PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
21674341-4	2011	The N-terminal cysteine is generated by the endogenous yeast protease Kex2 in the yeast secretory pathway.	Cysteine	15-23	kexin KEX2	Saccharomyces cerevisiae S288C	70-74
20356564-4	2010	However, the current mechanism of conditional lysis is based on the use of the MET3 promoter which requires addition of methionine and cysteine for down-regulation of SRB1 and PKC1.	Methionine	120-130	kexin KEX2	Saccharomyces cerevisiae S288C	167-171
20356564-4	2010	However, the current mechanism of conditional lysis is based on the use of the MET3 promoter which requires addition of methionine and cysteine for down-regulation of SRB1 and PKC1.	Cysteine	135-143	kexin KEX2	Saccharomyces cerevisiae S288C	167-171
18625069-2	2008	In the yeast Saccharomyces cerevisiae the Kex2 protein is biochemically well investigated, however, with the exception of a few well known proteins such as the alpha-pheromone precursors, killer toxin precursors and aspartic proteinase propeptides, very few substrates are known.	propeptides	236-247	kexin KEX2	Saccharomyces cerevisiae S288C	42-46
19654332-3	2009	ASP preferentially cleaves peptide bonds that follow dibasic amino acid residues, as do Kex2 (Saccharomyces cerevisiae serine protease) and furin, which are representative kexin family proteases.	Aspartic Acid	0-3	kexin KEX2	Saccharomyces cerevisiae S288C	88-92
18625069-5	2008	We identified CaEce1, CA0365, one member of the Pry protein family and CaOps4-homolog proteins as novel Kex2 substrates.	caece1	14-20	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
18625069-5	2008	We identified CaEce1, CA0365, one member of the Pry protein family and CaOps4-homolog proteins as novel Kex2 substrates.	ca0365	22-28	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
16229820-3	2005	We first randomly mutated three Asp residues (D176, D210, and D211) that constitute the S2 pocket of Kex2 and then isolated from the resulting library Kex2 variants that preferred substrates with Met (poorly preferred by wild type Kex2) at the P2 position using a yeast-based screening method.	Aspartic Acid	32-35	kexin KEX2	Saccharomyces cerevisiae S288C	101-105
16229820-5	2005	Four out of the 16 isolated Kex2 variants showed greater preference for Met than for Lys (preferred by the wild-type Kex2) at the P2 position.	Lysine	85-88	kexin KEX2	Saccharomyces cerevisiae S288C	28-32
16229820-5	2005	Four out of the 16 isolated Kex2 variants showed greater preference for Met than for Lys (preferred by the wild-type Kex2) at the P2 position.	Lysine	85-88	kexin KEX2	Saccharomyces cerevisiae S288C	117-121
14992578-8	2004	In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed.	Potassium	110-119	kexin KEX2	Saccharomyces cerevisiae S288C	102-106
15870316-7	2005	The different substrate specificities of both proteases and their mutual redundancy for propeptide processing indicate that P. pastoris kex2 and yps1 single-gene disruptants can be used for the alpha-factor leader-directed secretion of heterologous proteins otherwise degraded at basic residues.	propeptide	88-98	kexin KEX2	Saccharomyces cerevisiae S288C	136-140
15140896-3	2004	Here we report that the small and highly stable compounds M(chelate)Cl(2) (M is copper or zinc) inhibit furin and Kex2, with Cu(TTP)Cl(2) and Zn(TTP)Cl(2) as the most efficient inhibitors.	Copper	80-86	kexin KEX2	Saccharomyces cerevisiae S288C	114-118
15710404-4	2005	Proteolytic cleavage occurs in the first extracellular loop of the protein at residues KR136/137 and is carried out by the Kex2p protease.	kr136	87-92	kexin KEX2	Saccharomyces cerevisiae S288C	123-128
15140896-11	2004	Target specificity is indicated by the fact that these metal chelate inhibitors are much less potent toward Kex2, the yeast homologue of furin.	Metals	55-60	kexin KEX2	Saccharomyces cerevisiae S288C	108-112
15140896-12	2004	For example, k(on) with Zn(TTP)Cl(2) is 120 +/- 20 s(-1) for furin, but only 1.2 +/- 0.1 s(-1) for Kex2.	zn(ttp)cl(2)	24-36	kexin KEX2	Saccharomyces cerevisiae S288C	99-103
11988505-2	2002	In vivo processing of the 345 aa toxin precursor (preprotoxin; pptox) involves multiple internal and carboxy-terminal cleavage events by the prohormone convertases Kex2p and Kex1p.	preprotoxin	50-61	kexin KEX2	Saccharomyces cerevisiae S288C	164-169
12832612-3	2003	We began with a modified eglin c, Arg-42-Arg-45-eglin, in which the reactive site loop had been optimized for subtilisin-related processing proteases of the Kex2/furin family.	Arginine	34-37	kexin KEX2	Saccharomyces cerevisiae S288C	157-161
9772752-2	1998	BPTI was linked to part of the fungal glucoamylase protein (GAM) with a dibasic amino acid (KEX2) processing site at the fusion junction.	Amino Acids, Diamino	72-90	kexin KEX2	Saccharomyces cerevisiae S288C	92-96
11561725-4	2001	The sequences around the proposed active site Asp, His, and Ser residues of KpcA are similar to those of other Kex2p family members.	Aspartic Acid	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	111-116
11561725-4	2001	The sequences around the proposed active site Asp, His, and Ser residues of KpcA are similar to those of other Kex2p family members.	Histidine	51-54	kexin KEX2	Saccharomyces cerevisiae S288C	111-116
11561725-4	2001	The sequences around the proposed active site Asp, His, and Ser residues of KpcA are similar to those of other Kex2p family members.	Serine	60-63	kexin KEX2	Saccharomyces cerevisiae S288C	111-116
11561725-4	2001	The sequences around the proposed active site Asp, His, and Ser residues of KpcA are similar to those of other Kex2p family members.	kpca	76-80	kexin KEX2	Saccharomyces cerevisiae S288C	111-116
11297433-3	2001	Pre-steady-state studies have shown that both Kex2 and furin exhibit an initial burst of 7-amino-4-methylcoumarin release in cleavage of peptidyl methylcoumarinamide substrates that are based on physiological cleavage sites.	7-amino-4-methylcoumarin	89-113	kexin KEX2	Saccharomyces cerevisiae S288C	46-50
11297433-3	2001	Pre-steady-state studies have shown that both Kex2 and furin exhibit an initial burst of 7-amino-4-methylcoumarin release in cleavage of peptidyl methylcoumarinamide substrates that are based on physiological cleavage sites.	peptidyl methylcoumarinamide	137-165	kexin KEX2	Saccharomyces cerevisiae S288C	46-50
11297433-6	2001	k(cat) for cleavage of a tetrapeptidyl methylcoumarinamide substrate based on the physiological yeast substrate pro-alpha-factor exhibits a weak solvent isotope effect, but neither this isotope effect nor temperature dependence studies with this substrate conclusively identify the rate-limiting step for Kex2 cleavage of this substrate.	methylcoumarinamide	39-58	kexin KEX2	Saccharomyces cerevisiae S288C	305-309
10790301-0	2000	Synthesis of peptidyl methylcoumarin esters as substrates and active-site titrants for the prohormone processing proteases Kex2 and PC2.	peptidyl methylcoumarin esters	13-43	kexin KEX2	Saccharomyces cerevisiae S288C	123-127
10790301-2	2000	We have devised techniques for the synthesis and deprotection of extended peptidyl methylcoumarin esters in good to moderate yields, and we have demonstrated their suitability for steady-state characterization and active-site titration of the Saccharomyces cerevisiae processing protease Kex2.	methylcoumarin esters	83-104	kexin KEX2	Saccharomyces cerevisiae S288C	288-292
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
11514565-8	2001	These results demonstrate that Kex2 utilizes enzyme-substrate interactions in different ways at different steps in the catalytic cycle, with the S(1)-P(1) contact providing a key specificity determinant at the acylation step.	Sulfur	145-146	kexin KEX2	Saccharomyces cerevisiae S288C	31-35
11297433-9	2001	These experiments demonstrate that cleavage of the acylenzyme ester bond, as opposed to either the initial attack on the amide bond or product release, is rate-limiting for the action of Kex2 at physiological sequences.	acylenzyme ester	51-67	kexin KEX2	Saccharomyces cerevisiae S288C	187-191
11297433-9	2001	These experiments demonstrate that cleavage of the acylenzyme ester bond, as opposed to either the initial attack on the amide bond or product release, is rate-limiting for the action of Kex2 at physiological sequences.	Amides	121-126	kexin KEX2	Saccharomyces cerevisiae S288C	187-191
9488470-3	1998	The VMA45 gene was cloned by complementation of the pH-conditional growth of the vma45-1 mutant strain and shown to be allelic to the previously characterized KEX2 gene, which encodes a serine endoprotease localized to the late Golgi compartment.	Serine	186-192	kexin KEX2	Saccharomyces cerevisiae S288C	4-9
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Lysine	54-57	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Arginine	61-64	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Arginine	75-78	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Lys-Arg	86-93	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Arginine	75-78	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9521659-3	1998	Kex2 exhibits optimal activity toward substrates with Lys or Arg at P2 and Arg at P1 (Lys-Arg or Arg-Arg cleavage sites).	Arginine	75-78	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
9488470-3	1998	The VMA45 gene was cloned by complementation of the pH-conditional growth of the vma45-1 mutant strain and shown to be allelic to the previously characterized KEX2 gene, which encodes a serine endoprotease localized to the late Golgi compartment.	Serine	186-192	kexin KEX2	Saccharomyces cerevisiae S288C	159-163
8991091-1	1996	The yeast membrane protein Kex2p uses a tyrosine-containing motif within the cytoplasmic domain for localization to a late Golgi compartment.	Tyrosine	40-48	kexin KEX2	Saccharomyces cerevisiae S288C	27-32
10099200-6	1998	To examine whether l-arginine affects the activities of intracellular proteases such as KEX2 endoproteinase or extracellular proteases, the proteolysis experiments were performed by incubating the commercial intact hPTH in a yeast host culture supernatant.	Arginine	19-29	kexin KEX2	Saccharomyces cerevisiae S288C	88-92
9092503-9	1997	This suggests that mammalian Kex2-like serine proteases may process pro-CCK at single arginine residues.	Arginine	86-94	kexin KEX2	Saccharomyces cerevisiae S288C	29-33
9048578-6	1997	While no evidence for positive interactions with the P3 residue emerged, Kex2 was found to discriminate against at least one residue Asp.	Aspartic Acid	133-136	kexin KEX2	Saccharomyces cerevisiae S288C	73-77
9048578-9	1997	Kex2 was demonstrated to be exquisitely selective for Arg at P1.	Arginine	54-57	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
8887651-2	1996	Previous studies identified a TGN localization signal (TLS) in the C-terminal cytosolic tail of Kex2p consisting of Tyr-713 and contextual sequences.	Tyrosine	116-119	kexin KEX2	Saccharomyces cerevisiae S288C	96-101
7819327-7	1994	In addition, Kex2 also hydrolyzed C-terminal to the Pro-Arg motif to release a tripeptide-extended form of SRIF-14.	prolylarginine	52-59	kexin KEX2	Saccharomyces cerevisiae S288C	13-17
7961747-3	1994	Also, as in the case of Kex2p, retention of GMP51 in yeast Golgi membranes was dependent on clathrin function.	gmp51	44-49	kexin KEX2	Saccharomyces cerevisiae S288C	24-29
7961747-5	1994	The collective data are most consistent with a model where GMP36, GMP77, and GMP95 are present in all Kex2p-containing membranes, but Kex2p is present in only a subpopulation of membranes that contain these GMPs, thereby suggesting that either these particular GMPs exhibit overlapping distributions in compartments of the yeast Golgi complex or are also present in non-Golgi compartments.	gmp95	77-82	kexin KEX2	Saccharomyces cerevisiae S288C	102-107
7941736-4	1994	P, a 67 residue "processing" segment with three sites for N-glycosylation, terminates in a Lys Arg site for cleavage by the Kex2 protease.	Lys-Arg	91-98	kexin KEX2	Saccharomyces cerevisiae S288C	124-128
8918261-3	1996	These vectors allow the production in high yield of either native proteins or of fusion proteins which contain, at their amino terminus, the peptide Met Gly His6 Ser Gly Leu Phe Lys Arg/, where Leu Phe Lys Arg/ is the recognition site for Kex2 protease which cleaves at the site indicated by /.	Glycine	153-156	kexin KEX2	Saccharomyces cerevisiae S288C	239-243
8918261-3	1996	These vectors allow the production in high yield of either native proteins or of fusion proteins which contain, at their amino terminus, the peptide Met Gly His6 Ser Gly Leu Phe Lys Arg/, where Leu Phe Lys Arg/ is the recognition site for Kex2 protease which cleaves at the site indicated by /.	Glycine	166-169	kexin KEX2	Saccharomyces cerevisiae S288C	239-243
8918261-3	1996	These vectors allow the production in high yield of either native proteins or of fusion proteins which contain, at their amino terminus, the peptide Met Gly His6 Ser Gly Leu Phe Lys Arg/, where Leu Phe Lys Arg/ is the recognition site for Kex2 protease which cleaves at the site indicated by /.	Leucine	170-173	kexin KEX2	Saccharomyces cerevisiae S288C	239-243
7755581-5	1995	In contrast to the mammalian endoproteases furin and the hepatic proalbumin convertase, the Kex2 protease was adversely affected by a P4 arginine.	Arginine	137-145	kexin KEX2	Saccharomyces cerevisiae S288C	92-96
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	45-48	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Glycine	49-52	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Phenylalanine	57-60	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
7755581-6	1995	There was an 85% decrease in the cleavage of Arg-Gly-Arg-Phe-Arg-Arg-albumin compared with normal; also chicken proalbumin with an Arg-Phe-Ala-Arg processing site sequence was not a substrate for Kex2.	Arginine	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	196-200
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
8039662-3	1994	The largest complementation group has been designated QDS1, for increased quinidine-sensitivity.	Quinidine	74-83	kexin KEX2	Saccharomyces cerevisiae S288C	54-58
8039662-4	1994	Exposure of qds1 cells to lethal concentrations of quinidine results in a novel small-budded terminal morphology in about 70% of the cells in the culture.	Quinidine	51-60	kexin KEX2	Saccharomyces cerevisiae S288C	12-16
8039662-9	1994	Loss of QDS1/KEX2 function results in quinidine sensitivity.	Quinidine	38-47	kexin KEX2	Saccharomyces cerevisiae S288C	8-12
8039662-9	1994	Loss of QDS1/KEX2 function results in quinidine sensitivity.	Quinidine	38-47	kexin KEX2	Saccharomyces cerevisiae S288C	13-17
7819327-7	1994	In addition, Kex2 also hydrolyzed C-terminal to the Pro-Arg motif to release a tripeptide-extended form of SRIF-14.	tripeptide K-26	79-89	kexin KEX2	Saccharomyces cerevisiae S288C	13-17
7819331-0	1994	T4-lymphocyte endoprotease responsible for the proteolytic processing of HIV-1 gp160, like Kex2p endoprotease, is a calcium-dependent enzyme.	Calcium	116-123	kexin KEX2	Saccharomyces cerevisiae S288C	91-96
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
7866429-10	1994	All of the beta-APP fused to the alpha-factor leader proceeded to the trans-Golgi, where Kex2 endopeptidase removed the leader and released the normal amino-terminus of beta-APP.	beta-app	11-19	kexin KEX2	Saccharomyces cerevisiae S288C	89-93
7866429-10	1994	All of the beta-APP fused to the alpha-factor leader proceeded to the trans-Golgi, where Kex2 endopeptidase removed the leader and released the normal amino-terminus of beta-APP.	beta-app	169-177	kexin KEX2	Saccharomyces cerevisiae S288C	89-93
15335687-3	1993	Curiously, the mammalian protease PC2, a Kex2 homolog that is likely to be required for pro-insulin processing, has an aspartate in place of asparagine at the "oxyanion hole".	Aspartic Acid	119-128	kexin KEX2	Saccharomyces cerevisiae S288C	41-45
8226855-5	1993	Efficient cleavage of the paired dibasic amino acid cleaving enzyme (PACE) propeptide was achieved by coexpression with human PACE or yeast KEX2.	dibasic	33-40	kexin KEX2	Saccharomyces cerevisiae S288C	140-144
8226855-5	1993	Efficient cleavage of the paired dibasic amino acid cleaving enzyme (PACE) propeptide was achieved by coexpression with human PACE or yeast KEX2.	propeptide	75-85	kexin KEX2	Saccharomyces cerevisiae S288C	140-144
8344247-8	1993	Organelle fractionation by sucrose density gradient centrifugation shows that Kex2p is not retained in the Golgi complex of lam1 cells.	Sucrose	27-34	kexin KEX2	Saccharomyces cerevisiae S288C	78-83
15335687-4	1993	RESULTS: We have tested the effect of making substitutions of the conserved oxyanion-hole asparagine (Asn 314) of the Kex2 protease.	Asparagine	90-100	kexin KEX2	Saccharomyces cerevisiae S288C	118-122
15335687-4	1993	RESULTS: We have tested the effect of making substitutions of the conserved oxyanion-hole asparagine (Asn 314) of the Kex2 protease.	Asparagine	102-105	kexin KEX2	Saccharomyces cerevisiae S288C	118-122
15335687-9	1993	We found that, with three peptides that are good substrates of wild-type Kex2, the k(cal) of the Asp 314 enzyme was reduced approximately 4500-fold and its K(M) approximately 4-fold, relative to the wild-type enzyme.	Aspartic Acid	97-100	kexin KEX2	Saccharomyces cerevisiae S288C	73-77
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
8328974-3	1993	The most potent inhibitor, Pro-Nvl-Tyr-Lys-Arg-chloromethane, was based on cleavage sites in the natural Kex2 substrate pro-alpha-factor.	pro-nvl-tyr-lys-arg-chloromethane	27-60	kexin KEX2	Saccharomyces cerevisiae S288C	105-109
8328974-4	1993	This inhibitor exhibited a Ki of 3.7 nM and a second-order inactivation rate constant (k2/Ki) of 1.3 x 10(7) M-1.s-1 comparable with the value of kcat./Km obtained with Kex2 for the corresponding peptidyl methylcoumarinylamide substrate.	peptidyl methylcoumarinylamide	196-226	kexin KEX2	Saccharomyces cerevisiae S288C	169-173
1644796-1	1992	Furin, a mammalian homolog of the yeast Kex2 protease, is associated with Golgi membranes and is involved in cleavage of precursor proteins at sites marked by the Arg-X-Lys/Arg-Arg (RXK/RR) motif.	Arginine	163-166	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	32-35	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	lys-x-lys	36-45	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Lysine	36-39	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	x-x-x-lys	65-74	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
8462689-1	1993	We have recently shown that the Arg/Lys-X-Lys/Arg-Arg or Arg/Lys-X-X-X-Lys/Arg-Arg sequence serves as a signal for cleavage of precursor proteins within the constitutive secretory pathway, and this cleavage is catalyzed by furin, a mammalian homolog of the yeast Kex2 protease.	Arginine	46-49	kexin KEX2	Saccharomyces cerevisiae S288C	263-267
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
8094050-6	1993	The Kex2 endoprotease appears to be essential for the formation of lysine somatostatin-14 and is involved either directly or indirectly in the release of mature somatostatin-14.	lysine somatostatin-14	67-89	kexin KEX2	Saccharomyces cerevisiae S288C	4-8
1493334-0	1992	Mutation of a tyrosine localization signal in the cytosolic tail of yeast Kex2 protease disrupts Golgi retention and results in default transport to the vacuole.	Tyrosine	14-22	kexin KEX2	Saccharomyces cerevisiae S288C	74-78
1493334-2	1992	The first approximately 30 residues of the 115 amino acid CO2H-terminal cytosolic tail (C-tail) of the Kex2 protein (Kex2p) contain a Golgi retention signal that resembles coated-pit localization signals in mammalian cell surface receptors.	co2h	58-62	kexin KEX2	Saccharomyces cerevisiae S288C	103-107
1493334-2	1992	The first approximately 30 residues of the 115 amino acid CO2H-terminal cytosolic tail (C-tail) of the Kex2 protein (Kex2p) contain a Golgi retention signal that resembles coated-pit localization signals in mammalian cell surface receptors.	co2h	58-62	kexin KEX2	Saccharomyces cerevisiae S288C	117-122
8394962-1	1993	The recent discovery of mammalian endoproteinases which show extensive sequence homology with the yeast Kex 2 gene product (kexin) has lead to the hypothesis that processing enzymes of pro-hormone precursor proteins belong to a family of calcium dependent, subtilisin-like serine proteinases.	Calcium	238-245	kexin KEX2	Saccharomyces cerevisiae S288C	104-109
1644796-1	1992	Furin, a mammalian homolog of the yeast Kex2 protease, is associated with Golgi membranes and is involved in cleavage of precursor proteins at sites marked by the Arg-X-Lys/Arg-Arg (RXK/RR) motif.	Lysine	169-172	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
1644796-1	1992	Furin, a mammalian homolog of the yeast Kex2 protease, is associated with Golgi membranes and is involved in cleavage of precursor proteins at sites marked by the Arg-X-Lys/Arg-Arg (RXK/RR) motif.	Arginine	173-176	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
1644796-1	1992	Furin, a mammalian homolog of the yeast Kex2 protease, is associated with Golgi membranes and is involved in cleavage of precursor proteins at sites marked by the Arg-X-Lys/Arg-Arg (RXK/RR) motif.	Arginine	173-176	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
1618297-0	1992	A modified Kex2 enzyme retained in the endoplasmic reticulum prevents disulfide-linked dimerisation of recombinant human insulin-like growth factor-1 secreted from yeast.	Disulfides	70-79	kexin KEX2	Saccharomyces cerevisiae S288C	11-15
1368916-0	1992	In-vitro cleavage of a fusion protein bound to cellulose using the soluble yscFs (Kex2) variant.	Cellulose	47-56	kexin KEX2	Saccharomyces cerevisiae S288C	82-86
1368916-2	1992	The two fusion partners were separated by a Lys-Arg-containing recognition sequence for the yeast endoprotease yscF (Kex2).	Lys-Arg	44-51	kexin KEX2	Saccharomyces cerevisiae S288C	117-121
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	kex2phdel	73-82	kexin KEX2	Saccharomyces cerevisiae S288C	50-55
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	Disulfides	111-120	kexin KEX2	Saccharomyces cerevisiae S288C	50-55
1618297-5	1992	We find that co-expression of a novel ER-retained Kex2p variant, soluble Kex2pHDEL, can prevent intermolecular disulfide bond formation between two IGF1 molecules, implying that the presence of the proregion during the folding of IGF1 in the ER could be a reason for disulfide-linked dimerisation.	Disulfides	267-276	kexin KEX2	Saccharomyces cerevisiae S288C	50-55
1545235-2	1992	The deduced protein is structurally similar to the yeast KEX2 prohormone endoprotease including the conserved Asp, His, and Ser catalytic triad residues characteristic of the subtilisin family.	Aspartic Acid	110-113	kexin KEX2	Saccharomyces cerevisiae S288C	57-61
1569080-1	1992	We have recently demonstrated that the Arg-X-Lys/Arg-Arg sequence is a signal for precursor cleavage catalyzed by furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, within the constitutive secretory pathway.	Arginine	39-42	kexin KEX2	Saccharomyces cerevisiae S288C	190-194
1569080-1	1992	We have recently demonstrated that the Arg-X-Lys/Arg-Arg sequence is a signal for precursor cleavage catalyzed by furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, within the constitutive secretory pathway.	Lysine	45-48	kexin KEX2	Saccharomyces cerevisiae S288C	190-194
1569080-1	1992	We have recently demonstrated that the Arg-X-Lys/Arg-Arg sequence is a signal for precursor cleavage catalyzed by furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, within the constitutive secretory pathway.	Arginine	49-52	kexin KEX2	Saccharomyces cerevisiae S288C	190-194
1569080-1	1992	We have recently demonstrated that the Arg-X-Lys/Arg-Arg sequence is a signal for precursor cleavage catalyzed by furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, within the constitutive secretory pathway.	Arginine	49-52	kexin KEX2	Saccharomyces cerevisiae S288C	190-194
1587790-0	1992	Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.	Arginine	104-107	kexin KEX2	Saccharomyces cerevisiae S288C	47-51
1587790-0	1992	Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.	x-lys	108-113	kexin KEX2	Saccharomyces cerevisiae S288C	47-51
1587790-0	1992	Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.	Arginine	114-117	kexin KEX2	Saccharomyces cerevisiae S288C	47-51
1587790-0	1992	Molecular and enzymatic properties of furin, a Kex2-like endoprotease involved in precursor cleavage at Arg-X-Lys/Arg-Arg sites.	Arginine	114-117	kexin KEX2	Saccharomyces cerevisiae S288C	47-51
1587790-1	1992	We have recently shown that furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, is involved in precursor cleavage at sites marked by the Arg-X-Lys/Arg-Arg motif within the constitutive secretory pathway.	Arginine	167-170	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
1587790-1	1992	We have recently shown that furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, is involved in precursor cleavage at sites marked by the Arg-X-Lys/Arg-Arg motif within the constitutive secretory pathway.	Lysine	173-176	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
1587790-1	1992	We have recently shown that furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, is involved in precursor cleavage at sites marked by the Arg-X-Lys/Arg-Arg motif within the constitutive secretory pathway.	Arginine	177-180	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
1587790-1	1992	We have recently shown that furin, a mammalian homologue of the yeast precursor-processing endoprotease Kex2, is involved in precursor cleavage at sites marked by the Arg-X-Lys/Arg-Arg motif within the constitutive secretory pathway.	Arginine	177-180	kexin KEX2	Saccharomyces cerevisiae S288C	104-108
1599477-0	1992	Kex2-like proteolytic activity in adrenal medullary chromaffin granules.	chromaffin	52-62	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
1599477-1	1992	This study demonstrates the presence of boc-Gln-Arg-Arg-MCA cleaving activity in bovine chromaffin granule membranes that resembles yeast Kex2 proteolytic activity.	Boc-Gln-OH	40-47	kexin KEX2	Saccharomyces cerevisiae S288C	138-142
1599477-1	1992	This study demonstrates the presence of boc-Gln-Arg-Arg-MCA cleaving activity in bovine chromaffin granule membranes that resembles yeast Kex2 proteolytic activity.	Arginine	48-51	kexin KEX2	Saccharomyces cerevisiae S288C	138-142
1599477-1	1992	This study demonstrates the presence of boc-Gln-Arg-Arg-MCA cleaving activity in bovine chromaffin granule membranes that resembles yeast Kex2 proteolytic activity.	Arginine	52-55	kexin KEX2	Saccharomyces cerevisiae S288C	138-142
1599477-1	1992	This study demonstrates the presence of boc-Gln-Arg-Arg-MCA cleaving activity in bovine chromaffin granule membranes that resembles yeast Kex2 proteolytic activity.	chromaffin	88-98	kexin KEX2	Saccharomyces cerevisiae S288C	138-142
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	chromaffin	4-14	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Boc-Gln-OH	23-30	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Arginine	31-34	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Arginine	35-38	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Calcium	100-107	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Arginine	35-38	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Arginine	35-38	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Lysine	263-266	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Arginine	35-38	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Lysine	277-280	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1599477-2	1992	The chromaffin granule boc-Gln-Arg-Arg-MCA cleaving activity, like Kex2 proteolytic activity, shows calcium dependence, optimum activity at pH 7.5-8.2, inhibition by serine protease inhibitors, and preference for cleavage at the COOH-terminal side of Arg-Arg and Lys-Arg, over Lys-Lys, paired basic residues.	Lysine	277-280	kexin KEX2	Saccharomyces cerevisiae S288C	67-71
1514325-5	1992	However SP-beta la, produced by deletion of ppTox residues 35-176, expressed 10-fold higher beta la activity and the precursor was now secreted with similar efficiency in a kex2-null strain.	sp-beta la	8-18	kexin KEX2	Saccharomyces cerevisiae S288C	173-177
1514325-6	1992	Fusions of beta la to ppTox at Ala34 or Ala46 also led to efficient secretion in both KEX2 and kex2-null strains.	beta la	11-18	kexin KEX2	Saccharomyces cerevisiae S288C	86-90
1514325-6	1992	Fusions of beta la to ppTox at Ala34 or Ala46 also led to efficient secretion in both KEX2 and kex2-null strains.	beta la	11-18	kexin KEX2	Saccharomyces cerevisiae S288C	95-99
1514325-6	1992	Fusions of beta la to ppTox at Ala34 or Ala46 also led to efficient secretion in both KEX2 and kex2-null strains.	pptox	22-27	kexin KEX2	Saccharomyces cerevisiae S288C	86-90
1514325-6	1992	Fusions of beta la to ppTox at Ala34 or Ala46 also led to efficient secretion in both KEX2 and kex2-null strains.	pptox	22-27	kexin KEX2	Saccharomyces cerevisiae S288C	95-99
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
1545235-2	1992	The deduced protein is structurally similar to the yeast KEX2 prohormone endoprotease including the conserved Asp, His, and Ser catalytic triad residues characteristic of the subtilisin family.	Histidine	115-118	kexin KEX2	Saccharomyces cerevisiae S288C	57-61
1545235-2	1992	The deduced protein is structurally similar to the yeast KEX2 prohormone endoprotease including the conserved Asp, His, and Ser catalytic triad residues characteristic of the subtilisin family.	Serine	124-127	kexin KEX2	Saccharomyces cerevisiae S288C	57-61
1736307-3	1992	Amino acid sequence analysis revealed that the N terminus of mature Kex2 protease is created by a potentially autoproteolytic cleavage at Lys108-Arg109, prior to the domain homologous to subtilisin, followed by trimming of Leu-Pro and Val-Pro dipeptides by the Ste13 dipeptidyl aminopeptidase.	leucylproline	223-230	kexin KEX2	Saccharomyces cerevisiae S288C	68-72
1740121-7	1992	Deleting the carboxyl-terminal tail and the transmembrane domain of Kex2p (Kex2 delta p, 666 amino acids) does not measurably interfere with the enzyme characteristics and results in the secretion of up to 90% of the total enzyme activity.	delta p	80-87	kexin KEX2	Saccharomyces cerevisiae S288C	68-73
1740121-7	1992	Deleting the carboxyl-terminal tail and the transmembrane domain of Kex2p (Kex2 delta p, 666 amino acids) does not measurably interfere with the enzyme characteristics and results in the secretion of up to 90% of the total enzyme activity.	delta p	80-87	kexin KEX2	Saccharomyces cerevisiae S288C	68-72
1736307-3	1992	Amino acid sequence analysis revealed that the N terminus of mature Kex2 protease is created by a potentially autoproteolytic cleavage at Lys108-Arg109, prior to the domain homologous to subtilisin, followed by trimming of Leu-Pro and Val-Pro dipeptides by the Ste13 dipeptidyl aminopeptidase.	val-pro dipeptides	235-253	kexin KEX2	Saccharomyces cerevisiae S288C	68-72
1560780-5	1992	A fourth Kex2-dependent cleavage occurs at LysArg-188.	lysarg	43-49	kexin KEX2	Saccharomyces cerevisiae S288C	9-13
1918142-3	1991	Kex2 protein is initially synthesized as a prepro-enzyme that undergoes cotranslational signal peptide cleavage and addition of Asn-linked core oligosaccharide and Ser/Thr-linked mannose in the ER.	asn-linked core oligosaccharide	128-159	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
1937055-5	1991	The role of the KEX2 protease cleavage site was investigated by mutation of the yeast alpha-factor KEX2 site (cleavage after Lys-Arg).	Lysine	125-128	kexin KEX2	Saccharomyces cerevisiae S288C	99-103
1937055-5	1991	The role of the KEX2 protease cleavage site was investigated by mutation of the yeast alpha-factor KEX2 site (cleavage after Lys-Arg).	Arginine	129-132	kexin KEX2	Saccharomyces cerevisiae S288C	99-103
1918142-3	1991	Kex2 protein is initially synthesized as a prepro-enzyme that undergoes cotranslational signal peptide cleavage and addition of Asn-linked core oligosaccharide and Ser/Thr-linked mannose in the ER.	Serine	164-167	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
1918142-3	1991	Kex2 protein is initially synthesized as a prepro-enzyme that undergoes cotranslational signal peptide cleavage and addition of Asn-linked core oligosaccharide and Ser/Thr-linked mannose in the ER.	Threonine	168-171	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
1918142-3	1991	Kex2 protein is initially synthesized as a prepro-enzyme that undergoes cotranslational signal peptide cleavage and addition of Asn-linked core oligosaccharide and Ser/Thr-linked mannose in the ER.	Mannose	179-186	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
1897312-3	1991	Here we report that the srb1 mutation, which is the genetic determinant of cell lysis, is responsible for quantitative and structural changes of glucans.	Glucans	145-152	kexin KEX2	Saccharomyces cerevisiae S288C	24-28
1892395-2	1991	For secretion by yeast cells of HGH with the same NH2 terminus as native HGH, an artificial Lys-Arg linker, which is one of the potential KEX2 recognition sequences, was introduced at the junction between the M. pusillus rennin secretion leader and mature HGH.	Lysine	92-95	kexin KEX2	Saccharomyces cerevisiae S288C	138-142
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
1897312-4	1991	Experiments with isogenic single mutation strains, genetic studies coupled with quantitative measurements of glucan content per cell, and methylation analysis of glucans provide evidence that srb1 mutation leads to i) formation of mechanically unstable cell wall network made of insoluble glucan fibrils which are shorter and contain beta(1-6) inter-residue linkages and ii) insufficient filling of the space between the fibrils due to a shortage of the alkali-soluble glucan.	Glucans	109-115	kexin KEX2	Saccharomyces cerevisiae S288C	192-196
1897312-4	1991	Experiments with isogenic single mutation strains, genetic studies coupled with quantitative measurements of glucan content per cell, and methylation analysis of glucans provide evidence that srb1 mutation leads to i) formation of mechanically unstable cell wall network made of insoluble glucan fibrils which are shorter and contain beta(1-6) inter-residue linkages and ii) insufficient filling of the space between the fibrils due to a shortage of the alkali-soluble glucan.	Glucans	162-169	kexin KEX2	Saccharomyces cerevisiae S288C	192-196
1897312-4	1991	Experiments with isogenic single mutation strains, genetic studies coupled with quantitative measurements of glucan content per cell, and methylation analysis of glucans provide evidence that srb1 mutation leads to i) formation of mechanically unstable cell wall network made of insoluble glucan fibrils which are shorter and contain beta(1-6) inter-residue linkages and ii) insufficient filling of the space between the fibrils due to a shortage of the alkali-soluble glucan.	Glucans	162-168	kexin KEX2	Saccharomyces cerevisiae S288C	192-196
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
1986005-5	1991	The transmembrane Kex2 protease, which processes precursors of secreted peptides within the yeast secretory pathway, is also localized by indirect immunofluorescence to multiple structures in the yeast cell (Redding, K., and R. Fuller, manuscript submitted for publication).	Peptides	72-80	kexin KEX2	Saccharomyces cerevisiae S288C	18-22
1367016-4	1991	A comparison of the dipeptide distributions of 33 secreted and 34 cytoplasmic proteins from fungal producers of extracellular enzymes indicated a significant bias for some doublets, including the basic dipeptides Lys-Arg, Arg-Arg and Arg-Lys which have also been demonstrated to be KEX2 substrates.	Dipeptides	20-29	kexin KEX2	Saccharomyces cerevisiae S288C	282-286
1892395-5	1991	These results clearly showed that the leader peptide with the Lys-Arg linker was recognized and specifically cleaved by the yeast KEX2 protease.	Lysine	62-65	kexin KEX2	Saccharomyces cerevisiae S288C	130-134
1892395-5	1991	These results clearly showed that the leader peptide with the Lys-Arg linker was recognized and specifically cleaved by the yeast KEX2 protease.	Arginine	66-69	kexin KEX2	Saccharomyces cerevisiae S288C	130-134
2151557-2	1990	Combined genetic and biochemical analysis shows that the srb1 mutation is responsible for the reduction of alkali-soluble glucan.	Glucans	122-128	kexin KEX2	Saccharomyces cerevisiae S288C	57-61
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
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-).	lysarg	299-305	kexin KEX2	Saccharomyces cerevisiae S288C	91-95
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-).	arginylarginine	312-318	kexin KEX2	Saccharomyces cerevisiae S288C	91-95
2269657-2	1990	The fur-directed activity (furin) shared many properties with Kex2p including activity at pH 7.3 and a requirement for calcium.	fur	4-7	kexin KEX2	Saccharomyces cerevisiae S288C	62-67
2269657-2	1990	The fur-directed activity (furin) shared many properties with Kex2p including activity at pH 7.3 and a requirement for calcium.	Calcium	119-126	kexin KEX2	Saccharomyces cerevisiae S288C	62-67
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
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
2116982-2	1990	This processing did not take place when form A was obtained from protoplasts lysed in the presence of either EDTA or leupeptin, two wel-characterized inhibitors of KEX2 endoprotease from Saccharomyces cerevisiae.	Edetic Acid	109-113	kexin KEX2	Saccharomyces cerevisiae S288C	164-168
2116982-2	1990	This processing did not take place when form A was obtained from protoplasts lysed in the presence of either EDTA or leupeptin, two wel-characterized inhibitors of KEX2 endoprotease from Saccharomyces cerevisiae.	leupeptin	117-126	kexin KEX2	Saccharomyces cerevisiae S288C	164-168
2116982-3	1990	Sequencing of the amino terminus of an A-like form of enzyme secreted by a kex2 mutant indicated the presence of 4 amino acids, with a pair of basic residues (Lys-Arg) at their carboxyl side, preceding the amino terminus of the wild-type external exoglucanase.	Lysine	159-162	kexin KEX2	Saccharomyces cerevisiae S288C	75-79
2116982-3	1990	Sequencing of the amino terminus of an A-like form of enzyme secreted by a kex2 mutant indicated the presence of 4 amino acids, with a pair of basic residues (Lys-Arg) at their carboxyl side, preceding the amino terminus of the wild-type external exoglucanase.	Arginine	163-166	kexin KEX2	Saccharomyces cerevisiae S288C	75-79
1368606-4	1990	This sequence suggests that the Sfamy gene product is synthesized as a pre-pro-precursor, and the pro-sequence is cleaved after a Lys-Arg sequence with the calpain-like endopeptidase encode by the KEX2 gene, resulting in mature Sfamy protein composed of 468 amino acids.	Lys-Arg	130-137	kexin KEX2	Saccharomyces cerevisiae S288C	197-201
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.	arg25lys26	65-75	kexin KEX2	Saccharomyces cerevisiae S288C	127-131
2183521-1	1990	Mutants of Saccharomyces cerevisiae which lack the KEX2-encoded endopeptidase are unable to process proteolytically the mating factor alpha (MF alpha) propheromone produced from the chromosomal MF alpha 1 and MF alpha 2 genes (Julius et al., 1983).	propheromone	151-163	kexin KEX2	Saccharomyces cerevisiae S288C	51-55
2183521-6	1990	The gene isolated in this way was shown also to be essential for the KEX2-independent processing of propheromone overproduced from plasmid-borne MF alpha 1.	propheromone	100-112	kexin KEX2	Saccharomyces cerevisiae S288C	69-73
2683070-1	1989	The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment.	Asparagine	167-177	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
2154467-3	1990	Within this region 49 and 27% of the amino acids are identical to those in the aligned Kex2 and subtilisin BPN" sequences, respectively, and the catalytically essential Asp, His, and Ser residues are all conserved.	Serine	183-186	kexin KEX2	Saccharomyces cerevisiae S288C	87-91
2683070-1	1989	The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment.	Serine	189-195	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
2683070-1	1989	The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment.	threonine-linked oligosaccharide	201-233	kexin KEX2	Saccharomyces cerevisiae S288C	40-44
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
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.	dibasic	141-148	kexin KEX2	Saccharomyces cerevisiae S288C	8-13
3278932-0	1988	Calcium-dependent KEX2-like protease found in hepatic secretory vesicles converts proalbumin to albumin.	Calcium	0-7	kexin KEX2	Saccharomyces cerevisiae S288C	18-22
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
2845974-1	1988	Yeast Saccharomyces cerevisiae KEX2 gene previously isolated, was characterized as the gene encoding a calcium-dependent endopeptidase required for processing of precursors of alpha-factor and killer toxin.	Calcium	103-110	kexin KEX2	Saccharomyces cerevisiae S288C	31-35
3066674-5	1988	It was found that a significant proportion of human granulocyte-macrophage colony stimulating factor was degraded by the yeast KEX2 protease that was cleaving after the dibasic sequence Arg-Arg at positions 23-24 of the mature protein.	Arginine	186-189	kexin KEX2	Saccharomyces cerevisiae S288C	127-131
3066674-5	1988	It was found that a significant proportion of human granulocyte-macrophage colony stimulating factor was degraded by the yeast KEX2 protease that was cleaving after the dibasic sequence Arg-Arg at positions 23-24 of the mature protein.	Arginine	190-193	kexin KEX2	Saccharomyces cerevisiae S288C	127-131
6430565-5	1984	All kex2 mutants examined (three independent alleles) lack a Zn++-sensitive membrane-associated endopeptidase with specificity for cleaving on the carboxyl side of a pair of basic residues.	Zinc	61-65	kexin KEX2	Saccharomyces cerevisiae S288C	4-8
3301840-8	1987	The COOH terminal side of the paired basic residues (Arg-148 Arg-149 and Lys-232 Arg-233 of preprotoxin) are endoproteolytic processing sites for the product of the KEX2 gene (Julius, D., Brake, A., Blair, L., Kunisawa, R., and Thorner, J.	Carbonic Acid	4-8	kexin KEX2	Saccharomyces cerevisiae S288C	165-169
3301840-8	1987	The COOH terminal side of the paired basic residues (Arg-148 Arg-149 and Lys-232 Arg-233 of preprotoxin) are endoproteolytic processing sites for the product of the KEX2 gene (Julius, D., Brake, A., Blair, L., Kunisawa, R., and Thorner, J.	preprotoxin	92-103	kexin KEX2	Saccharomyces cerevisiae S288C	165-169
773743-5	1976	Kex2 is located on chromosome XIV, but it does not show meiotic linkage to any gene previously located on this chromosome.--When the killer plasmid of kex1 or kex2 strains is eliminated by curing with heat or cycloheximide, the strains become sensitive to killing.	Cycloheximide	209-222	kexin KEX2	Saccharomyces cerevisiae S288C	0-4
773743-5	1976	Kex2 is located on chromosome XIV, but it does not show meiotic linkage to any gene previously located on this chromosome.--When the killer plasmid of kex1 or kex2 strains is eliminated by curing with heat or cycloheximide, the strains become sensitive to killing.	Cycloheximide	209-222	kexin KEX2	Saccharomyces cerevisiae S288C	159-163
32163000-7	2020	Endogenous proteases Kex2 and Ste13 in Golgi apparatus recognize and excise Lys-Arg and Glu-Ala pair to release short CGA-N12 peptides from the tandem repeat sequences, respectively.	Lys-Arg	76-83	kexin KEX2	Saccharomyces cerevisiae S288C	21-25
32163000-7	2020	Endogenous proteases Kex2 and Ste13 in Golgi apparatus recognize and excise Lys-Arg and Glu-Ala pair to release short CGA-N12 peptides from the tandem repeat sequences, respectively.	Glutamic Acid	88-91	kexin KEX2	Saccharomyces cerevisiae S288C	21-25
32163000-7	2020	Endogenous proteases Kex2 and Ste13 in Golgi apparatus recognize and excise Lys-Arg and Glu-Ala pair to release short CGA-N12 peptides from the tandem repeat sequences, respectively.	Alanine	92-95	kexin KEX2	Saccharomyces cerevisiae S288C	21-25
23408788-5	2013	Ser(780) in the Kex2p C-tail is crucial for binding: an Ala substitution blocks but an Asp substitution permits binding.	Serine	0-3	kexin KEX2	Saccharomyces cerevisiae S288C	16-21
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
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.	Arginine	205-213	kexin KEX2	Saccharomyces cerevisiae S288C	39-43
28432839-3	2017	Unlike Kex2, however, ASP lacks an intramolecular chaperone N-terminal propeptide, instead utilizes the external chaperone ORF2 for proper folding, therefore, ASP and its homologues constitute a new subfamily in the subtilisin family.	Aspartic Acid	159-162	kexin KEX2	Saccharomyces cerevisiae S288C	7-11
27965112-4	2017	It was further shown that non-covalently bound Scw4 (SDS released) underwent the Kex2 proteolytic processing.	Sodium Dodecyl Sulfate	53-56	kexin KEX2	Saccharomyces cerevisiae S288C	81-85
27720750-3	2016	Our goal was to study the prime region subsite S" of Kex2 because previous studies have only taken into account non-prime sites using AMC substrates but not the specificity of prime sites identified through structural modeling or predicted cleavage sites.	7-amino-4-methylcoumarin	134-137	kexin KEX2	Saccharomyces cerevisiae S288C	53-57
30475911-0	2018	Propeptide genesis by Kex2-dependent cleavage of yeast wall protein 1 (Ywp1) of Candida albicans.	propeptide	0-10	kexin KEX2	Saccharomyces cerevisiae S288C	22-26
29432900-0	2018	Thermodynamic analysis of Kex2 activity: The acylation and deacylation steps are potassium- and substrate-dependent.	Potassium	81-90	kexin KEX2	Saccharomyces cerevisiae S288C	26-30
29432900-3	2018	Potassium bound Kex2 with KD=20.3mM.	Potassium	0-9	kexin KEX2	Saccharomyces cerevisiae S288C	16-20
27977123-9	2017	This information is particularly important for those using yeast display technology, as library members with Ali/Leu-X-Lys/Arg-Arg patterns are likely being removed from screens via Kex2 cleavage without the researcher"s knowledge.	Leucine	113-116	kexin KEX2	Saccharomyces cerevisiae S288C	182-186
27977123-9	2017	This information is particularly important for those using yeast display technology, as library members with Ali/Leu-X-Lys/Arg-Arg patterns are likely being removed from screens via Kex2 cleavage without the researcher"s knowledge.	Lysine	119-122	kexin KEX2	Saccharomyces cerevisiae S288C	182-186
27977123-9	2017	This information is particularly important for those using yeast display technology, as library members with Ali/Leu-X-Lys/Arg-Arg patterns are likely being removed from screens via Kex2 cleavage without the researcher"s knowledge.	Arginine	123-126	kexin KEX2	Saccharomyces cerevisiae S288C	182-186
27977123-9	2017	This information is particularly important for those using yeast display technology, as library members with Ali/Leu-X-Lys/Arg-Arg patterns are likely being removed from screens via Kex2 cleavage without the researcher"s knowledge.	Arginine	127-130	kexin KEX2	Saccharomyces cerevisiae S288C	182-186
23408788-5	2013	Ser(780) in the Kex2p C-tail is crucial for binding: an Ala substitution blocks but an Asp substitution permits binding.	Alanine	56-59	kexin KEX2	Saccharomyces cerevisiae S288C	16-21
23408788-5	2013	Ser(780) in the Kex2p C-tail is crucial for binding: an Ala substitution blocks but an Asp substitution permits binding.	Aspartic Acid	87-90	kexin KEX2	Saccharomyces cerevisiae S288C	16-21
23408788-6	2013	Biochemical assays using purified Gga2p VHS-GGA and TOM1 (GAT) and glutathione S-transferase-Kex2p C-tail fusions show that Gga2p binds directly to the Kex2p C-tail, with relative affinities Asp(780) > Ser(780) > Ala(780).	Aspartic Acid	191-194	kexin KEX2	Saccharomyces cerevisiae S288C	152-157
23408788-6	2013	Biochemical assays using purified Gga2p VHS-GGA and TOM1 (GAT) and glutathione S-transferase-Kex2p C-tail fusions show that Gga2p binds directly to the Kex2p C-tail, with relative affinities Asp(780) > Ser(780) > Ala(780).	Serine	205-208	kexin KEX2	Saccharomyces cerevisiae S288C	152-157
23408788-6	2013	Biochemical assays using purified Gga2p VHS-GGA and TOM1 (GAT) and glutathione S-transferase-Kex2p C-tail fusions show that Gga2p binds directly to the Kex2p C-tail, with relative affinities Asp(780) > Ser(780) > Ala(780).	Alanine	219-222	kexin KEX2	Saccharomyces cerevisiae S288C	152-157
23408788-7	2013	Affinity-purified antibody against a peptide containing phospho-Ser-(780) recognizes wild-type Kex2p but not S(780)A Kex2p, showing that Ser(780) is phosphorylated in vivo; phosphorylation of Ser(780) is up-regulated by cell wall-damaging drugs.	Serine	64-67	kexin KEX2	Saccharomyces cerevisiae S288C	95-100
23408788-8	2013	Finally, mutation of Ser(780) alters trafficking of Kex2p both in vivo and in cell-free trans-Golgi network (TGN)-prevacuolar compartment (PVC) transport.	Serine	21-24	kexin KEX2	Saccharomyces cerevisiae S288C	52-57
22487308-6	2012	Replacement of the native URA3 promoter with the HXT1, KEX2 or URA3-d promoter resulted in an increase in the PCN and LacZ activity by about 30-100%.	PREGNENOLONE CARBONITRILE	110-113	kexin KEX2	Saccharomyces cerevisiae S288C	55-59