oocytes.	Amino Acids, Basic	171-188	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	193-197
8825523-3	1996	In the present paper, aminoisobutyric acid (AIB), a neutral amino acid analogue, was shown to induce outward currents (efflux of basic amino acids) through rBAT similar to those caused by alanine in terms of affinity, maximal currents and I-V curves.	Amino Acids, Basic	129-146	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	156-160
8983022-1	1996	The proprotein processing enzyme furin is the mammalian prototype of a novel family of subtilisin-like serine endoproteases which possess cleavage specificity for sites involving multiple basic amino acid residues and are involved in the processing of precursor proteins of a variety of regulatory peptides and proteins.	Amino Acids, Basic	188-204	furin, paired basic amino acid cleaving enzyme	Homo sapiens	33-38
9082618-5	1996	It is found that the clusters of basic amino acids (e.g. forming BBXXB-motifs) and serine residues, located in RRR, coincide with similar amino acids present in IR primary structure.	Amino Acids, Basic	33-50	insulin receptor	Homo sapiens	161-163
8618839-4	1995	When expressed in yeast, AAT1 mediates high-affinity transport of basic amino acids, but to a lower extent also recognizes acidic and neutral amino acids.	Amino Acids, Basic	66-83	aspartate transaminase AAT1	Saccharomyces cerevisiae S288C	25-29
8777717-5	1995	Nucleolar localization of RAG1 is mediated by several domains containing stretches of basic amino acids, indicating that RAG1 has affinity for RNA or ssDNA.	Amino Acids, Basic	86-103	recombination activating 1	Homo sapiens	26-30
8777717-5	1995	Nucleolar localization of RAG1 is mediated by several domains containing stretches of basic amino acids, indicating that RAG1 has affinity for RNA or ssDNA.	Amino Acids, Basic	86-103	recombination activating 1	Homo sapiens	121-125
7595540-5	1995	Recombinant PC1 processed the 26-kDa TRH precursor by initially cleaving the prohormone after the basic amino acid at either position 153 or 159.	Amino Acids, Basic	98-114	proprotein convertase subtilisin/kexin type 1	Rattus norvegicus	12-15
7595540-5	1995	Recombinant PC1 processed the 26-kDa TRH precursor by initially cleaving the prohormone after the basic amino acid at either position 153 or 159.	Amino Acids, Basic	98-114	thyrotropin releasing hormone	Rattus norvegicus	37-40
7492557-9	1995	Basic amino acids found at the same position within the alpha-helices of fingers 2 and 3 of TFIIIA are required for high-affinity DNA binding activity.	Amino Acids, Basic	0-17	general transcription factor 3A L homeolog	Xenopus laevis	92-98
7592764-9	1995	Together these data demonstrate that the heparin binding properties of fibroblast growth factor-1 are dictated by structural features more complex than clusters of basic amino acids.	Amino Acids, Basic	164-181	fibroblast growth factor 1	Homo sapiens	71-97
7673244-6	1995	Nine basic amino acids that are essential for activating DNA synthesis by pol delta are positioned at the internal alpha-helices of PCNA.	Amino Acids, Basic	5-22	proliferating cell nuclear antigen	Homo sapiens	132-136
7478569-4	1995	However, a mutation in Mos that removed two basic amino acid residues (R94 and K97) downstream from the lysine at the ATP binding site (K90) markedly enhanced autophosphorylation activity.	Amino Acids, Basic	44-60	MOS proto-oncogene, serine/threonine kinase L homeolog	Xenopus laevis	23-26
7670961-1	1995	The amino acid sequence of interferon gamma (IFN-gamma) has basic amino acid clusters similar to the heparin-binding consensus sequences found in other proteins that bind to proteoglycans (PGs).	Amino Acids, Basic	60-76	interferon gamma	Homo sapiens	27-54
7475095-7	1995	In light of these transcription factor-like docking motifs reported for AFP, the present report purposes various subdomain regions which might constitute basic amino acid sequences resembling recognition signals for binding (dimerizing) proteins.	Amino Acids, Basic	154-170	alpha fetoprotein	Homo sapiens	72-75
11854844-0	1995	The Basic Amino Acid-Rich DNA-Binding Element of the NF-IL6 Transcription Factor Contains Two Functionally Distinct Subdomains.	Amino Acids, Basic	4-20	CCAAT enhancer binding protein beta	Homo sapiens	53-59
8558079-2	1995	It has been established that basic amino acids situated between apoE residues 136 and 150 participate in the interaction of apoE with the LDLr.	Amino Acids, Basic	29-46	apolipoprotein E	Homo sapiens	64-68
7657670-1	1995	The yeast YAP3 gene encodes an aspartyl endoprotease that cleaves precursor proteins at selected pairs of basic amino acids and after single arginine residues.	Amino Acids, Basic	106-123	Yap3p	Saccharomyces cerevisiae S288C	10-14
8558079-2	1995	It has been established that basic amino acids situated between apoE residues 136 and 150 participate in the interaction of apoE with the LDLr.	Amino Acids, Basic	29-46	apolipoprotein E	Homo sapiens	124-128
8558079-2	1995	It has been established that basic amino acids situated between apoE residues 136 and 150 participate in the interaction of apoE with the LDLr.	Amino Acids, Basic	29-46	low density lipoprotein receptor	Homo sapiens	138-142
7627718-0	1995	Apolipoprotein B and E basic amino acid clusters influence low-density lipoprotein association with lipoprotein lipase anchored to the subendothelial matrix.	Amino Acids, Basic	23-39	lipoprotein lipase	Homo sapiens	100-118
8674818-8	1995	These findings indicate that post-translational processing of CPH is mediated by an endoprotease which cleaves at sites containing multiple basic amino acid residues upon segregation of the enzyme to the secretory granules.	Amino Acids, Basic	140-156	carboxypeptidase E	Rattus norvegicus	62-65
7556150-9	1995	The feature common to the most efficiently processed factor VIII deletion derivatives was that they contained the recognition motif for proteolytic cleavage by the membrane-bound subtilisin-like protease furin, which is expressed in most types of cells; that is, basic amino acid residues at positions -1 and -4 relative to the cleavage site at Glu1649.	Amino Acids, Basic	263-279	furin	Cricetulus griseus	204-209
7608192-8	1995	Mutagenesis of the mature IL-1 beta sequence revealed that a region of basic amino acids may play an important role in the optimal secretion of mature IL-1 beta in P388D1 cells, but not in Jurkat cells.	Amino Acids, Basic	71-88	interleukin 1 beta	Mus musculus	26-35
7628645-1	1995	Homologous proteins (NBAT) which mediate sodium-independent transport of neutral as well as basic amino acids and cystine when expressed in Xenopus oocytes were recently cloned from mammalian kidneys.	Amino Acids, Basic	92-109	solute carrier family 3 member 1	Homo sapiens	21-25
7608192-8	1995	Mutagenesis of the mature IL-1 beta sequence revealed that a region of basic amino acids may play an important role in the optimal secretion of mature IL-1 beta in P388D1 cells, but not in Jurkat cells.	Amino Acids, Basic	71-88	interleukin 1 beta	Mus musculus	151-160
7608199-5	1995	AAP3 and AAP5 efficiently transport arginine and lysine and are involved in basic amino acid transport.	Amino Acids, Basic	76-92	amino acid permease 3	Arabidopsis thaliana	0-4
7608199-5	1995	AAP3 and AAP5 efficiently transport arginine and lysine and are involved in basic amino acid transport.	Amino Acids, Basic	76-92	amino acid permease 5	Arabidopsis thaliana	9-13
8578445-4	1995	Several substrates (fibrinogen, thrombin receptor, heparin cofactor II) or ligands (thrombomodulin, glycoprotein Ib) interact with a large exosite located on the surface of the loop segment 65-76, mainly constituted of basic amino acids, designated anion binding exosite 1.	Amino Acids, Basic	219-236	fibrinogen beta chain	Homo sapiens	20-30
7498165-4	1995	Immunoreactive spots were present on the acidic side of the transferrin isoelectric series, suggesting a modification mechanism similar to that observed in HSA, i.e., acylation of basic amino acid residues.	Amino Acids, Basic	180-196	transferrin	Homo sapiens	60-71
8578445-4	1995	Several substrates (fibrinogen, thrombin receptor, heparin cofactor II) or ligands (thrombomodulin, glycoprotein Ib) interact with a large exosite located on the surface of the loop segment 65-76, mainly constituted of basic amino acids, designated anion binding exosite 1.	Amino Acids, Basic	219-236	coagulation factor II, thrombin	Homo sapiens	32-40
7782286-7	1995	This segment contains a pair of basic amino acid residues which may represent a recognition motif for PC2.	Amino Acids, Basic	32-48	proprotein convertase subtilisin/kexin type 2	Homo sapiens	102-105
7781597-2	1995	Cleavage occurs at the C-terminus of basic amino acid sequences, such as R-X-K/R-R and R-X-X-R. Furin was found predominantly in the trans-Golgi network (TGN), but also in clathrin-coated vesicles dispatched from the TGN, on the plasma membrane as an integral membrane protein and in the medium as an anchorless enzyme.	Amino Acids, Basic	37-53	furin (paired basic amino acid cleaving enzyme)	Rattus norvegicus	96-101
7577441-6	1995	Proacrosin, therefore, has many properties in common with other polysulfate binding proteins, such as antithrombin III and sea urchin sperm binding, in having a conformation-dependent domain containing basic amino acids that mediates specific protein-protein interactions.	Amino Acids, Basic	202-219	acrosin	Homo sapiens	0-10
7584919-1	1995	Renin is synthesized from an inactive precursor, prorenin, through cleavage at a pair of basic amino acids catalyzed by prorenin processing enzyme (PPE).	Amino Acids, Basic	89-106	renin	Homo sapiens	0-5
7711030-6	1995	Peptide KILIKNKK (P2), which comprises only the basic amino acid consensus motif, also stimulated PLC beta 2, although higher concentrations were required to observe this stimulatory effect.	Amino Acids, Basic	48-64	phospholipase C beta 2	Homo sapiens	98-108
12114688-2	1995	The primary amino acid sequence of CgA, elucidated by cDNA analysis, has been revealed to include several pairs of basic amino acid residues that are homologous to the bioactive peptides, such as pancreastatin (PST) and chromostatin (CST).	Amino Acids, Basic	115-131	chromogranin A	Homo sapiens	35-38
11725049-6	1995	These data confirm that active HIV-1 tat must first interact with TAR RNA via basic amino acid residues in order to stimulate transcription of downstream sequences.	Amino Acids, Basic	78-94	RNA binding motif protein 8A	Homo sapiens	66-69
7890750-7	1995	The single basic amino acid close to Thr-431 (Arg-429) is essential for recognition of the peptide as a substrate by PKC delta and for the selectivity of this recognition.	Amino Acids, Basic	11-27	protein kinase C, delta	Mus musculus	117-126
7883050-3	1995	Both PC1 and PC2 can cleave the secretogranin II precursor at sites of pairs of basic amino acids to yield intermediate-sized fragments.	Amino Acids, Basic	80-97	proprotein convertase subtilisin/kexin type 1	Homo sapiens	5-8
7883050-3	1995	Both PC1 and PC2 can cleave the secretogranin II precursor at sites of pairs of basic amino acids to yield intermediate-sized fragments.	Amino Acids, Basic	80-97	chromobox 4	Homo sapiens	13-16
7883050-3	1995	Both PC1 and PC2 can cleave the secretogranin II precursor at sites of pairs of basic amino acids to yield intermediate-sized fragments.	Amino Acids, Basic	80-97	secretogranin II	Homo sapiens	32-48
7706950-7	1995	Helical net models of all receptor active peptides indicated that the LDL-receptor binding activity of the 141-155 dimer is dependent on at least two clusters of basic amino acids present on the hydrophilic face of the amphipathic alpha-helix of the 141-155, 141-150, 141-155 (lys143-->ala) and 141-155 (arg150-->ala) dimer peptides.	Amino Acids, Basic	162-179	low density lipoprotein receptor	Homo sapiens	70-82
7608116-2	1995	TREB5 is a member of the CREB/ATF family, containing a basic amino acid region and leucine zipper structure (b-Zip structure).	Amino Acids, Basic	55-71	X-box binding protein 1	Homo sapiens	0-5
7608116-2	1995	TREB5 is a member of the CREB/ATF family, containing a basic amino acid region and leucine zipper structure (b-Zip structure).	Amino Acids, Basic	55-71	cAMP responsive element binding protein 1	Homo sapiens	25-29
7768066-5	1995	Some conserved features of the mature CgA protein are polyglutamic acids, calcium-binding sites, and several pairs of basic amino acids.	Amino Acids, Basic	118-135	chromogranin A	Homo sapiens	38-41
7503675-3	1995	Analysis of mutants truncated from the carboxy-terminal end of the 1460-amino acid polypeptide showed that two regions including a short sequence of basic amino acid residues were associated with the nuclear localization of IE180.	Amino Acids, Basic	149-165	transcriptional regulator ICP4	Suid alphaherpesvirus 1	224-229
7798220-7	1994	The most prominent cluster of basic amino acids in the TSHR extracellular region (residues 287-293) was studied in a second series of mutations designed to eliminate the classical proprotein convertase sites in this region and yet be compatible with TSHR function.	Amino Acids, Basic	30-47	thyroid stimulating hormone receptor	Homo sapiens	55-59
7798220-7	1994	The most prominent cluster of basic amino acids in the TSHR extracellular region (residues 287-293) was studied in a second series of mutations designed to eliminate the classical proprotein convertase sites in this region and yet be compatible with TSHR function.	Amino Acids, Basic	30-47	thyroid stimulating hormone receptor	Homo sapiens	250-254
7966558-2	1994	We previously analyzed the quasispecies of the third hypervariable region (V3) in the viral envelope glycoprotein gp120 in an infected individual and found that the species with a basic amino acid substitution (lysine for aspartic acid) at a particular position evolved and became a distinct population within a short period, followed by progression to the typical immunodeficiency stage (S. Oka et al., AIDS Res.	Amino Acids, Basic	180-196	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	114-119
7982963-3	1994	Peptides that bound with highest affinity to all three hsp70 proteins contained stretches of at least 7 residues that included large hydrophobic and basic amino acids, but few or no acidic residues.	Amino Acids, Basic	149-166	heat shock protein family A (Hsp70) member 4	Homo sapiens	55-60
7991544-1	1994	Examination of the interferon gamma (IFN-gamma) amino acid sequence revealed two conserved basic amino acid clusters similar to the prototype nuclear localization signal.	Amino Acids, Basic	91-107	interferon gamma	Mus musculus	19-46
7972056-7	1994	Comparisons of the amino acid sequences of the basic-leucine zipper domains of ATF-2(195) and ATF-2(192) suggest that HMG I(Y) interacts with a short stretch of basic amino acids near the amino terminus of the basic-leucine zipper domain of ATF-2(195).	Amino Acids, Basic	161-178	activating transcription factor 2	Homo sapiens	79-84
7725800-0	1994	CAN1, a gene encoding a permease for basic amino acids in Candida albicans.	Amino Acids, Basic	37-54	arginine permease CAN1	Saccharomyces cerevisiae S288C	0-4
7725800-5	1994	The protein sequence is strongly homologous to both permeases for basic amino acids (Can1 and Lyp1) of Saccharomyces cerevisiae.	Amino Acids, Basic	66-83	arginine permease CAN1	Saccharomyces cerevisiae S288C	85-89
7725800-5	1994	The protein sequence is strongly homologous to both permeases for basic amino acids (Can1 and Lyp1) of Saccharomyces cerevisiae.	Amino Acids, Basic	66-83	lysine permease	Saccharomyces cerevisiae S288C	94-98
7898639-1	1994	A number of candidate mammalian prohormone processing enzymes related to the yeast Kex2 endoprotease have been cloned and demonstrated to cleave several prohormone precursors at single, pairs and tetra basic amino acid processing sites.	Amino Acids, Basic	202-218	kexin KEX2	Saccharomyces cerevisiae S288C	83-87
7972056-7	1994	Comparisons of the amino acid sequences of the basic-leucine zipper domains of ATF-2(195) and ATF-2(192) suggest that HMG I(Y) interacts with a short stretch of basic amino acids near the amino terminus of the basic-leucine zipper domain of ATF-2(195).	Amino Acids, Basic	161-178	activating transcription factor 2	Homo sapiens	94-99
7972056-7	1994	Comparisons of the amino acid sequences of the basic-leucine zipper domains of ATF-2(195) and ATF-2(192) suggest that HMG I(Y) interacts with a short stretch of basic amino acids near the amino terminus of the basic-leucine zipper domain of ATF-2(195).	Amino Acids, Basic	161-178	high mobility group AT-hook 1	Homo sapiens	118-126
7972056-7	1994	Comparisons of the amino acid sequences of the basic-leucine zipper domains of ATF-2(195) and ATF-2(192) suggest that HMG I(Y) interacts with a short stretch of basic amino acids near the amino terminus of the basic-leucine zipper domain of ATF-2(195).	Amino Acids, Basic	161-178	activating transcription factor 2	Homo sapiens	94-99
7519670-1	1994	Using the highly sensitive HPLC-fluorophotometry technique, anterograde and retrograde axonal transport of carboxypeptidase H (CPH), a putative prohormone processing enzyme that removes a basic amino acid from the C-terminus of a precursor peptide, was measured 12-72 h after double ligations of rat sciatic nerves.	Amino Acids, Basic	188-204	carboxypeptidase E	Rattus norvegicus	107-125
8093031-1	1994	Midkine is a 13kDa heparin-binding polypeptide rich in basic amino acids and cysteine and has neurite outgrowth, neuronal cell survival and other activities.	Amino Acids, Basic	55-72	midkine	Homo sapiens	0-7
8071367-13	1994	Molecular modeling studies of the decasaccharide indicate that it presents a linear array of negatively charged sulfate groups that may adopt a favorable disposition to bind to peptide region(s) comprised of basic amino acid residues of LpL with high affinity.	Amino Acids, Basic	208-224	lipoprotein lipase	Bos taurus	237-240
7896748-5	1994	Porcine ATIII showed high sequence similarity to other mammalian ATIIIs, including the reactive site, heparin-binding basic amino acid residues, and disulfide bonds.	Amino Acids, Basic	118-134	serpin family C member 1	Homo sapiens	8-13
7519670-1	1994	Using the highly sensitive HPLC-fluorophotometry technique, anterograde and retrograde axonal transport of carboxypeptidase H (CPH), a putative prohormone processing enzyme that removes a basic amino acid from the C-terminus of a precursor peptide, was measured 12-72 h after double ligations of rat sciatic nerves.	Amino Acids, Basic	188-204	carboxypeptidase E	Rattus norvegicus	127-130
8120052-6	1994	The Zfp-57 cDNA encoded a protein consisting of 421 amino acids with an extremely high content of basic amino acid residues and multiple zinc finger motifs.	Amino Acids, Basic	98-114	ZFP57 zinc finger protein	Homo sapiens	4-10
7941748-0	1994	APL1, a yeast gene encoding a putative permease for basic amino acids.	Amino Acids, Basic	52-69	Apl1p	Saccharomyces cerevisiae S288C	0-4
8159751-4	1994	The deduced sequence of mature TFPI-2 revealed a short acidic amino-terminal region, three tandem Kunitz-type domains, and a carboxyl-terminal tail highly enriched in basic amino acids.	Amino Acids, Basic	167-184	tissue factor pathway inhibitor 2	Homo sapiens	31-37
8051106-10	1994	A peptide consists of 14 amino acids corresponding to residues 30-43 of PLC-delta 1, which contains 6 basic amino acids, binds to an Ins(1,4,5)P3-immobilized matrix.	Amino Acids, Basic	102-119	phospholipase C, delta 1	Rattus norvegicus	72-83
8052624-12	1994	The specificity of enterokinase for the DDDDK-I sequence of trypsinogen may be explained by complementary basic-amino acid residues clustered in potential S2-S5 subsites.	Amino Acids, Basic	106-122	transmembrane serine protease 15	Bos taurus	19-31
8046441-2	1994	Following endoproteolytic cleavage, the carboxyl-terminal basic amino acid residues are removed by carboxypeptidase E (CPE).	Amino Acids, Basic	58-74	carboxypeptidase E	Rattus norvegicus	99-117
8046441-2	1994	Following endoproteolytic cleavage, the carboxyl-terminal basic amino acid residues are removed by carboxypeptidase E (CPE).	Amino Acids, Basic	58-74	carboxypeptidase E	Rattus norvegicus	119-122
8041717-5	1994	Frog DBI contains two paired basic amino acids (Lys-Lys) at positions 14-15 and 62-63 and a single cysteine within the biologically active region of the molecule.	Amino Acids, Basic	29-46	diazepam binding inhibitor, acyl-CoA binding protein	Homo sapiens	5-8
7986586-0	1994	HIV type 1 infection of CD4+ T cells depends critically on basic amino acid residues in the V3 domain of envelope glycoprotein 120.	Amino Acids, Basic	59-75	CD4 molecule	Homo sapiens	24-27
7986586-0	1994	HIV type 1 infection of CD4+ T cells depends critically on basic amino acid residues in the V3 domain of envelope glycoprotein 120.	Amino Acids, Basic	59-75	endogenous retrovirus group K member 20	Homo sapiens	105-126
8011684-8	1994	Modification of the arginine residues of Lf with 1,2-cyclohexanedione abolished its ability to bind to AcLDL, suggesting that a region rich in basic amino acid residues near the N-terminus of Lf, which resembles the ligand-binding site of the scavenger receptor, may be responsible for this binding ability.	Amino Acids, Basic	143-159	lactotransferrin	Bos taurus	41-43
8147883-7	1994	We noticed that Nuc includes two units of sequence similar to the EF hand motif, a calcium-binding motif, between a region rich in basic amino acids, which is presumably a DNA-binding site, and a leucine zipper which is a dimerization motif.	Amino Acids, Basic	131-148	nucleobindin 1	Homo sapiens	16-19
8117736-2	1994	Tat uses a single arginine residue within a short region of basic amino acids to recognize a bulge region in TAR.	Amino Acids, Basic	60-77	tyrosine aminotransferase	Homo sapiens	0-3
8117736-2	1994	Tat uses a single arginine residue within a short region of basic amino acids to recognize a bulge region in TAR.	Amino Acids, Basic	60-77	RNA binding motif protein 8A	Homo sapiens	109-112
8038719-5	1994	Cloning and sequencing of this p12 gag homologue has revealed a high (63% to 89%) amino acid derived sequence identity with other retroviruses and shown that the major differences among p12 of pathogenic viral strains compared to non-pathogenic ones consist of a four amino acids deletion and a high abundance of proline and basic amino acids in their p12 region.	Amino Acids, Basic	325-342	polymerase (DNA-directed), delta 4	Mus musculus	31-34
8038719-5	1994	Cloning and sequencing of this p12 gag homologue has revealed a high (63% to 89%) amino acid derived sequence identity with other retroviruses and shown that the major differences among p12 of pathogenic viral strains compared to non-pathogenic ones consist of a four amino acids deletion and a high abundance of proline and basic amino acids in their p12 region.	Amino Acids, Basic	325-342	melanoma antigen	Mus musculus	35-38
8288571-7	1994	The hairpin loop in HGF possesses a cluster of basic amino acid residues and a highly positive net charge, when compared with hairpin loop structures in the other proteins, plasminogen and HGF-like protein.	Amino Acids, Basic	47-63	hepatocyte growth factor	Homo sapiens	20-23
8294457-1	1994	A metalloendopeptidase that selectively cleaves doublets of basic amino acids on the amino-terminal side of arginine residues was purified to homogeneity from rat testes and analyzed further.	Amino Acids, Basic	60-77	thimet oligopeptidase 1	Rattus norvegicus	2-22
8017900-2	1994	The column has excellent capabilities to quantitatively remove carboxy-terminal basic amino acids from peptides, as is demonstrated using the synthetic peptide substrate hippuryl-L-arginine and the nonapeptide bradykinin, and remains stable for several months.	Amino Acids, Basic	80-97	kininogen 1	Homo sapiens	210-220
7508860-7	1994	The altered RHAMM protein did not bind HA, confirming that the basic amino acids and their spacing are critical for binding.	Amino Acids, Basic	63-80	hyaluronan mediated motility receptor	Homo sapiens	12-17
8288594-0	1994	Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III.	Amino Acids, Basic	18-34	coagulation factor II, thrombin	Homo sapiens	47-55
8288594-0	1994	Identification of basic amino acid residues in thrombin essential for heparin-catalyzed inactivation by antithrombin III.	Amino Acids, Basic	18-34	serpin family C member 1	Homo sapiens	104-120
8288571-8	1994	The second kringle domain in HGF has the basic amino acid cluster in the central region.	Amino Acids, Basic	41-57	hepatocyte growth factor	Homo sapiens	29-32
8245119-4	1993	Deletion of either basic amino acid stretch results in the mislocation of NSR1 to the cytoplasm.	Amino Acids, Basic	19-35	scavenger receptor class F member 2	Homo sapiens	74-78
8203153-5	1994	The deduced amino acid sequence had significant homology to Saccharomyces cerevisiae Kex2p, a processing endoprotease that cleaves after pairs of basic amino acids.	Amino Acids, Basic	146-163	kexin KEX2	Saccharomyces cerevisiae S288C	85-90
8155258-4	1993	The CDR3 sequences for both the antibodies had a predominance of basic amino acids, with RT-79 having five and D-5 two arginine residues respectively.	Amino Acids, Basic	65-82	CDR3	Homo sapiens	4-8
8262218-1	1993	Proprotein processing activity of the Kex2-like mammalian endoprotease PACE4 and its cleavage selectivity for sites with basic amino acid residues were determined.	Amino Acids, Basic	121-137	proprotein convertase subtilisin/kexin type 6	Homo sapiens	71-76
8281191-4	1993	Thus, AAP2 is less selective as compared with AAP1 and transports basic amino acids such as histidine as shown by expression in a histidine transport-deficient yeast strain.	Amino Acids, Basic	66-83	amino acid permease 2	Arabidopsis thaliana	6-10
8245689-0	1993	The effect of chemical modification of basic amino acid residues on the activation and amidolytic activity of Hageman factor (factor XII).	Amino Acids, Basic	39-55	coagulation factor XII	Homo sapiens	110-124
8245689-5	1993	Thus, basic amino acid residues essential to the activation or activity of Hageman factor appear to be variably accessible to chemical modification.	Amino Acids, Basic	6-22	coagulation factor XII	Homo sapiens	75-89
8281191-6	1993	Alterations in the charged residues as compared with AAP1 in four regions might be involved in the difference in selectivity towards basic amino acids.	Amino Acids, Basic	133-150	amino acid permease 1	Arabidopsis thaliana	53-57
7693462-6	1993	The structure of the possible calmodulin-binding site, consisting of a strongly hydrophobic region surrounded by basic amino acids, is present.	Amino Acids, Basic	113-130	calmodulin 1	Rattus norvegicus	30-40
8226974-5	1993	Furin is a mammalian endoprotease that cleaves proproteins at a consensus sequence of basic amino acids found in the insulin proreceptor.	Amino Acids, Basic	86-103	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
8226974-5	1993	Furin is a mammalian endoprotease that cleaves proproteins at a consensus sequence of basic amino acids found in the insulin proreceptor.	Amino Acids, Basic	86-103	insulin	Homo sapiens	117-124
7690756-4	1993	The Apn1 C terminus is rich in basic amino acids and includes two lysine/arginine clusters related to the nuclear transport signals of some other proteins.	Amino Acids, Basic	31-48	DNA-(apurinic or apyrimidinic site) lyase APN1	Saccharomyces cerevisiae S288C	4-8
8352764-6	1993	TTR-Lys61 is the first variant TTR with a replacement of the acidic with basic amino acid to be found in the amyloid precursor proteins of FAP.	Amino Acids, Basic	73-89	transthyretin	Homo sapiens	0-3
8103045-2	1993	We have previously demonstrated that a basic amino acid residue of interleukin (IL)-8, namely Arg-6, is critical for the binding of IL-8 to its receptor.	Amino Acids, Basic	39-55	C-X-C motif chemokine ligand 8	Homo sapiens	67-85
8103045-2	1993	We have previously demonstrated that a basic amino acid residue of interleukin (IL)-8, namely Arg-6, is critical for the binding of IL-8 to its receptor.	Amino Acids, Basic	39-55	C-X-C motif chemokine ligand 8	Homo sapiens	132-136
8352764-6	1993	TTR-Lys61 is the first variant TTR with a replacement of the acidic with basic amino acid to be found in the amyloid precursor proteins of FAP.	Amino Acids, Basic	73-89	transthyretin	Homo sapiens	31-34
8344358-6	1993	Purified AP-B cleaved N-terminal basic amino acid-containing peptides such as thymopentin (H-Arg-Lys-Asp-Val-Tyr-OH), indicating that it might play a role in the regulation of the concentration of important soluble mediators of T cell activation.	Amino Acids, Basic	33-49	arginyl aminopeptidase	Homo sapiens	9-13
8344192-4	1993	The presence of several highly conserved pairs of basic amino acids, putative cleavage sites, in the CgA molecule suggests that other yet unidentified bioactive peptides might exist within the molecule.	Amino Acids, Basic	50-67	chromogranin A	Rattus norvegicus	101-104
8373517-9	1993	These results suggest that the basic amino acid residues at positions 2 and 104 in hCG-beta participate, either directly or indirectly, in receptor binding.	Amino Acids, Basic	31-47	chorionic gonadotropin subunit beta 3	Homo sapiens	83-91
8392601-12	1993	In addition, a potential binding domain rich in basic amino acids (positions 179 to 222) and a highly conserved sequence among foamy virus transactivators (positions 93 to 109) were found to be critical for Taf activity.	Amino Acids, Basic	48-65	TATA-box binding protein associated factor 8	Homo sapiens	207-210
8318003-3	1993	The purpose of the present work was to identify proteinases recognizing substrates with basic amino acids in the P1 substrate site that are present in MOLT-4 cells, a human CD4-positive T helper lymphocyte cell line, and to characterize these enzymes in terms of substrate, pH and ionic-strength preferences, size and susceptibility to various inhibitors, including 24- and 36-amino-acid-long V3 loop peptides.	Amino Acids, Basic	88-105	CD4 molecule	Homo sapiens	173-176
1429728-2	1992	To investigate this proposal, 10 basic amino acids within the regulatory region of rabbit smooth muscle myosin light chain kinase (Lys961-Lys979) were replaced either singularly or in combination with acidic or nonpolar residues by site-directed mutagenesis.	Amino Acids, Basic	33-50	myosin light chain kinase, smooth muscle	Oryctolagus cuniculus	90-129
8495725-2	1993	Kex2p is specific for pairs of basic amino acid residues.	Amino Acids, Basic	31-47	kexin KEX2	Saccharomyces cerevisiae S288C	0-5
8394980-6	1993	The amino acid sequence of OprE had some clusters of sequence homologous with that of OprD of P. aeruginosa, which might be responsible for the outer membrane permeability of imipenem and basic amino acids.	Amino Acids, Basic	188-205	anaerobically-induced outer membrane porin OprE	Pseudomonas aeruginosa PAO1	27-31
8479902-7	1993	Adjacent to the N-terminal of the zinc finger motifs, a short sequence rich in basic amino acids is conserved between BTEB2 and Sp1.	Amino Acids, Basic	79-96	Kruppel-like factor 5	Mus musculus	118-123
8468556-2	1993	The mutations were made by site-directed mutagenesis to alter basic amino acids (lysine or arginine) in the surface glycoprotein gp70.	Amino Acids, Basic	62-79	embigin	Mus musculus	129-133
8486232-7	1993	These findings suggest that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), may contribute to the susceptibility to autoimmune hepatitis of Japanese.	Amino Acids, Basic	32-48	major histocompatibility complex, class II, DR beta 4	Homo sapiens	102-105
8486232-7	1993	These findings suggest that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), may contribute to the susceptibility to autoimmune hepatitis of Japanese.	Amino Acids, Basic	32-48	major histocompatibility complex, class II, DR beta 4	Homo sapiens	142-145
8440710-5	1993	CRE-BPa protein is highly homologous with CRE-BP1 in four regions: two of them are the regions containing the putative metal finger or the DNA-binding domain consisting of the basic amino acid cluster and the leucine zipper.	Amino Acids, Basic	176-192	cAMP responsive element binding protein 5	Homo sapiens	0-7
8440710-5	1993	CRE-BPa protein is highly homologous with CRE-BP1 in four regions: two of them are the regions containing the putative metal finger or the DNA-binding domain consisting of the basic amino acid cluster and the leucine zipper.	Amino Acids, Basic	176-192	activating transcription factor 2	Homo sapiens	42-49
7510502-4	1993	The recently demonstrated presence of 4 basic amino acids (1 arginine, 3 histidine) in the cleaved fragment of the amyloid precursor protein (APP) suggest us to hypothesise that this APP portion may represent the common constitutive element of the many morphologically different alterations found in the brains of senile demented patients.	Amino Acids, Basic	40-57	amyloid beta precursor protein	Homo sapiens	115-140
8420571-7	1993	The first known eukaryotic enzyme with the exquisite cleavage specificity for paired basic amino acid residues was the prohormone processing enzyme kexin (EC 3.4.21.61), a subtilisin-like serine protease that is encoded by the KEX2 gene of yeast Saccharomyces cerevisiae.	Amino Acids, Basic	85-101	kexin KEX2	Saccharomyces cerevisiae S288C	227-231
7510003-1	1993	Recently it was documented that furin, a calcium-dependent serine endoprotease, cleaves many protein precursors at pairs of basic amino acids, thus liberating the biologically active peptides.	Amino Acids, Basic	124-141	furin, paired basic amino acid cleaving enzyme	Homo sapiens	32-37
7681586-2	1993	There are two basic amino acid clusters in the SDGF molecule which are homologous to the nuclear targeting signal of the simian virus 40-encoded large tumor antigen.	Amino Acids, Basic	14-30	amphiregulin	Mus musculus	47-51
8382303-10	1993	Between these two basic amino acid blocks in the nuclear transport signal, at threonine 102, is a putative site for phosphorylation by the cell cycle regulated kinase p34cdc2.	Amino Acids, Basic	18-34	cyclin dependent kinase 1	Homo sapiens	167-174
8452364-4	1993	These results indicate that panipenem, as well as imipenem, uses the OprD channel, which functions as a specific channel for diffusion of basic amino acids.	Amino Acids, Basic	138-155	porin D	Pseudomonas aeruginosa PAO1	69-73
8452364-8	1993	In contrast, such a change in the activities of carbapenems was not observed with an OprD protein-deficient mutant, suggesting that the main reason for the strong activities of carbapenems in biological fluids is a decrease in competition between the antibiotics and basic amino acids for permeation through the OprD channel.	Amino Acids, Basic	267-284	porin D	Pseudomonas aeruginosa PAO1	312-316
8096552-7	1993	Comparison of the amino acid residues of DRB1 chain suggested that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), contributes to the susceptibility to autoimmune hepatitis among Japanese.	Amino Acids, Basic	71-87	major histocompatibility complex, class II, DR beta 1	Homo sapiens	41-45
8096552-7	1993	Comparison of the amino acid residues of DRB1 chain suggested that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), contributes to the susceptibility to autoimmune hepatitis among Japanese.	Amino Acids, Basic	71-87	major histocompatibility complex, class II, DR beta 4	Homo sapiens	141-144
8096552-7	1993	Comparison of the amino acid residues of DRB1 chain suggested that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), contributes to the susceptibility to autoimmune hepatitis among Japanese.	Amino Acids, Basic	71-87	major histocompatibility complex, class II, DR beta 4	Homo sapiens	181-184
8416959-12	1993	The specificity of the enzyme for COOH-terminal basic amino acid residues of the peptides used in this study and its high affinity for alpha-factor-Lys-Arg confirms the role that Kex1p plays in polypeptide precursor processing in yeast.	Amino Acids, Basic	48-64	serine-type carboxypeptidase	Saccharomyces cerevisiae S288C	179-184
1472066-6	1992	PTHrP 1-139 lacks the carboxy-terminal arginine and histidine residues of PTHrP 1-141; these two basic amino acids could have significant effects on the biological activity of PTHrP.	Amino Acids, Basic	97-114	parathyroid hormone like hormone	Homo sapiens	0-5
1472066-6	1992	PTHrP 1-139 lacks the carboxy-terminal arginine and histidine residues of PTHrP 1-141; these two basic amino acids could have significant effects on the biological activity of PTHrP.	Amino Acids, Basic	97-114	parathyroid hormone like hormone	Homo sapiens	74-79
1472066-6	1992	PTHrP 1-139 lacks the carboxy-terminal arginine and histidine residues of PTHrP 1-141; these two basic amino acids could have significant effects on the biological activity of PTHrP.	Amino Acids, Basic	97-114	parathyroid hormone like hormone	Homo sapiens	74-79
1431901-1	1992	Carboxypeptidase M (CPM), a plasma membrane-bound enzyme, cleaves C-terminal basic amino acids with a neutral pH optimum.	Amino Acids, Basic	77-94	carboxypeptidase M	Canis lupus familiaris	0-18
1431901-1	1992	Carboxypeptidase M (CPM), a plasma membrane-bound enzyme, cleaves C-terminal basic amino acids with a neutral pH optimum.	Amino Acids, Basic	77-94	carboxypeptidase M	Canis lupus familiaris	20-23
1512259-8	1992	Furthermore, we show that Dfur2 encodes an endoproteolytic enzyme with specificity for paired basic amino acid residues as, in cotransfection experiments, correct cleavage was demonstrated of the precursor of the von Willebrand factor but not of a cleavage mutant.	Amino Acids, Basic	94-110	Furin 2	Drosophila melanogaster	26-31
1517248-10	1992	We conclude that the cluster of six basic amino acids forms the essential part of the heparin-binding domain and that the composition of the four subunits in the EC-SOD tetramer determines the affinity for heparin.	Amino Acids, Basic	36-53	superoxide dismutase 3	Rattus norvegicus	162-168
1517251-2	1992	The cDNA-predicted amino acid sequence of parathyroid hormone-related protein (PTHrP) contains multiple basic amino acid motifs, suggesting that PTHrP undergoes extensive post-translational processing prior to secretion.	Amino Acids, Basic	104-120	parathyroid hormone like hormone	Homo sapiens	42-77
1517251-2	1992	The cDNA-predicted amino acid sequence of parathyroid hormone-related protein (PTHrP) contains multiple basic amino acid motifs, suggesting that PTHrP undergoes extensive post-translational processing prior to secretion.	Amino Acids, Basic	104-120	parathyroid hormone like hormone	Homo sapiens	79-84
1517251-2	1992	The cDNA-predicted amino acid sequence of parathyroid hormone-related protein (PTHrP) contains multiple basic amino acid motifs, suggesting that PTHrP undergoes extensive post-translational processing prior to secretion.	Amino Acids, Basic	104-120	parathyroid hormone like hormone	Homo sapiens	145-150
1505450-1	1992	Carboxypeptidase H (CP-H, EC 3.4.17.10) removes C-terminal basic amino acids from insulin and many other peptide hormone intermediates in endocrine and neural tissues.	Amino Acids, Basic	59-76	carboxypeptidase E	Rattus norvegicus	0-18
1505450-1	1992	Carboxypeptidase H (CP-H, EC 3.4.17.10) removes C-terminal basic amino acids from insulin and many other peptide hormone intermediates in endocrine and neural tissues.	Amino Acids, Basic	59-76	carboxypeptidase E	Rattus norvegicus	20-24
1501882-1	1992	rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region.	Amino Acids, Basic	154-171	RAP1A, member of RAS oncogene family	Homo sapiens	0-11
1501882-1	1992	rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region.	Amino Acids, Basic	154-171	H3 histone pseudogene 16	Homo sapiens	16-19
1501882-1	1992	rap1/Krev-1/smg p21 (smg p21), a member of the small GTP-binding protein (G protein) superfamily, has a geranylgeranylated cysteine residue and clustered basic amino acids in the C-terminal region.	Amino Acids, Basic	154-171	H3 histone pseudogene 16	Homo sapiens	25-28
1282507-7	1992	Studies with the anaphylatoxin, C3a, and its analogues 21R and C3ades Arg on skin mast cells emphasized the importance of basic amino acids for histamine-liberating peptides.	Amino Acids, Basic	122-139	complement C3	Homo sapiens	32-35
1354193-9	1992	These findings suggest that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), contributes to the susceptibility to autoimmune hepatitis among the Japanese.	Amino Acids, Basic	32-48	major histocompatibility complex, class II, DR beta 4	Homo sapiens	102-105
1354193-9	1992	These findings suggest that the basic amino acid at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), contributes to the susceptibility to autoimmune hepatitis among the Japanese.	Amino Acids, Basic	32-48	major histocompatibility complex, class II, DR beta 4	Homo sapiens	142-145
1435788-3	1992	A major part of this processing requires endoproteolytic cleavage at specific pairs of basic amino acid residues, an event necessary for the maturation of a variety of important biologically active proteins, such as insulin and nerve growth factor.	Amino Acids, Basic	87-103	insulin	Homo sapiens	216-223
1637178-9	1992	These results suggest that the heparin-binding site may occur on a "cluster" of basic amino acids at the C-terminal end of EC-SOD C. EC-SOD is speculated to be primarily synthesized as type C, and types A and B are probably the result of secondary modifications.	Amino Acids, Basic	80-97	superoxide dismutase 3	Homo sapiens	123-129
1322111-1	1992	We have characterized the basic amino acid methylation of three members of the 70,000-Da heat shock protein superfamily, hsp68, hsc70, and BiP, in Balb/c 3T3 cells.	Amino Acids, Basic	26-42	heat shock protein 1A	Mus musculus	121-126
1322111-1	1992	We have characterized the basic amino acid methylation of three members of the 70,000-Da heat shock protein superfamily, hsp68, hsc70, and BiP, in Balb/c 3T3 cells.	Amino Acids, Basic	26-42	heat shock protein 8	Mus musculus	128-133
1322111-1	1992	We have characterized the basic amino acid methylation of three members of the 70,000-Da heat shock protein superfamily, hsp68, hsc70, and BiP, in Balb/c 3T3 cells.	Amino Acids, Basic	26-42	heat shock protein 5	Mus musculus	139-142
1637178-9	1992	These results suggest that the heparin-binding site may occur on a "cluster" of basic amino acids at the C-terminal end of EC-SOD C. EC-SOD is speculated to be primarily synthesized as type C, and types A and B are probably the result of secondary modifications.	Amino Acids, Basic	80-97	superoxide dismutase 3	Homo sapiens	133-139
1634553-11	1992	This indicated that posttranslational processing of PC2 itself occurs C-terminally to basic amino acids to produce the mature enzyme.	Amino Acids, Basic	86-103	proprotein convertase subtilisin/kexin type 2	Rattus norvegicus	52-55
1515063-0	1992	Basic amino acids preferring broad specificity aminopeptidase from human erythrocytes.	Amino Acids, Basic	0-17	carboxypeptidase Q	Homo sapiens	47-61
1612132-6	1992	Structure/function analysis suggested a bipartite structure of NL1, analogous to that of other nuclear targeting signals (the carboxy-terminal part of DBD between amino acids 478 and 487 and the beginning of the hinge region which includes a basic amino acid stretch between 491 and 498).	Amino Acids, Basic	242-258	neuroligin 1	Homo sapiens	63-66
1633858-1	1992	The multifunctional prohormone, proopiomelanocortin (POMC), is processed in the melanotrope cells of the pituitary pars intermedia at pairs of basic amino acid residues to give a number of peptides, including alpha-melanophore-stimulating hormone (alpha-MSH).	Amino Acids, Basic	143-159	proopiomelanocortin L homeolog	Xenopus laevis	32-51
1633858-1	1992	The multifunctional prohormone, proopiomelanocortin (POMC), is processed in the melanotrope cells of the pituitary pars intermedia at pairs of basic amino acid residues to give a number of peptides, including alpha-melanophore-stimulating hormone (alpha-MSH).	Amino Acids, Basic	143-159	proopiomelanocortin L homeolog	Xenopus laevis	53-57
1558971-1	1992	IL-6-PE4E is a recombinant protein consisting of interleukin-6 (IL-6) fused to a mutant form of Pseudomonas exotoxin in which four basic amino acids are changed to glutamate (PE4E).	Amino Acids, Basic	131-148	interleukin 6	Homo sapiens	0-4
1586149-6	1992	Bikunin has been shown to be synthesized by liver cells as a 42-kDa precursor, in which it is linked to alpha 1-microglobulin by two basic amino acids.	Amino Acids, Basic	133-150	alpha-1-microglobulin/bikunin precursor	Homo sapiens	0-7
1453687-1	1992	CRE-BP1 is a transcriptional activator binding to the cyclic AMP response element, which has a putative metal finger structure and the leucine zipper motif linked to a cluster of basic amino acids in the amino and carboxyl-terminal regions, respectively.	Amino Acids, Basic	179-196	activating transcription factor 2	Homo sapiens	0-7
1544507-4	1992	Residue Leu109 is preceded by a pair of basic amino acid residues (Lys107-Arg108) which is a potential processing site for the Kex2 endopeptidase.	Amino Acids, Basic	40-56	kexin KEX2	Saccharomyces cerevisiae S288C	127-131
1536576-4	1992	Isoelectric focusing and amino acid analysis of the differently loaded ferritins showed that ferrous ammonium sulfate loading of apoferritin resulted in the depletion of the basic amino acids, lysine and histidine, probably as a result of protein oxidation.	Amino Acids, Basic	174-191	ferritin heavy chain 1	Homo sapiens	129-140
1563042-1	1992	The hts1.1 temperature-sensitive histidinyl-tRNA synthetase mutation enables Saccharomyces cerevisiae to be starved for His-tRNAHis by upshift to the non-permissive temperature of 38 degrees C. If yeast behaves similarly to bacterial and mammalian cells, this lack of His-tRNAHis should greatly enhance misreading at histidine codons (CAU/CAC) by Gln-tRNAGln, resulting in substitution of the neutral amino acid glutamine in place of histidine, a basic amino acid.	Amino Acids, Basic	447-463	histidine--tRNA ligase	Saccharomyces cerevisiae S288C	4-8
1547787-6	1992	Analysis of LAR mutants suggested that cleavage occurs in the LAR extracellular region at a paired basic amino acid site by a subtilisin-like endoprotease.	Amino Acids, Basic	99-115	protein tyrosine phosphatase receptor type F	Homo sapiens	12-15
1547787-6	1992	Analysis of LAR mutants suggested that cleavage occurs in the LAR extracellular region at a paired basic amino acid site by a subtilisin-like endoprotease.	Amino Acids, Basic	99-115	protein tyrosine phosphatase receptor type F	Homo sapiens	62-65
1350267-0	1992	A possible association between basic amino acids of position 13 of DRB1 chains and autoimmune hepatitis.	Amino Acids, Basic	31-48	major histocompatibility complex, class II, DR beta 1	Homo sapiens	67-71
1316544-1	1992	PC1 and PC2 are enzymes involved in the activation of prohormones via the cleavage of pairs of basic amino acids.	Amino Acids, Basic	95-112	proprotein convertase subtilisin/kexin type 1	Rattus norvegicus	0-3
1316544-1	1992	PC1 and PC2 are enzymes involved in the activation of prohormones via the cleavage of pairs of basic amino acids.	Amino Acids, Basic	95-112	proprotein convertase subtilisin/kexin type 2	Rattus norvegicus	8-11
1346754-1	1992	I-POU, a POU domain nuclear protein that lacks two conserved basic amino acids of the POU homeodomain is coexpressed in the developing Drosophila nervous system with a second POU domain transcription factor, Cf1-a.	Amino Acids, Basic	61-78	abnormal chemosensory jump 6	Drosophila melanogaster	0-5
1346754-4	1992	twin of I-POU, an alternatively spliced transcript of the I-POU gene, encodes a protein containing the two basic amino acid residues absent in I-POU.	Amino Acids, Basic	107-123	abnormal chemosensory jump 6	Drosophila melanogaster	8-13
1346754-4	1992	twin of I-POU, an alternatively spliced transcript of the I-POU gene, encodes a protein containing the two basic amino acid residues absent in I-POU.	Amino Acids, Basic	107-123	abnormal chemosensory jump 6	Drosophila melanogaster	58-63
1346754-4	1992	twin of I-POU, an alternatively spliced transcript of the I-POU gene, encodes a protein containing the two basic amino acid residues absent in I-POU.	Amino Acids, Basic	107-123	abnormal chemosensory jump 6	Drosophila melanogaster	58-63
1586966-2	1992	Cofilin has a stretch of five basic amino acids, KKRKK, which was assumed to be the sequence involved in the heat shock-dependent accumulation of cofilin in nuclei.	Amino Acids, Basic	30-47	cofilin 1	Homo sapiens	0-7
1586966-2	1992	Cofilin has a stretch of five basic amino acids, KKRKK, which was assumed to be the sequence involved in the heat shock-dependent accumulation of cofilin in nuclei.	Amino Acids, Basic	30-47	cofilin 1	Homo sapiens	146-153
1731113-8	1992	Thus, the HDAg NLS belongs to a newly identified class of NLS which consists of two discontiguous stretches of basic amino acids.	Amino Acids, Basic	111-128	delta antigen	Hepatitis delta virus	10-14
1732061-2	1992	The nuclear localization signal of VirD2 consists of two regions containing 4-5 basic amino acids (KRPR and RKRER), located within the C-terminal 34 amino acids.	Amino Acids, Basic	80-97	type IV secretion system T-DNA border endonuclease VirD2	Agrobacterium tumefaciens	35-40
1739432-5	1992	PACAP and PRP were preceded and followed by paired basic amino acids, recognized as important for post-translational processing.	Amino Acids, Basic	51-68	adenylate cyclase activating polypeptide 1	Homo sapiens	0-5
1350267-7	1992	Taken together, these results imply that the basic amino acids at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), are most important for determining the predisposition to autoimmune hepatitis.	Amino Acids, Basic	45-62	major histocompatibility complex, class II, DR beta 4	Homo sapiens	116-119
1350267-7	1992	Taken together, these results imply that the basic amino acids at position 13, which is present only on the DR2 and DR4 B1 molecules (Arg on DR2 and His on DR4), are most important for determining the predisposition to autoimmune hepatitis.	Amino Acids, Basic	45-62	major histocompatibility complex, class II, DR beta 4	Homo sapiens	156-159
1732513-5	1992	In the three-dimensional structure of CD4, these two basic amino acids are located proximal to phenylalanine 43, which we confirmed to be important for gp120 binding.	Amino Acids, Basic	53-70	CD4 molecule	Homo sapiens	38-41
1732513-5	1992	In the three-dimensional structure of CD4, these two basic amino acids are located proximal to phenylalanine 43, which we confirmed to be important for gp120 binding.	Amino Acids, Basic	53-70	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	152-157
1764034-1	1991	Carboxypeptidase E (CPE) catalyses the removal of C-terminal basic amino acids and is implicated in the processing of peptides and hormones in secretory vesicles.	Amino Acids, Basic	61-78	carboxypeptidase E	Homo sapiens	0-18
1764034-1	1991	Carboxypeptidase E (CPE) catalyses the removal of C-terminal basic amino acids and is implicated in the processing of peptides and hormones in secretory vesicles.	Amino Acids, Basic	61-78	carboxypeptidase E	Homo sapiens	20-23
1944284-1	1991	It has been proposed that the helix-loop-helix (HLH) protein Id serves as a general antagonist of cell differentiation by inhibiting bHLH (HLH with an adjacent stretch of basic amino acids) proteins specifically required for developmental programs (such as MyoD).	Amino Acids, Basic	171-188	myogenic differentiation 1	Mus musculus	257-261
1756723-6	1991	We also present evidence that a stretch of four basic amino acids, similar to a sequence found in the other proteins belonging to the rel/NF-kappa B family, is required for translocation of the processed p50 protein into the nucleus and thus could be the target for the retention mechanism.	Amino Acids, Basic	48-65	nuclear factor kappa B subunit 1	Homo sapiens	138-148
1756723-6	1991	We also present evidence that a stretch of four basic amino acids, similar to a sequence found in the other proteins belonging to the rel/NF-kappa B family, is required for translocation of the processed p50 protein into the nucleus and thus could be the target for the retention mechanism.	Amino Acids, Basic	48-65	nuclear factor kappa B subunit 1	Homo sapiens	204-207
1807166-3	1991	A "cleanup" procedure for the isolation of the basic amino acids using a weakly acidic cation exchange resin, Biorex-70 (Bio-Rad), is described in detail.	Amino Acids, Basic	47-64	RRAD, Ras related glycolysis inhibitor and calcium channel regulator	Homo sapiens	125-128
1939237-12	1991	We propose that the primary sequence of substrates for ERK1 and ERK2 protein kinases can be generalized as -Pro-Xaan-Ser/Thr-Pro- (where Xaa is a neutral or basic amino acid and n = 1 or 2).	Amino Acids, Basic	157-173	mitogen-activated protein kinase 3	Homo sapiens	55-59
1939237-12	1991	We propose that the primary sequence of substrates for ERK1 and ERK2 protein kinases can be generalized as -Pro-Xaan-Ser/Thr-Pro- (where Xaa is a neutral or basic amino acid and n = 1 or 2).	Amino Acids, Basic	157-173	mitogen-activated protein kinase 1	Homo sapiens	64-68
1916262-9	1991	We have however, identified a cluster of basic amino acids, found only in TEF and DBP, that is necessary for the proper DNA-binding site specificity of TEF.	Amino Acids, Basic	41-58	TEF transcription factor, PAR bZIP family member	Rattus norvegicus	74-77
1945842-1	1991	The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure.	Amino Acids, Basic	146-163	myogenic differentiation 1	Homo sapiens	31-35
1945842-1	1991	The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure.	Amino Acids, Basic	146-163	myogenin	Homo sapiens	37-41
1945842-1	1991	The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure.	Amino Acids, Basic	146-163	myogenic factor 5	Homo sapiens	43-47
1945842-1	1991	The muscle regulatory proteins Myf3, Myf4, Myf5, and Myf6 share a highly conserved DNA binding and dimerization domain consisting of a cluster of basic amino acids and a potential helix-loop-helix structure.	Amino Acids, Basic	146-163	myogenic factor 6	Homo sapiens	53-57
1680673-4	1991	Comparison of the obtained protein sequence with the cDNA sequence of mammalian PC2 also suggests that the active enzyme is derived from a precursor by cleavage at a site containing four consecutive basic amino acids.	Amino Acids, Basic	199-216	proprotein convertase subtilisin/kexin type 2	Homo sapiens	80-83
1915263-2	1991	Within the alpha chain of the multisubunit T-cell antigen receptor (TCR) complex, a transmembrane sequence containing two basic amino acid residues has been shown to act as a determinant for retention and rapid degradation in the ER.	Amino Acids, Basic	122-138	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	43-66
1915263-2	1991	Within the alpha chain of the multisubunit T-cell antigen receptor (TCR) complex, a transmembrane sequence containing two basic amino acid residues has been shown to act as a determinant for retention and rapid degradation in the ER.	Amino Acids, Basic	122-138	T cell receptor beta variable 20/OR9-2 (non-functional)	Homo sapiens	68-71
1916262-9	1991	We have however, identified a cluster of basic amino acids, found only in TEF and DBP, that is necessary for the proper DNA-binding site specificity of TEF.	Amino Acids, Basic	41-58	D-box binding PAR bZIP transcription factor	Rattus norvegicus	82-85
1916262-9	1991	We have however, identified a cluster of basic amino acids, found only in TEF and DBP, that is necessary for the proper DNA-binding site specificity of TEF.	Amino Acids, Basic	41-58	TEF transcription factor, PAR bZIP family member	Rattus norvegicus	152-155
1883381-6	1991	ARAP contains 10 cysteines and 30 basic amino acids (23 lysines and 7 arginines).	Amino Acids, Basic	34-51	midkine	Homo sapiens	0-4
1930163-6	1991	The results suggest that not only a basic amino acid at position -4 but also Leu at position +1 significantly affect the processing of prorenin catalyzed by the COS cell endoprotease or furin.	Amino Acids, Basic	36-52	furin, paired basic amino acid cleaving enzyme	Homo sapiens	186-191
1367896-1	1991	The Saccharomyces cerevisiae KEX2 gene encodes the membrane-bound endoprotease yscF, which is responsible for the site-specific endoproteolytic cleavages at pairs of basic amino acid residues in the alpha-factor precursor.	Amino Acids, Basic	166-182	kexin KEX2	Saccharomyces cerevisiae S288C	29-33
2022638-8	1991	In addition to the CAAX box, xlcaax-1 contains a series of basic amino acids upstream of the CAAX sequence similar to several nonpalmitoylated forms of the ras-related proteins.	Amino Acids, Basic	59-76	paralemmin 3 L homeolog	Xenopus laevis	29-37
1906785-1	1991	Association of Fos and Jun with the AP-1 site results in a conformational change in the basic amino acid regions that constitute the DNA-binding domain.	Amino Acids, Basic	88-104	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	15-18
2051232-6	1991	The results indicate that a range of essential and nonessential neutral and basic amino acids stimulate the release of GIP in ob/ob mice.	Amino Acids, Basic	76-93	gastric inhibitory polypeptide	Mus musculus	119-122
1904542-2	1991	Fos and Jun are members of a family of related transcription factors that dimerize via a leucine zipper structure and interact with DNA through a bipartite domain formed between regions of each protein that are rich in basic amino acids.	Amino Acids, Basic	219-236	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	0-3
2063194-4	1991	Basic amino acids important for LDL receptor binding are clustered into a surface patch on one long helix.	Amino Acids, Basic	0-17	low density lipoprotein receptor	Homo sapiens	32-44
2041050-7	1991	The SRB binds to the basic amino acids of cellular macromolecules; the solubilized stain is measured spectrophotometrically to determine relative cell growth or viability in treated and untreated cells.	Amino Acids, Basic	21-38	chaperonin containing TCP1 subunit 4	Homo sapiens	4-7
2025642-2	1991	Bovine chromogranin B consists of 626 amino acids and contains 16 pairs of basic amino acids which might be used for generation of biological active peptides.	Amino Acids, Basic	75-92	chromogranin B	Bos taurus	7-21
1856197-2	1991	Many neuroendocrine precursor proteins, such as proopiomelanocortin (POMC), are cleaved in a tissue specific manner at distinct pairs of basic amino acids.	Amino Acids, Basic	137-154	pro-opiomelanocortin-alpha	Mus musculus	48-67
1856197-2	1991	Many neuroendocrine precursor proteins, such as proopiomelanocortin (POMC), are cleaved in a tissue specific manner at distinct pairs of basic amino acids.	Amino Acids, Basic	137-154	pro-opiomelanocortin-alpha	Mus musculus	69-73
1713771-6	1991	As with KEX2, the expressed human protease was shown to cleave mammalian proproteins at their paired basic amino acid processing sites.	Amino Acids, Basic	101-117	kexin KEX2	Saccharomyces cerevisiae S288C	8-12
2019589-8	1991	DNA sequence analysis of cM32 indicated that MAGP contains two structurally dissimilar regions, an amino-terminal domain containing high levels of glutamine, proline, and acidic amino acids and a carboxyl-terminal domain containing all 13 of the cysteine residues and most of the basic amino acids.	Amino Acids, Basic	280-297	microfibril associated protein 2	Bos taurus	45-49
1987379-5	1991	A basic amino acid at the p17-p24 scissile bond is not tolerated.	Amino Acids, Basic	2-18	family with sequence similarity 72 member B	Homo sapiens	26-29
1826685-5	1991	266, 229-237) suggested that the conserved basic amino acid sequence which characterizes the two proteins and which corresponds to the PKC phosphorylation and calmodulin binding domain also serves as phospholipid binding site.	Amino Acids, Basic	43-59	calmodulin 1	Homo sapiens	159-169
1826736-0	1991	In vitro synthesis of West Nile virus proteins indicates that the amino-terminal segment of the NS3 protein contains the active centre of the protease which cleaves the viral polyprotein after multiple basic amino acids.	Amino Acids, Basic	202-219	KRAS proto-oncogene, GTPase	Homo sapiens	96-99
2005104-0	1991	Substitution of basic amino acids within endonuclease V enhances nontarget DNA binding.	Amino Acids, Basic	16-33	endonuclease V	Homo sapiens	41-55
1901275-1	1991	Using three different approaches (domain mapping with monoclonal antibodies, limited enzymatic digestion and competition with synthetic peptides), we demonstrated that a cluster of basic amino acids on interferon-gamma is involved in its binding to heparan sulfate.	Amino Acids, Basic	181-198	interferon gamma	Homo sapiens	202-218
1999411-2	1991	Activity of PLA-2 toward Escherichia coli treated with the bactericidal/permeability-increasing protein (BPI) of granulocytes has been detected only in "Group II" PLA-2 (lacking Cys11-Cys77) and correlates with overall basicity and the presence of a cluster of basic amino acids within a variable surface region near the NH2 terminus (including residues 6, 7, 10, 11, and 15).	Amino Acids, Basic	261-278	phospholipase A2 group IB	Homo sapiens	12-17
1999411-2	1991	Activity of PLA-2 toward Escherichia coli treated with the bactericidal/permeability-increasing protein (BPI) of granulocytes has been detected only in "Group II" PLA-2 (lacking Cys11-Cys77) and correlates with overall basicity and the presence of a cluster of basic amino acids within a variable surface region near the NH2 terminus (including residues 6, 7, 10, 11, and 15).	Amino Acids, Basic	261-278	bactericidal permeability increasing protein	Sus scrofa	105-108
1851554-5	1991	Two domains rich in basic amino-acids are required for the nuclear localization of EB1.	Amino Acids, Basic	20-37	microtubule associated protein RP/EB family member 1	Homo sapiens	83-86
2018506-3	1991	The sequence of RI-HB contains 121 amino acid residues and is very rich in basic amino acids and cysteines.	Amino Acids, Basic	75-92	midkine (neurite growth-promoting factor 2)	Gallus gallus	16-21
2016053-6	1991	Amino acid sequence comparisons of the E74A protein reveal a highly conserved C-terminal region that is rich in basic amino acid residues and which has been proposed to possess sequence-specific DNA binding activity.	Amino Acids, Basic	112-128	Ecdysone-induced protein 74EF	Drosophila melanogaster	39-43
1653894-1	1991	Mouse pro-ACTH/endorphin (or POMC) contains in its sequence each of the four possible pairs of basic amino acids recognized as potential cleavage sites in the production of bioactive peptides from higher mol wt precursors: KR (lysine-arginine), RR, RK, and KK.	Amino Acids, Basic	95-112	pro-opiomelanocortin-alpha	Mus musculus	29-33
1987379-5	1991	A basic amino acid at the p17-p24 scissile bond is not tolerated.	Amino Acids, Basic	2-18	transmembrane p24 trafficking protein 2	Homo sapiens	30-33
1773057-4	1991	We found that pairs of arginine residues flanking gastrin 34, the typical processing site sequence of all other preprogastrins and many peptide hormones, were arginines in the bovine preprogastrin, but the first basic amino acid pair had changed to Arg-Trp (57-58 residues) instead of Arg-Arg in the feline preprogastrin.	Amino Acids, Basic	212-228	gastrin	Homo sapiens	50-57
1784247-4	1991	Substitution of basic amino acids at the P450 N terminus or replacing the N terminus of P450 with a secretory signal sequence results in partial or complete translocation across the membrane.	Amino Acids, Basic	16-33	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	41-45
1837490-2	1991	The deduced amino acid sequence revealed that CREB2 contains a leucine zipper structure (residue 295 to 316), a basic amino acid domain (residue 268 to 291) and several potential phosphorylation sites.	Amino Acids, Basic	112-128	activating transcription factor 2	Bos taurus	46-51
1843280-2	1991	Furin, the translational product of the recently discovered fur gene, appears to be the first known mammalian member of the subtilisin family of serine proteases and the first known mammalian proprotein-processing enzyme with cleavage selectivity for paired basic amino acid residues.	Amino Acids, Basic	258-274	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
1843280-8	1991	Finally, the cleavage specificity for paired basic amino acid residues of human and mouse furin is demonstrated by the correct processing of the precursor for von Willebrand factor.	Amino Acids, Basic	45-61	furin (paired basic amino acid cleaving enzyme)	Mus musculus	90-95
2266110-5	1990	It has been proposed that furin is a mammalian prohormone processing enzyme which cleaves precursors at paired basic amino acids, based on the fact that the Kex2 protease is responsible for processing of alpha-mating factor and killer toxin precursors at dibasic sites.	Amino Acids, Basic	111-128	furin, paired basic amino acid cleaving enzyme	Homo sapiens	26-31
2266110-5	1990	It has been proposed that furin is a mammalian prohormone processing enzyme which cleaves precursors at paired basic amino acids, based on the fact that the Kex2 protease is responsible for processing of alpha-mating factor and killer toxin precursors at dibasic sites.	Amino Acids, Basic	111-128	kexin KEX2	Saccharomyces cerevisiae S288C	157-161
2269657-1	1990	Extracts from BSC-40 cells infected with vaccinia recombinants expressing either the yeast KEX2 prohormone endoprotease or a human structural homologue (fur gene product) contained an elevated level of a membrane-associated endoproteolytic activity that could cleave at pairs of basic amino acids (-LysArg- and -ArgArg-).	Amino Acids, Basic	279-296	kexin KEX2	Saccharomyces cerevisiae S288C	91-95
2251280-0	1990	Expression of a human proprotein processing enzyme: correct cleavage of the von Willebrand factor precursor at a paired basic amino acid site.	Amino Acids, Basic	120-136	von Willebrand factor	Homo sapiens	76-97
2251280-5	1990	The encoded protein, called PACE (paired basic amino acid cleaving enzyme), has structural homology to the well-characterized subtilisin-like protease Kex2 from yeast.	Amino Acids, Basic	41-57	furin, paired basic amino acid cleaving enzyme	Homo sapiens	28-32
2263631-6	1990	The carboxyl terminus of bombesin is flanked by two basic amino acids; the amino terminus is not flanked by basic amino acids but is flanked by a chymotryptic-like cleavage site.	Amino Acids, Basic	52-69	gastrin releasing peptide	Homo sapiens	25-33
2251280-5	1990	The encoded protein, called PACE (paired basic amino acid cleaving enzyme), has structural homology to the well-characterized subtilisin-like protease Kex2 from yeast.	Amino Acids, Basic	41-57	kexin KEX2	Saccharomyces cerevisiae S288C	151-155
2251280-6	1990	The functional specificity of PACE for mediating propeptide cleavage at paired basic amino acid residues was demonstrated by the enhancement of propeptide processing of human von Willebrand factor when coexpressed with PACE in COS-1 cells.	Amino Acids, Basic	79-95	furin, paired basic amino acid cleaving enzyme	Homo sapiens	30-34
2251280-6	1990	The functional specificity of PACE for mediating propeptide cleavage at paired basic amino acid residues was demonstrated by the enhancement of propeptide processing of human von Willebrand factor when coexpressed with PACE in COS-1 cells.	Amino Acids, Basic	79-95	von Willebrand factor	Homo sapiens	175-196
2251280-6	1990	The functional specificity of PACE for mediating propeptide cleavage at paired basic amino acid residues was demonstrated by the enhancement of propeptide processing of human von Willebrand factor when coexpressed with PACE in COS-1 cells.	Amino Acids, Basic	79-95	furin, paired basic amino acid cleaving enzyme	Homo sapiens	219-223
2120592-2	1990	Protein dimerization is mediated primarily by a coiled-coil-like structure termed the leucine-zipper and DNA binding occurs primarily through regions of each protein rich in basic amino acids that contact both strands of the AP-1 site.	Amino Acids, Basic	174-191	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	225-229
2152133-7	1990	OCSBF-1 contained a small basic amino acid region and a potential leucine zipper motif homologous to the DNA-binding domains of the basic region-leucine zipper family of transcription factors such as Jun and GCN4.	Amino Acids, Basic	26-42	ocs element-binding factor 1	Zea mays	0-7
2211623-1	1990	We have studied the specificity requirements for processing of the human insulin proreceptor by successively replacing each basic amino acid in the tetrabasic cleavage site with alanine.	Amino Acids, Basic	124-140	insulin	Homo sapiens	73-80
2196176-3	1990	All three proteins, TREB5, TREB7 and TREB36, contained a leucine zipper structure and basic amino acid domain, which are conserved in FOS, JUN and CREB, and also had multiple potential phosphorylation sites.	Amino Acids, Basic	86-102	X-box binding protein 1	Homo sapiens	20-25
2196176-3	1990	All three proteins, TREB5, TREB7 and TREB36, contained a leucine zipper structure and basic amino acid domain, which are conserved in FOS, JUN and CREB, and also had multiple potential phosphorylation sites.	Amino Acids, Basic	86-102	activating transcription factor 2	Homo sapiens	27-32
2196176-3	1990	All three proteins, TREB5, TREB7 and TREB36, contained a leucine zipper structure and basic amino acid domain, which are conserved in FOS, JUN and CREB, and also had multiple potential phosphorylation sites.	Amino Acids, Basic	86-102	activating transcription factor 1	Homo sapiens	37-43
2196176-3	1990	All three proteins, TREB5, TREB7 and TREB36, contained a leucine zipper structure and basic amino acid domain, which are conserved in FOS, JUN and CREB, and also had multiple potential phosphorylation sites.	Amino Acids, Basic	86-102	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	134-137
2196176-3	1990	All three proteins, TREB5, TREB7 and TREB36, contained a leucine zipper structure and basic amino acid domain, which are conserved in FOS, JUN and CREB, and also had multiple potential phosphorylation sites.	Amino Acids, Basic	86-102	cAMP responsive element binding protein 1	Homo sapiens	147-151
2156209-2	1990	Mutation of basic amino acid residues in this region of p53 (residues 312 to 323; SSSPQPKKKP) compromises transport of p53 protein to the nucleus.	Amino Acids, Basic	12-28	tumor protein p53	Homo sapiens	56-59
2115122-4	1990	Whereas Fos bound to the AP-1 site through a domain rich in basic amino acids and associated with Jun via a leucine zipper interaction, mutant Fos proteins lacking these structures were still capable of causing repression.	Amino Acids, Basic	60-77	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	8-11
2274116-2	1990	VIP contains paired basic aminoacid residues at which posttranslational cleavage of these peptides might occur.	Amino Acids, Basic	20-35	vasoactive intestinal peptide	Rattus norvegicus	0-3
2162825-1	1990	Atrial natriuretic factor (ANF) is stored within atrial myocyte secretory granules as pro-ANF (ANF-(1-126] and is proteolytically processed co-secretionally C-terminal to a single basic amino acid to form ANF-(1-98) and the bioactive product ANF-(99-126).	Amino Acids, Basic	180-196	natriuretic peptide type A	Mus musculus	0-25
2162825-1	1990	Atrial natriuretic factor (ANF) is stored within atrial myocyte secretory granules as pro-ANF (ANF-(1-126] and is proteolytically processed co-secretionally C-terminal to a single basic amino acid to form ANF-(1-98) and the bioactive product ANF-(99-126).	Amino Acids, Basic	180-196	natriuretic peptide type A	Mus musculus	27-30
2205532-5	1990	The major cleavage site, after a pair of basic amino acids (aa) (Arg25Lys26 decreases Lys27), resembles that recognized by the KEX2 gene product on which the MF alpha expression-secretion system depends.	Amino Acids, Basic	41-58	kexin KEX2	Saccharomyces cerevisiae S288C	127-131
2345170-4	1990	Bovine secretogranin II is a 586-amino acid protein of 67,455 Da which is preceded by a signal peptide of 27 residues and contains 9 pairs of basic amino acids in its sequence which are used as potential cleavage sites for generation of physiologically active peptides.	Amino Acids, Basic	142-159	secretogranin II	Bos taurus	7-23
2373961-2	1990	Clearance is mediated by the interaction of a domain enriched in basic amino acid residues on apoB-100 with clusters of acidic residues on the apoB,E (LDL) receptor.	Amino Acids, Basic	65-81	apolipoprotein B	Homo sapiens	94-102
2373961-2	1990	Clearance is mediated by the interaction of a domain enriched in basic amino acid residues on apoB-100 with clusters of acidic residues on the apoB,E (LDL) receptor.	Amino Acids, Basic	65-81	apolipoprotein B	Homo sapiens	94-98
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Amino Acids, Basic	109-125	insulin receptor	Homo sapiens	3-19
2187866-1	1990	An insulin receptor mutant was constructed utilizing site-directed mutagenesis to delete the Arg-Lys-Arg-Arg basic amino acid cleavage site (positions 720-723) from the cDNA encoding the human insulin proreceptor.	Amino Acids, Basic	109-125	insulin	Homo sapiens	3-10
2110481-3	1990	In contrast, two basic amino acid transport systems in a gap1 mutant of Saccharomyces cerevisiae are influenced by NH4+ ions in such a way that only the Jmax decreases while the KT of L-lysine transport is unchanged.	Amino Acids, Basic	17-33	amino acid permease GAP1	Saccharomyces cerevisiae S288C	57-61
2318889-3	1990	One of these regions, which encompasses a dimeric structure enriched in basic amino acids, is required for both glycosaminoglycan binding and glycosaminoglycan-mediated acceleration of thrombin inhibition.	Amino Acids, Basic	72-89	coagulation factor II, thrombin	Homo sapiens	185-193
2193026-1	1990	A vaccinia virus vector was used to express the yeast KEX1 gene, which encodes a prohormone carboxypeptidase specific for the removal of basic amino acids from prohormone processing intermediates, in mammalian cells.	Amino Acids, Basic	137-154	serine-type carboxypeptidase	Saccharomyces cerevisiae S288C	54-58
2078567-4	1990	A putative HBD consisting of two clusters of basic amino acid residues located close to each other in the linear amino acid sequence of NCAM has previously been identified.	Amino Acids, Basic	45-61	exocyst complex component 6	Mus musculus	11-14
2078567-4	1990	A putative HBD consisting of two clusters of basic amino acid residues located close to each other in the linear amino acid sequence of NCAM has previously been identified.	Amino Acids, Basic	45-61	neural cell adhesion molecule 1	Mus musculus	136-140
2078567-9	1990	Furthermore, whereas a synthetic peptide that contains both basic amino acid clusters inhibits retinal-cell adhesion to NCAM-coated dishes, synthetic peptides in which either one of the two basic regions is altered to contain only neutral amino acids do not inhibit this adhesion.	Amino Acids, Basic	60-76	neural cell adhesion molecule 1	Mus musculus	120-124
2156209-2	1990	Mutation of basic amino acid residues in this region of p53 (residues 312 to 323; SSSPQPKKKP) compromises transport of p53 protein to the nucleus.	Amino Acids, Basic	12-28	tumor protein p53	Homo sapiens	119-122
2306477-1	1990	Wheat embryo Ca2+-dependent protein kinase (CDPK) is inhibited by a variety of polypeptides including actin, gramicidin S, melittin, protamine, various histone preparations, histone H4 and by basic amino-acid homopolymers.	Amino Acids, Basic	192-208	calcium-dependent protein kinase 19	Triticum aestivum	13-42
2107100-4	1990	In this report, we attempted to delineate the region of hirudin which binds to these basic amino acids of thrombin.	Amino Acids, Basic	85-102	coagulation factor II, thrombin	Homo sapiens	106-114
2303410-2	1990	To investigate the specificity of these endoproteases, cDNAs encoding pro-neuropeptide Y (pro-NPY) containing all four pairs of basic amino acids were expressed in AtT-20 cells.	Amino Acids, Basic	128-145	neuropeptide Y	Mus musculus	70-88
2303410-2	1990	To investigate the specificity of these endoproteases, cDNAs encoding pro-neuropeptide Y (pro-NPY) containing all four pairs of basic amino acids were expressed in AtT-20 cells.	Amino Acids, Basic	128-145	neuropeptide Y	Mus musculus	90-97
2306477-1	1990	Wheat embryo Ca2+-dependent protein kinase (CDPK) is inhibited by a variety of polypeptides including actin, gramicidin S, melittin, protamine, various histone preparations, histone H4 and by basic amino-acid homopolymers.	Amino Acids, Basic	192-208	calcium-dependent protein kinase 19	Triticum aestivum	44-48
2306477-4	1990	Various basic amino-acid homopolymers are also potent, apparently competitive inhibitors of wheat embryo CDPK, namely poly(L-lysine) (IC50 2 nM), poly(L-ornithine) (IC50 3 nM) and poly(L-arginine) (IC50 17 nM) and also inhibit the leaf CDPKs, albeit at higher concentrations.	Amino Acids, Basic	8-24	calcium-dependent protein kinase 19	Triticum aestivum	105-109
2140277-8	1990	The variations in the screening effect of the negative charges of the CF1 surface by K+ ions can indeed explain the changes in the anchorage of these 3 basic amino acids with concomitant variation in ATPase activity.	Amino Acids, Basic	152-169	dynein axonemal heavy chain 8	Homo sapiens	200-206
2133107-4	1990	In addition to the leucine zipper, DNA binding requires two clusters of basic amino acids adjacent to the leucine zipper domains of both Fos and Jun.	Amino Acids, Basic	72-89	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	137-140
2183181-4	1990	By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids.	Amino Acids, Basic	300-317	SKI proto-oncogene	Homo sapiens	42-45
2183181-4	1990	By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids.	Amino Acids, Basic	300-317	SKI proto-oncogene	Homo sapiens	109-112
2183181-4	1990	By use of a series of deletion mutants of Ski synthesized in an in vitro translation system, two portions in Ski were found to be necessary for the DNA binding of the Ski complex: the N-proximal portion containing a cystein/histidine-rich domain and the C-terminal portion including a region rich in basic amino acids.	Amino Acids, Basic	300-317	SKI proto-oncogene	Homo sapiens	109-112
2153894-1	1990	Carboxypeptidase H is an exopeptidase which is highly specific for C-terminal basic amino acids and thought to play a role in neuropeptide biosynthesis.	Amino Acids, Basic	78-95	carboxypeptidase E	Rattus norvegicus	0-18
19619244-0	2009	Conserved aromatic and basic amino acid residues in the pore region of Caenorhabditis elegans spastin play critical roles in microtubule severing.	Amino Acids, Basic	23-39	spastin	Homo sapiens	94-101
2115424-5	1990	Mutations of the basic amino acids in fos protein prevent binding to the tumour promoter response element (TRE) in the presence of wild-type jun protein.	Amino Acids, Basic	17-34	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	38-41
2122147-5	1990	The in vivo intragranular concentrations of lysine and arginine are similar to the measured Ki values, indicating that product inhibition of CPH by basic amino acids may occur in vivo.	Amino Acids, Basic	148-165	carboxypeptidase E	Bos taurus	141-144
7805649-4	1994	It contains eight pairs of basic amino acids and one sequence of four basic amino acids, which are the sites of cleavage for the recently identified prohormone convertases (PC1 and PC2), which have different specificities.	Amino Acids, Basic	27-44	polycystin 1, transient receptor potential channel interacting	Homo sapiens	173-176
7805649-4	1994	It contains eight pairs of basic amino acids and one sequence of four basic amino acids, which are the sites of cleavage for the recently identified prohormone convertases (PC1 and PC2), which have different specificities.	Amino Acids, Basic	27-44	chromobox 4	Homo sapiens	181-184
7805649-4	1994	It contains eight pairs of basic amino acids and one sequence of four basic amino acids, which are the sites of cleavage for the recently identified prohormone convertases (PC1 and PC2), which have different specificities.	Amino Acids, Basic	70-87	polycystin 1, transient receptor potential channel interacting	Homo sapiens	173-176
7805649-4	1994	It contains eight pairs of basic amino acids and one sequence of four basic amino acids, which are the sites of cleavage for the recently identified prohormone convertases (PC1 and PC2), which have different specificities.	Amino Acids, Basic	70-87	chromobox 4	Homo sapiens	181-184
34380107-7	2022	Results showed a mixed type of inhibition behavior and, the docking molecular analyzes suggest that the inhibition AChE occurred due to the basic amino acids, mainly by arginine.	Amino Acids, Basic	140-157	acetylcholinesterase (Cartwright blood group)	Homo sapiens	115-119
34669168-11	2022	This gene encodes a putative subunit of the neutral and basic amino acid transport protein, BAT1.	Amino Acids, Basic	56-72	solute carrier family 7 member 9	Homo sapiens	92-96
34704591-2	2021	Different from conventional syntaxins, Stx17 has a long C-terminal hydrophobic region with a hairpin-like structure flanked by a basic amino acid-enriched C-terminal tail.	Amino Acids, Basic	129-145	syntaxin 17	Homo sapiens	39-44
34827083-0	2021	Abnormal Enhancement of Protein Disulfide Isomerase-like Activity of a Cyclic Diselenide Conjugated with a Basic Amino Acid by Inserting a Glycine Spacer.	Amino Acids, Basic	107-123	prolyl 4-hydroxylase subunit beta	Homo sapiens	24-51
34849194-0	2021	Structural determinants of ligands recognition by the human mitochondrial basic amino acids transporter SLC25A29.	Amino Acids, Basic	74-91	solute carrier family 25 member 29	Homo sapiens	104-112
34849194-3	2021	This task is accomplished by the Mitochondrial Carrier Family members (also known as SLC25), among which the SLC25A29 is responsible for the translocation of basic amino acids.	Amino Acids, Basic	158-175	solute carrier family 25 member 29	Homo sapiens	109-117
34582889-7	2021	Mxr1N250, containing the N-terminal 250 amino acids of Mxr1p, localized to the nucleus of cells metabolizing ethanol dependent on basic amino acid residues present between amino acids 75 and 85.	Amino Acids, Basic	130-146	peptide-methionine-S-sulfoxide reductase	Saccharomyces cerevisiae S288C	55-60
34294141-7	2021	We found Nsp3 interacted with N through its acidic region at N-terminus, while N interacted with Nsp3 through its NTD, which is rich in the basic amino acids.	Amino Acids, Basic	140-157	nucleocapsid phosphoprotein	Severe acute respiratory syndrome coronavirus 2	79-80
34163035-6	2021	Although the precise changes in A.23.1 differ from those reported in the first three SARS-CoV-2 variants of concern (VOCs), the A.23.1 spike-protein-coding region has changes similar to VOCs including a change at position 613, a change in the furin cleavage site that extends the basic amino acid motif and multiple changes in the immunogenic N-terminal domain.	Amino Acids, Basic	280-296	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	135-140
34294141-7	2021	We found Nsp3 interacted with N through its acidic region at N-terminus, while N interacted with Nsp3 through its NTD, which is rich in the basic amino acids.	Amino Acids, Basic	140-157	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	97-101
34069243-10	2021	Overall, the replacement of lysine in SVS-1 with other basic amino acids significantly influenced its binding and internalization into cancer cells, as well as its in vivo pharmacokinetic profile.	Amino Acids, Basic	55-72	amine oxidase copper containing 1-like 3	Mus musculus	38-43
35367451-1	2022	We herein report the identification of the lantanide praseodymium trivalent ion Pr3+ as inhibitor of mitochondrial transporters for basic amino acids and phylogenetically related carriers belonging to the Slc25 family.	Amino Acids, Basic	132-149	proteinase 3	Homo sapiens	80-83
35569376-1	2022	SLC6A14 is a plasma membrane transporter specific for neutral and basic amino acids, upregulated in many tumors.	Amino Acids, Basic	66-83	solute carrier family 6 member 14	Homo sapiens	0-7
35551672-7	2022	The C-terminal Helix 8 region of CCR2A contains few basic amino acids, which may be unfavorable for cell surface localization, as confirmed with the HiBiT assay.	Amino Acids, Basic	52-69	chemokine (C-C motif) receptor 2	Mus musculus	33-38
2479987-6	1989	Clusters of basic amino acids in the COOH-terminal halves of human VPF and PDGF-B are also prevalent.	Amino Acids, Basic	12-29	vascular endothelial growth factor A	Homo sapiens	67-70
35367451-2	2022	The inhibitory effect of Pr3+ has been tested using mitochondrial transporters reconstituted into liposomes being effective in the micromolar range, acting as a competitive inhibitor of the human basic amino acids carrier (BAC, Slc25A29), the human carnitine/acylcarnitine carrier (CAC, Slc25A20).	Amino Acids, Basic	196-213	proteinase 3	Homo sapiens	25-28
35409362-7	2022	The basic amino acid arginine enhances glucagon secretion via voltage-dependent calcium channels (VDCC).	Amino Acids, Basic	4-20	glucagon	Cricetulus griseus	39-47
35563446-8	2022	Fragment molecular orbital calculation revealed a strong binding of sulfated hyaluronan tetrasaccharide to the heparanase molecule based on electrostatic interactions, particularly characterized by interactions of (-1)- and (-2)-positioned sulfated sugar residues with basic amino acid residues composing the heparin-binding domain-1 of heparanase.	Amino Acids, Basic	269-285	heparanase	Mus musculus	111-121
35247648-5	2022	There are four cysteine residues forming two disulfide linkage and 14 basic amino acid residues which result in a very basic property for the binding of IL-8 to heparan sulfate-proteoglycan.	Amino Acids, Basic	70-86	C-X-C motif chemokine ligand 8	Homo sapiens	153-157
35343766-3	2022	The "priming" of the surface S protein at S1/S2 (PRRAR685 ) (the underlined basic amino acids refer to critical residues needed for the furin recognition) by furin has been shown to be important for SARS-CoV-2 infectivity in cells and small-animal models.	Amino Acids, Basic	76-93	furin, paired basic amino acid cleaving enzyme	Homo sapiens	136-141
35343766-3	2022	The "priming" of the surface S protein at S1/S2 (PRRAR685 ) (the underlined basic amino acids refer to critical residues needed for the furin recognition) by furin has been shown to be important for SARS-CoV-2 infectivity in cells and small-animal models.	Amino Acids, Basic	76-93	furin, paired basic amino acid cleaving enzyme	Homo sapiens	158-163
34261912-4	2022	SRB dye interacts with protein"s basic amino acids and viable cell number is determined based on the cellular protein content.	Amino Acids, Basic	33-50	chaperonin containing TCP1 subunit 4	Homo sapiens	0-3
2479987-6	1989	Clusters of basic amino acids in the COOH-terminal halves of human VPF and PDGF-B are also prevalent.	Amino Acids, Basic	12-29	platelet derived growth factor subunit B	Homo sapiens	75-81
2479639-2	1989	It is thought that the binding of apoB to the low density lipoprotein (LDL) receptor involves an interaction between basic amino acids of the ligand and acidic residues of the receptor.	Amino Acids, Basic	117-134	apolipoprotein B	Homo sapiens	34-38
2479639-2	1989	It is thought that the binding of apoB to the low density lipoprotein (LDL) receptor involves an interaction between basic amino acids of the ligand and acidic residues of the receptor.	Amino Acids, Basic	117-134	low density lipoprotein receptor	Homo sapiens	46-84
2479639-3	1989	Three alternative models have been proposed to describe this interaction: 1) a single region of apoB is involved in receptor binding; 2) groups of basic amino acids from throughout the apoB primary structure act in concert in apoB receptor binding; and 3) apoB contains multiple independent binding regions.	Amino Acids, Basic	147-164	apolipoprotein B	Homo sapiens	185-189
2479639-3	1989	Three alternative models have been proposed to describe this interaction: 1) a single region of apoB is involved in receptor binding; 2) groups of basic amino acids from throughout the apoB primary structure act in concert in apoB receptor binding; and 3) apoB contains multiple independent binding regions.	Amino Acids, Basic	147-164	apolipoprotein B	Homo sapiens	185-189
2479639-3	1989	Three alternative models have been proposed to describe this interaction: 1) a single region of apoB is involved in receptor binding; 2) groups of basic amino acids from throughout the apoB primary structure act in concert in apoB receptor binding; and 3) apoB contains multiple independent binding regions.	Amino Acids, Basic	147-164	apolipoprotein B	Homo sapiens	185-189
2506856-1	1989	Bleomycin hydrolase, which hydrolyzes the carboxamide bond in the pyrimidoblamic acid moiety of the bleomycin molecule, also cleaved several p-nitroanilide substrates with a neutral or basic amino acid residue and dipeptide substrates such as L-leucyl-glycine.	Amino Acids, Basic	185-201	bleomycin hydrolase	Homo sapiens	0-19
2559542-0	1989	A region of basic amino-acid cluster in HIV-1 Tat protein is essential for trans-acting activity and nucleolar localization.	Amino Acids, Basic	12-28	Tat	Human immunodeficiency virus 1	46-49
2559542-1	1989	The trans-acting factor of human immunodeficiency virus (HIV), Tat, has a basic amino-acid cluster that is highly conserved among different HIV isolates.	Amino Acids, Basic	74-90	Tat	Human immunodeficiency virus 1	63-66
2668738-5	1989	After a Kex2p-mediated cleavage event at specific pairs of basic amino acids, alpha-factor and K1 killer toxin precursors have COOH-terminal dibasic residue extensions and require a carboxypeptidase B-like enzyme to process the precursors to maturity.	Amino Acids, Basic	59-76	kexin KEX2	Saccharomyces cerevisiae S288C	8-13
2605684-4	1989	This result suggests that basic amino acid residues at the P1 position play an important role in binding with the S1 subsite of ACE in this series.	Amino Acids, Basic	26-42	angiotensin I converting enzyme	Homo sapiens	128-131
2760115-8	1989	The heparin-binding domain of TSP is a compact globular amino-terminal moiety that contains two clusters of basic amino acids and a single intrachain disulphide bond.	Amino Acids, Basic	108-125	thrombospondin 1	Homo sapiens	30-33
2668738-6	1989	A carboxypeptidase activity, with apparent specificity for basic amino acids, was detected in KEX1 cells.	Amino Acids, Basic	59-76	serine-type carboxypeptidase	Saccharomyces cerevisiae S288C	94-98
2911604-5	1989	The 105 amino acid segment that distinguishes the two forms of atrial PAM contains a consensus N-glycosylation site and a paired basic amino acid site of potential importance in endoproteolytic processing.	Amino Acids, Basic	129-145	peptidylglycine alpha-amidating monooxygenase	Rattus norvegicus	70-73
2721498-8	1989	The myc homology region and a preceding cluster of basic amino acids are located in a larger sequence domain with strong similarity to the mouse myogenic factor MyoD1.	Amino Acids, Basic	51-68	myogenic differentiation 1	Mus musculus	161-166
2920029-3	1989	The basic amino acid residues of the known myosin light-chain kinase inhibitor Lys-Lys-Arg-Ala-Ala-Arg-Ala-Thr-Ser-NH2 (IC50 = 14 microM) [Pearson, Misconi & Kemp (1986) J. Biol.	Amino Acids, Basic	4-20	myosin light chain kinase	Sus scrofa	43-68
2518685-5	1989	Mutations of the basic amino acids in fos protein prevent binding to TPA (phorbol ester)-responsive element (TRE) in the presence of wild-type jun protein.	Amino Acids, Basic	17-34	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	38-41
2550051-16	1989	Key residues in the RSKG-50 gene product indicate a serine protease with kallikrein-like cleavage specificity at basic amino acids.	Amino Acids, Basic	113-130	kallikrein 1-related peptidase C3	Rattus norvegicus	20-27
2550051-16	1989	Key residues in the RSKG-50 gene product indicate a serine protease with kallikrein-like cleavage specificity at basic amino acids.	Amino Acids, Basic	113-130	kallikrein 1-related peptidase C8	Rattus norvegicus	52-67
2780421-2	1989	VIP and PHI both contain paired basic amino acid residues at which posttranslational cleavage of these peptides might occur.	Amino Acids, Basic	32-48	vasoactive intestinal peptide	Rattus norvegicus	0-3
2784437-1	1989	Carboxypeptidase H is a putative post-translational processing enzyme which removes basic amino acid residues from intermediates during protein hormone biosynthesis.	Amino Acids, Basic	84-100	carboxypeptidase E	Rattus norvegicus	0-18
2494191-9	1989	These results demonstrate that cytochrome P450, which is normally localized on the cytoplasmic side of the membrane, can be entirely translocated to the luminal side when two basic amino acids precede the hydrophobic core of its NH2-terminal insertion/stop-transfer signal.	Amino Acids, Basic	175-192	cytochrome P-450	Oryctolagus cuniculus	31-46
2494702-4	1989	Dimerization is required for DNA binding and results in the appropriate juxtaposition of basic amino acid regions from Fos and Jun, both of which are required for association with DNA.	Amino Acids, Basic	89-105	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	119-122
2524646-6	1989	A cys-3 mutant and a cys-3 temperature-sensitive mutant lead to substitutions of glutamine for basic amino acids within the charged region and thus may alter DNA-binding properties of the cys-3 protein.	Amino Acids, Basic	95-112	cystathionine gamma-lyase CYS3	Saccharomyces cerevisiae S288C	2-7
2524646-6	1989	A cys-3 mutant and a cys-3 temperature-sensitive mutant lead to substitutions of glutamine for basic amino acids within the charged region and thus may alter DNA-binding properties of the cys-3 protein.	Amino Acids, Basic	95-112	cystathionine gamma-lyase CYS3	Saccharomyces cerevisiae S288C	21-26
2524646-6	1989	A cys-3 mutant and a cys-3 temperature-sensitive mutant lead to substitutions of glutamine for basic amino acids within the charged region and thus may alter DNA-binding properties of the cys-3 protein.	Amino Acids, Basic	95-112	cystathionine gamma-lyase CYS3	Saccharomyces cerevisiae S288C	21-26
2536749-2	1989	Proopiomelanocortin (POMC) is a neuroendocrine precursor protein which is processed at paired basic amino acids in a tissue-specific manner.	Amino Acids, Basic	94-111	proopiomelanocortin	Rattus norvegicus	0-19
2536749-2	1989	Proopiomelanocortin (POMC) is a neuroendocrine precursor protein which is processed at paired basic amino acids in a tissue-specific manner.	Amino Acids, Basic	94-111	proopiomelanocortin	Rattus norvegicus	21-25
2497053-6	1989	A truncated Fra-1 protein that contains the leucine zipper region but not an adjacent basic amino acid domain, complexes with Jun in vitro but fails to bind AP-1 oligonucleotides.	Amino Acids, Basic	86-102	FOS like 1, AP-1 transcription factor subunit	Rattus norvegicus	12-17
2497688-2	1989	With an oligonucleotide probe directed against a presumptive TRH progenitor sequence, a frog skin cDNA library was screened and a clone identified coding for a peptide of 123 amino acids containing four copies of the TRH progenitor sequence (Gln-His-Pro-Gly) flanked by paired basic amino acid residues.	Amino Acids, Basic	277-293	thyrotropin releasing hormone	Rattus norvegicus	217-220
2648696-1	1989	The KEX2 protease (product of the KEX2 gene) functions late in the secretory pathway of Saccharomyces cerevisiae by cleaving the polypeptide chains of prepro-killer toxin and prepro-alpha-factor at paired basic amino acid residues.	Amino Acids, Basic	205-221	kexin KEX2	Saccharomyces cerevisiae S288C	4-8
2648696-1	1989	The KEX2 protease (product of the KEX2 gene) functions late in the secretory pathway of Saccharomyces cerevisiae by cleaving the polypeptide chains of prepro-killer toxin and prepro-alpha-factor at paired basic amino acid residues.	Amino Acids, Basic	205-221	kexin KEX2	Saccharomyces cerevisiae S288C	34-38
3233203-0	1988	Role of basic amino acids in the interaction of bindin with sulfated fucans.	Amino Acids, Basic	8-25	bindin	Strongylocentrotus purpuratus	48-54
2849988-8	1988	Sequence comparisons of RSKG-7, RSKG-3, and other kallikrein-related enzymes reveal the key amino acid residues needed for both serine protease activity (His/Asp/Ser) and kallikrein-like cleavage specificity at basic amino acids.	Amino Acids, Basic	211-228	kallikrein 1	Rattus norvegicus	24-30
2849988-8	1988	Sequence comparisons of RSKG-7, RSKG-3, and other kallikrein-related enzymes reveal the key amino acid residues needed for both serine protease activity (His/Asp/Ser) and kallikrein-like cleavage specificity at basic amino acids.	Amino Acids, Basic	211-228	kallikrein 1-related peptidase C12	Rattus norvegicus	32-38
2849988-8	1988	Sequence comparisons of RSKG-7, RSKG-3, and other kallikrein-related enzymes reveal the key amino acid residues needed for both serine protease activity (His/Asp/Ser) and kallikrein-like cleavage specificity at basic amino acids.	Amino Acids, Basic	211-228	kallikrein 1-related peptidase C8	Rattus norvegicus	128-143
3333846-3	1987	Hydrophilic insulins, more positively charged than human insulin at neutral pH, have been prepared by substitution with basic amino acids at the termini of the B-chain and by blocking the C-terminal carboxyl group of the B-chain.	Amino Acids, Basic	120-137	insulin	Homo sapiens	12-19
3041989-2	1988	Comparison of reaction rates in trypsin-catalysed transamidation of this compound and porcine insulin with threonine ether ester showed that this reaction is determined only by conformational effects and structural features of amino acids leaving from and entering into B30, not by the structure and the pKa value of the basic amino acid in B29.	Amino Acids, Basic	321-337	insulin	Homo sapiens	94-101
3678488-3	1987	This peptide, denoted GAWK, could originate from chromogranin B following specific cleavage at the basic amino acids flanking both termini of GAWK.	Amino Acids, Basic	99-116	chromogranin B	Homo sapiens	49-63
3678488-5	1987	Here again, this peptide, occupying positions 597-653 and located at the COOH-terminal region of chromogranin B, could derive from specific processing at basic amino acids, Arg-Lys-Lys, present at positions 594-596.	Amino Acids, Basic	154-171	chromogranin B	Homo sapiens	97-111
3153462-9	1987	The forms of PAM purified from bovine neurointermediate pituitary may be generated by endoproteolytic cleavage at a subset of the 10 pairs of basic amino acids in the precursor.	Amino Acids, Basic	142-159	peptidylglycine alpha-amidating monooxygenase	Bos taurus	13-16
3436955-0	1987	Site-directed mutagenesis of basic amino acid residues in the extension peptide of P-450(SCC) precursor: effects on the import of the precursor into mitochondria.	Amino Acids, Basic	29-45	serpin family B member 3	Homo sapiens	83-93
3041026-8	1987	The amino acid sequence of the presumptive polypeptide encoded by ORF3, a 33.6-kDa molecule, exhibited an unusual, clustered 16-fold repeat of the dipeptide arginine-serine in a protein that showed an overall preponderance of basic amino acids.	Amino Acids, Basic	226-243	ankyrin repeat, SAM and basic leucine zipper domain containing 1	Homo sapiens	66-70
3146347-2	1988	Since thrombin has a primary specificity for basic amino acids, each of the three basic residues and the histidine in hirudin were mutated to glutamine.	Amino Acids, Basic	45-62	coagulation factor II, thrombin	Homo sapiens	6-14
2969057-9	1988	NLS1 and NLS2 contain basic amino acids and are similar to previously defined nuclear signal sequences of other proteins.	Amino Acids, Basic	22-39	phosphoserine aminotransferase 1	Homo sapiens	9-13
3211139-5	1988	In the small-cell lung cancer cell line, GRP1-27 was cleaved as expected from the endogenous prohormone at a pair of basic amino acids (29 and 30) and alpha-amidated at its C-terminal methionine; however, a number of novel peptides were generated by additional cleavages in the pro-GRP31-125 domain.	Amino Acids, Basic	117-134	cytohesin 3	Homo sapiens	41-45
3136859-1	1988	The sequence of rat hypothalamic pro-thyrotropin releasing hormone, deduced by sequencing of cDNA, in addition to 5 TRH progenitor sequences contains leader, trailer and 4 intervening sequences separated by paired basic amino acid sequences.	Amino Acids, Basic	214-230	thyrotropin releasing hormone	Rattus norvegicus	33-66
3127097-5	1988	Exposure of rIFN-gamma to cell extracts resulted in a shift in its pI from 8 to 6, presumably due to proteolytic cleavage of carboxy-terminal basic amino acids.	Amino Acids, Basic	142-159	interferon gamma	Rattus norvegicus	12-22
3355557-5	1988	From the nucleotide sequence, MK1 gene was predicted to code a polypeptide of molecular weight 9,971, which was rich in basic amino acids.	Amino Acids, Basic	120-137	potassium voltage-gated channel, shaker-related subfamily, member 1	Mus musculus	30-33
2897826-2	1988	The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules; (c) CPE is able to remove C-terminal basic amino acids from a variety of synthetic peptides without further hydrolyzing the peptide; (d) CPE is active at pH 5.6, the internal pH of secretory granules.	Amino Acids, Basic	271-288	carboxypeptidase E	Bos taurus	30-33
2897826-2	1988	The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules; (c) CPE is able to remove C-terminal basic amino acids from a variety of synthetic peptides without further hydrolyzing the peptide; (d) CPE is active at pH 5.6, the internal pH of secretory granules.	Amino Acids, Basic	271-288	carboxypeptidase E	Bos taurus	163-166
2897826-2	1988	The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules; (c) CPE is able to remove C-terminal basic amino acids from a variety of synthetic peptides without further hydrolyzing the peptide; (d) CPE is active at pH 5.6, the internal pH of secretory granules.	Amino Acids, Basic	271-288	carboxypeptidase E	Bos taurus	163-166
2897826-2	1988	The evidence for this is: (a) CPE is present in tissues that produce bioactive peptides; (b) in tissues that have been subjected to subcellular fractionation, the CPE activity is associated with peptide-containing secretory granules; (c) CPE is able to remove C-terminal basic amino acids from a variety of synthetic peptides without further hydrolyzing the peptide; (d) CPE is active at pH 5.6, the internal pH of secretory granules.	Amino Acids, Basic	271-288	carboxypeptidase E	Bos taurus	163-166
3683386-8	1987	Thus, the tsBN51 protein consists of periodic repetitive clusters of acidic and basic amino acids.	Amino Acids, Basic	80-97	RNA polymerase III subunit D	Homo sapiens	10-16
3472221-2	1987	Nucleotide sequence analysis has revealed the primary structure of a 170-amino acid precursor protein that encodes both neurotensin and the neurotensin-like peptide neuromedin N. The peptide-coding domains are located in tandem near the carboxyl terminus of the precursor and are bounded and separated by the paired, basic amino acid residues Lys-Arg.	Amino Acids, Basic	317-333	neurotensin	Canis lupus familiaris	120-131
3472221-2	1987	Nucleotide sequence analysis has revealed the primary structure of a 170-amino acid precursor protein that encodes both neurotensin and the neurotensin-like peptide neuromedin N. The peptide-coding domains are located in tandem near the carboxyl terminus of the precursor and are bounded and separated by the paired, basic amino acid residues Lys-Arg.	Amino Acids, Basic	317-333	neurotensin	Canis lupus familiaris	140-151
3026846-1	1987	Evidence from the inhibition of the IRCM-serine protease 1 cleavage of pro-enkephalin and ACTH at pairs of basic amino acids.	Amino Acids, Basic	107-124	proenkephalin	Bos taurus	71-85
3026846-3	1987	On larger substrates, chromogranin A is a reversible competitive inhibitor of the cleavage at pairs of basic amino acids by IRCM-SP1.	Amino Acids, Basic	103-120	chromogranin A	Bos taurus	22-36
3473966-0	1987	Chromogranin A: the primary structure deduced from cDNA clones reveals the presence of pairs of basic amino acids.	Amino Acids, Basic	96-113	chromogranin A	Homo sapiens	0-14
3439470-4	1987	Analysing this phosphate fraction in the alkaline hydrolysate of RNA- and lipid-free preparations of myosin it was confirmed that phosphate was linked to the basic amino acid residues and their hydrolytic derivatives.	Amino Acids, Basic	158-174	myosin heavy chain 14	Homo sapiens	101-107
6548696-6	1984	Glucagon and the two glucagon-like peptides are flanked in the precursor by pairs of basic amino acids characteristic of the sites that are cleaved during the posttranslational processing of pro-hormones.	Amino Acids, Basic	85-102	glucagon	Rattus norvegicus	0-8
3103606-5	1986	We show that digestion of plasma samples with carboxypeptidase B, which removes C-terminal basic amino acids, before electrophoresis, produces a single, sharp, distinct band for each allotype and allows identification of the biochemical basis of the multiple banding pattern previously observed in C4 phenotype determination.	Amino Acids, Basic	91-108	carboxypeptidase B1	Homo sapiens	46-64
2871191-2	1986	Inhibition of dihydrofolate reductase and folylpolyglutamate synthetase activity and in vitro tumor cell growth by methotrexate and aminopterin analogues containing a basic amino acid side chain.	Amino Acids, Basic	167-183	dihydrofolate reductase	Mus musculus	14-37
2871191-2	1986	Inhibition of dihydrofolate reductase and folylpolyglutamate synthetase activity and in vitro tumor cell growth by methotrexate and aminopterin analogues containing a basic amino acid side chain.	Amino Acids, Basic	167-183	folylpolyglutamyl synthetase	Mus musculus	42-71
3517880-6	1986	Our data on the structure of a gamma-trace variant protein suggests that its gene expresses a polyprotein precursor in which active peptides are flanked by basic amino acid residues that permit cleavage to liberate small internal peptides.	Amino Acids, Basic	156-172	cystatin C	Homo sapiens	31-42
2864927-0	1985	Endopeptidase in human cerebrospinal fluid which cleaves proenkephalin B opioid peptides at consecutive basic amino acids.	Amino Acids, Basic	104-121	prodynorphin	Homo sapiens	57-72
4044551-8	1985	FBA was also similar to SBA in amino acid composition, and contained much less basic amino acids than SBB 1 through 5.	Amino Acids, Basic	79-96	F-box protein 3	Homo sapiens	0-3
2993267-8	1985	These results showed that CANP prefers basic amino acid side chains but its specificity is very restricted.	Amino Acids, Basic	39-55	calpain 1	Homo sapiens	26-30
3888200-8	1985	The fast migrating band corresponds to the rat insulin II position, and the slower corresponds to rat insulin I, which has one more basic amino acid residue in comparison with rat insulin II.	Amino Acids, Basic	132-148	insulin	Homo sapiens	102-109
3925116-1	1985	The two spectrally distinguishable bound forms of 2-(4"-hydroxyphenylazo) benzoic acid (HABA) on bovine serum albumin (BSA), i.e, the azo and hydrazone forms, were suggested to form ion pairs with basic amino acid residues in our previous study.	Amino Acids, Basic	197-213	albumin	Homo sapiens	104-117
6096378-3	1984	The apo-A-II prosegment resembles the propeptides of prohormones and proalbumin: it ends with paired basic amino acids.	Amino Acids, Basic	101-118	apolipoprotein A2	Homo sapiens	4-12
6442339-7	1984	The cleavage site of pro-apoA-II is characterized by two basic amino acid residues Arg-Arg, present also in other known pro-proteins.	Amino Acids, Basic	57-73	apolipoprotein A2	Homo sapiens	25-32
3079917-3	1986	This protein contained five copies of the sequence Gln-His-Pro-Gly flanked by paired basic amino acids and could therefore generate five TRH molecules.	Amino Acids, Basic	85-102	thyrotropin releasing hormone	Rattus norvegicus	137-140
2987247-1	1985	Pro-opiomelanocortin (adrenocorticotropin/endorphin prohormone) is processed to yield active hormones by cleavages at paired basic amino acid residues.	Amino Acids, Basic	125-141	proopiomelanocortin	Bos taurus	0-20
6548696-6	1984	Glucagon and the two glucagon-like peptides are flanked in the precursor by pairs of basic amino acids characteristic of the sites that are cleaved during the posttranslational processing of pro-hormones.	Amino Acids, Basic	85-102	glucagon	Rattus norvegicus	21-29
6144640-4	1984	Their maturation processes are following a highly similar pattern with cleavage of the precursors at sites characterized by the presence of pairs of basic amino acid as noted in 1967-68 for the LPH and the pro-insulin models.	Amino Acids, Basic	149-165	lactase	Homo sapiens	194-197
6195531-3	1983	This new tachykinin sequence is bounded by paired basic amino acids Lys-Arg, which suggests that, like substance P, it can be liberated from the precursor and may serve as an endogenous hormone or neuromediator in mammalian organisms.	Amino Acids, Basic	50-67	tachykinin precursor 1	Homo sapiens	103-114
6688942-3	1983	The proposed sequence reveals a high content of basic amino acids (Arg and Lys) and Leu, is consistent with the amino acid composition, and predicts the correct number of peptides derived from tryptic digests reported for ligandin.	Amino Acids, Basic	48-65	glutathione S-transferase alpha 2	Rattus norvegicus	222-230
6129251-4	1983	The protein sequence predicted by the cDNA shows mouse POMC to consist of 235 amino acids with seven potential tryptic cleavage sites consisting of pairs of basic amino acid residues.	Amino Acids, Basic	157-173	pro-opiomelanocortin-alpha	Mus musculus	55-59
6207529-4	1984	hGRP is flanked at its carboxyl terminus by two basic amino acids, following a glycine used for amidation of the carboxyl-terminal methionine.	Amino Acids, Basic	48-65	gastrin releasing peptide	Homo sapiens	0-4
6432779-4	1984	The deletion of this single basic amino acid residue is sufficient to account for the charge difference between the variant and normal apo-A-I as seen on isoelectric focusing gels.	Amino Acids, Basic	28-44	apolipoprotein A1	Homo sapiens	135-142
6280176-5	1982	Phosphorylated tyrosines in several other proteins resemble of the tyrosine in p60src in that they are located 7 residues to the COOH-terminal side of a basic amino acid and either 4 residues to the COOH-terminal side of, or in close proximity to, a glutamic acid residue.	Amino Acids, Basic	153-169	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	79-85
6761648-4	1982	The sequence of cloned cDNA shows that the preproenkephalin mRNA encodes four copies of met-enkephalin, two copies of met-enkephalin extended sequences and one copy of leu-enkephalin; each copy is flanked by paired basic amino acids which are presumably recognised by the processing protease.	Amino Acids, Basic	215-232	proenkephalin	Homo sapiens	43-59
6750606-1	1982	Carboxypeptidase N (kininase I, arginine carboxypeptidase; EC 3.4.17.3) cleaves COOH-terminal basic amino acids of kinins, anaphylatoxins, and other peptides.	Amino Acids, Basic	94-111	carboxypeptidase N subunit 1	Homo sapiens	20-30
6750606-1	1982	Carboxypeptidase N (kininase I, arginine carboxypeptidase; EC 3.4.17.3) cleaves COOH-terminal basic amino acids of kinins, anaphylatoxins, and other peptides.	Amino Acids, Basic	94-111	carboxypeptidase N subunit 1	Homo sapiens	32-57
6178843-7	1982	EIAV p11 apparently focused at a pI of greater than 10, reflecting its high content of basic amino acids.	Amino Acids, Basic	87-104	endonuclease, poly(U) specific	Homo sapiens	5-8
6283170-5	1982	Internal cleavage of the env precursor to generate gp70 and p15E occurs immediately adjacent to several basic amino acids at the carboxyl terminus of gp70.	Amino Acids, Basic	104-121	endogenous retrovirus group K member 20	Homo sapiens	25-28
6283170-5	1982	Internal cleavage of the env precursor to generate gp70 and p15E occurs immediately adjacent to several basic amino acids at the carboxyl terminus of gp70.	Amino Acids, Basic	104-121	embigin	Homo sapiens	150-154
7041967-0	1982	Substrate specificity of an adenohypophyseal endopeptidase capable of hydrolyzing luteinizing hormone-releasing hormone: preferential cleavage of peptide bones involving the carboxyl terminus of hydrophobic and basic amino acids.	Amino Acids, Basic	211-228	gonadotropin releasing hormone 1	Homo sapiens	82-119
7041967-2	1982	While trypsin and chymotrypsin inhibitors from plants and animals are without any effect, many microbial protease inhibitors and synthetic peptides containing hydrophobic and basic amino acids inhibit the degradation of radiolabeled LH-RH by this enzyme.	Amino Acids, Basic	175-192	gonadotropin releasing hormone 1	Homo sapiens	233-238
7074985-8	1982	Other hypotensive peptides such as neurotensin, xenopsin and VIP which also possess adjacent basic amino acids but are not known to be vasoactive were also hypotensive in our assays.	Amino Acids, Basic	93-110	vasoactive intestinal peptide	Bos taurus	61-64
7295676-2	1981	This half-molecule fragment (CaM72-148) contains 11 of calmodulin"s 15 basic amino acids (including one trimethyllysine) and demonstrates a higher isoelectric point.	Amino Acids, Basic	71-88	calmodulin 1	Homo sapiens	55-65
6271191-3	1981	Purified MP-1 and MP-2 contained an above average content of hydrophobic amino acids, while MP-2 and MP-3 had an above average content of acid and/or amide amino acids and a below average content of basic amino acids.	Amino Acids, Basic	199-216	tryptase pseudogene 1	Homo sapiens	92-105
6264603-2	1981	Analyses of the nucleotide sequences of cloned complementary DNA"s comprising the entire coding sequence of the messenger RNA revealed that calcitonin is flanked at both its amino and carboxyl termini by peptide extensions linked to the hormone by short sequences of basic amino acids.	Amino Acids, Basic	267-284	calcitonin related polypeptide alpha	Homo sapiens	140-150
6167109-4	1981	In human skin, VIP was more potent than the other neuropeptides and had roughly the same potency as substance P. The two adjacent basic amino-acid residues and the amide substitution of the terminal C-group of VIP, in addition to its strong net basic charge, may explain its potency as a histamine releaser.	Amino Acids, Basic	130-146	vasoactive intestinal peptide	Homo sapiens	15-18
6801083-8	1981	These results may be explained by swelling of the trimellityl-human serum albumin molecule due to the additional negative charges of the trimellityl carboxyl groups and loss of positive charges at basic amino acid binding sites of trimellityl.	Amino Acids, Basic	197-213	albumin	Homo sapiens	68-81
6801083-9	1981	The lesser changes in diphenylmethane diisocyanate-human serum albumin may result from only the delection of positive charges on basic amino acids of human serum albumin since diphenylmethane diisocyanate contributes no additional charge.	Amino Acids, Basic	129-146	albumin	Homo sapiens	57-70
6801083-9	1981	The lesser changes in diphenylmethane diisocyanate-human serum albumin may result from only the delection of positive charges on basic amino acids of human serum albumin since diphenylmethane diisocyanate contributes no additional charge.	Amino Acids, Basic	129-146	albumin	Homo sapiens	156-169
7237450-0	1981	Improved antitumor activity of basic amino acid and dipeptide derivatives of daunorubicin on EL4 leukemia cells in mice.	Amino Acids, Basic	31-47	epilepsy 4	Mus musculus	93-96
196085-5	1977	In contrast, the carrier mediated transport of basic amino acids is neither inhibited by this mercurial agent nor accelerated by insulin.	Amino Acids, Basic	47-64	insulin	Homo sapiens	129-136
7011318-5	1980	The 2-naphthylamide derivatives of neutral and basic amino acids were also hydrolysed by aminopeptidase A, but at rates about two orders of magnitude lower, and Ca2+ was inhibitory.	Amino Acids, Basic	47-64	alanyl aminopeptidase, membrane	Sus scrofa	89-103
719151-1	1978	The paper treats of the correlations between the position geometry of the extended successions of the residue of basic amino acids and those nonbearing any positive charge along the polypeptide chains of the histone H2A, H2B, H3, H4 molecules forming nucleosomes protein frame.	Amino Acids, Basic	113-130	H2A clustered histone 18	Homo sapiens	216-219
719151-1	1978	The paper treats of the correlations between the position geometry of the extended successions of the residue of basic amino acids and those nonbearing any positive charge along the polypeptide chains of the histone H2A, H2B, H3, H4 molecules forming nucleosomes protein frame.	Amino Acids, Basic	113-130	H2B clustered histone 21	Homo sapiens	221-228
6933496-3	1980	Two basic amino acids precede and three basic amino acids follow the hormone sequence, suggesting that calcitonin is generated by the proteolytic cleavage of a larger precursor in a manner analogous to that of other small polypeptide hormones.	Amino Acids, Basic	4-21	calcitonin-related polypeptide alpha	Rattus norvegicus	103-113
6933496-3	1980	Two basic amino acids precede and three basic amino acids follow the hormone sequence, suggesting that calcitonin is generated by the proteolytic cleavage of a larger precursor in a manner analogous to that of other small polypeptide hormones.	Amino Acids, Basic	40-57	calcitonin-related polypeptide alpha	Rattus norvegicus	103-113
7013400-1	1980	Purified bovine cathepsin B, when incubated with isolated rat islets of Langerhans, completely converts proinsulin to insulin as demonstrated by the incorporation of 14C-leucine into islet proteins, releasing lysine as the only basic amino acid.	Amino Acids, Basic	228-244	cathepsin B	Bos taurus	16-27
6777326-8	1980	The functional role of the basic amino acid residues for the cosubstrate binding by the NADPH-cytochrome P450 reductase cannot be established therefore by the modification experiments described.	Amino Acids, Basic	27-43	cytochrome p450 oxidoreductase	Homo sapiens	88-119
6773464-5	1980	Basic structural features of the hinge region of the IgD molecule (extreme susceptibility to proteolytic enzymes, presence of basic amino acids near its COOH-terminus) have been found for the IR-731 molecule.	Amino Acids, Basic	126-143	Ig delta chain C region	Rattus norvegicus	53-56
224122-4	1979	Dose-dependent inhibition was also noted with synthetic proteinase substrates, especially those of chymotrypsin-like specificity, phenylalanine and tryptophan methyl esters (ID50S approximately 1.5 X 10(-4)M), as compared to derivatives of basic amino acids, arginine and acetyl-lysine methyl esters, which caused negligible inhibition at 10(-3M.	Amino Acids, Basic	240-257	endogenous retrovirus group K member 18	Homo sapiens	56-66
667683-0	1978	Effect of the basic amino-acid side chain length and the penultimate residue on the hydrolysis of benzoldipeptides by carboxypeptidase B.	Amino Acids, Basic	14-30	carboxypeptidase B1	Homo sapiens	118-136
616370-4	1977	High intraluminal concentrations of basic amino acids inhibited the cellular uptake of lysozyme, while neutral amino acids had no effect.	Amino Acids, Basic	36-53	lysozyme	Homo sapiens	87-95
61030-0	1976	Phosphorylation on basic amino acids in myelin basic protein.	Amino Acids, Basic	19-36	myelin basic protein	Homo sapiens	40-60
193558-3	1977	The amino acid composition shows that protein C-14 has an acidic:basic amino acid ratio of 1.8.	Amino Acids, Basic	65-81	anti-Mullerian hormone receptor type 2	Rattus norvegicus	46-50
4589953-0	1974	Inhibition of thymidine and basic amino acid metabolism in P1798 lymphosarcoma by L-asparaginase.	Amino Acids, Basic	28-44	asparaginase and isoaspartyl peptidase 1	Homo sapiens	82-96
1101948-2	1975	The methyl group of [Me-3H] methionine is incorporated into basic amino acid residues with the formation of Nepsilon-monomethyllysine, Nepsilon-dimethyllysine, Nepsilon-trimethyllysine, 3-methylhistidine, NG-monomethylarginine, and NG-dimethylarginine which are isolated from acid hydrolysates of purified myosin, and of proteins from polysomes and from the cytosol of the cultured muscle cells.	Amino Acids, Basic	60-76	myosin, heavy chain 15	Gallus gallus	306-312
1122293-8	1975	Of the basic amino acids platelet factor 4 (molecular weight 27 100) contained 5.97% arginine, 3.18% histidine, and 12.31% lysine compared to protamine sulphate with 64.2% arginine, 0.6% lysine and no histidine.	Amino Acids, Basic	7-24	platelet factor 4	Homo sapiens	25-42
5725439-1	1968	I. Biochemical demonstration of an aminopeptidase in rat skin specific for N-Terminal basic amino acids (Aminopeptidase B).	Amino Acids, Basic	86-103	arginyl aminopeptidase	Rattus norvegicus	105-121
4342281-0	1972	Studies on the role of basic amino acid residues of ACTH peptide in steroidogenesis by isolated adrenal cells.	Amino Acids, Basic	23-39	proopiomelanocortin	Homo sapiens	52-56
4974308-22	1969	It is believed that the substitution of a strongly basic amino acid with a neutral hydroxy acid may result in considerable conformational changes in the N-terminal disulfide knot of fibrinogen which might affect the "active site" for polymerization.	Amino Acids, Basic	51-67	fibrinogen beta chain	Homo sapiens	182-192
5705291-0	1968	A modified two-column procedure for the analysis of the basic amino acids found in elastin, collagen and antibiotics.	Amino Acids, Basic	56-73	elastin	Homo sapiens	83-90
33466626-7	2021	FN3K is a unique protein that mediates deglycation by phosphorylating basic amino acids lysine and arginine in various proteins such as Nrf2.	Amino Acids, Basic	70-87	fructosamine 3 kinase	Homo sapiens	0-4
14953937-0	1952	[New method of determination of basic amino acids in lysozyme].	Amino Acids, Basic	32-49	lysozyme	Homo sapiens	53-61
33989998-4	2021	The present study aims to study the effect of charge-specific modification of basic amino acids (Lys, Arg) and guanidination on the interaction of insulin with its receptor using molecular modelling.	Amino Acids, Basic	78-95	insulin	Homo sapiens	147-154
33566051-6	2021	The highest adsorption energy of Pd2+ cations on GOx was found during their interaction with the side chains of basic amino acids and methionine.	Amino Acids, Basic	112-129	hydroxyacid oxidase 1	Homo sapiens	49-52
33786368-4	2021	The simulations revealed that the SGDs: 1) develop multivalent binding with polybasic regions within and outside of the V3 loop on glycoprotein 120 (gp120) for HIV-1, and consecutively bind with multiple gp120 subunits, and 2) interact with basic amino acids in both the angiotensin-converting enzyme 2 (ACE2) and HSPG binding regions of the Receptor Binding Domain (RBD) from SARS-CoV-2.	Amino Acids, Basic	241-258	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	149-154
33786368-4	2021	The simulations revealed that the SGDs: 1) develop multivalent binding with polybasic regions within and outside of the V3 loop on glycoprotein 120 (gp120) for HIV-1, and consecutively bind with multiple gp120 subunits, and 2) interact with basic amino acids in both the angiotensin-converting enzyme 2 (ACE2) and HSPG binding regions of the Receptor Binding Domain (RBD) from SARS-CoV-2.	Amino Acids, Basic	241-258	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	204-209
33189720-0	2021	Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids in Schizosaccharomyces pombe.	Amino Acids, Basic	64-81	Stm1p	Saccharomyces cerevisiae S288C	0-4
33189720-6	2021	These results suggest that Stm1 is a vacuolar PQ-loop protein involved in the transport of basic amino acids across the vacuolar membrane.	Amino Acids, Basic	91-108	Stm1p	Saccharomyces cerevisiae S288C	27-31
32638513-6	2021	Using site-directed mutagenesis of the N-terminal domain of Dna2, we discovered that five consecutive basic amino acid residues were essential for the ability of Dna2 to bind hairpin DNA in vitro.	Amino Acids, Basic	102-118	DNA replication helicase/nuclease 2	Homo sapiens	60-64
32638513-6	2021	Using site-directed mutagenesis of the N-terminal domain of Dna2, we discovered that five consecutive basic amino acid residues were essential for the ability of Dna2 to bind hairpin DNA in vitro.	Amino Acids, Basic	102-118	DNA replication helicase/nuclease 2	Homo sapiens	162-166
33624780-1	2021	In Saccharomyces cerevisiae, Avt4 exports neutral and basic amino acids from vacuoles.	Amino Acids, Basic	54-71	Avt4p	Saccharomyces cerevisiae S288C	29-33
33671652-4	2021	Peptides of five to six amino acids with a basic amnio acid in the head, acidic amnio acid in the neck, hydrophobicity group in the middle, and basic amino acids in the tail showed higher binding to COVID-19 virus main protease (Mpro), while those with basic amino acids and acidic amino acids in the two sides and aromatic amino acids in the middle might have stronger interaction with COVID-19 virus RNA-dependent RNA polymerase (RdRp).	Amino Acids, Basic	144-161	NEWENTRY	Severe acute respiratory syndrome-related coronavirus	229-233
33671652-4	2021	Peptides of five to six amino acids with a basic amnio acid in the head, acidic amnio acid in the neck, hydrophobicity group in the middle, and basic amino acids in the tail showed higher binding to COVID-19 virus main protease (Mpro), while those with basic amino acids and acidic amino acids in the two sides and aromatic amino acids in the middle might have stronger interaction with COVID-19 virus RNA-dependent RNA polymerase (RdRp).	Amino Acids, Basic	144-161	ORF1a polyprotein;ORF1ab polyprotein	Severe acute respiratory syndrome coronavirus 2	432-436
33466626-7	2021	FN3K is a unique protein that mediates deglycation by phosphorylating basic amino acids lysine and arginine in various proteins such as Nrf2.	Amino Acids, Basic	70-87	NFE2 like bZIP transcription factor 2	Homo sapiens	136-140
33428938-1	2021	The G protein-coupled receptor GPRC6A regulates various physiological processes in response to its interaction with multiple ligands such as extracellular basic amino acids, divalent cations, testosterone, and the uncarboxylated form of osteocalcin (GluOC).	Amino Acids, Basic	155-172	G protein-coupled receptor, family C, group 6, member A	Mus musculus	31-37
32661559-5	2021	These chaperones are activated by HOCl through thiol oxidation (Hsp33) or N-chlorination of basic amino acid side-chains (RidA and CnoX) and contribute to bacterial survival during HOCl stress.	Amino Acids, Basic	92-108	ecto-NOX disulfide-thiol exchanger 1	Homo sapiens	131-135
32546608-0	2020	Erratum for Sun et al., "Basic Amino Acid Substitution at Residue 367 of the Envelope Protein of Tembusu Virus Plays a Critical Role in Pathogenesis".	Amino Acids, Basic	25-41	endogenous retrovirus group K member 6, envelope	Homo sapiens	77-93
33251463-5	2020	We show that electrostatic interactions with the negatively charged plane substantially modify probabilities of different protonation states of lysozyme and shift protonation equilibria of both acidic and basic amino acid side chains toward higher pH values.	Amino Acids, Basic	205-221	lysozyme	Homo sapiens	144-152
32662226-3	2020	Following the amino acid sequence of the active center in PDI, basic amino acid conjugates of 1,2-diselenan-4-amine ( 1 ), which show oxidoreductase- and isomerase-like activities for SS-relating reactions, were designed as a novel PDI model compound.	Amino Acids, Basic	63-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	58-61
32662226-3	2020	Following the amino acid sequence of the active center in PDI, basic amino acid conjugates of 1,2-diselenan-4-amine ( 1 ), which show oxidoreductase- and isomerase-like activities for SS-relating reactions, were designed as a novel PDI model compound.	Amino Acids, Basic	63-79	prolyl 4-hydroxylase subunit beta	Homo sapiens	232-235
32817565-5	2020	Here we report the cryogenic electron microscopy structure of the neutral and basic amino acid transport complex (b[0,+]AT1-rBAT) which reveals a heterotetrameric protein assembly composed of two heavy and light chain subunits, respectively.	Amino Acids, Basic	78-94	solute carrier family 33 member 1	Homo sapiens	120-123
32817565-5	2020	Here we report the cryogenic electron microscopy structure of the neutral and basic amino acid transport complex (b[0,+]AT1-rBAT) which reveals a heterotetrameric protein assembly composed of two heavy and light chain subunits, respectively.	Amino Acids, Basic	78-94	bile acid CoA:amino acid N-acyltransferase	Rattus norvegicus	124-128
32873993-7	2020	Furthermore, we were able to determine that a basic amino acid cluster exists in the C-terminal region of Rab35 and that Rab35 localization shifts to the Golgi membrane when the number of basic amino acids in this region is reduced.	Amino Acids, Basic	46-62	RAB35, member RAS oncogene family	Mus musculus	106-111
32873993-7	2020	Furthermore, we were able to determine that a basic amino acid cluster exists in the C-terminal region of Rab35 and that Rab35 localization shifts to the Golgi membrane when the number of basic amino acids in this region is reduced.	Amino Acids, Basic	188-205	RAB35, member RAS oncogene family	Mus musculus	121-126
32592613-2	2020	The C-terminal domain of insulin-like growth factor-binding protein-3 (IGFBP-3) is known to contain an 18-basic amino acid motif capable of interacting with either humanin (HN) or hyaluronan (HA).	Amino Acids, Basic	106-122	insulin like growth factor binding protein 3	Homo sapiens	25-69
32592613-2	2020	The C-terminal domain of insulin-like growth factor-binding protein-3 (IGFBP-3) is known to contain an 18-basic amino acid motif capable of interacting with either humanin (HN) or hyaluronan (HA).	Amino Acids, Basic	106-122	insulin like growth factor binding protein 3	Homo sapiens	71-78
31882261-4	2021	Certain Siglecs (Siglec-14, -15, -16 and -H) containing no intracellular domain carry certain basic amino acid in transmembrane domain coupled with immunoreceptor tyrosine-based activating motif for cell activation.	Amino Acids, Basic	94-110	sialic acid binding Ig like lectin 14	Homo sapiens	17-44
32905794-5	2020	This inhibition is attributed to an interaction of polyP with a basic amino acid stretch on the surface of the receptor binding domain of S-protein.	Amino Acids, Basic	64-80	vitronectin	Homo sapiens	138-147
33051007-4	2020	Conversely, renin was shown to have increased levels of basic amino acids.	Amino Acids, Basic	56-73	renin	Homo sapiens	12-17
33254528-4	2020	The proteins commonly found in neutrophil extracellular traps such as CCDC25, myeloperoxidase (MPO), histone H3, peptidylarginine deiminase 4 (PAD4) possess basic amino acid content at about 20.2%, 12.8%, 24.3% and 13.0% respectively, which attracts anions such as chloride.	Amino Acids, Basic	157-173	coiled-coil domain containing 25	Homo sapiens	70-76
33254528-4	2020	The proteins commonly found in neutrophil extracellular traps such as CCDC25, myeloperoxidase (MPO), histone H3, peptidylarginine deiminase 4 (PAD4) possess basic amino acid content at about 20.2%, 12.8%, 24.3% and 13.0% respectively, which attracts anions such as chloride.	Amino Acids, Basic	157-173	myeloperoxidase	Homo sapiens	78-93
33254528-4	2020	The proteins commonly found in neutrophil extracellular traps such as CCDC25, myeloperoxidase (MPO), histone H3, peptidylarginine deiminase 4 (PAD4) possess basic amino acid content at about 20.2%, 12.8%, 24.3% and 13.0% respectively, which attracts anions such as chloride.	Amino Acids, Basic	157-173	myeloperoxidase	Homo sapiens	95-98
33254528-4	2020	The proteins commonly found in neutrophil extracellular traps such as CCDC25, myeloperoxidase (MPO), histone H3, peptidylarginine deiminase 4 (PAD4) possess basic amino acid content at about 20.2%, 12.8%, 24.3% and 13.0% respectively, which attracts anions such as chloride.	Amino Acids, Basic	157-173	peptidyl arginine deiminase 4	Homo sapiens	113-141
33254528-4	2020	The proteins commonly found in neutrophil extracellular traps such as CCDC25, myeloperoxidase (MPO), histone H3, peptidylarginine deiminase 4 (PAD4) possess basic amino acid content at about 20.2%, 12.8%, 24.3% and 13.0% respectively, which attracts anions such as chloride.	Amino Acids, Basic	157-173	peptidyl arginine deiminase 4	Homo sapiens	143-147
33254528-5	2020	The striking 20.2% basic amino acid content in CCDC25 is similar to that of typical oncoproteins.	Amino Acids, Basic	19-35	coiled-coil domain containing 25	Homo sapiens	47-53
33211253-0	2020	Basic Amino Acids Within the Juxtamembrane Domain of the Epidermal Growth Factor Receptor Regulate Receptor Dimerization and Auto-phosphorylation.	Amino Acids, Basic	0-17	epidermal growth factor receptor	Homo sapiens	57-89
32662226-0	2020	Basic amino acid conjugates of 1,2-diselenan-4-amine with protein disulfide isomerase-like functions as a manipulator of protein quality control.	Amino Acids, Basic	0-16	prolyl 4-hydroxylase subunit beta	Homo sapiens	58-85
32638018-8	2020	Furthermore, we discovered that other S protein proteases, CTSL (cathepsin L) and FURIN (furin, paired basic amino acid cleaving enzyme), were expressed in the adult heart at a similar level to that in the lung, which may compensate for TMPRSS2, mediating cardiac involvement in COVID-19.	Amino Acids, Basic	103-119	furin, paired basic amino acid cleaving enzyme	Homo sapiens	82-87
32638018-8	2020	Furthermore, we discovered that other S protein proteases, CTSL (cathepsin L) and FURIN (furin, paired basic amino acid cleaving enzyme), were expressed in the adult heart at a similar level to that in the lung, which may compensate for TMPRSS2, mediating cardiac involvement in COVID-19.	Amino Acids, Basic	103-119	furin, paired basic amino acid cleaving enzyme	Homo sapiens	89-94
32605194-4	2020	Our analyses speculate that the efficient replication and transmission of SARS-CoV-2 might be due to the high-density basic amino acid residues, preferably positioned in close proximity at both the furin-like cleavage sites (S1/S2 and S2") within the spike protein.	Amino Acids, Basic	118-134	furin, paired basic amino acid cleaving enzyme	Homo sapiens	198-203
32605194-4	2020	Our analyses speculate that the efficient replication and transmission of SARS-CoV-2 might be due to the high-density basic amino acid residues, preferably positioned in close proximity at both the furin-like cleavage sites (S1/S2 and S2") within the spike protein.	Amino Acids, Basic	118-134	surface glycoprotein	Severe acute respiratory syndrome coronavirus 2	251-256
31505788-10	2019	A specific domain of basic amino acid residues (R526/R531/K532/R535) present at this TRPM6 domain has been identified as crucial to maintain non-covalent interactions with the ligands.	Amino Acids, Basic	21-37	transient receptor potential cation channel subfamily M member 6	Homo sapiens	85-90
32236862-1	2020	Aminopeptidase B (APB, EC 3.4.11.6) preferentially hydrolyzes basic amino acids of synthetic substrates and requires a physiological concentration of chloride anions for optimal activity.	Amino Acids, Basic	62-79	arginyl aminopeptidase	Homo sapiens	0-16
32236862-1	2020	Aminopeptidase B (APB, EC 3.4.11.6) preferentially hydrolyzes basic amino acids of synthetic substrates and requires a physiological concentration of chloride anions for optimal activity.	Amino Acids, Basic	62-79	arginyl aminopeptidase	Homo sapiens	18-21
32481593-6	2020	Replacement of the acidic exosite 1 residues of KLK1 with basic amino acids as in thrombin resulted in accelerated inhibition.	Amino Acids, Basic	58-75	kallikrein 1	Homo sapiens	48-52
32481593-6	2020	Replacement of the acidic exosite 1 residues of KLK1 with basic amino acids as in thrombin resulted in accelerated inhibition.	Amino Acids, Basic	58-75	coagulation factor II, thrombin	Homo sapiens	82-90
32242892-0	2020	Interaction of the neutral amino acid transporter ASCT2 with basic amino acids.	Amino Acids, Basic	61-78	solute carrier family 1 member 5	Homo sapiens	50-55
32242892-4	2020	Therefore, we tested whether basic amino acids with side chains shorter than lysine can interact with the ASCT2 binding site.	Amino Acids, Basic	29-46	solute carrier family 1 member 5	Homo sapiens	106-111
32024774-0	2020	Basic Amino Acid Substitution at Residue 367 of the Envelope Protein of Tembusu Virus Plays a Critical Role in Pathogenesis.	Amino Acids, Basic	0-16	endogenous retrovirus group K member 6, envelope	Homo sapiens	52-68
31794784-4	2020	Electrostatic interactions can be generated between the highly sulphated HS region and specific basic amino acid residues in the IFN-gamma structure, thereby detaining IFN-gamma on the cell surface, and the concentration of IFN-gamma on the cell surface is thus, changed.	Amino Acids, Basic	96-112	interferon gamma	Homo sapiens	129-138
31794784-4	2020	Electrostatic interactions can be generated between the highly sulphated HS region and specific basic amino acid residues in the IFN-gamma structure, thereby detaining IFN-gamma on the cell surface, and the concentration of IFN-gamma on the cell surface is thus, changed.	Amino Acids, Basic	96-112	interferon gamma	Homo sapiens	168-177
31794784-4	2020	Electrostatic interactions can be generated between the highly sulphated HS region and specific basic amino acid residues in the IFN-gamma structure, thereby detaining IFN-gamma on the cell surface, and the concentration of IFN-gamma on the cell surface is thus, changed.	Amino Acids, Basic	96-112	interferon gamma	Homo sapiens	168-177
31348608-3	2020	The lysine-arginine-ornithine binding protein (LAO) is a PBP of 238 residues that binds the basic amino acids l-arginine and l-histidine with nm and mum affinity, respectively.	Amino Acids, Basic	92-109	interleukin 4 induced 1	Homo sapiens	4-45
31348608-3	2020	The lysine-arginine-ornithine binding protein (LAO) is a PBP of 238 residues that binds the basic amino acids l-arginine and l-histidine with nm and mum affinity, respectively.	Amino Acids, Basic	92-109	interleukin 4 induced 1	Homo sapiens	47-50
31348608-3	2020	The lysine-arginine-ornithine binding protein (LAO) is a PBP of 238 residues that binds the basic amino acids l-arginine and l-histidine with nm and mum affinity, respectively.	Amino Acids, Basic	92-109	phosphatidylethanolamine binding protein 1	Homo sapiens	57-60
31326539-1	2019	Plasma membrane transporter SLC6A14 transports all neutral and basic amino acids in a Na/Cl - dependent way and it is up-regulated in many types of cancer.	Amino Acids, Basic	63-80	solute carrier family 6 member 14	Homo sapiens	28-35
30670150-5	2019	The basic amino acids, combined with myristoylation within the N-terminal 20 amino acids of PRMT8, are critical for plasma membrane targeting.	Amino Acids, Basic	4-21	protein arginine methyltransferase 8	Homo sapiens	92-97
31515451-7	2019	Mutagenesis of basic amino acids near the membrane-cytosol interface found 3 regions of ANO1 critical for PI(4,5)P2 regulation that correspond to the same 3 sites identified by MD.	Amino Acids, Basic	15-32	anoctamin 1	Homo sapiens	88-92
32449780-3	2020	The aim of this study was to look for new treatment options for melanoma, by investigating the role of the prohormone convertase Paired basic Amino acid-Cleaving Enzyme 4 (PACE4/PCSK6) in melanoma cell lines and human melanoma tissue.	Amino Acids, Basic	136-152	proprotein convertase subtilisin/kexin type 6	Homo sapiens	172-177
32449780-3	2020	The aim of this study was to look for new treatment options for melanoma, by investigating the role of the prohormone convertase Paired basic Amino acid-Cleaving Enzyme 4 (PACE4/PCSK6) in melanoma cell lines and human melanoma tissue.	Amino Acids, Basic	136-152	proprotein convertase subtilisin/kexin type 6	Homo sapiens	178-183
31023825-4	2019	Modeling of the cytosolic N-terminal domain of Vph1 identified two membrane-oriented sequences that contain clustered basic amino acids.	Amino Acids, Basic	118-135	H(+)-transporting V0 sector ATPase subunit a	Saccharomyces cerevisiae S288C	47-51
30794654-6	2019	These results suggested that the C-terminal part of ghrelin, which has clusters of basic amino acid residues and a BX7B motif, might contribute to the retention of ASB20123 in the extracellular matrix of the growth plate.	Amino Acids, Basic	83-99	ghrelin and obestatin prepropeptide	Rattus norvegicus	52-59
30802433-3	2019	Purified recombinant PRMT7 displays a number of unique enzymatic properties including a substrate preference for arginine residues in R-X-R motifs with additional flanking basic amino acid residues and a temperature optimum well below 37  C. Evidence has been presented for crosstalk between PRMT7 and PRMT5, where methylation of a histone H4 peptide at R17, a PRMT7 substrate, may activate PRMT5 for methylation of R3.	Amino Acids, Basic	172-188	protein arginine methyltransferase 7	Homo sapiens	21-26
30941009-1	2019	Carboxypeptidase E, also known as neurotrophic factor-alpha1 (CPE-NFalpha1), was first discovered as an exopeptidase and is known to work by cleaving C-terminal basic amino acids from prohormone intermediates to produce mature peptide hormones and neuropeptides in the endocrine and central nervous systems, respectively.	Amino Acids, Basic	161-178	carboxypeptidase E	Homo sapiens	0-18
30521896-3	2019	For interaction, the three oligopeptides from the HIV gp120 were peptide A 297TRPNNNTRKRIRIQRGPGRA316 with several lysine (K) and arginine (R) in the V3 loop region, peptide B 493PLGVAPTKAKRRVVQREKR511 with several K and R in the C-terminus region, and oligopeptide C 362KQSSGGDPEIVTHSFNCGG380 with few basic amino acids in the CD4 binding domain.	Amino Acids, Basic	303-320	inter-alpha-trypsin inhibitor heavy chain 4	Homo sapiens	54-59
31018591-7	2019	We also show that HS and heparin bind to, and block, another set of basic amino acids required for unimpaired Shh binding to Ptc receptors on receiving cells.	Amino Acids, Basic	68-85	sonic hedgehog signaling molecule	Homo sapiens	110-113
30706700-1	2019	FURIN is a proprotein convertase subtilisin/kexin enzyme important in pro-renin receptor processing, and FURIN (furin, paired basic amino acid cleaving enzyme) variants are involved in multiple aspects of blood pressure (BP) regulation.	Amino Acids, Basic	126-142	furin, paired basic amino acid cleaving enzyme	Homo sapiens	105-110
30445147-1	2019	A plasma membrane amino acid transporter B0,+ (ATB0,+), encoded by the SLC6A14 gene, is specific for neutral and basic amino acids.	Amino Acids, Basic	113-130	solute carrier family 1 member 5	Homo sapiens	47-51
30445147-1	2019	A plasma membrane amino acid transporter B0,+ (ATB0,+), encoded by the SLC6A14 gene, is specific for neutral and basic amino acids.	Amino Acids, Basic	113-130	solute carrier family 6 member 14	Homo sapiens	71-78
30706700-1	2019	FURIN is a proprotein convertase subtilisin/kexin enzyme important in pro-renin receptor processing, and FURIN (furin, paired basic amino acid cleaving enzyme) variants are involved in multiple aspects of blood pressure (BP) regulation.	Amino Acids, Basic	126-142	furin, paired basic amino acid cleaving enzyme	Homo sapiens	112-117
30229400-3	2018	Furthermore, ortholog of Cathepsin L, CPL-1 are found in C. elegans and can potentially cleave paired basic amino acids at the N-terminal suggesting the presence of both pathways.	Amino Acids, Basic	102-119	Cathepsin L-like	Caenorhabditis elegans	38-43
30413416-6	2019	Linker segment aa 155 to 196 contains a nuclear localization signal rich in basic amino acids that is necessary for RRM2 activity in mud1  complementation.	Amino Acids, Basic	76-93	Mud1p	Saccharomyces cerevisiae S288C	133-137
31353333-3	2019	On page 126, on the bottom line of the left column, the sentence opening "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to aspartic acid did not affect cell growth," should be changed to "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to alanine did not affect cell growth,".	Amino Acids, Basic	108-125	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	136-140
31353333-3	2019	On page 126, on the bottom line of the left column, the sentence opening "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to aspartic acid did not affect cell growth," should be changed to "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to alanine did not affect cell growth,".	Amino Acids, Basic	108-125	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	296-300
31353333-3	2019	On page 126, on the bottom line of the left column, the sentence opening "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to aspartic acid did not affect cell growth," should be changed to "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to alanine did not affect cell growth,".	Amino Acids, Basic	268-285	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	136-140
31353333-3	2019	On page 126, on the bottom line of the left column, the sentence opening "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to aspartic acid did not affect cell growth," should be changed to "Conversion of these two conserved basic amino acids in either Mcm4, 6 or 7 in S. cerevisiae to alanine did not affect cell growth,".	Amino Acids, Basic	268-285	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	296-300
31353333-5	2019	3 legend, the second sentence "Two conserved basic amino acids in the amino-terminal region of Mcm4, 6 and 7 proteins were mutated to aspartic acid in S. cerevisiae (Froelich et al., 2014)."	Amino Acids, Basic	45-62	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	95-99
31353333-6	2019	should be changed to "Two conserved basic amino acids in the amino-terminal region of Mcm4, 6 and 7 proteins were mutated to alanine in S. cerevisiae (Froelich et al., 2014); the suffix D indicates double-alanine mutation".	Amino Acids, Basic	36-53	MCM DNA helicase complex subunit MCM4	Saccharomyces cerevisiae S288C	86-90
29069492-8	2018	These results suggest that ZG16p interacts with the cell surface via basic amino acids substituted in ZG16p-M5 and inhibits Caco-2 cell proliferation via Asp151.	Amino Acids, Basic	69-86	zymogen granule protein 16	Homo sapiens	27-32
29069492-8	2018	These results suggest that ZG16p interacts with the cell surface via basic amino acids substituted in ZG16p-M5 and inhibits Caco-2 cell proliferation via Asp151.	Amino Acids, Basic	69-86	zymogen granule protein 16	Homo sapiens	102-107
30617637-2	2019	For the effective transfection of p11 gene intracellularly, two cationic lipids based on phospholipid DOPE conjugated to basic amino acids histidine and arginine were synthesised, used for liposome formulation and evaluated for their ability as gene delivery vectors.	Amino Acids, Basic	121-138	S100 calcium binding protein A10	Homo sapiens	34-37
31037164-8	2018	Chromatography of amino acids in the urine showed increased basic amino acids evoking a deficit of the urea cycle due to deficit of the enzyme argininosuccinate lyase.	Amino Acids, Basic	60-77	argininosuccinate lyase	Homo sapiens	143-166
30375474-2	2018	MALT1 is a unique enzyme among this clan because it recognizes the basic amino acid arginine in the P1 pocket.	Amino Acids, Basic	67-83	MALT1 paracaspase	Homo sapiens	0-5
30333730-5	2018	Besides, we find that the 10 basic amino acids in C1 domain determine the nuclear localization of GluN1 C-terminus.	Amino Acids, Basic	29-46	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	98-103
30333730-8	2018	Our data suggested that the 10 basic amino acids in C1 domain determine translocation of GluN1 C-terminus into nucleus and regulate synaptic transmission.	Amino Acids, Basic	31-48	glutamate ionotropic receptor NMDA type subunit 1	Homo sapiens	89-94
30008699-13	2018	Overall, data presented here describe the primary role of Alr as important for basic amino acid metabolism.	Amino Acids, Basic	79-95	alanine racemase	Pseudomonas putida KT2440	58-61
29973722-4	2018	Specific recognition of thymine residues in the ACS is carried out by a conserved basic amino acid motif of Orc1 in the minor groove, and by a species-specific helical insertion motif of Orc4 in the major groove.	Amino Acids, Basic	82-98	origin recognition complex subunit 1	Saccharomyces cerevisiae S288C	108-112
29657074-7	2018	This caused the reduction in molecular weight of PRM2 from 2157.66 to 1931.33 Da due to reduction in the number of basic amino acids.	Amino Acids, Basic	115-132	protamine 2	Bos taurus	49-53
29883024-3	2018	The substrate specificities of CPB2 and CPN are similar; they both remove C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them.	Amino Acids, Basic	85-102	carboxypeptidase B2 (plasma)	Mus musculus	31-35
29883024-3	2018	The substrate specificities of CPB2 and CPN are similar; they both remove C-terminal basic amino acids from bioactive peptides and proteins, thereby inactivating them.	Amino Acids, Basic	85-102	carboxypeptidase N, polypeptide 1	Mus musculus	40-43
29751762-4	2018	The lysine 28 and lysine 50 residues of Tat, or the acetylation and methylation modifications of these basic amino acids, were essential for Tat transcriptional control, and also for the proviral expression effects elicited by histone deacetylase inhibitors (HDACi) or the bromodomain inhibitor JQ1.	Amino Acids, Basic	103-120	tyrosine aminotransferase	Homo sapiens	40-43
29751762-4	2018	The lysine 28 and lysine 50 residues of Tat, or the acetylation and methylation modifications of these basic amino acids, were essential for Tat transcriptional control, and also for the proviral expression effects elicited by histone deacetylase inhibitors (HDACi) or the bromodomain inhibitor JQ1.	Amino Acids, Basic	103-120	tyrosine aminotransferase	Homo sapiens	141-144
29507109-7	2018	There was a higher frequency of basic amino acids in DRB1*1404/*1301-specific epitopes compared with hydrophobic and polar amino acids in DRB1*1501-specific epitopes at anchor residues pocket 4 and pocket 6, which interact with residues at DRB1 positions 11 and 13.	Amino Acids, Basic	32-49	major histocompatibility complex, class II, DR beta 1	Homo sapiens	53-57
29491167-1	2018	In addition to specific RNA-binding zinc finger domains, the retroviral Gag polyprotein contains clusters of basic amino acid residues that are thought to support Gag-viral genomic RNA (gRNA) interactions.	Amino Acids, Basic	109-125	Pr78	Mason-Pfizer monkey virus	72-75
29491167-1	2018	In addition to specific RNA-binding zinc finger domains, the retroviral Gag polyprotein contains clusters of basic amino acid residues that are thought to support Gag-viral genomic RNA (gRNA) interactions.	Amino Acids, Basic	109-125	Pr78	Mason-Pfizer monkey virus	163-166
28964831-1	2017	Neutral metallo-aminopeptidase (APN) catalyzes the cleavage of neutral and basic amino acids from the N-terminus of protein or peptide substrates.	Amino Acids, Basic	75-92	alanyl aminopeptidase, membrane	Homo sapiens	32-35
29113979-9	2018	Substitution of the basic amino acid repeats in the Ure2 relief sequence or phosphomimetic aspartate substitutions for the serine residues between them abolishes nuclear Gln3-Myc13 localization in response to both limiting nitrogen and rapamycin treatment.	Amino Acids, Basic	20-36	glutathione peroxidase	Saccharomyces cerevisiae S288C	52-56
28939768-3	2017	Electrostatic interactions between negatively charged PM phospholipids and basic amino acids found in K-Ras4B (K-Ras) but not in H-Ras are important for permanent K-Ras localization to the PM.	Amino Acids, Basic	75-92	KRAS proto-oncogene, GTPase	Homo sapiens	102-109
28939768-3	2017	Electrostatic interactions between negatively charged PM phospholipids and basic amino acids found in K-Ras4B (K-Ras) but not in H-Ras are important for permanent K-Ras localization to the PM.	Amino Acids, Basic	75-92	KRAS proto-oncogene, GTPase	Homo sapiens	102-107
28939768-3	2017	Electrostatic interactions between negatively charged PM phospholipids and basic amino acids found in K-Ras4B (K-Ras) but not in H-Ras are important for permanent K-Ras localization to the PM.	Amino Acids, Basic	75-92	KRAS proto-oncogene, GTPase	Homo sapiens	111-116
28833090-2	2018	It has multiple ligands, including hyaluronic acid (HA) and growth factors/cytokines (e.g., PDGF-BB and VEGF-A) containing CRS motifs (clusters of basic amino-acid residues).	Amino Acids, Basic	147-163	vascular endothelial growth factor A	Homo sapiens	104-110
29463753-4	2018	An additional signature in Env involves the overrepresentation of basic amino acid residues at a specific position in the Env signal peptide (SP).	Amino Acids, Basic	66-82	endogenous retrovirus group K member 6, envelope	Homo sapiens	27-30
29463753-4	2018	An additional signature in Env involves the overrepresentation of basic amino acid residues at a specific position in the Env signal peptide (SP).	Amino Acids, Basic	66-82	endogenous retrovirus group K member 6, envelope	Homo sapiens	122-125
28432839-2	2017	ASP resembles Saccharomyces cerevisiae Kex2, a member of the subtilisin family, and preferentially cleaves peptide bonds at the C-terminal side of paired basic amino acid residues; also accepting unpaired arginine at the P1 site.	Amino Acids, Basic	154-170	kexin KEX2	Saccharomyces cerevisiae S288C	39-43
28627371-5	2017	The obtained results of the inhibitory activity and modeling by molecular dynamics indicate that simultaneous interactions of the basic amino acid residues in position 1 and 4 (Arg) with Neuropilin-1 are crucial and their cooperation strongly affects the inhibitory activity.	Amino Acids, Basic	130-146	neuropilin 1	Homo sapiens	187-199
28413120-0	2017	Endosome to trans-Golgi network transport of Proprotein Convertase 7 is mediated by a cluster of basic amino acids and palmitoylated cysteines.	Amino Acids, Basic	97-114	proprotein convertase subtilisin/kexin type 7	Homo sapiens	45-68
28413120-1	2017	Proprotein Convertase 7 (PC7) is a Furin-like endoprotease that cleaves precursor proteins at basic amino acids.	Amino Acids, Basic	94-111	proprotein convertase subtilisin/kexin type 7	Homo sapiens	0-23
28413120-1	2017	Proprotein Convertase 7 (PC7) is a Furin-like endoprotease that cleaves precursor proteins at basic amino acids.	Amino Acids, Basic	94-111	proprotein convertase subtilisin/kexin type 7	Homo sapiens	25-28
28413120-1	2017	Proprotein Convertase 7 (PC7) is a Furin-like endoprotease that cleaves precursor proteins at basic amino acids.	Amino Acids, Basic	94-111	furin, paired basic amino acid cleaving enzyme	Homo sapiens	35-40
27936608-2	2017	MS2 experiments using different ion activation techniques validated the sequences of the synthetic, bioactive peptides HA and BMP2, which contained highly basic amino acid residues either at the N-terminus (BMP2) or C-terminus (HA).	Amino Acids, Basic	155-171	bone morphogenetic protein 2	Homo sapiens	126-130
28695314-0	2017	Bacterial production and reconstitution in proteoliposomes of Solanum lycopersicum CAT2: a transporter of basic amino acids and organic cations.	Amino Acids, Basic	106-123	catalase isozyme 2	Solanum lycopersicum	83-87
28254587-0	2017	Activity of human kallikrein-related peptidase 6 (KLK6) on substrates containing sequences of basic amino acids.	Amino Acids, Basic	94-111	kallikrein related peptidase 6	Homo sapiens	18-48
28254587-0	2017	Activity of human kallikrein-related peptidase 6 (KLK6) on substrates containing sequences of basic amino acids.	Amino Acids, Basic	94-111	kallikrein related peptidase 6	Homo sapiens	50-54
28240595-3	2017	In experiments with rat neuroendocrine cells, we find that a few basic amino acids in the cysteine-rich region of SNAP25 and SNAP23 are essential for plasma membrane targeting.	Amino Acids, Basic	65-82	synaptosome associated protein 25	Rattus norvegicus	114-120
28240595-3	2017	In experiments with rat neuroendocrine cells, we find that a few basic amino acids in the cysteine-rich region of SNAP25 and SNAP23 are essential for plasma membrane targeting.	Amino Acids, Basic	65-82	synaptosome associated protein 23	Rattus norvegicus	125-131
28222195-10	2017	De novo sequencing showed that there was a mutation at either of the SS positions on the CDR1 region, which changed one of the serine residues to a basic amino acid, i.e., arginine or lysine.	Amino Acids, Basic	148-164	cerebellar degeneration related protein 1	Homo sapiens	89-93
28508285-7	2017	Results from analyses of AAs and insulin indicated that HNO3 could not only react with basic amino acid residues, but also with disulfide bonds to form [M-3H+(HNO3)n]3- complex ions.	Amino Acids, Basic	87-103	insulin	Homo sapiens	33-40
27749002-5	2017	During intracellular processing, hFVIII is predominantly cleaved at a paired basic amino acid cleaving enzyme (PACE) or furin cleavage site to yield a heterodimer that is the major form of secreted protein.	Amino Acids, Basic	77-93	coagulation factor VIII	Homo sapiens	33-39
27989698-6	2017	Through four basic amino acid replacements within the NLSs, we obtained a cytoplasm-located RYBP mutant (RYBPmut).	Amino Acids, Basic	13-29	RING1 and YY1 binding protein	Homo sapiens	92-96
27581177-2	2016	Basic amino acids improved insulin solubility in water while 200 and 400 mug/mL lysine significantly increased insulin solubility in HBSS.	Amino Acids, Basic	0-17	insulin	Homo sapiens	27-34
28180060-2	2017	GPRC6A is activated by multiple ligands, including osteocalcin (Ocn), testosterone (T), basic amino acids, and various cations.	Amino Acids, Basic	88-105	G protein-coupled receptor class C group 6 member A	Homo sapiens	0-6
28026803-5	2016	Furin relates to enzymes with a narrow substrate specificity: it hydrolyzes peptide bonds at the site of paired basic amino acids and furin activity exhibits in a wide pH range 5-8.	Amino Acids, Basic	112-129	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
27707755-5	2016	We describe a novel patient-derived DIAPH1 mutation (c.3610C>T) in two unrelated families, which results in early termination prior to a basic amino acid motif (RRKR1204-1207) at the DAD C-terminus.	Amino Acids, Basic	140-156	diaphanous related formin 1	Homo sapiens	36-42
27016482-0	2016	Non-basic amino acids in the ROMK1 channels via an appropriate distance modulate PIP2 regulated pHi-gating.	Amino Acids, Basic	4-21	potassium inwardly rectifying channel subfamily J member 1	Homo sapiens	29-34
27312421-6	2016	Computational studies using molecular docking and dynamic simulation revealed that PTS directly interacts with the basic amino acids of kelch domain of Keap1 and perturb Keap1-Nrf2 interaction pattern.	Amino Acids, Basic	115-132	kelch like ECH associated protein 1	Homo sapiens	152-157
27460989-3	2016	Membrane binding by the CD28 cytoplasmic domain required two clusters of basic amino acid residues, which interacted with the negatively charged inner leaflet of the plasma membrane.	Amino Acids, Basic	73-89	CD28 antigen	Mus musculus	24-28
27064749-6	2016	Consistent with the results of pH titration analysis, site-directed mutagenesis revealed several basic amino acid residues in the intermolecular (R267) and intramolecular (K82 and R159) subdomains that are essential for Purbeta transcriptional repressor function in Acta2 promoter-reporter assays.	Amino Acids, Basic	97-113	purine rich element binding protein B	Mus musculus	220-227
27064749-6	2016	Consistent with the results of pH titration analysis, site-directed mutagenesis revealed several basic amino acid residues in the intermolecular (R267) and intramolecular (K82 and R159) subdomains that are essential for Purbeta transcriptional repressor function in Acta2 promoter-reporter assays.	Amino Acids, Basic	97-113	actin alpha 2, smooth muscle, aorta	Mus musculus	266-271
27177968-6	2016	We analyzed FPR2 sequence for the search of a nuclear localization sequence (NLS) and we found a stretch of basic aminoacids (227-KIHKK-231) in the third cytoplasmic loop of the receptor.	Amino Acids, Basic	108-124	formyl peptide receptor 2	Homo sapiens	12-16
26928127-4	2016	The vacuolar membrane vesicles isolated from the resulting quadruple deletion mutant ypq1Deltaypq2Deltaypq3Deltaavt1Delta completely lost the uptake activity of basic amino acids, and that of histidine, but not lysine and arginine, was evidently enhanced by overexpressing YPQ3 in the mutant.	Amino Acids, Basic	161-178	cationic amino acid transporter	Saccharomyces cerevisiae S288C	273-277
27016482-0	2016	Non-basic amino acids in the ROMK1 channels via an appropriate distance modulate PIP2 regulated pHi-gating.	Amino Acids, Basic	4-21	glucose-6-phosphate isomerase	Homo sapiens	96-99
26941104-3	2016	The mutational hotspot in RPGR(ORF15)is an unusual C-terminal domain encoded by exon ORF15, which is rich in polyglutamates and glycine residues (Glu-Gly domain) followed by a short stretch of basic amino acid residues (RPGR(C2)domain; residues 1072-1152).	Amino Acids, Basic	193-209	retinitis pigmentosa GTPase regulator	Mus musculus	26-36
26454877-4	2016	The replacement of Asn203 with a basic amino acid was suggested to stabilize alpha-helix 2, which is important for the Mpr1 structure, probably by neutralizing its dipole.	Amino Acids, Basic	33-49	proteasome regulatory particle lid subunit RPN11	Saccharomyces cerevisiae S288C	119-123
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 22 member 5	Homo sapiens	79-84
26687946-5	2016	And the interactive motifs of PKR2 were mapped to YFK (343-345) and HWR (351-353), which shared a similar sequence of two aromatic amino acids followed by a basic amino acid.	Amino Acids, Basic	157-173	prokineticin receptor 2	Homo sapiens	30-34
26325352-1	2016	In the vacuolar basic amino acid (VBA) transporter family of Saccharomyces cerevisiae, VBA4 encodes a vacuolar membrane protein with 14 putative transmembrane helices.	Amino Acids, Basic	16-32	Vba4p	Saccharomyces cerevisiae S288C	87-91
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 22 member 5	Homo sapiens	86-93
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 22 member 16	Homo sapiens	129-132
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 22 member 16	Homo sapiens	134-142
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 1 member 5	Homo sapiens	195-199
28132459-2	2016	It enters the cell due to the activity of organic cation/carnitine transporter OCTN2 (SLC22A5), it can be as well transported by CT2 (SLC22A16) and a transporter of neutral and basic amino acids ATB0, + (SLC6A14).	Amino Acids, Basic	177-194	solute carrier family 6 member 14	Homo sapiens	204-211
26269593-10	2015	Purified zebrafish POLN protein is capable of thymine glycol bypass and strand displacement, with activity dependent on a basic amino acid residue known to stabilize the primer-template.	Amino Acids, Basic	122-138	polymerase (DNA directed) nu	Danio rerio	19-23
26456171-5	2015	Both HA and regions of tubulin (s-tubulin) are anionic and bind to basic amino acid-rich regions in partner proteins, such as in HA and tubulin binding regions of RHAMM.	Amino Acids, Basic	67-83	hyaluronan mediated motility receptor	Homo sapiens	163-168
26362868-12	2015	Thus, several basic amino acids located on the cytoplasmic tail of ST3G5 play important roles in both ER export and Golgi retention.	Amino Acids, Basic	14-31	ST3 beta-galactoside alpha-2,3-sialyltransferase 5	Homo sapiens	67-72
26597985-4	2016	In this study, we showed that SBP1, -2, and -3 individually bind different basic amino acids with exquisite specificity.	Amino Acids, Basic	75-92	high mobility group box 1	Homo sapiens	30-34
26577948-2	2015	The mammalian PQLC2 protein catalyzes efflux of basic amino acids from the lysosome, and the similar Ypq1, -2, and -3 proteins of yeast perform an equivalent function at the vacuole.	Amino Acids, Basic	48-65	solute carrier family 66 member 1	Homo sapiens	14-19
26352190-1	2015	Aminopeptidase B (APB, EC 3.4.11.6) preferentially hydrolyzes the N-terminal basic amino acids of synthetic and peptide substrates and requires a physiological concentration of NaCl for optimal activity.	Amino Acids, Basic	77-94	arginyl aminopeptidase	Homo sapiens	0-16
26352190-1	2015	Aminopeptidase B (APB, EC 3.4.11.6) preferentially hydrolyzes the N-terminal basic amino acids of synthetic and peptide substrates and requires a physiological concentration of NaCl for optimal activity.	Amino Acids, Basic	77-94	arginyl aminopeptidase	Homo sapiens	18-21
25947322-12	2015	Furthermore, basic amino acids on the XLF CTR are highly conserved among domestic animals including cattle, goat and horses, suggesting that the CTR is essential for the function of XLF in domestic animals.	Amino Acids, Basic	13-30	non-homologous end joining factor 1	Mus musculus	38-41
26002808-8	2015	Human ORC1, ORC2, and SLC25A29 are likely to be involved in the biosynthesis and transport of arginine, which can be used as a precursor for the synthesis of NO, agmatine, polyamines, creatine, glutamine, glutamate, and proline, as well as in the degradation of basic amino acids.	Amino Acids, Basic	262-279	origin recognition complex subunit 1	Homo sapiens	6-10
26002808-8	2015	Human ORC1, ORC2, and SLC25A29 are likely to be involved in the biosynthesis and transport of arginine, which can be used as a precursor for the synthesis of NO, agmatine, polyamines, creatine, glutamine, glutamate, and proline, as well as in the degradation of basic amino acids.	Amino Acids, Basic	262-279	origin recognition complex subunit 2	Homo sapiens	12-16
26002808-8	2015	Human ORC1, ORC2, and SLC25A29 are likely to be involved in the biosynthesis and transport of arginine, which can be used as a precursor for the synthesis of NO, agmatine, polyamines, creatine, glutamine, glutamate, and proline, as well as in the degradation of basic amino acids.	Amino Acids, Basic	262-279	solute carrier family 25 member 29	Homo sapiens	22-30
25947322-12	2015	Furthermore, basic amino acids on the XLF CTR are highly conserved among domestic animals including cattle, goat and horses, suggesting that the CTR is essential for the function of XLF in domestic animals.	Amino Acids, Basic	13-30	non-homologous end joining factor 1	Mus musculus	182-185
26072378-6	2015	Although a direct interaction of Girdin and kinesin-1 has not been determined, it is of interest to find that Girdin loss-of-function mutant mice with the mutation of a basic amino acid residue-rich region (Basic mut mice) exhibit limited interaction with kinesin-1.	Amino Acids, Basic	169-185	coiled coil domain containing 88A	Mus musculus	110-116
25050844-9	2014	These results indicated C5a release from C5 by a cancer cell membrane-bound serine protease that can cleave peptide bonds at the carboxy-terminal site of paired basic amino acid residues.	Amino Acids, Basic	161-177	complement C5a receptor 1	Homo sapiens	24-27
26244740-2	2015	In the case of the membrane-bound nonreceptor tyrosine kinase Src from Rous sarcoma virus, these interactions are mediated by an N-terminal myristoyl chain and an adjacent cluster of six basic amino-acid residues, respectively.	Amino Acids, Basic	187-203	p60 src	Rous sarcoma virus	62-65
25805498-0	2015	Microtubule severing by katanin p60 AAA+ ATPase requires the C-terminal acidic tails of both alpha- and beta-tubulins and basic amino acid residues in the AAA+ ring pore.	Amino Acids, Basic	122-138	interferon induced protein with tetratricopeptide repeats 3	Homo sapiens	32-35
26539469-7	2015	bFGF has a highly basic amino acid domain.	Amino Acids, Basic	18-34	fibroblast growth factor 2	Homo sapiens	0-4
25600804-0	2015	Basic amino acid residues located in the N-terminal region of BEND3 are essential for its nuclear localization.	Amino Acids, Basic	0-16	BEN domain containing 3	Homo sapiens	62-67
25600804-4	2015	We found that three basic amino acid residues located in the N-terminal region of BEND3 (BEND356-58, KRK) are essential, suggesting that these residues play a role as a functional NLS.	Amino Acids, Basic	20-36	BEN domain containing 3	Homo sapiens	82-87
25600804-4	2015	We found that three basic amino acid residues located in the N-terminal region of BEND3 (BEND356-58, KRK) are essential, suggesting that these residues play a role as a functional NLS.	Amino Acids, Basic	20-36	BEN domain containing 3	Homo sapiens	89-99
25320314-8	2015	Moreover, based on three-dimensional (3D) modeling of protein-protein interactions (i.e., protein-protein docking) and further validation by a virus capture assay, we found that a series of acidic residues in the MA domain interact with basic amino acids located in the ICAM-1 cytoplasmic tail.	Amino Acids, Basic	237-254	intercellular adhesion molecule 1	Homo sapiens	270-276
25050844-9	2014	These results indicated C5a release from C5 by a cancer cell membrane-bound serine protease that can cleave peptide bonds at the carboxy-terminal site of paired basic amino acid residues.	Amino Acids, Basic	161-177	coagulation factor II, thrombin	Homo sapiens	76-91
24661926-6	2014	The disulfide loop and the basic amino acids in the LPS-binding domain (LBD) of ALF played key roles in its antibacterial activities.	Amino Acids, Basic	27-44	general transcription factor IIA subunit 1 like	Homo sapiens	80-83
24463069-8	2014	Both aromatic rings (F5, F6, F17, and F27) and interfacial basic amino acids of LL-37 directly interact with anionic phosphatidylglycerols (PG).	Amino Acids, Basic	59-76	cathelicidin antimicrobial peptide	Homo sapiens	80-85
24953096-5	2014	Second, we demonstrate that the XPA-PAR interaction is mediated by specific basic amino acids within a highly conserved PAR-binding motif, which overlaps the DNA damage-binding protein 2 (DDB2) and transcription factor II H (TFIIH) interaction domains of XPA.	Amino Acids, Basic	76-93	XPA, DNA damage recognition and repair factor	Homo sapiens	32-35
24953096-5	2014	Second, we demonstrate that the XPA-PAR interaction is mediated by specific basic amino acids within a highly conserved PAR-binding motif, which overlaps the DNA damage-binding protein 2 (DDB2) and transcription factor II H (TFIIH) interaction domains of XPA.	Amino Acids, Basic	76-93	damage specific DNA binding protein 2	Homo sapiens	158-186
24953096-5	2014	Second, we demonstrate that the XPA-PAR interaction is mediated by specific basic amino acids within a highly conserved PAR-binding motif, which overlaps the DNA damage-binding protein 2 (DDB2) and transcription factor II H (TFIIH) interaction domains of XPA.	Amino Acids, Basic	76-93	damage specific DNA binding protein 2	Homo sapiens	188-192
24953096-5	2014	Second, we demonstrate that the XPA-PAR interaction is mediated by specific basic amino acids within a highly conserved PAR-binding motif, which overlaps the DNA damage-binding protein 2 (DDB2) and transcription factor II H (TFIIH) interaction domains of XPA.	Amino Acids, Basic	76-93	XPA, DNA damage recognition and repair factor	Homo sapiens	255-258
24802393-6	2014	Furthermore, a short cluster of basic amino acid residues KRRK within this bipartite NLS plays the primary role in nuclear localization and is evolutionarily conserved in USP22 homologues.	Amino Acids, Basic	32-48	ubiquitin specific peptidase 22	Homo sapiens	171-176
25005938-0	2014	The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.	Amino Acids, Basic	4-21	SH3 domain containing kinase binding protein 1	Homo sapiens	51-56
25005938-0	2014	The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.	Amino Acids, Basic	4-21	Cbl proto-oncogene	Homo sapiens	87-92
25005938-0	2014	The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.	Amino Acids, Basic	4-21	epidermal growth factor receptor	Homo sapiens	122-154
25005938-0	2014	The basic amino acids in the coiled-coil domain of CIN85 regulate its interaction with c-Cbl and phosphatidic acid during epidermal growth factor receptor (EGFR) endocytosis.	Amino Acids, Basic	4-21	epidermal growth factor receptor	Homo sapiens	156-160
25005938-5	2014	RESULTS: Mutations of the basic amino acids in the coiled-coil domain, especially K645, K646, R648 and R650, into neutral amino acid alanine completely blocked the interaction of CIN85 with c-Cbl or phosphatidic acid.	Amino Acids, Basic	26-43	SH3 domain containing kinase binding protein 1	Homo sapiens	179-184
25005938-5	2014	RESULTS: Mutations of the basic amino acids in the coiled-coil domain, especially K645, K646, R648 and R650, into neutral amino acid alanine completely blocked the interaction of CIN85 with c-Cbl or phosphatidic acid.	Amino Acids, Basic	26-43	Cbl proto-oncogene	Homo sapiens	190-195
25005938-9	2014	Mutations in the coiled-coil domain (deletion of the coiled-coil domain or point mutations of the basic amino acids) dissociated CIN85 from endosomes.	Amino Acids, Basic	98-115	SH3 domain containing kinase binding protein 1	Homo sapiens	129-134
25005938-12	2014	The positive charges of basic amino acids in the coiled-coil domain are not only involved in the interaction with phosphatidic acid, but also regulate the interaction of CIN85 with c-Cbl.	Amino Acids, Basic	24-41	SH3 domain containing kinase binding protein 1	Homo sapiens	170-175
25005938-12	2014	The positive charges of basic amino acids in the coiled-coil domain are not only involved in the interaction with phosphatidic acid, but also regulate the interaction of CIN85 with c-Cbl.	Amino Acids, Basic	24-41	Cbl proto-oncogene	Homo sapiens	181-186
25076951-2	2014	The Arabidopsis nuclear gene BASIC AMINO ACID CARRIER 2 (BAC2) encodes a mitochondria-located carrier that transports basic amino acids in vitro.	Amino Acids, Basic	118-135	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	29-55
25076951-2	2014	The Arabidopsis nuclear gene BASIC AMINO ACID CARRIER 2 (BAC2) encodes a mitochondria-located carrier that transports basic amino acids in vitro.	Amino Acids, Basic	118-135	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	57-61
25076951-4	2014	When BAC2 is overexpressed in vivo, it triggers catabolism of arginine, a basic amino acid, leading to arginine depletion and urea accumulation in leaves.	Amino Acids, Basic	74-90	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	5-9
24798548-2	2014	The anionic phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) is a known positive modulator of TRPV1 channels and the negatively charged phosphate groups interact with several basic amino acid residues in the proximal C-terminal TRP domain of the TRPV1 channel.	Amino Acids, Basic	184-200	transient receptor potential cation channel subfamily V member 1	Homo sapiens	103-108
24412328-1	2014	BACKGROUND: Aminopeptidase B (EC 3.4.11.6, APB) preferentially hydrolyzes N-terminal basic amino acids of synthetic and peptide substrates.	Amino Acids, Basic	85-102	arginyl aminopeptidase	Homo sapiens	12-28
24412328-1	2014	BACKGROUND: Aminopeptidase B (EC 3.4.11.6, APB) preferentially hydrolyzes N-terminal basic amino acids of synthetic and peptide substrates.	Amino Acids, Basic	85-102	arginyl aminopeptidase	Homo sapiens	43-46
24412328-2	2014	APB is involved in the production and maturation of peptide hormones and neurotransmitters such as miniglucagon, cholecystokinin and enkephalin by cleaving N-terminal basic amino acids in extended precursor proteins.	Amino Acids, Basic	167-184	arginyl aminopeptidase	Homo sapiens	0-3
24412328-3	2014	Therefore, the specificity for basic amino acids is crucial for the biological function of APB.	Amino Acids, Basic	31-48	arginyl aminopeptidase	Homo sapiens	91-94
24412328-4	2014	METHODS: Site-directed mutagenesis and molecular modeling of the S1 site were used to identify amino acid residues of the human APB responsible for the basic amino acid preference and enzymatic efficiency.	Amino Acids, Basic	152-168	arginyl aminopeptidase	Homo sapiens	128-131
24412328-11	2014	CONCLUSION: Gln169 is crucial for obtaining optimal enzymatic activity and the unique basic amino acid preference of APB via maintaining the appropriate catalytic pocket structure and thus for its function as a processing enzyme of peptide hormones and neurotransmitters.	Amino Acids, Basic	86-102	arginyl aminopeptidase	Homo sapiens	117-120
24895758-2	2014	The H(+)-coupled plasma membrane transporter CAT1 (cationic amino acid transporter 1) facilitates the high-affinity uptake of basic amino acids.	Amino Acids, Basic	126-143	catalase 1	Arabidopsis thaliana	45-49
24850085-12	2014	The active peptide sequence alignments suggest that the syndecan-binding peptides contain a "basic amino acid (BAA)-Gly-BAA" motif in the middle of the molecule and that the integrin-binding peptides contain an "acidic amino acid (AAA)"-Gly-BAA motif.	Amino Acids, Basic	93-109	syndecan 1	Homo sapiens	56-64
24850085-12	2014	The active peptide sequence alignments suggest that the syndecan-binding peptides contain a "basic amino acid (BAA)-Gly-BAA" motif in the middle of the molecule and that the integrin-binding peptides contain an "acidic amino acid (AAA)"-Gly-BAA motif.	Amino Acids, Basic	111-114	syndecan 1	Homo sapiens	56-64
24850085-12	2014	The active peptide sequence alignments suggest that the syndecan-binding peptides contain a "basic amino acid (BAA)-Gly-BAA" motif in the middle of the molecule and that the integrin-binding peptides contain an "acidic amino acid (AAA)"-Gly-BAA motif.	Amino Acids, Basic	120-123	syndecan 1	Homo sapiens	56-64
24850085-12	2014	The active peptide sequence alignments suggest that the syndecan-binding peptides contain a "basic amino acid (BAA)-Gly-BAA" motif in the middle of the molecule and that the integrin-binding peptides contain an "acidic amino acid (AAA)"-Gly-BAA motif.	Amino Acids, Basic	120-123	syndecan 1	Homo sapiens	56-64
24652292-0	2014	The human gene SLC25A29, of solute carrier family 25, encodes a mitochondrial transporter of basic amino acids.	Amino Acids, Basic	93-110	solute carrier family 25 member 29	Homo sapiens	15-23
24652292-7	2014	The main physiological role of SLC25A29 is to import basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation.	Amino Acids, Basic	53-70	solute carrier family 25 member 29	Homo sapiens	31-39
24798548-2	2014	The anionic phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) is a known positive modulator of TRPV1 channels and the negatively charged phosphate groups interact with several basic amino acid residues in the proximal C-terminal TRP domain of the TRPV1 channel.	Amino Acids, Basic	184-200	transient receptor potential cation channel subfamily V member 1	Homo sapiens	255-260
24365672-1	2014	Carboxypeptidase E (CPE) cleaves basic amino acid residues at the C-terminal end and involves in the biosynthesis of numerous peptide hormones and neurotransmitters.	Amino Acids, Basic	33-49	carboxypeptidase E	Homo sapiens	0-18
24695318-0	2014	Both the C1 domain and a basic amino acid cluster at the C-terminus are important for the neurite and branch induction ability of DGKbeta.	Amino Acids, Basic	25-41	diacylglycerol kinase beta	Homo sapiens	130-137
24695318-9	2014	These results indicate that in addition to kinase activity, plasma membrane localization via the C1 domain and basic amino acids at the C-terminus were indispensable for neurite induction by DGKbeta.	Amino Acids, Basic	111-128	diacylglycerol kinase beta	Homo sapiens	191-198
24628338-11	2014	On the basis of our mutagenesis results, the basic amino acid cluster in the N-terminus of proHB-EGF-CT is the crucial binding site for mBAG-1-UBH, whereas another basic amino acid in the C-terminus facilitates this interaction.	Amino Acids, Basic	45-61	BCL2-associated athanogene 1	Mus musculus	136-146
24365672-1	2014	Carboxypeptidase E (CPE) cleaves basic amino acid residues at the C-terminal end and involves in the biosynthesis of numerous peptide hormones and neurotransmitters.	Amino Acids, Basic	33-49	carboxypeptidase E	Homo sapiens	20-23
24167501-4	2013	One year later, Donald Chance confirmed that the cleavage sites in proinsulin were also made of paired basic amino acids (3).	Amino Acids, Basic	103-120	insulin	Homo sapiens	67-77
25036121-0	2014	Vacuolar transporter Avt4 is involved in excretion of basic amino acids from the vacuoles of Saccharomyces cerevisiae.	Amino Acids, Basic	54-71	Avt4p	Saccharomyces cerevisiae S288C	21-25
25036121-2	2014	We found that the decrease of vacuolar basic amino acids in response to nitrogen starvation was impaired by the deletion of AVT4 gene encoding a vacuolar transporter.	Amino Acids, Basic	39-56	Avt4p	Saccharomyces cerevisiae S288C	124-128
25036121-3	2014	In addition, overexpression of AVT4 reduced the accumulation of basic amino acids in vacuoles under nutrient-rich condition.	Amino Acids, Basic	64-81	Avt4p	Saccharomyces cerevisiae S288C	31-35
25036121-6	2014	These results suggest that Avt4p is a vacuolar amino acid exporter involving in the recycling of basic amino acids.	Amino Acids, Basic	97-114	Avt4p	Saccharomyces cerevisiae S288C	27-32
25483586-8	2014	These studies conclusively demonstrate the ability of Cx40 and Cx43 to form rectifying heterotypic gap junctions, owing primarily to alternate amino-terminal (NT) domain acidic and basic amino acid differences that may play a significant role in the physiology and/or pathology of the cardiovascular tissues including cardiac conduction properties and myoendothelial intercellular communication.	Amino Acids, Basic	181-197	gap junction protein, alpha 5	Mus musculus	54-58
25483586-8	2014	These studies conclusively demonstrate the ability of Cx40 and Cx43 to form rectifying heterotypic gap junctions, owing primarily to alternate amino-terminal (NT) domain acidic and basic amino acid differences that may play a significant role in the physiology and/or pathology of the cardiovascular tissues including cardiac conduction properties and myoendothelial intercellular communication.	Amino Acids, Basic	181-197	gap junction protein, alpha 1	Mus musculus	63-67
24307932-0	2013	Structural location determines functional roles of the basic amino acids of KR-12, the smallest antimicrobial peptide from human cathelicidin LL-37.	Amino Acids, Basic	55-72	cathelicidin antimicrobial peptide	Homo sapiens	142-147
24167501-3	2013	Simultaneously and independently, Michel Chretien, based on amino acid sequence homologies between three pituitary peptides, beta-lipotropic hormone (beta-LPH), gamma-LPH, and beta-melanocyte-stimulating hormone (beta-MSH), concluded that active peptide hormones are derived from endoproteolytic cleavages of inactive precursors, apparently at pairs of basic amino acids (2).	Amino Acids, Basic	353-370	proopiomelanocortin	Homo sapiens	125-148
25763483-7	2014	The ectopic overexpression of a gene encoding a high affinity importer with preference to basic amino acids, such as lysine, cationic amino acid transporter1 (CAT1), improved the disease resistance to a hemibiotrophic bacterial pathogen in Arabidopsis via a constitutively activated salicylic acid pathway.	Amino Acids, Basic	90-107	amino acid transporter 1	Arabidopsis thaliana	125-157
25763483-7	2014	The ectopic overexpression of a gene encoding a high affinity importer with preference to basic amino acids, such as lysine, cationic amino acid transporter1 (CAT1), improved the disease resistance to a hemibiotrophic bacterial pathogen in Arabidopsis via a constitutively activated salicylic acid pathway.	Amino Acids, Basic	90-107	amino acid transporter 1	Arabidopsis thaliana	159-163
24142702-2	2013	Conserved in the ErbB family is a cluster of basic amino acid residues in the cytoplasmic juxtamembrane region.	Amino Acids, Basic	45-61	epidermal growth factor receptor	Homo sapiens	17-21
24255178-8	2013	Mutation of three basic amino acids that are part of a phospho-serine- and phospho-threonine-binding domain in human MOB1B prevented its interaction with MST1 and PP6 in cells treated with okadaic acid.	Amino Acids, Basic	18-35	MOB kinase activator 1B	Homo sapiens	117-122
24255178-8	2013	Mutation of three basic amino acids that are part of a phospho-serine- and phospho-threonine-binding domain in human MOB1B prevented its interaction with MST1 and PP6 in cells treated with okadaic acid.	Amino Acids, Basic	18-35	macrophage stimulating 1	Homo sapiens	154-158
24088021-0	2013	The role of basic amino acid surface clusters on the collagenase activity of cathepsin K.	Amino Acids, Basic	12-28	cathepsin K	Homo sapiens	77-88
24088021-10	2013	This study suggests that the basic amino acid clusters in cathepsin K are involved in alternative glycoasaminoglycan binding sites, play other roles in the formation of collagenolytically active protease complexes, or contribute in a yet unknown manner to the specific binding to collagen.	Amino Acids, Basic	29-45	cathepsin K	Homo sapiens	58-69
24396277-4	2013	The first characterized seven PCSK enzymes (PCSK1-2, FURIN, PCSK4-7) process their substrates at a motif made up of paired basic amino acid residues.	Amino Acids, Basic	123-139	proprotein convertase subtilisin/kexin type 1	Homo sapiens	44-51
24396277-4	2013	The first characterized seven PCSK enzymes (PCSK1-2, FURIN, PCSK4-7) process their substrates at a motif made up of paired basic amino acid residues.	Amino Acids, Basic	123-139	furin, paired basic amino acid cleaving enzyme	Homo sapiens	53-58
24396277-4	2013	The first characterized seven PCSK enzymes (PCSK1-2, FURIN, PCSK4-7) process their substrates at a motif made up of paired basic amino acid residues.	Amino Acids, Basic	123-139	proprotein convertase subtilisin/kexin type 4	Homo sapiens	60-67
23994058-1	2013	Inhibitor of DNA binding/differentiation 2 (Id2) belongs to a family of transcriptional modulators characterized by a helix-loop-helix (HLH) motif that lacks the basic amino acid domain necessary to bind DNA.	Amino Acids, Basic	162-178	inhibitor of DNA binding 2	Rattus norvegicus	44-47
24065103-0	2013	Basic amino acid residues of human eosinophil derived neurotoxin essential for glycosaminoglycan binding.	Amino Acids, Basic	0-16	ribonuclease A family member 2	Homo sapiens	35-64
24048853-6	2013	Loss-of-function experiments in zebrafish embryos demonstrate that OlfCc1 is required for olfactory responses to a diverse mixture of polar, nonpolar, acidic, and basic amino acids.	Amino Acids, Basic	163-180	vomeronasal 2, receptor 1	Danio rerio	67-73
24065103-5	2013	Furthermore, in silico computer modeling and in vitro binding assays suggest critical roles for the following basic amino acids located within heparin binding regions (HBRs) of EDN 34QRRCKN39 (HBR1), 65NKTRKN70 (HBR2), and 113NRDQRRD119 (HBR3) and in particular Arg35, Arg36, and Arg38 within HBR1, and Arg114 and Arg117 within HBR3.	Amino Acids, Basic	110-127	ribonuclease A family member 2	Homo sapiens	177-180
24010665-0	2013	CD44 receptor unfolding enhances binding by freeing basic amino acids to contact carbohydrate ligand.	Amino Acids, Basic	52-69	CD44 molecule (Indian blood group)	Homo sapiens	0-4
23969157-6	2013	Furthermore, we studied the effects of two clusters of basic amino acids located at the proximal region of Val274 on the cell surface expression and function of PROKR2.	Amino Acids, Basic	55-72	prokineticin receptor 2	Homo sapiens	161-167
23515315-10	2013	Examination of the structure revealed a cluster of conserved basic amino acids that protrude from the surface of Hha on the opposite side of the Hha/H-NS(1-46) interface.	Amino Acids, Basic	61-78	anosmin 1	Homo sapiens	113-116
24019944-0	2013	Basic amino acid mutations in the nuclear localization signal of hibiscus chlorotic ringspot virus p23 inhibit virus long distance movement.	Amino Acids, Basic	0-16	prostaglandin E synthase 3	Homo sapiens	99-102
23771350-6	2013	Mutagenesis analysis indicated that two basic amino acids, (84)K and (87)R, are essential to the function of NLS1, and that their mutation prevents interactions of Arx with importin alphas.	Amino Acids, Basic	40-57	major facilitator superfamily domain containing 2A	Homo sapiens	109-113
23771350-6	2013	Mutagenesis analysis indicated that two basic amino acids, (84)K and (87)R, are essential to the function of NLS1, and that their mutation prevents interactions of Arx with importin alphas.	Amino Acids, Basic	40-57	aristaless related homeobox	Homo sapiens	164-167
23836915-9	2013	These results support the idea that the chromosome binding of EBNA1 is mediated by electrostatic interactions between the basic amino acids within the CBDs and negatively charged cellular chromatin.	Amino Acids, Basic	122-139	EBNA-1	Human gammaherpesvirus 4	62-67
23442571-1	2013	Cpe(fat/fat) mice have a point mutation in carboxypeptidase E (Cpe), an exopeptidase that removes C-terminal basic amino acids from intermediates to produce bioactive peptides.	Amino Acids, Basic	109-126	carboxypeptidase E	Mus musculus	0-3
23442571-1	2013	Cpe(fat/fat) mice have a point mutation in carboxypeptidase E (Cpe), an exopeptidase that removes C-terminal basic amino acids from intermediates to produce bioactive peptides.	Amino Acids, Basic	109-126	carboxypeptidase E	Mus musculus	43-61
23442571-1	2013	Cpe(fat/fat) mice have a point mutation in carboxypeptidase E (Cpe), an exopeptidase that removes C-terminal basic amino acids from intermediates to produce bioactive peptides.	Amino Acids, Basic	109-126	carboxypeptidase E	Mus musculus	63-66
23639616-10	2013	Furthermore, basic amino acids on Rad52 CTR are highly conserved among mammalian, avian, and fish homologues, suggesting that Rad52 CTR is important for the regulation and function of Rad52 in vertebrates.	Amino Acids, Basic	13-30	RAD52 homolog, DNA repair protein	Homo sapiens	34-39
23639616-10	2013	Furthermore, basic amino acids on Rad52 CTR are highly conserved among mammalian, avian, and fish homologues, suggesting that Rad52 CTR is important for the regulation and function of Rad52 in vertebrates.	Amino Acids, Basic	13-30	calcitonin receptor	Homo sapiens	40-43
23639616-10	2013	Furthermore, basic amino acids on Rad52 CTR are highly conserved among mammalian, avian, and fish homologues, suggesting that Rad52 CTR is important for the regulation and function of Rad52 in vertebrates.	Amino Acids, Basic	13-30	RAD52 homolog, DNA repair protein	Homo sapiens	126-131
23639616-10	2013	Furthermore, basic amino acids on Rad52 CTR are highly conserved among mammalian, avian, and fish homologues, suggesting that Rad52 CTR is important for the regulation and function of Rad52 in vertebrates.	Amino Acids, Basic	13-30	calcitonin receptor	Homo sapiens	132-135
23639616-10	2013	Furthermore, basic amino acids on Rad52 CTR are highly conserved among mammalian, avian, and fish homologues, suggesting that Rad52 CTR is important for the regulation and function of Rad52 in vertebrates.	Amino Acids, Basic	13-30	RAD52 homolog, DNA repair protein	Homo sapiens	126-131
23510645-0	2013	Intact structure of EGAM1 homeoproteins and basic amino acid residues in the common homeodomain of EGAM1 and EGAM1C contribute to their nuclear localization in mouse embryonic stem cells.	Amino Acids, Basic	44-60	cone-rod homeobox, opposite strand	Mus musculus	99-104
23510645-6	2013	The introduction of mutations, such as mutations from K or R, both basic amino acid residues, to A, in this potential NLS resulted in significant impairment of the nuclear localization of both EGAM1 and EGAM1C.	Amino Acids, Basic	67-83	cone-rod homeobox, opposite strand	Mus musculus	193-198
23510645-8	2013	These results, when taken together, suggest that basic amino acid residues in the common homeodomain of EGAM1 and EGAM1C and the intact structures of the EGAM1 homeoproteins contribute, at least in part, to the nuclear localization of these proteins in mouse ES cells.	Amino Acids, Basic	49-65	cone-rod homeobox, opposite strand	Mus musculus	104-109
23510645-8	2013	These results, when taken together, suggest that basic amino acid residues in the common homeodomain of EGAM1 and EGAM1C and the intact structures of the EGAM1 homeoproteins contribute, at least in part, to the nuclear localization of these proteins in mouse ES cells.	Amino Acids, Basic	49-65	cone-rod homeobox, opposite strand	Mus musculus	114-119
23667177-4	2013	A human MCP-1 mutant in which basic amino acids Arg-18 and Lys-19 were replaced with Ala did not bind to OxLDL.	Amino Acids, Basic	30-47	C-C motif chemokine ligand 2	Homo sapiens	8-13
23734709-0	2013	Insights into the mechanism by which interferon-gamma basic amino acid clusters mediate protein binding to heparan sulfate.	Amino Acids, Basic	54-70	interferon gamma	Homo sapiens	37-53
23840386-2	2013	By site-directed mutatgenesis, we have previously shown that basic amino acids in positions 143 and 192 (Arg and Lys respectively) of the human mast cell chymase are responsible for an acidic amino acid residue preference in the P2" position of substrates.	Amino Acids, Basic	61-78	chymase 1	Homo sapiens	154-161
23439307-7	2013	The cell surface protein SasA, which is rich in basic amino acids (BR domain) at the N terminus, was responsible for binding to gp340.	Amino Acids, Basic	48-65	deleted in malignant brain tumors 1	Homo sapiens	128-133
23515315-10	2013	Examination of the structure revealed a cluster of conserved basic amino acids that protrude from the surface of Hha on the opposite side of the Hha/H-NS(1-46) interface.	Amino Acids, Basic	61-78	anosmin 1	Homo sapiens	145-148
23468493-6	2013	In this study, we tested whether ORF2 interacts with nucleic acids, because it contains 18% basic amino acids and localizes to the nucleus.	Amino Acids, Basic	92-109	OFD1, centriole and centriolar satellite protein	Mus musculus	33-37
23360476-7	2013	The interaction with CS-E required a decasaccharide length and a cluster of basic amino acids.	Amino Acids, Basic	76-93	cystathionase (cystathionine gamma-lyase)	Mus musculus	21-25
23546015-4	2013	Kv11.1 contains several conserved basic amino acids in the fourth transmembrane segment (S4) of the voltage sensor that are important for normal channel trafficking and gating.	Amino Acids, Basic	34-51	potassium voltage-gated channel subfamily H member 2	Homo sapiens	0-6
23663834-2	2013	Although the R174W mutation neutralizes the innermost basic amino acid in the voltage-sensing S4 helix of the first conserved membrane repeat of CaV1.1, the ability of the mutant channel to engage excitation-contraction coupling was largely unaffected by the introduction of the bulky tryptophan residue.	Amino Acids, Basic	54-70	calcium voltage-gated channel subunit alpha1 S	Homo sapiens	145-151
23357641-7	2013	Site-directed mutagenesis of the MAM domain revealed that multiple basic amino acid residues in the putative loop regions were involved in the binding of the MAM domain to agrin.	Amino Acids, Basic	67-83	agrin	Mus musculus	172-177
23460677-5	2013	Moreover, the basic amino acids within the luminal domain of PEX26 were essential for binding to PEX19 and thereby for peroxisomal targeting.	Amino Acids, Basic	14-31	Pex19p	Saccharomyces cerevisiae S288C	97-102
23266416-0	2013	The quantitative assessment of the role played by basic amino acid clusters in the nuclear uptake of human ribosomal protein L7.	Amino Acids, Basic	50-66	ribosomal protein L7	Homo sapiens	107-127
23123190-5	2013	In addition, we have identified a nuclear localization signal (NLS)-like motif within the primary amino acid sequence of ASK1 composed of two clusters of basic amino acids separated by an intervening 16 amino acid spacer, KR[ACANDLLVDEFLKVSS]KKKK.	Amino Acids, Basic	154-171	mitogen-activated protein kinase kinase kinase 5	Homo sapiens	121-125
23266416-2	2013	The system was first validated by a FRAP assay, and then was applied to evaluate the essential and multifaceted nature of basic amino acid clusters during the nuclear import of ribosomal protein L7.	Amino Acids, Basic	122-138	ribosomal protein L7	Homo sapiens	177-197
22714012-1	2013	GPRC6A is a seven-transmembrane receptor activated by a wide range of L-alpha-amino acids, most potently by L-arginine and other basic amino acids.	Amino Acids, Basic	129-146	G protein-coupled receptor, family C, group 6, member A	Mus musculus	0-6
23369442-4	2013	V3 loop envelop glycoprotein gp120 sequence changes that are predictive of a CXCR4 (X4)-using phenotype in HIV-1 subtype B primary isolates, specifically basic amino acid substations at positions 11 (S11R), 24 (G24R) and 25 (D25K) of the loop were detected in the two infected macaques.	Amino Acids, Basic	154-170	C-X-C motif chemokine receptor 4	Macaca mulatta	77-82
23009930-0	2013	Modification of SR-PSOX functions by multi-point mutations of basic amino acid residues.	Amino Acids, Basic	62-78	C-X-C motif chemokine ligand 16	Homo sapiens	16-23
23009930-2	2013	Our previous studies demonstrated that basic amino acid residues in the chemokine domain of SR-PSOX are critical for its functions.	Amino Acids, Basic	39-55	C-X-C motif chemokine ligand 16	Homo sapiens	92-99
23009930-3	2013	In this study the combinations of the key basic amino acids in the chemokine domain of SR-PSOX have been identified.	Amino Acids, Basic	42-59	C-X-C motif chemokine ligand 16	Homo sapiens	87-94
23009930-4	2013	Five combinations of basic amino acid residues that may form conformational motif for SR-PSOX functions were selected for multi-point mutants.	Amino Acids, Basic	21-37	C-X-C motif chemokine ligand 16	Homo sapiens	86-93
23009930-10	2013	This study revealed that some conformational motifs of basic amino acid residues, especially R76 with K79 in SR-PSOX, may form a common functional motif for its critical functions.	Amino Acids, Basic	55-71	keratin 79	Homo sapiens	102-105
23009930-10	2013	This study revealed that some conformational motifs of basic amino acid residues, especially R76 with K79 in SR-PSOX, may form a common functional motif for its critical functions.	Amino Acids, Basic	55-71	C-X-C motif chemokine ligand 16	Homo sapiens	109-116
23361001-5	2013	The escape of FKBP38 and Bcl-2 from the mitochondria is determined by the number of basic amino acids in their COOH-terminal signal sequences.	Amino Acids, Basic	84-101	FKBP prolyl isomerase 8	Homo sapiens	14-20
23811565-10	2013	The region responsible for nuclear localization of Drosophila RecQ5 contained a short stretch of positively charged basic amino acids, 2 of which were particularly important for the nuclear localization.	Amino Acids, Basic	116-133	RecQ5 helicase	Drosophila melanogaster	62-67
24018691-1	2013	A vacuolar membrane protein, Vba2p of Schizosaccharomyces pombe, is involved in basic amino acid uptake by intact cells.	Amino Acids, Basic	80-96	Vba2p	Saccharomyces cerevisiae S288C	29-34
23166320-4	2013	Two stretches of basic amino acids (basic motifs) are present in p17 N and C termini.	Amino Acids, Basic	17-34	family with sequence similarity 72 member B	Homo sapiens	65-68
23361001-5	2013	The escape of FKBP38 and Bcl-2 from the mitochondria is determined by the number of basic amino acids in their COOH-terminal signal sequences.	Amino Acids, Basic	84-101	BCL2 apoptosis regulator	Homo sapiens	25-30
23301044-5	2013	Fra-1, another member of the FOS family of proteins, is over-expressed in human breast cancer cells and its BD is highly homologous to that of c-Fos with two conservative substitutions in its basic amino acids.	Amino Acids, Basic	192-209	FOS like 1, AP-1 transcription factor subunit	Homo sapiens	0-5
23301044-5	2013	Fra-1, another member of the FOS family of proteins, is over-expressed in human breast cancer cells and its BD is highly homologous to that of c-Fos with two conservative substitutions in its basic amino acids.	Amino Acids, Basic	192-209	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	143-148
23301044-5	2013	Fra-1, another member of the FOS family of proteins, is over-expressed in human breast cancer cells and its BD is highly homologous to that of c-Fos with two conservative substitutions in its basic amino acids.	Amino Acids, Basic	192-209	Fos proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	29-32
22733759-10	2012	PI(3,5)P(2) activation and PI(4,5)P(2) inhibition of TRPML1 were mediated by distinct basic amino acid residues in a common PIP(2)-interacting domain.	Amino Acids, Basic	86-102	mucolipin TRP cation channel 1	Homo sapiens	53-59
22591857-5	2012	In the present study, we determined the motifs responsible for the nuclear localization of ASL18/LBD16 by using protoplast transfection assays with a variety N- or C-terminal deletion polypeptide fragments and the polypeptides harboring changes in basic amino acids that are fused to enhanced green fluorescent protein.	Amino Acids, Basic	248-265	lateral organ boundaries-domain 16	Arabidopsis thaliana	91-96
22591857-5	2012	In the present study, we determined the motifs responsible for the nuclear localization of ASL18/LBD16 by using protoplast transfection assays with a variety N- or C-terminal deletion polypeptide fragments and the polypeptides harboring changes in basic amino acids that are fused to enhanced green fluorescent protein.	Amino Acids, Basic	248-265	lateral organ boundaries-domain 16	Arabidopsis thaliana	97-102
22591857-6	2012	The results demonstrated that ASL18/LBD16 harbors two distinct domains comprising an atypical nuclear localization signal (NLS) with basic amino acid residues in the coiled-coil motif and a monopartite-like NLS in the C-terminal region for nuclear targeting.	Amino Acids, Basic	133-149	lateral organ boundaries-domain 16	Arabidopsis thaliana	30-35
22591857-6	2012	The results demonstrated that ASL18/LBD16 harbors two distinct domains comprising an atypical nuclear localization signal (NLS) with basic amino acid residues in the coiled-coil motif and a monopartite-like NLS in the C-terminal region for nuclear targeting.	Amino Acids, Basic	133-149	lateral organ boundaries-domain 16	Arabidopsis thaliana	36-41
22409200-4	2012	For example, a 17+ ion of bovine ubiquitin was formed by nESI of a 100 mM ammonium bicarbonate, pH 7.0, solution, which is three more charges than the total number of basic amino acids plus the N-terminus.	Amino Acids, Basic	167-184	ubiquitin	Bos taurus	33-42
22615398-7	2012	We further showed that the interaction with Geminin is homeodomain subclass-selective and Hox paralog-specific, which relies on the stapling role of residues R43 and M54 in helix III and the basic amino acid cluster in the N terminus.	Amino Acids, Basic	191-207	geminin DNA replication inhibitor	Homo sapiens	44-51
22667591-7	2012	Our model properly describes the saturation of lipids on membrane surfaces, and correctly predicts that the MARCKS peptide can consistently sequester three multivalent phosphatidylinositol 4,5-bisphosphate lipids through its basic amino acid residues, regardless of a wide range of the percentage of monovalent phosphatidylserine in the membrane.	Amino Acids, Basic	225-241	myristoylated alanine rich protein kinase C substrate	Homo sapiens	108-114
22790219-3	2012	The NLS sequence of PTHrP is not exception to this finding; however, PTHrP(87-107) contains 2 acidic glutamate residues at 99 and 101 within the basic amino acid stretch, which is not commonly observed in other CPPs such as HIV-1 Tat(48-60).	Amino Acids, Basic	145-161	parathyroid hormone like hormone	Homo sapiens	20-25
22790219-3	2012	The NLS sequence of PTHrP is not exception to this finding; however, PTHrP(87-107) contains 2 acidic glutamate residues at 99 and 101 within the basic amino acid stretch, which is not commonly observed in other CPPs such as HIV-1 Tat(48-60).	Amino Acids, Basic	145-161	parathyroid hormone like hormone	Homo sapiens	69-74
22157759-7	2012	Substitution of six basic amino acid residues within the CaM-binding domain (CaM-BD) of the EGFR by alanine resulted in a decreased phosphorylation of the receptor and of its downstream substrate phospholipase Cgamma1.	Amino Acids, Basic	20-36	calmodulin 1	Homo sapiens	57-60
22303007-2	2012	CRL4(Cdt2) substrates contain a "PIP degron," which consists of a canonical proliferating cell nuclear antigen (PCNA) interaction motif (PIP box) and an adjacent basic amino acid.	Amino Acids, Basic	162-178	denticleless E3 ubiquitin protein ligase homolog S homeolog	Xenopus laevis	5-9
22303007-5	2012	This PCNA residue, which adjoins the basic amino acid of the bound PIP degron, is dispensable for substrate binding to PCNA but essential for CRL4(Cdt2) recruitment to chromatin.	Amino Acids, Basic	37-53	proliferating cell nuclear antigen S homeolog	Xenopus laevis	5-9
22303007-5	2012	This PCNA residue, which adjoins the basic amino acid of the bound PIP degron, is dispensable for substrate binding to PCNA but essential for CRL4(Cdt2) recruitment to chromatin.	Amino Acids, Basic	37-53	denticleless E3 ubiquitin protein ligase homolog S homeolog	Xenopus laevis	147-151
21948871-8	2012	Site-directed mutational analysis revealed that the basic amino acid residues located in two putative carbohydrate-binding sites (CBSs) of ZG16p, which were found in association with the crystal structure of BanLec, are responsible for the recognition of heparin.	Amino Acids, Basic	52-68	zymogen granule protein 16	Rattus norvegicus	139-144
22155237-4	2012	This basic amino acid is important in maintaining the upstream consensus sequence for PKA phosphorylation of Ser 16 in PLN.	Amino Acids, Basic	5-21	phospholamban	Homo sapiens	119-122
22286034-7	2012	From the relationship between structures of chimeric peptides and their corresponding plasma half-lives, the mid-region of ghrelin rich in basic amino acids ((15)RKESKK(20)) was considered to be the most important in prolonging the plasma half-life of motilin.	Amino Acids, Basic	139-156	ghrelin and obestatin prepropeptide	Rattus norvegicus	123-130
22157759-7	2012	Substitution of six basic amino acid residues within the CaM-binding domain (CaM-BD) of the EGFR by alanine resulted in a decreased phosphorylation of the receptor and of its downstream substrate phospholipase Cgamma1.	Amino Acids, Basic	20-36	calmodulin 1	Homo sapiens	77-80
22157759-7	2012	Substitution of six basic amino acid residues within the CaM-binding domain (CaM-BD) of the EGFR by alanine resulted in a decreased phosphorylation of the receptor and of its downstream substrate phospholipase Cgamma1.	Amino Acids, Basic	20-36	epidermal growth factor receptor	Homo sapiens	92-96
23047103-1	2012	Vba5p is closest to Vba3p in the vacuolar transporter for basic amino acids (VBA) family of Saccharomyces cerevisiae.	Amino Acids, Basic	58-75	basic amino acid transporter	Saccharomyces cerevisiae S288C	0-5
21671897-0	2012	Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop.	Amino Acids, Basic	107-124	purinergic receptor P2X 1	Homo sapiens	47-60
23047103-1	2012	Vba5p is closest to Vba3p in the vacuolar transporter for basic amino acids (VBA) family of Saccharomyces cerevisiae.	Amino Acids, Basic	58-75	basic amino acid transporter	Saccharomyces cerevisiae S288C	20-25
21700711-1	2011	The basic amino acid-specific proprotein convertase 5/6 (PC5/6) is an essential secretory protease, as knock-out mice die at birth and exhibit multiple homeotic transformation defects, including impaired bone morphogenesis and lung structure.	Amino Acids, Basic	4-20	proprotein convertase subtilisin/kexin type 5	Mus musculus	30-53
21788334-7	2011	In contrast to the yeast protein, the C terminus of PAPD5 contains a stretch of basic amino acids that is involved in binding the RNA substrate.	Amino Acids, Basic	80-97	terminal nucleotidyltransferase 4B	Homo sapiens	52-57
23300734-8	2012	This study shows that there exists a complex interplay between the basic amino acids located in HVR1 and other conserved E2 motifs with the HS, the SR-BI, and neutralizing antibodies and suggests that HCV-associated lipoproteins are implicated in these interactions.	Amino Acids, Basic	67-84	scavenger receptor class B member 1	Homo sapiens	148-153
22479563-1	2012	Carboxypeptidase M (CPM) targets the basic amino acids arginine and lysine present at the C-terminus of peptides or proteins.	Amino Acids, Basic	37-54	carboxypeptidase M	Homo sapiens	0-18
22479563-1	2012	Carboxypeptidase M (CPM) targets the basic amino acids arginine and lysine present at the C-terminus of peptides or proteins.	Amino Acids, Basic	37-54	carboxypeptidase M	Homo sapiens	20-23
22479563-5	2012	CCL1/I-309, with its three C-terminal basic amino acids, forms a potential natural substrate for CPM.	Amino Acids, Basic	38-55	C-C motif chemokine ligand 1	Homo sapiens	0-4
22479563-5	2012	CCL1/I-309, with its three C-terminal basic amino acids, forms a potential natural substrate for CPM.	Amino Acids, Basic	38-55	carboxypeptidase M	Homo sapiens	97-100
22069260-3	2011	Pathogenic T cells recognize the B:9-23 peptide presented by I-Ag7 in what is termed register 3, with the B22 basic amino acid (arginine) of the peptide bound in pocket 9 of I-Ag7.	Amino Acids, Basic	110-126	I-ag7	Mus musculus	61-66
22069260-3	2011	Pathogenic T cells recognize the B:9-23 peptide presented by I-Ag7 in what is termed register 3, with the B22 basic amino acid (arginine) of the peptide bound in pocket 9 of I-Ag7.	Amino Acids, Basic	110-126	I-ag7	Mus musculus	174-179
21700711-1	2011	The basic amino acid-specific proprotein convertase 5/6 (PC5/6) is an essential secretory protease, as knock-out mice die at birth and exhibit multiple homeotic transformation defects, including impaired bone morphogenesis and lung structure.	Amino Acids, Basic	4-20	proprotein convertase subtilisin/kexin type 5	Mus musculus	57-62
21543646-5	2011	In this study, we report that these basic amino acids enable CD3 zeta to complex the phosphoinositides PtdIns(3)P, PtdIns(4)P, PtdIns(5)P, PtdIns(3,5)P(2), and PtdIns(3,4,5)P(3) with high affinity.	Amino Acids, Basic	36-53	CD247 molecule	Homo sapiens	61-69
21690087-4	2011	We identified a minimal NLS in hPLSCR4 ((273)GSIIRKWN(280)) that contains only two basic amino acids.	Amino Acids, Basic	83-100	phospholipid scramblase 4	Homo sapiens	31-38
21515688-8	2011	Homology modeling and mutagenesis identified a cluster of basic amino acid residues (Lys(51), Arg(56), and Arg(80)) on the surface of human CTRC that interact with the P4" acidic residue of the inhibitor.	Amino Acids, Basic	58-74	chymotrypsin C	Homo sapiens	140-144
21447033-6	2011	Ephrin-B3 binding to B lymphocytes is partially affected by heparin, and a basic amino acid in the extracellular juxtamembrane region, Arg-188, is here shown to be involved in this binding.	Amino Acids, Basic	75-91	ephrin B3	Homo sapiens	0-9
21454486-10	2011	A series of mutation analysis indicated that the basic amino acids at the C terminus of IL2 loop may function cooperatively in GPCRs.	Amino Acids, Basic	49-66	interleukin 2	Homo sapiens	88-91
21513304-3	2011	The purified GGT had an optimal pH and temperature of 10 and 37  C, respectively, and it was stable at pH 4.0-11.0 or <50  C. The enzyme exhibited the highest affinity to imino acids (L-Pro) and then decreasing affinities for aromatic amino acids, ethylamine and basic amino acids.	Amino Acids, Basic	266-283	gamma-glutamyltransferase 2, pseudogene	Homo sapiens	13-16
21228347-3	2011	Furthermore, the extent to which a cis-acting CD3epsilon basic amino acid-rich stretch (BRS), with its unique phosphoinositide-binding capability, might impact PRS accessibility is not clear.	Amino Acids, Basic	57-73	CD3 antigen, epsilon polypeptide	Mus musculus	46-56
21490302-8	2011	Resequencing analysis pinpointed the association to a histidine (basic amino acid) for aspartic acid (acidic amino acid) substitution in the encoded protein domain that defines GST substrate specificity and biochemical activity.	Amino Acids, Basic	65-81	glutathione S-transferase	Zea mays	177-180
21492481-0	2011	Function modification of SR-PSOX by point mutations of basic amino acids.	Amino Acids, Basic	55-72	C-X-C motif chemokine ligand 16	Homo sapiens	25-32
21492481-5	2011	In this study the key basic amino acids in the chemokine domain of SR-PSOX have been identified for its functions.	Amino Acids, Basic	22-39	C-X-C motif chemokine ligand 16	Homo sapiens	67-74
21492481-9	2011	In addition, we have also found that mutagenesis of either of those amino acids strongly reduced the adhesive activity of SR-PSOX by using a highly non-overlapping set of basic amino acid residues.	Amino Acids, Basic	171-187	C-X-C motif chemokine ligand 16	Homo sapiens	122-129
21492481-10	2011	CONCLUSION: Our study demonstrates that basic amino acid residues in the non-conservative region of the chemokine domain of SR-PSOX are critical for its functions.	Amino Acids, Basic	40-56	C-X-C motif chemokine ligand 16	Homo sapiens	124-131
21492481-12	2011	All the basic amino acids in this region are important in the cells adhesion via SR-PSOX.	Amino Acids, Basic	8-25	C-X-C motif chemokine ligand 16	Homo sapiens	81-88
21492481-13	2011	These findings suggest that mutagenesis of the basic amino acids in the chemokine domain of SR-PSOX may contribute to atherogenesis.	Amino Acids, Basic	47-64	C-X-C motif chemokine ligand 16	Homo sapiens	92-99
21188584-2	2011	We found that the peptides containing basic amino acids (cations) at N -terminus and tyrosine at C-terminus interfered with activating ability of PGN.	Amino Acids, Basic	38-55	SPG7 matrix AAA peptidase subunit, paraplegin	Homo sapiens	146-149
21239886-2	2011	We examined the binding of the F loop (P1107-A1121) in SPRY2 to the ASI/basic region in RyR1 (T3471-G3500, containing both alternatively spliced (ASI) residues and neighboring basic amino acids).	Amino Acids, Basic	176-193	sprouty RTK signaling antagonist 2	Homo sapiens	55-60
21444752-1	2011	Cell-surface retention sequence (CRS) binding protein (CRSBP-1) is a membrane glycoprotein identified by its ability to bind PDGF-BB and VEGF-A via their CRS motifs (clusters of basic amino acid residues).	Amino Acids, Basic	178-194	lymphatic vessel endothelial hyaluronan receptor 1	Mus musculus	55-62
21444752-1	2011	Cell-surface retention sequence (CRS) binding protein (CRSBP-1) is a membrane glycoprotein identified by its ability to bind PDGF-BB and VEGF-A via their CRS motifs (clusters of basic amino acid residues).	Amino Acids, Basic	178-194	vascular endothelial growth factor A	Mus musculus	137-143
21360678-5	2011	Mutation of PP5, replacing key basic amino acids (K97A and R101A) in the tetratricopeptide repeat (TPR) region known to be necessary for the interactions with Hsp90, abolished both the known interaction of PP5 with cell division cycle 37 homolog and the novel interaction of PP5 with stress-induced phosphoprotein 1.	Amino Acids, Basic	31-48	protein phosphatase 5 catalytic subunit	Homo sapiens	12-15
21360678-5	2011	Mutation of PP5, replacing key basic amino acids (K97A and R101A) in the tetratricopeptide repeat (TPR) region known to be necessary for the interactions with Hsp90, abolished both the known interaction of PP5 with cell division cycle 37 homolog and the novel interaction of PP5 with stress-induced phosphoprotein 1.	Amino Acids, Basic	31-48	heat shock protein 90 alpha family class A member 1	Homo sapiens	159-164
21360678-5	2011	Mutation of PP5, replacing key basic amino acids (K97A and R101A) in the tetratricopeptide repeat (TPR) region known to be necessary for the interactions with Hsp90, abolished both the known interaction of PP5 with cell division cycle 37 homolog and the novel interaction of PP5 with stress-induced phosphoprotein 1.	Amino Acids, Basic	31-48	stress induced phosphoprotein 1	Homo sapiens	284-315
21209099-2	2011	Among the proprotein convertases (PCs), only the membrane-bound PC7, the most ancient and conserved basic amino acid-specific PC family member, induces the processing of pro-EGF into an ~115-kDa transmembrane form (EGF-115) at an unusual VHPR(290) A motif.	Amino Acids, Basic	100-116	proprotein convertase subtilisin/kexin type 7	Homo sapiens	64-67
21071054-2	2011	Basic amino acid substitutions at position 11 were strong determinants of CXCR4-mediated entry but required multiple compensatory mutations to overcome associated reductions in infectivity.	Amino Acids, Basic	0-16	C-X-C motif chemokine receptor 4	Homo sapiens	74-79
21071054-3	2011	In contrast, basic amino acid substitutions at position 25, or substitutions at positions 6-8 resulting in the loss of a potential N-linked glycosylation site, contributed to CXCR4-mediated entry but required additional substitutions acting cooperatively to confer efficient CXCR4 use.	Amino Acids, Basic	13-29	C-X-C motif chemokine receptor 4	Homo sapiens	175-180
21071054-3	2011	In contrast, basic amino acid substitutions at position 25, or substitutions at positions 6-8 resulting in the loss of a potential N-linked glycosylation site, contributed to CXCR4-mediated entry but required additional substitutions acting cooperatively to confer efficient CXCR4 use.	Amino Acids, Basic	13-29	C-X-C motif chemokine receptor 4	Homo sapiens	275-280
21512259-7	2011	The identified region (aa337-aa470) responsible for nuclear localization of dG9a contains four short stretches of positively charged basic amino acids (NLS1, aa334-aa345; NLS2, aa366-aa378; NLS3, aa407-aa419; NLS4, aa461-aa472).	Amino Acids, Basic	133-150	G9a	Drosophila melanogaster	76-80
21047682-6	2010	Alignment of the IML2 sequences revealed that UCP1, UCP2 and UCP3 share a basic amino acid in positions 163, 164 and 167, while only UCP2 and UCP3 contain a second basic residue in positions 168 and 171, respectively.	Amino Acids, Basic	74-90	uncoupling protein 1	Homo sapiens	46-50
21143559-6	2011	Electrostatic surface images suggest that the basic amino acid at +4 is involved in a contact with PCNA, while +3 position extending to opposite direction is important to create a positively charged surface.	Amino Acids, Basic	46-62	proliferating cell nuclear antigen	Homo sapiens	99-103
20655338-1	2010	Carboxypeptidase E (CPE) is an exopeptidase that removes C-terminal basic amino acids from a variety of bioactive peptides.	Amino Acids, Basic	68-85	carboxypeptidase E	Mus musculus	0-18
20655338-1	2010	Carboxypeptidase E (CPE) is an exopeptidase that removes C-terminal basic amino acids from a variety of bioactive peptides.	Amino Acids, Basic	68-85	carboxypeptidase E	Mus musculus	20-23
20937035-3	2010	A basic amino acid-rich motif in LIMK2 was previously identified to be responsible for this shuttling function, as a nucleolar localization signal (NoLS).	Amino Acids, Basic	2-18	LIM motif-containing protein kinase 2	Mus musculus	33-38
21047682-6	2010	Alignment of the IML2 sequences revealed that UCP1, UCP2 and UCP3 share a basic amino acid in positions 163, 164 and 167, while only UCP2 and UCP3 contain a second basic residue in positions 168 and 171, respectively.	Amino Acids, Basic	74-90	uncoupling protein 2	Homo sapiens	52-56
21047682-6	2010	Alignment of the IML2 sequences revealed that UCP1, UCP2 and UCP3 share a basic amino acid in positions 163, 164 and 167, while only UCP2 and UCP3 contain a second basic residue in positions 168 and 171, respectively.	Amino Acids, Basic	74-90	uncoupling protein 3	Homo sapiens	61-65
20573066-8	2010	This led us to identify a cluster of basic amino acids (KKH) in the TC10 hypervariable region, constituting a secondary signal potentially involved in electrostatic interactions with membrane lipids.	Amino Acids, Basic	37-54	ras homolog family member Q	Homo sapiens	68-72
20676391-0	2010	The Role of Basic Amino Acids in the Molecular Recognition of Hydroxyapatite by Statherin using Solid State NMR.	Amino Acids, Basic	12-29	statherin	Homo sapiens	80-89
20483925-4	2010	In this study, a non-GAG-binding variant of NNY-CCL14 was generated by mutating basic amino acids within the identified GAG-binding 49BBXB52 motif.	Amino Acids, Basic	80-97	melanoma antigen	Mus musculus	21-24
20567258-5	2010	We also demonstrated that the region of amino acids 8-42 in pericentrin contains a tripartite nuclear localization signal (NLS) consisting of three clusters of basic amino acids.	Amino Acids, Basic	160-177	pericentrin	Homo sapiens	60-71
20483925-4	2010	In this study, a non-GAG-binding variant of NNY-CCL14 was generated by mutating basic amino acids within the identified GAG-binding 49BBXB52 motif.	Amino Acids, Basic	80-97	melanoma antigen	Mus musculus	120-123
20634319-2	2010	For the Drosophila Hox protein Sex combs reduced (Scr), Exd has been shown to position a normally unstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove of an Scr-specific DNA-binding site.	Amino Acids, Basic	138-154	tinman	Drosophila melanogaster	19-22
20471598-4	2010	Based on adsorption yield and residual activity of glutathione S-transferase (GST) after fusion with the PS19-6 peptide or its variants, it was found that the basic amino acid in the PS-tags, i.e., Arg was essential for the strong binding affinity of PS-tags in both the peptide and peptide-fused protein forms The aliphatic amino acids in PS19-6 and PS19-6L, such as Ile or Leu, were also effective.	Amino Acids, Basic	159-175	glutathione S-transferase kappa 1	Homo sapiens	51-76
20634319-2	2010	For the Drosophila Hox protein Sex combs reduced (Scr), Exd has been shown to position a normally unstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove of an Scr-specific DNA-binding site.	Amino Acids, Basic	138-154	Sex combs reduced	Drosophila melanogaster	50-53
20634319-2	2010	For the Drosophila Hox protein Sex combs reduced (Scr), Exd has been shown to position a normally unstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove of an Scr-specific DNA-binding site.	Amino Acids, Basic	138-154	extradenticle	Drosophila melanogaster	56-59
20634319-2	2010	For the Drosophila Hox protein Sex combs reduced (Scr), Exd has been shown to position a normally unstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove of an Scr-specific DNA-binding site.	Amino Acids, Basic	138-154	Sex combs reduced	Drosophila melanogaster	122-125
20634319-2	2010	For the Drosophila Hox protein Sex combs reduced (Scr), Exd has been shown to position a normally unstructured portion of Scr so that two basic amino acid side chains can insert into the minor groove of an Scr-specific DNA-binding site.	Amino Acids, Basic	138-154	Sex combs reduced	Drosophila melanogaster	122-125
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	tyrosine aminotransferase	Homo sapiens	0-3
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	CD44 molecule (Indian blood group)	Homo sapiens	56-84
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	CD44 molecule (Indian blood group)	Homo sapiens	86-90
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	tyrosine aminotransferase	Homo sapiens	162-165
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	tyrosine aminotransferase	Homo sapiens	162-165
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	kinase insert domain receptor	Homo sapiens	224-269
20398703-2	2010	Tat possesses a basic amino acid sequence implicated in heparan sulfate proteoglycan (HSPG)-mediated internalization, nuclear localization and transactivation by Tat and in the interaction of Tat with integrins and with the vascular endothelial growth factor receptor 2 (KDR) (kinase insert domain receptor).	Amino Acids, Basic	16-32	kinase insert domain receptor	Homo sapiens	271-274
20471598-4	2010	Based on adsorption yield and residual activity of glutathione S-transferase (GST) after fusion with the PS19-6 peptide or its variants, it was found that the basic amino acid in the PS-tags, i.e., Arg was essential for the strong binding affinity of PS-tags in both the peptide and peptide-fused protein forms The aliphatic amino acids in PS19-6 and PS19-6L, such as Ile or Leu, were also effective.	Amino Acids, Basic	159-175	glutathione S-transferase kappa 1	Homo sapiens	78-81
20143133-4	2010	Polypeptides encoded by 5" 24 bp of exons 17 and 18 are part of basic amino-acid-rich region inside Esrom RCC1-like domain (RLD).	Amino Acids, Basic	64-80	MYC binding protein 2	Danio rerio	100-105
20215589-2	2010	This interaction involves the C-terminal sequence of APX3 (i.e., a transmembrane domain plus a few basic amino acid residues).	Amino Acids, Basic	99-115	ascorbate peroxidase 3	Arabidopsis thaliana	53-57
20172963-3	2010	We investigated the biological role of the basic amino acid carrier Basic Amino Acid Carrier2 (BAC2) from Arabidopsis that is structurally and functionally similar to ARG11, a yeast ornithine and arginine carrier, and to Arabidopsis BAC1.	Amino Acids, Basic	43-59	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	68-93
20075868-4	2010	We show that a basic amino-acid motif within its N-terminus is required for nucleolar retention and for interaction with nucleophosmin (NPM).	Amino Acids, Basic	15-31	nucleophosmin 1	Homo sapiens	121-134
20075868-4	2010	We show that a basic amino-acid motif within its N-terminus is required for nucleolar retention and for interaction with nucleophosmin (NPM).	Amino Acids, Basic	15-31	nucleophosmin 1	Homo sapiens	136-139
21779451-5	2010	Here, the authors have identified 2 highly conserved clusters of basic amino acid residues that are essential for the RNA binding activity of Pdcd4.	Amino Acids, Basic	65-81	programmed cell death 4	Homo sapiens	142-147
20172963-3	2010	We investigated the biological role of the basic amino acid carrier Basic Amino Acid Carrier2 (BAC2) from Arabidopsis that is structurally and functionally similar to ARG11, a yeast ornithine and arginine carrier, and to Arabidopsis BAC1.	Amino Acids, Basic	43-59	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	95-99
20172963-3	2010	We investigated the biological role of the basic amino acid carrier Basic Amino Acid Carrier2 (BAC2) from Arabidopsis that is structurally and functionally similar to ARG11, a yeast ornithine and arginine carrier, and to Arabidopsis BAC1.	Amino Acids, Basic	43-59	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	233-237
20172963-8	2010	Our data suggest that BAC2 is a hyperosmotic stress-inducible transporter of basic amino acids that contributes to proline accumulation in response to hyperosmotic stress in Arabidopsis.	Amino Acids, Basic	77-94	Mitochondrial substrate carrier family protein	Arabidopsis thaliana	22-26
20188097-0	2010	Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.	Amino Acids, Basic	15-31	protein kinase C and casein kinase substrate in neurons 2	Homo sapiens	119-126
20188097-0	2010	Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II.	Amino Acids, Basic	15-31	protein kinase C and casein kinase substrate in neurons 2	Homo sapiens	127-138
20188097-4	2010	The hydrophobic loops and the basic amino-acid residues on the concave surface of the pacsin2 EFC/F-BAR domain are essential for both the microspike formation and tubulation.	Amino Acids, Basic	30-46	protein kinase C and casein kinase substrate in neurons 2	Homo sapiens	86-93
19700767-4	2009	Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain.	Amino Acids, Basic	90-107	proline and arginine rich end leucine rich repeat protein	Homo sapiens	26-31
20051954-7	2010	We show that the nuclear localisation signal of EWS-Oct-4B is dependent on the POU DNA-binding domain, and we identified a cluster of basic amino acids, (269)RKRKR(273), in the POU domain that specifically mediates the nuclear localisation of EWS-Oct-4B.	Amino Acids, Basic	134-151	EWS RNA binding protein 1	Homo sapiens	48-51
20051954-7	2010	We show that the nuclear localisation signal of EWS-Oct-4B is dependent on the POU DNA-binding domain, and we identified a cluster of basic amino acids, (269)RKRKR(273), in the POU domain that specifically mediates the nuclear localisation of EWS-Oct-4B.	Amino Acids, Basic	134-151	EWS RNA binding protein 1	Homo sapiens	243-246
19920768-5	2010	We found that there were eight basic amino acids downstream of the AI domain within the region (384-397), which were also involved in Best3 activation.	Amino Acids, Basic	31-48	bestrophin 3	Homo sapiens	134-139
19920768-6	2010	Mutations of these basic amino acids significantly activated Best3 as a Cl channel.	Amino Acids, Basic	19-36	bestrophin 3	Homo sapiens	61-66
20944394-0	2010	Vba2p, a vacuolar membrane protein involved in basic amino acid transport in Schizosaccharomyces pombe.	Amino Acids, Basic	47-63	Vba2p	Saccharomyces cerevisiae S288C	0-5
20944394-1	2010	A recent study filling the gap in the genome sequence in the left arm of chromosome 2 of Schizosaccharomyces pombe revealed a homolog of budding yeast Vba2p, a vacuolar transporter of basic amino acids.	Amino Acids, Basic	184-201	Vba2p	Saccharomyces cerevisiae S288C	151-156
20944394-5	2010	These findings suggest that Vba2p is involved in basic amino acid transport in S. pombe under diverse conditions.	Amino Acids, Basic	49-65	Vba2p	Saccharomyces cerevisiae S288C	28-33
19920768-7	2010	Led by the assumption that the basic amino acids may be involved in the Best3 C-terminal membrane association through binding to membranous phospholipids, we discovered that PI3Kalpha inhibitor IV could strongly activate Best3.	Amino Acids, Basic	31-48	bestrophin 3	Homo sapiens	72-77
19920768-7	2010	Led by the assumption that the basic amino acids may be involved in the Best3 C-terminal membrane association through binding to membranous phospholipids, we discovered that PI3Kalpha inhibitor IV could strongly activate Best3.	Amino Acids, Basic	31-48	bestrophin 3	Homo sapiens	221-226
19861127-4	2009	Mutations of basic amino acids within IC do not perturb the membrane position, but reduce shedding of the CA IX ectodomain as well as CA IX-mediated cell dissociation.	Amino Acids, Basic	13-30	carbonic anhydrase 9	Homo sapiens	106-111
19861127-4	2009	Mutations of basic amino acids within IC do not perturb the membrane position, but reduce shedding of the CA IX ectodomain as well as CA IX-mediated cell dissociation.	Amino Acids, Basic	13-30	carbonic anhydrase 9	Homo sapiens	134-139
19700767-4	2009	Two other family members, PRELP and chondroadherin, have distinctly different clusters of basic amino acids in their N and C termini, respectively, and PRELP is known to bind to heparin via this domain.	Amino Acids, Basic	90-107	chondroadherin	Homo sapiens	36-50
19700767-5	2009	Another heparin-binding protein is the cytokine Oncostatin M, with a different cluster of basic amino acids in its C terminus.	Amino Acids, Basic	90-107	oncostatin M	Homo sapiens	48-60
19496756-8	2009	C-terminal deletion and point mutations of PI3K-C2beta demonstrated that epidermal growth factor-driven translocation to the nucleus is dependent on a sequence of basic amino acid residues (KxKxK) that form a nuclear localization motif within the C-terminal C2 domain.	Amino Acids, Basic	163-179	phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta	Homo sapiens	43-54
19582790-4	2009	Three distinct motifs can be discerned in the SRrp37 protein: (1) a serine-arginine (SR) dipeptide enriched domain, (2) a polyserine stretch, and (3) a potential nucleolar localization signal comprising a long array of basic amino acids.	Amino Acids, Basic	219-236	ADP ribosylation factor like GTPase 6 interacting protein 4	Homo sapiens	46-52
19657145-7	2009	This was due to a short stretch of basic amino acids located at the N terminus of the collagen domain that confers EDA1 with proteoglycan binding ability.	Amino Acids, Basic	35-52	ectodysplasin-A	Mus musculus	115-119
19707690-2	2009	Here we highlight a crucial role of a basic amino acid triad the entrance of the heme pocket in rHSA (Arg-114, His-146, Lys-190) for O(2) and CO binding to the prosthetic Fe(2+)PP group.	Amino Acids, Basic	38-54	CD24 molecule	Rattus norvegicus	96-100
19515423-5	2009	We show that nuclear transport of SOCS1 particularly depends on the second cluster of basic amino acid residues within the NLS.	Amino Acids, Basic	86-102	suppressor of cytokine signaling 1	Homo sapiens	34-39
19496756-8	2009	C-terminal deletion and point mutations of PI3K-C2beta demonstrated that epidermal growth factor-driven translocation to the nucleus is dependent on a sequence of basic amino acid residues (KxKxK) that form a nuclear localization motif within the C-terminal C2 domain.	Amino Acids, Basic	163-179	epidermal growth factor	Homo sapiens	73-96
19391098-3	2009	Aromatic amino acids have low ionization energies, are easily oxidized and delocalize the charge and spin over the ring systems; basic amino acids facilitate formation of alpha-radicals that have captodative structures in which the charge and spin are formally separated, although feeding back some of the charge onto the amide or carboxyl group adjacent to the radical center through hydrogen bonding enriches the electron-withdrawing properties and is highly stabilizing.	Amino Acids, Basic	129-146	spindlin 1	Homo sapiens	243-247
19595719-4	2009	Using Xenopus egg extracts, we identify two sequence elements in CRL4(Cdt2) substrates that promote their proteolysis: a specialized PIP box that confers exceptionally efficient PCNA binding and a basic amino acid 4 residues downstream of the PIP box, which recruits CRL4(Cdt2) to the substrate-PCNA complex.	Amino Acids, Basic	197-213	denticleless E3 ubiquitin protein ligase homolog S homeolog	Xenopus laevis	70-74
19422463-5	2009	The FXIII-B*3 isoform had a C-terminus 15 residues longer than the other isoforms, containing two additional basic amino acids and one extra acidic amino acid.	Amino Acids, Basic	109-126	coagulation factor XIII B chain	Homo sapiens	4-11
19413971-2	2009	The nonreceptor tyrosine kinase Src is equipped with an N-terminal myristoyl chain and a cluster of basic amino acids for the stable membrane association of the protein.	Amino Acids, Basic	100-117	SRC proto-oncogene, non-receptor tyrosine kinase	Homo sapiens	32-35
19208757-4	2009	USP36 localized to nucleoli via the C-terminal region, which contains basic amino acid stretches.	Amino Acids, Basic	70-86	ubiquitin specific peptidase 36	Homo sapiens	0-5
19218565-5	2009	Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17.	Amino Acids, Basic	56-72	importin 13	Homo sapiens	155-166
19218565-5	2009	Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17.	Amino Acids, Basic	56-72	chromatin accessibility complex subunit 1	Homo sapiens	203-211
19218565-5	2009	Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17.	Amino Acids, Basic	56-72	DNA polymerase epsilon 3, accessory subunit	Homo sapiens	212-220
19218565-5	2009	Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17.	Amino Acids, Basic	56-72	DNA polymerase epsilon 4, accessory subunit	Homo sapiens	225-228
19218565-5	2009	Mutational analysis shows that stepwise substitution of basic amino acid residues conserved among the histone fold subunits leads to a progressive loss of importin 13 binding and nuclear accumulation of CHRAC-15/CHRAC-17 and p12/CHRAC-17.	Amino Acids, Basic	56-72	DNA polymerase epsilon 3, accessory subunit	Homo sapiens	229-237
19218565-6	2009	The distribution of basic amino acid residues among the histone fold subunits essential for nuclear uptake suggests that heterodimerization of the histone fold motif-containing proteins forms an importin 13-specific binding platform.	Amino Acids, Basic	20-36	importin 13	Homo sapiens	195-206
19204001-8	2009	The results let us propose that the interaction between basic amino acid residues and the negatively charged exit tunnel of the ribosome leads to translation arrest followed by Not4p-mediated ubiquitination and protein degradation by the proteasome.	Amino Acids, Basic	56-72	CCR4-NOT transcription complex subunit 4	Homo sapiens	177-182
19342663-5	2009	Additional experiments show that the membrane proximal basic amino acid rich sequence in the IC domain of CD3epsilon is sufficient for the DN to DP differentiation, whereas the proline rich sequence is required for efficient proliferation.	Amino Acids, Basic	55-71	CD3 antigen, epsilon polypeptide	Mus musculus	106-116
18847325-1	2009	Carboxypeptidase Z (CPZ) removes carboxyl-terminal basic amino acid residues, particularly arginine residues, from proteins.	Amino Acids, Basic	51-67	carboxypeptidase Z	Rattus norvegicus	0-18
19234454-7	2009	Dsh recruitment by Fz can be abolished by converting these basic amino-acid residues into acidic ones, as in the mutant, DshKR/E.	Amino Acids, Basic	59-75	dishevelled	Drosophila melanogaster	0-3
18847325-1	2009	Carboxypeptidase Z (CPZ) removes carboxyl-terminal basic amino acid residues, particularly arginine residues, from proteins.	Amino Acids, Basic	51-67	carboxypeptidase Z	Rattus norvegicus	20-23
19340293-3	2009	GDAP1 is a mitochondrial fission factor with two neighboring hydrophobic domains each flanked by basic amino acids (aa).	Amino Acids, Basic	97-114	ganglioside induced differentiation associated protein 1	Homo sapiens	0-5
19084525-3	2009	We found that point mutations of several basic amino acids in the PPIase domain of Pin1 significantly compromise its nuclear localization.	Amino Acids, Basic	41-58	peptidylprolyl cis/trans isomerase, NIMA-interacting 1	Homo sapiens	83-87
19053255-5	2008	Intriguingly, UL42-NLSbip is composed of two stretches of basic amino acids matching the consensus for classical monopartite NLSs (NLSA, PTTKRGR(397); NLSB, KKPK(413)), neither of which are capable of targeting GFP to the nucleus on their own, consistent with the hypothesis that P and G residues in position +3 of monopartite NLSs are not compatible with nuclear transport in the absence of additional basic sequences located in close proximity.	Amino Acids, Basic	58-75	DNA polymerase processivity subunit	Human alphaherpesvirus 1	14-18
19390581-0	2009	Clusters of basic amino acids contribute to RNA binding and nucleolar localization of ribosomal protein L22.	Amino Acids, Basic	12-29	ribosomal protein L22	Homo sapiens	86-107
18378898-1	2008	The proprotein convertase PC5/6 cleaves protein precursors after basic amino acids and is essential for implantation in CD1/129/Sv/C57BL/6 mixed-background mice.	Amino Acids, Basic	65-82	proprotein convertase subtilisin/kexin type 5	Mus musculus	4-29
18653447-8	2008	Component I of the PARS overlaps the DBIS but can be differentiated from the DBIS by specific substitution of basic amino acid residues.	Amino Acids, Basic	110-126	glutamyl-prolyl-tRNA synthetase 1	Homo sapiens	19-23
18373558-5	2008	Amino acids encoded by exons 19 and 20 of 4.1B and a stretch of four basic amino acids present in the mGluR8 C-termini mediate the protein interaction.	Amino Acids, Basic	69-86	glutamate receptor, metabotropic 8	Mus musculus	102-108
18329376-0	2008	Nucleolar targeting of proteins by the tandem array of basic amino acid stretches identified in the RNA polymerase I-associated factor PAF49.	Amino Acids, Basic	55-71	RNA polymerase I subunit G	Homo sapiens	100-140
18329376-4	2008	Combinatorial point mutation analysis indicated that the individual basic amino acid stretches (BS) within the central (BS1-4) and the C-terminal (BS5 and 6) regions may cooperatively confer the nucleolar localization of PAF49.	Amino Acids, Basic	68-84	negative regulator of ubiquitin like proteins 1	Homo sapiens	120-125
18329376-4	2008	Combinatorial point mutation analysis indicated that the individual basic amino acid stretches (BS) within the central (BS1-4) and the C-terminal (BS5 and 6) regions may cooperatively confer the nucleolar localization of PAF49.	Amino Acids, Basic	68-84	RNA polymerase I subunit G	Homo sapiens	221-226
18593381-5	2008	Replacement of Gln(181) by aspartic acid resulted in a significant change in substrate specificity, with Q181D ERAP-1 showing a preference for basic amino acids.	Amino Acids, Basic	143-160	endoplasmic reticulum aminopeptidase 1	Homo sapiens	111-117
18593381-6	2008	In addition, Q181D ERAP-1 cleaved natural peptides possessing a basic amino acid at the N-terminal end more efficiently than did the wild-type enzyme, whereas its cleavage of peptides with a non-basic amino acid was significantly reduced.	Amino Acids, Basic	64-80	endoplasmic reticulum aminopeptidase 1	Homo sapiens	19-25
18330902-5	2008	Nuclear localization of hTAF(II)68-TEC was dependent on the DNA binding domain, and we identified a cluster of basic amino acids in the DNA binding domain, KRRR, that specifically mediate the nuclear localization of hTAF(II)68-TEC.	Amino Acids, Basic	111-128	TATA-box binding protein associated factor 15	Homo sapiens	24-34
18330902-5	2008	Nuclear localization of hTAF(II)68-TEC was dependent on the DNA binding domain, and we identified a cluster of basic amino acids in the DNA binding domain, KRRR, that specifically mediate the nuclear localization of hTAF(II)68-TEC.	Amino Acids, Basic	111-128	TATA-box binding protein associated factor 15	Homo sapiens	216-226
17981585-6	2008	Enzymatic properties of the recombinant soluble MSPL and TMPRSS13 show that these enzymes preferentially recognize the sites consisting of paired basic amino acid residues, and are strongly inhibited by aprotinin, benzamidine and Bowman-Birk trypsin inhibitor, but poorly inhibited by alpha 1-antitrypsin and leupeptin.	Amino Acids, Basic	146-162	transmembrane serine protease 13	Homo sapiens	48-52
18285446-2	2008	Although anchored to the membrane by means of glycosylphosphatidylinositol (GPI), PrPC on neurons is rapidly and constitutively endocytosed by means of coated pits, a property dependent upon basic amino acids at its N-terminus.	Amino Acids, Basic	191-208	prion protein	Homo sapiens	82-86
17981585-6	2008	Enzymatic properties of the recombinant soluble MSPL and TMPRSS13 show that these enzymes preferentially recognize the sites consisting of paired basic amino acid residues, and are strongly inhibited by aprotinin, benzamidine and Bowman-Birk trypsin inhibitor, but poorly inhibited by alpha 1-antitrypsin and leupeptin.	Amino Acids, Basic	146-162	transmembrane serine protease 13	Homo sapiens	57-65
17981585-6	2008	Enzymatic properties of the recombinant soluble MSPL and TMPRSS13 show that these enzymes preferentially recognize the sites consisting of paired basic amino acid residues, and are strongly inhibited by aprotinin, benzamidine and Bowman-Birk trypsin inhibitor, but poorly inhibited by alpha 1-antitrypsin and leupeptin.	Amino Acids, Basic	146-162	serpin family A member 1	Homo sapiens	285-318
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	proprotein convertase subtilisin/kexin type 1	Homo sapiens	60-65
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	keratin 6B	Homo sapiens	67-70
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	furin, paired basic amino acid cleaving enzyme	Homo sapiens	72-77
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	keratin 6B	Homo sapiens	79-82
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	proprotein convertase subtilisin/kexin type 5	Homo sapiens	84-89
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	proprotein convertase subtilisin/kexin type 6	Homo sapiens	91-96
18343183-2	2008	Seven of them cleave after basic amino acids and are called PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7.	Amino Acids, Basic	27-44	proprotein convertase subtilisin/kexin type 7	Homo sapiens	101-104
18681934-5	2008	* Momentaneous root uptake of basic amino acids was strongly affected in AAP5 mutant lines, but their uptake of other types of amino acids was only marginally affected.	Amino Acids, Basic	30-47	amino acid permease 5	Arabidopsis thaliana	73-77
17638012-9	2007	Furthermore, the removal of the outermost basic amino acids from the IVS4 and IIIS4 and, to a lesser extent, from IS4 segments stabilised the open state of the channel, whereas neutralization from that of IIS4 destabilised it.	Amino Acids, Basic	42-59	IS4	Homo sapiens	80-83
18712106-4	2007	Furin is a very specific enzyme: it recognizes the cleavage-site sequence Arg-Xaa-Lys/Arg-Arg and catalyzes the hydrolysis of the precursors, containing a pair of basic amino acids Arg-Arg or Lys-Arg.	Amino Acids, Basic	163-180	furin, paired basic amino acid cleaving enzyme	Homo sapiens	0-5
17608956-11	2007	For the DRB1*1302 allele for instance, the TEPITOPE method favors basic amino acids at most anchor positions, whereas the SMM-align method identifies a preference for hydrophobic or neutral amino acids at the anchors.	Amino Acids, Basic	66-83	dopamine receptor binding 1	Mus musculus	8-12
17658762-6	2007	These adducts could have significant effects considering that His-33, Lys-72, and Lys-100 are present in clusters of basic amino acid residues, which are believed to participate in the interaction of cytochrome c with cardiolipin in the inner mitochondrial membrane and cytochrome c oxidase.	Amino Acids, Basic	117-133	cytochrome c, somatic	Homo sapiens	200-212
17658762-6	2007	These adducts could have significant effects considering that His-33, Lys-72, and Lys-100 are present in clusters of basic amino acid residues, which are believed to participate in the interaction of cytochrome c with cardiolipin in the inner mitochondrial membrane and cytochrome c oxidase.	Amino Acids, Basic	117-133	cytochrome c, somatic	Homo sapiens	270-282
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	membrane bound transcription factor peptidase, site 1	Homo sapiens	213-218
17563123-6	2007	The influence of improved solvation on substrate specificity determination was successfully demonstrated by the difference in specificity observed between the two libraries employing the human cathepsin S (accepts acidic, basic, or neutral amino acids at P1 position) and Dengue 2 virus NS2B-NS3 protease (high specificity to the pair of basic amino acids K-R, R-R, or Q-R/K at P2-P1 positions).	Amino Acids, Basic	338-355	cathepsin S	Homo sapiens	193-204
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 1	Homo sapiens	148-153
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	membrane bound transcription factor peptidase, site 1	Homo sapiens	220-246
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 2	Homo sapiens	155-158
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	furin, paired basic amino acid cleaving enzyme	Homo sapiens	160-165
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 4	Homo sapiens	167-170
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 5	Homo sapiens	172-177
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 6	Homo sapiens	179-184
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 7	Homo sapiens	189-192
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	membrane bound transcription factor peptidase, site 1	Homo sapiens	248-251
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	membrane bound transcription factor peptidase, site 1	Homo sapiens	253-268
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 9	Homo sapiens	274-279
17351764-1	2007	The family of the secretory proprotein convertases (PCs) comprises seven basic amino acid (aa)-specific subtilisin-like serine proteinases known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other PCs, SKI-1 (subtilisin-kexin isozyme-1)/S1P (site-1 protease) and PCSK9 (proprotein convertase subtilisin kexin 9) that cleave at nonbasic residues.	Amino Acids, Basic	73-89	proprotein convertase subtilisin/kexin type 9	Homo sapiens	281-321
17452462-4	2007	The PB1 domains bind in a front-to-back arrangement, with a cluster of basic amino acids in the front of the MEKK2 PB1 domain binding to the back-end acidic clusters of the MEK5 PB1 domain.	Amino Acids, Basic	71-88	submaxillary gland androgen regulated protein 3A	Homo sapiens	4-7
17536787-5	2007	Basic amino acids, predicted to constitute the putative heparin/heparan sulfate binding site of NKp44, were mutated.	Amino Acids, Basic	0-17	natural cytotoxicity triggering receptor 2	Homo sapiens	96-101
17376915-7	2007	NLS2 includes basic amino acids at positions 219, 220, 224, 229, 231, and 232.	Amino Acids, Basic	14-31	phosphoserine aminotransferase 1	Homo sapiens	0-4
17494888-7	2007	The N terminus mediates receptor binding, whereas two clusters of basic amino acid residues ((44)RKNR(47) and (55)KKWVR(59)) are involved in the presentation of CCL5 by extracellular structures.	Amino Acids, Basic	66-82	C-C motif chemokine ligand 5	Homo sapiens	161-165
17452462-4	2007	The PB1 domains bind in a front-to-back arrangement, with a cluster of basic amino acids in the front of the MEKK2 PB1 domain binding to the back-end acidic clusters of the MEK5 PB1 domain.	Amino Acids, Basic	71-88	mitogen-activated protein kinase kinase kinase 2	Homo sapiens	109-114
17452462-4	2007	The PB1 domains bind in a front-to-back arrangement, with a cluster of basic amino acids in the front of the MEKK2 PB1 domain binding to the back-end acidic clusters of the MEK5 PB1 domain.	Amino Acids, Basic	71-88	submaxillary gland androgen regulated protein 3A	Homo sapiens	115-118
17452462-4	2007	The PB1 domains bind in a front-to-back arrangement, with a cluster of basic amino acids in the front of the MEKK2 PB1 domain binding to the back-end acidic clusters of the MEK5 PB1 domain.	Amino Acids, Basic	71-88	mitogen-activated protein kinase kinase 5	Homo sapiens	173-177
17452462-4	2007	The PB1 domains bind in a front-to-back arrangement, with a cluster of basic amino acids in the front of the MEKK2 PB1 domain binding to the back-end acidic clusters of the MEK5 PB1 domain.	Amino Acids, Basic	71-88	submaxillary gland androgen regulated protein 3A	Homo sapiens	115-118
17064696-6	2006	These studies demonstrate that SK1 is cleaved by cathepsin B in a sequential manner after basic amino acids, and that the initial cleavages at the two identified sites occur independently of each other.	Amino Acids, Basic	90-107	sphingosine kinase 1	Homo sapiens	31-34
16973377-2	2007	Among these proteases, S1P displays unique substrate specificity, by showing preferred cleavage after non-basic amino acids.	Amino Acids, Basic	106-123	membrane bound transcription factor peptidase, site 1	Homo sapiens	23-26
17045734-10	2007	A hFSHR mutant with all basic amino acids present in the iL3 BXXBB motif replaced by alanine failed to bind agonist and activate effector, and was expressed as an immature < or =62kDa form of the receptor.	Amino Acids, Basic	24-41	follicle stimulating hormone receptor	Homo sapiens	2-7
17045734-10	2007	A hFSHR mutant with all basic amino acids present in the iL3 BXXBB motif replaced by alanine failed to bind agonist and activate effector, and was expressed as an immature < or =62kDa form of the receptor.	Amino Acids, Basic	24-41	interleukin 3	Homo sapiens	57-60
17165155-7	2007	RESULTS: All patients carried the same novel MSH2 germline missense mutation (R359S) in exon 7, which determines the substitution of an Arginine, which is a basic amino acid, with a polar Serine residue (R359S).	Amino Acids, Basic	157-173	mutS homolog 2	Homo sapiens	45-49
17534424-8	2007	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.	Amino Acids, Basic	35-52	chloride voltage-gated channel 6	Homo sapiens	185-190
17534424-8	2007	Mutating a juxtamembrane string of basic amino acids (amino acids 71-75: KKGRR) disturbs the association with detergent-resistant membrane fractions and also affects the segregation of ClC-6 and ClC-7 when cotransfected in COS-1 cells.	Amino Acids, Basic	35-52	chloride voltage-gated channel 7	Homo sapiens	195-200
17298301-2	2007	Deletion of a basic amino-acid-rich sequence of 16 residues N-terminal to the first cysteine of the transforming growth factor beta domain of GDNF results in a marked reduction in heparin binding, whereas removal of a neighbouring sequence, and replacement of pairs of other basic residues with alanine had no effect.	Amino Acids, Basic	14-30	glial cell derived neurotrophic factor	Homo sapiens	142-146
17376810-4	2007	ALE2 encodes a previously uncharacterized RLK with a cluster of basic amino acid residues followed by a cysteine-containing sequence in the putative extracellular domain.	Amino Acids, Basic	64-80	Protein kinase superfamily protein	Arabidopsis thaliana	0-4
17376810-4	2007	ALE2 encodes a previously uncharacterized RLK with a cluster of basic amino acid residues followed by a cysteine-containing sequence in the putative extracellular domain.	Amino Acids, Basic	64-80	cysteine-rich RLK (RECEPTOR-like protein kinase) 6	Arabidopsis thaliana	42-45
17341489-7	2007	In addition, increasing the intracellular levels of arginine through overexpression of Can1p, the plasma membrane basic amino acid permease, results in increased cell volume and a severe growth defect specific to basic amino acid availability for btn1-Delta, but not wild-type cells.	Amino Acids, Basic	114-130	arginine permease CAN1	Saccharomyces cerevisiae S288C	87-92
17341489-7	2007	In addition, increasing the intracellular levels of arginine through overexpression of Can1p, the plasma membrane basic amino acid permease, results in increased cell volume and a severe growth defect specific to basic amino acid availability for btn1-Delta, but not wild-type cells.	Amino Acids, Basic	114-130	amino acid transporter YHC3	Saccharomyces cerevisiae S288C	247-251
17341489-7	2007	In addition, increasing the intracellular levels of arginine through overexpression of Can1p, the plasma membrane basic amino acid permease, results in increased cell volume and a severe growth defect specific to basic amino acid availability for btn1-Delta, but not wild-type cells.	Amino Acids, Basic	213-229	arginine permease CAN1	Saccharomyces cerevisiae S288C	87-92
17341489-7	2007	In addition, increasing the intracellular levels of arginine through overexpression of Can1p, the plasma membrane basic amino acid permease, results in increased cell volume and a severe growth defect specific to basic amino acid availability for btn1-Delta, but not wild-type cells.	Amino Acids, Basic	213-229	amino acid transporter YHC3	Saccharomyces cerevisiae S288C	247-251
17391007-0	2007	Thermodynamic roles of basic amino acids in statherin recognition of hydroxyapatite.	Amino Acids, Basic	23-40	statherin	Homo sapiens	44-53
17283074-5	2007	In this study, we have shown that the juxtamembrane region of EGFR harbors a putative NLS with three clusters of basic amino acids (RRRHIVRKRTLRR (amino acids 645-657)) that mediates the nuclear localization of EGFR.	Amino Acids, Basic	113-130	epidermal growth factor receptor	Homo sapiens	62-66
17283074-5	2007	In this study, we have shown that the juxtamembrane region of EGFR harbors a putative NLS with three clusters of basic amino acids (RRRHIVRKRTLRR (amino acids 645-657)) that mediates the nuclear localization of EGFR.	Amino Acids, Basic	113-130	epidermal growth factor receptor	Homo sapiens	211-215
17283074-8	2007	We have demonstrated that mutating one of the three basic amino acid clusters (R or K --> A) leads to significant impairment of the nuclear localization of EGFR and that of a green fluorescent protein-pyruvate kinase-NLS reporter protein.	Amino Acids, Basic	52-68	epidermal growth factor receptor	Homo sapiens	159-163
17420605-3	2007	Each of four concentrated fractions extracted from sake (respectively consisting mainly of basic amino acids, neutral and acidic amino acids, organic acids and sugars) suppressed the GalN-induced elevation of ALT and AST activities.	Amino Acids, Basic	91-108	glutamic pyruvic transaminase, soluble	Mus musculus	209-212
17420605-3	2007	Each of four concentrated fractions extracted from sake (respectively consisting mainly of basic amino acids, neutral and acidic amino acids, organic acids and sugars) suppressed the GalN-induced elevation of ALT and AST activities.	Amino Acids, Basic	91-108	solute carrier family 17 (anion/sugar transporter), member 5	Mus musculus	217-220
17207774-5	2007	In order to understand the mechanism of neurotrophin processing, we focused on the two basic amino acid clusters in the pro-region of nerve growth factor (NGF).	Amino Acids, Basic	87-103	nerve growth factor	Rattus norvegicus	134-153
17207774-5	2007	In order to understand the mechanism of neurotrophin processing, we focused on the two basic amino acid clusters in the pro-region of nerve growth factor (NGF).	Amino Acids, Basic	87-103	nerve growth factor	Rattus norvegicus	155-158
17207774-7	2007	The results indicated that these basic amino acid clusters were actually cleaved in the cells by furin, but that their cleavage contributed little to the production of mature NGF.	Amino Acids, Basic	33-49	furin (paired basic amino acid cleaving enzyme)	Rattus norvegicus	97-102
18000017-10	2007	The basic amino acid motif shown to be required for PA binding in Raf-1 is conserved in CTR1-K.	Amino Acids, Basic	4-20	Raf-1 proto-oncogene, serine/threonine kinase	Homo sapiens	66-71
18000017-10	2007	The basic amino acid motif shown to be required for PA binding in Raf-1 is conserved in CTR1-K.	Amino Acids, Basic	4-20	Protein kinase superfamily protein	Arabidopsis thaliana	88-92
17202862-7	2006	These results suggest that some basic amino acid residues in IpTxa are important for activation of RyR1, and that Lys8 plays an important role in regulating the gating mode of RyR1.	Amino Acids, Basic	32-48	ryanodine receptor 1	Oryctolagus cuniculus	99-103
16963768-6	2006	However, when introduced into the full-length NTPase/helicase domains, these mutations caused a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I was required to maintain a reaction-competent conformation of the TGBp1 ATPase active site.	Amino Acids, Basic	186-202	inosine triphosphatase	Homo sapiens	46-52
16930531-5	2006	We produced mutants of FGF1 and p40 Syt1, in which specific basic amino acid residues in the regions that bind acidic pL were substituted.	Amino Acids, Basic	60-76	fibroblast growth factor 1	Homo sapiens	23-27
16930531-5	2006	We produced mutants of FGF1 and p40 Syt1, in which specific basic amino acid residues in the regions that bind acidic pL were substituted.	Amino Acids, Basic	60-76	interleukin 9	Homo sapiens	32-35
16930531-5	2006	We produced mutants of FGF1 and p40 Syt1, in which specific basic amino acid residues in the regions that bind acidic pL were substituted.	Amino Acids, Basic	60-76	synaptotagmin 1	Homo sapiens	36-40
17046996-3	2006	Here, we found that human podoplanin directly interacts with ezrin (and moesin) in vitro and in vivo through a cluster of basic amino acids within its cytoplasmic tail, mainly through a juxtamembrane dipeptide RK.	Amino Acids, Basic	122-139	podoplanin	Homo sapiens	26-36
17046996-3	2006	Here, we found that human podoplanin directly interacts with ezrin (and moesin) in vitro and in vivo through a cluster of basic amino acids within its cytoplasmic tail, mainly through a juxtamembrane dipeptide RK.	Amino Acids, Basic	122-139	moesin	Homo sapiens	72-78
16829516-2	2006	Three nuclear localization signals (NLSs), NLS1 (amino acids (aa 101-107), NLS2 (aa 121-130), and NLS3 (aa 143-152), were identified in the N terminus of the ORF57 protein, and each of the three represents a short stretch of basic amino acid residues.	Amino Acids, Basic	225-241	ORF57	Human gammaherpesvirus 8	158-163
16899214-4	2006	Parapoxvirus-encoded VEGFs (PV-VEGFs), which recognize KDR, possess basic amino acid clusters in their C-terminal regions.	Amino Acids, Basic	68-84	kinase insert domain receptor	Homo sapiens	55-58
16449324-6	2006	The basic amino acid residues direct nucleolar localization of SMN mutants.	Amino Acids, Basic	4-20	survival of motor neuron 1, telomeric	Homo sapiens	63-66
16820362-5	2006	Through site-directed mutagenesis, we identified the basic amino acid-rich motif KKRTLRKNDRKKR (amino acids 491-503) as the functional nuclear and nucleolar localization signal of LIMK2.	Amino Acids, Basic	53-69	LIM domain kinase 2	Homo sapiens	180-185
16820362-10	2006	Our findings identify a unique basic amino acid-rich motif (amino acids 491-503) in LIMK2 which is not present in LIMK1 that serves to target the protein not only to the nucleus but also to the nucleolus.	Amino Acids, Basic	31-47	LIM domain kinase 2	Homo sapiens	84-89
16913836-1	2006	The proprotein convertases represent a family of nine proteinases, comprising seven basic amino acid-specific subtilisin-like serine proteinases related to yeast kexin, known as PC1/3, PC2, furin, PC4, PC5/6, PACE4 and PC7, and two other subtilases that cleave at non-basic residues, called SKI-1/S1P and NARC-1/PCSK9.	Amino Acids, Basic	84-100	chromatin-binding exonuclease XRN1	Saccharomyces cerevisiae S288C	291-296
16875678-5	2006	RAC3 binds strongly to importin alpha3, which also depends on the basic amino acids.	Amino Acids, Basic	66-83	Rac family small GTPase 3	Homo sapiens	0-4
16875678-5	2006	RAC3 binds strongly to importin alpha3, which also depends on the basic amino acids.	Amino Acids, Basic	66-83	karyopherin subunit alpha 3	Homo sapiens	23-38
16873242-2	2006	In the present study, we generated a series of mutations in the normal prion protein (PrP(C)) in which a single glutamine residue was replaced with a basic amino acid and compared their abilities to convert to PrP(Sc) in cultured neuronal N2a58 cells infected with either the Chandler or 22L mouse-adapted scrapie strain.	Amino Acids, Basic	150-166	prion protein	Mus musculus	86-89
16841905-3	2006	Interestingly, two of the phage surface displayed peptides enriched with basic amino acid residues, STB1 (HKKPSKS) and STB2 (TKRNNKR), showed a cross binding affinity to both metal oxides.	Amino Acids, Basic	73-89	VANGL planar cell polarity protein 2	Homo sapiens	100-104
16841905-3	2006	Interestingly, two of the phage surface displayed peptides enriched with basic amino acid residues, STB1 (HKKPSKS) and STB2 (TKRNNKR), showed a cross binding affinity to both metal oxides.	Amino Acids, Basic	73-89	VANGL planar cell polarity protein 1	Homo sapiens	119-123
16818797-7	2006	We also report that FVIII-hydrolyzing IgG from each patient exhibit multiple cleavage sites on FVIII and that, while the specificity of cleavage varies from one patient to another, catalytic IgG preferentially hydrolyze peptide bonds containing basic amino acids.	Amino Acids, Basic	245-262	coagulation factor VIII	Homo sapiens	20-25
16641371-4	2006	We found that Chp membrane association and transforming activity was dependent on the integrity of a stretch of basic amino acids in the carboxy terminus of Chp and that the basic amino acids were not simply part of a palmitoyl acyltransferase recognition motif.	Amino Acids, Basic	112-129	ras homolog family member V	Homo sapiens	14-17
16641371-4	2006	We found that Chp membrane association and transforming activity was dependent on the integrity of a stretch of basic amino acids in the carboxy terminus of Chp and that the basic amino acids were not simply part of a palmitoyl acyltransferase recognition motif.	Amino Acids, Basic	112-129	ras homolog family member V	Homo sapiens	157-160
16525503-2	2006	Here, we demonstrate that such a motif consisting of four basic amino acids in the polyglutamine protein ataxin-3 (Atx-3) serves as a recognition site for the interaction with the molecular chaperone VCP.	Amino Acids, Basic	58-75	TER94	Drosophila melanogaster	200-203
16525503-5	2006	Strikingly, a stretch of four basic amino acids in the ubiquitin chain assembly factor E4B was also discovered to be critical for VCP binding, indicating that arginine/lysine-rich motifs might be generally utilized by VCP for the targeting of proteins.	Amino Acids, Basic	30-47	uncharacterized protein	Drosophila melanogaster	87-90
16525503-5	2006	Strikingly, a stretch of four basic amino acids in the ubiquitin chain assembly factor E4B was also discovered to be critical for VCP binding, indicating that arginine/lysine-rich motifs might be generally utilized by VCP for the targeting of proteins.	Amino Acids, Basic	30-47	TER94	Drosophila melanogaster	130-133
16525503-5	2006	Strikingly, a stretch of four basic amino acids in the ubiquitin chain assembly factor E4B was also discovered to be critical for VCP binding, indicating that arginine/lysine-rich motifs might be generally utilized by VCP for the targeting of proteins.	Amino Acids, Basic	30-47	TER94	Drosophila melanogaster	218-221
16491103-3	2006	Agonists for GPRC6A are basic amino acids, particularly the analogues and derivatives of L-arginine and L-ornithine.	Amino Acids, Basic	24-41	G protein-coupled receptor class C group 6 member A	Homo sapiens	13-19
16023765-3	2006	Amino acid sequence analysis showed cleavage sites located between two basic amino acids at Arg93-Arg94 resulting in the production of prepro-IMD(95-147), namely IMD(1-53).	Amino Acids, Basic	71-88	adrenomedullin 2	Rattus norvegicus	142-145
16284078-2	2006	To further examine the molecular basis for block, we mutated a portion of a basic amino acid (HKH) motif on the Cx40 amino-terminal domain.	Amino Acids, Basic	76-92	gap junction protein, alpha 5	Rattus norvegicus	112-116
16230346-9	2006	These studies identified a cluster of basic amino acids likely at the TM15/CL7 interface as a region important for both MRP1 expression and activity and demonstrated that each of the three residues plays a distinct role in the substrate specificity and catalytic activity of the transporter.	Amino Acids, Basic	38-55	ATP binding cassette subfamily B member 1	Homo sapiens	120-124
16039772-5	2006	In surface plasmon resonance (SPR) measurements, with FXa covalently attached to the sensor chip, we show that the FXa-binding site on AtxA includes several basic amino acid residues at the C-terminal and beta-wing regions of the molecule.	Amino Acids, Basic	157-173	coagulation factor X	Homo sapiens	115-118
16023765-3	2006	Amino acid sequence analysis showed cleavage sites located between two basic amino acids at Arg93-Arg94 resulting in the production of prepro-IMD(95-147), namely IMD(1-53).	Amino Acids, Basic	71-88	adrenomedullin 2	Rattus norvegicus	162-165
16363805-0	2005	A cluster of basic amino acid residues in the gamma370-381 sequence of fibrinogen comprises a binding site for platelet integrin alpha(IIb)beta3 (glycoprotein IIb/IIIa).	Amino Acids, Basic	13-29	fibrinogen beta chain	Homo sapiens	71-81
16166082-5	2005	Small clusters of basic amino acids in possible alpha-helical regions in TFII-I and IRAG were found to mediate their interaction with PKG Ibeta.	Amino Acids, Basic	18-35	general transcription factor IIi	Homo sapiens	73-79
16246571-7	2005	Tandem mass spectrometry of a synthetic peptide encompassing the C-terminal half of the structurally more labile second zinc finger of ER (ZnF2B) demonstrates that the two nucleophilic thiols in ZnF2B (Cys-237, Cys-240) are not chemically equivalent in their reactivity to bromobimane or menadione, consistent with their unequal positioning near basic amino acids that affect thiol pKa, thereby rendering Cys-240 more reactive than Cys-237.	Amino Acids, Basic	346-363	estrogen receptor 1	Homo sapiens	135-137
16166082-5	2005	Small clusters of basic amino acids in possible alpha-helical regions in TFII-I and IRAG were found to mediate their interaction with PKG Ibeta.	Amino Acids, Basic	18-35	inositol 1,4,5-triphosphate receptor associated 1	Homo sapiens	84-88
16166082-5	2005	Small clusters of basic amino acids in possible alpha-helical regions in TFII-I and IRAG were found to mediate their interaction with PKG Ibeta.	Amino Acids, Basic	18-35	protein kinase cGMP-dependent 1	Homo sapiens	134-137
16262248-5	2005	On the basis of both the electrostatic potential map and comparison to the heparin binding site on human fibronectin, we predicted a continuous region containing the basic amino acids K133, R136, H139, R142, and K146 to be involved in NKp46 binding to heparan sulfate.	Amino Acids, Basic	166-183	fibronectin 1	Homo sapiens	105-116
16007194-4	2005	E12 and E47 each contain two regions of basic amino acids, which, when mutated, lead to cytoplasmic accumulation of the proteins.	Amino Acids, Basic	40-57	epididymal sperm binding protein 1	Homo sapiens	0-3
16007194-4	2005	E12 and E47 each contain two regions of basic amino acids, which, when mutated, lead to cytoplasmic accumulation of the proteins.	Amino Acids, Basic	40-57	transcription factor 3	Homo sapiens	8-11
15935375-6	2005	Furthermore, the extracellular localization of the LOX-1 C-terminus is disrupted when we mutated the cytoplasmic basic amino acids, Lys-22, Lys-23 and Lys-25 to Glu.	Amino Acids, Basic	113-130	oxidized low density lipoprotein receptor 1	Homo sapiens	51-56
15995960-6	2005	The presence of basic amino acids at codon 11 and/or codon 25 of HIV-1 V3 (n = 109 of 955; 11.4%) was associated with a 9.1 times higher risk of harboring X4 variants (multivariate P < .0001), regardless of CCR5 Delta 32 genotype.	Amino Acids, Basic	16-33	C-C motif chemokine receptor 5	Homo sapiens	210-214
15946855-3	2005	HR6B participates in "N-end rule degradation" that is implicated in the cleavage of proteins with destabilizing N-terminal residues (bulky hydrophobic or basic amino acids) and requires UBR1, the ubiquitin ligase binding N-end rule target proteins.	Amino Acids, Basic	154-171	ubiquitin-conjugating enzyme E2B	Rattus norvegicus	0-4
15946855-3	2005	HR6B participates in "N-end rule degradation" that is implicated in the cleavage of proteins with destabilizing N-terminal residues (bulky hydrophobic or basic amino acids) and requires UBR1, the ubiquitin ligase binding N-end rule target proteins.	Amino Acids, Basic	154-171	ubiquitin protein ligase E3 component n-recognin 1	Rattus norvegicus	186-190
16055207-4	2005	By transiently transfecting RL-34 cells with various mutated rat CAR segments, we identified two nuclear localization signals: a basic amino acid-rich sequence (RRARQARRR) between amino acids 100 and 108; and an assembly of noncontiguous residues widely spread over amino acid residues 111 to 320 within the ligand binding domain.	Amino Acids, Basic	129-145	nuclear receptor subfamily 1, group I, member 3	Rattus norvegicus	65-68
16262248-5	2005	On the basis of both the electrostatic potential map and comparison to the heparin binding site on human fibronectin, we predicted a continuous region containing the basic amino acids K133, R136, H139, R142, and K146 to be involved in NKp46 binding to heparan sulfate.	Amino Acids, Basic	166-183	natural cytotoxicity triggering receptor 1	Homo sapiens	235-240
16101009-8	2005	At the P2" position, TACE can accommodate basic amino acids, such as arginine and lysine, as well as certain non-basic amino acids such as citrulline, methionine sulfoxide and threonine.	Amino Acids, Basic	42-59	ADAM metallopeptidase domain 17	Homo sapiens	21-25
15806159-2	2005	Deletion of an amphiphilic basic amino-acid sequence (residues 243-256) predicted to form an alpha-helix located in the proximal region of its pleckstrin homology (PH) domain demonstrates the location of the CaM-binding domain.	Amino Acids, Basic	27-43	calmodulin 1	Homo sapiens	208-211
15899858-5	2005	Basic amino acid residues within the nucleolar targeting domain are important for both retaining CDC14B in the nucleolus and preventing microtubule bundling.	Amino Acids, Basic	0-16	cell division cycle 14B	Homo sapiens	97-103
15817634-3	2005	Using large-scale mutagenesis, acidic and basic amino acids putatively involved in ion transport mediated by the predominant variant of NBC1 expressed in the kidney (kNBC1) were mutated to neutral and/or oppositely charged amino acids.	Amino Acids, Basic	42-59	solute carrier family 4 member 4	Homo sapiens	136-140
15851487-4	2005	We show that the TNF homology domain of APRIL binds BCMA and TACI, whereas a basic amino acid sequence (QKQKKQ) close to the NH2 terminus of the mature protein is required for binding to the APRIL-specific "receptor."	Amino Acids, Basic	77-93	TNF superfamily member 13	Homo sapiens	191-196
15896001-3	2005	The lipid binding domain of apoE has been localized to the carboxyl-terminal domain, whereas a cluster of basic amino acid residues within the N-terminal domain is responsible for its receptor binding activity.	Amino Acids, Basic	106-122	apolipoprotein E	Homo sapiens	28-32
15896001-10	2005	Taken together, these results localized the antioxidant domain of apoE to its receptor binding domain and the basic amino acids in this domain are important for its antioxidant activity.	Amino Acids, Basic	110-127	apolipoprotein E	Homo sapiens	66-70
15944009-4	2005	Within the sequence of human GALP (1-60) a potential proteolytic cleavage site between two basic amino acids is present at position 33, which might lead to a shorter C-terminally amidated peptide.	Amino Acids, Basic	91-108	galanin like peptide	Homo sapiens	29-33
15726636-9	2005	Docking the structure of the FMN domain of human cytochrome P450 reductase to the CYP2D6 model suggests that Arg440 is a key member of a cluster of basic amino acid residues important for reductase binding.	Amino Acids, Basic	148-164	cytochrome P450 family 2 subfamily D member 6	Homo sapiens	82-88
15836774-2	2005	Human Snail is a 264-amino acid nuclear protein with an amino-terminal basic amino acid-rich domain (SNAG domain) and a carboxyl-terminal DNA-binding domain (zinc finger domain).	Amino Acids, Basic	71-87	snail family transcriptional repressor 1	Homo sapiens	6-11
15992355-1	2005	Aminopeptidase N (APN; CD13) is a member of zinc-containing ectoenzymes family involved in the degradation of neutral or basic amino acids (Ala>Phe>Leu>Gly) from N-terminal of bioactive peptides and amide or arylamide derivatives of amino acids.	Amino Acids, Basic	121-138	alanyl aminopeptidase, membrane	Homo sapiens	0-16
15992355-1	2005	Aminopeptidase N (APN; CD13) is a member of zinc-containing ectoenzymes family involved in the degradation of neutral or basic amino acids (Ala>Phe>Leu>Gly) from N-terminal of bioactive peptides and amide or arylamide derivatives of amino acids.	Amino Acids, Basic	121-138	alanyl aminopeptidase, membrane	Homo sapiens	18-21
15992355-1	2005	Aminopeptidase N (APN; CD13) is a member of zinc-containing ectoenzymes family involved in the degradation of neutral or basic amino acids (Ala>Phe>Leu>Gly) from N-terminal of bioactive peptides and amide or arylamide derivatives of amino acids.	Amino Acids, Basic	121-138	alanyl aminopeptidase, membrane	Homo sapiens	23-27