PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
16243715-3	2005	CSK and CHK inactivate SFKs by specifically phosphorylating a consensus tyrosine (called Y(T)) near their C-termini.	Tyrosine	72-80	C-terminal Src kinase	Homo sapiens	0-3
16262686-4	2005	In addition, Csk and PAG, inhibitory molecules of the TCR signalling cascade, are also contained in the BCtheta-bound membranes.	bctheta	104-111	C-terminal Src kinase	Homo sapiens	13-16
16227616-6	2005	Notably, alpha4-stimulated cell motility was inhibited by catalytically inactive receptor protein-tyrosine phosphatase alpha overexpression and blocked by the p50Csk phosphorylation of c-Src at Tyr-529.	Tyrosine	194-197	C-terminal Src kinase	Homo sapiens	159-165
15958730-0	2005	Tyrosine phosphorylation of caveolin 1 by oxidative stress is reversible and dependent on the c-src tyrosine kinase but not mitogen-activated protein kinase pathways in placental artery endothelial cells.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	94-115
15958730-6	2005	Acute treatment with H(2)O(2) activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2, and MAPK11-p38(mapk)) and the c-src tyrosine kinase (CSK).	Hydrogen Peroxide	21-29	C-terminal Src kinase	Homo sapiens	195-216
15958730-6	2005	Acute treatment with H(2)O(2) activated multiple signaling pathways, including the mitogen-activated protein kinases (MAPK) members (MAPK3/1-ERK2/1, MAPK8/9-JNK1/2, and MAPK11-p38(mapk)) and the c-src tyrosine kinase (CSK).	Hydrogen Peroxide	21-29	C-terminal Src kinase	Homo sapiens	218-221
15958730-7	2005	Pharmacological studies demonstrated that, among these pathways, only the blockade of CSK activation abolished H(2)O(2)-induced CAV1 phosphorylation.	Hydrogen Peroxide	111-119	C-terminal Src kinase	Homo sapiens	86-89
15743820-3	2005	Instead, Csk becomes associated with an approximately 72-kDa tyrosine-phosphorylated protein, which we identify here as G3BP, a phosphoprotein reported to bind the SH3 domain of Ras GTPase-activating protein.	Tyrosine	61-69	C-terminal Src kinase	Homo sapiens	9-12
15914012-1	2005	Three-dimensional quantitative structure-activity relationship (3D-QSAR) analyses were carried out on quinazoline, quinoline, and cyanoquinoline derivatives inhibiting c-Src kinase.	Quinazolines	102-113	C-terminal Src kinase	Homo sapiens	168-180
15914012-1	2005	Three-dimensional quantitative structure-activity relationship (3D-QSAR) analyses were carried out on quinazoline, quinoline, and cyanoquinoline derivatives inhibiting c-Src kinase.	quinoline	115-124	C-terminal Src kinase	Homo sapiens	168-180
15914012-1	2005	Three-dimensional quantitative structure-activity relationship (3D-QSAR) analyses were carried out on quinazoline, quinoline, and cyanoquinoline derivatives inhibiting c-Src kinase.	Quinoline-2-carbonitrile	130-144	C-terminal Src kinase	Homo sapiens	168-180
16002086-5	2005	Previous studies demonstrated that the regulation of Csk activity is linked to conformational changes in the enzyme that can be probed with hydrogen-deuterium exchange methods.	Hydrogen	140-148	C-terminal Src kinase	Homo sapiens	53-56
16002086-5	2005	Previous studies demonstrated that the regulation of Csk activity is linked to conformational changes in the enzyme that can be probed with hydrogen-deuterium exchange methods.	Deuterium	149-158	C-terminal Src kinase	Homo sapiens	53-56
15890649-7	2005	Mutating these residues in the Csk or Chk SH2 domain to the Src counterpart resulted in dramatic gain of function similar to Src SH2 domain, whereas mutating Lys200 in Src SH2 domain to Glu (the Csk counterpart) resulted in loss of Src SH2 function.	Glutamic Acid	186-189	C-terminal Src kinase	Homo sapiens	195-198
15845350-2	2005	The initially described phosphorylation sites of Src include an activating phosphotyrosine 416 that results from autophosphorylation, and an inhibiting phosphotyrosine 527 that results from phosphorylation by C-terminal Src kinase (Csk) and Csk homologous kinase.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	209-230
15831486-6	2005	We further illustrate that EGF-dependent phosphorylation of Dok-R requires SFK activity and, more specifically, that SFK-dependent phosphorylation of tyrosine 402 on Dok-R facilitates the inducible recruitment of Csk.	Tyrosine	150-158	C-terminal Src kinase	Homo sapiens	213-216
15626731-6	2005	CD45 also bound to phosphoprotein associated with glycosphingolipid-enriched microdomains (PAGs), which were subsequently dephosphorylated, resulting in the release of C-terminal src kinase (Csk) from lipid rafts.	Glycosphingolipids	50-67	C-terminal Src kinase	Homo sapiens	168-189
15626731-6	2005	CD45 also bound to phosphoprotein associated with glycosphingolipid-enriched microdomains (PAGs), which were subsequently dephosphorylated, resulting in the release of C-terminal src kinase (Csk) from lipid rafts.	Glycosphingolipids	50-67	C-terminal Src kinase	Homo sapiens	191-194
15637072-13	2005	(viii) 5-HT stimulated tyrosine phosphorylation of c-Src kinase and PKC delta.	Tyrosine	23-31	C-terminal Src kinase	Homo sapiens	51-63
15474475-7	2004	Mutational analyses and phospho-peptide mapping suggested that the SH2 domain of Csk may preferentially bind to ITIM Y562 of CD85j; yet, mutation to phenylalanine of Y533, Y614, and Y644 also significantly reduced Csk recruitment by CD85j.	Phenylalanine	149-162	C-terminal Src kinase	Homo sapiens	81-84
14712234-5	2004	Conversely, expression of a dominant-negative Csk resulted in elevated SFK activation, enhanced phosphorylation of FAK and paxilllin, enhanced cell scattering, an increased number of focal contacts, dramatic rearrangement of actin cytoskeleton and increased cell adhesion/migration and in vitro invasiveness.	paxilllin	123-132	C-terminal Src kinase	Homo sapiens	46-49
15208781-4	2004	We show that the risk allele, which is present in approximately 17% of white individuals from the general population and in approximately 28% of white individuals with RA, disrupts the P1 proline-rich motif that is important for interaction with Csk, potentially altering these proteins" normal function as negative regulators of T-cell activation.	Proline	188-195	C-terminal Src kinase	Homo sapiens	246-249
15312765-6	2004	Based on hydrogen-deuterium exchange experiments, glycine substitution reduces flexibility in several polypeptide regions in Csk, tyrosine substitution increases flexibility, and alanine substitution leads to mixed effects compared to wild-type.	Glycine	50-57	C-terminal Src kinase	Homo sapiens	125-128
15008512-4	2003	The docking results showed that compounds (4), (25) and (26) were bound to the active site of the enzyme Lys 295 of p60(c-Src) tyrosine kinase.	Lysine	105-108	C-terminal Src kinase	Homo sapiens	120-142
14657361-5	2003	C-terminal Src kinase (Csk) is a PTK that specifically phosphorylates Src family kinases on a C-terminal Tyr.	Tyrosine	105-108	C-terminal Src kinase	Homo sapiens	0-21
14657361-5	2003	C-terminal Src kinase (Csk) is a PTK that specifically phosphorylates Src family kinases on a C-terminal Tyr.	Tyrosine	105-108	C-terminal Src kinase	Homo sapiens	23-26
15674841-0	2004	Studies on the mechanism of rapid activation of protein tyrosine phosphorylation activities, particularly c-Src kinase, by TCDD in MCF10A.	Polychlorinated Dibenzodioxins	123-127	C-terminal Src kinase	Homo sapiens	106-118
15674841-10	2004	These results support the conclusion that c-Src kinase is at least one of the earliest and the most upstream components of toxic signaling of the Ah-receptor activated by TCDD through the post-transcriptional process.	Polychlorinated Dibenzodioxins	171-175	C-terminal Src kinase	Homo sapiens	42-54
15674848-0	2004	TCDD causes suppression of growth and differentiation of MCF10A, human mammary epithelial cells by interfering with their insulin receptor signaling through c-Src kinase and ERK activation.	Polychlorinated Dibenzodioxins	0-4	C-terminal Src kinase	Homo sapiens	157-169
15674848-5	2004	To test the hypothesis that TCDD-induced c-Src kinase activation is casually related to this compound"s antagonistic action against insulin, we treated MCF10A cells with two c-Src blocking agents, an anti-Src antisense oligonucleotides blocker and a known specific inhibitor of c-Src kinase, PP-2 and studied the effect of insulin and TCDD on cell proliferation.	Polychlorinated Dibenzodioxins	28-32	C-terminal Src kinase	Homo sapiens	41-53
15674848-5	2004	To test the hypothesis that TCDD-induced c-Src kinase activation is casually related to this compound"s antagonistic action against insulin, we treated MCF10A cells with two c-Src blocking agents, an anti-Src antisense oligonucleotides blocker and a known specific inhibitor of c-Src kinase, PP-2 and studied the effect of insulin and TCDD on cell proliferation.	Polychlorinated Dibenzodioxins	28-32	C-terminal Src kinase	Homo sapiens	278-290
14692742-2	2003	Here, we show using expressed protein ligation with the signaling protein Src that it is feasible to install a covalently linked ATP moiety into the tail of Src, generating a semisynthetic protein with a high affinity for its cognate tyrosine kinase, Csk.	Adenosine Triphosphate	129-132	C-terminal Src kinase	Homo sapiens	251-254
14692742-3	2003	It is also established that this Src-ATP conjugate can be used to selectively pull down Csk from a complex protein mixture.	Adenosine Triphosphate	37-40	C-terminal Src kinase	Homo sapiens	88-91
12767803-8	2003	Chk (no inhibition up to 18.5 microM) and Csk (IC(50)= 1 microM) were differentially inhibited by PP2, probably due to the size difference of one residue (Thr265 in Csk versus Met304 in Chk) in the ATP-binding domain.	Adenosine Triphosphate	198-201	C-terminal Src kinase	Homo sapiens	42-45
14573751-8	2003	Supportively, inhibition of Src activity by overexpression of Csk resulted in attenuation of the tyrosine phosphorylation of VE-cadherin and endothelial cell (EC) tube formation.	Tyrosine	97-105	C-terminal Src kinase	Homo sapiens	62-65
12795607-2	2003	Tyrosine 892 is now thought to be the principal site for recognition by the c-Src tyrosine kinase; however, little is known about the regulation of this phosphorylation event in vivo.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	76-97
12938237-6	2003	We also demonstrate that anti-CD4 treatment stimulated Csk kinase associated to the membrane adapter, PAG/Cbp, without affecting the total amount of Csk bound to PAG/Cbp.	phenylacetylglycine	102-105	C-terminal Src kinase	Homo sapiens	55-58
12686554-2	2003	PTKs in the Csk family, Csk and Chk, are rare exceptions for lacking Tyr residues in this loop.	Tyrosine	69-72	C-terminal Src kinase	Homo sapiens	12-15
12686554-2	2003	PTKs in the Csk family, Csk and Chk, are rare exceptions for lacking Tyr residues in this loop.	Tyrosine	69-72	C-terminal Src kinase	Homo sapiens	24-27
12753909-2	2003	This study establishes that HER2/HRG signaling selectively upregulates Tyr phosphorylation of c-Src at Tyr-215 located within the SH2 domain, increases c-Src kinase activity and selectively upregulates Tyr phosphorylation of FAK at Tyr-861.	Tyrosine	71-74	C-terminal Src kinase	Homo sapiens	152-164
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	14-35
12665526-3	2003	While TCR-triggering resulted in transient dissociation of Csk from Cbp/PAG/rafts allowing TCR-induced tyrosine phosphorylation to occur, pretreatment with PGE(2) reduced Csk dissociation upon TCR triggering.	Tyrosine	103-111	C-terminal Src kinase	Homo sapiens	59-62
12665526-3	2003	While TCR-triggering resulted in transient dissociation of Csk from Cbp/PAG/rafts allowing TCR-induced tyrosine phosphorylation to occur, pretreatment with PGE(2) reduced Csk dissociation upon TCR triggering.	Prostaglandins E	156-159	C-terminal Src kinase	Homo sapiens	59-62
12665526-3	2003	While TCR-triggering resulted in transient dissociation of Csk from Cbp/PAG/rafts allowing TCR-induced tyrosine phosphorylation to occur, pretreatment with PGE(2) reduced Csk dissociation upon TCR triggering.	Prostaglandins E	156-159	C-terminal Src kinase	Homo sapiens	171-174
12665526-5	2003	Moreover, competition of endogenous Csk from lipid rafts abolished PGE(2)-mediated inhibition of TCR-induced zeta-chain phosphorylation and activation of the nuclear factor of activated T cells (NFAT) activator protein 1 (AP-1).	Dinoprostone	67-73	C-terminal Src kinase	Homo sapiens	36-39
12665526-6	2003	Finally, raft-associated Csk already activated via Cbp/PAG binding, gained additional increase in phosphotransferase activity upon protein kinase A-mediated phosphorylation of Csk.	phenylacetylglycine	55-58	C-terminal Src kinase	Homo sapiens	25-28
12665526-7	2003	We propose that cAMP regulates Csk via both spatial and enzymatic mechanisms, thereby inhibiting signaling through the TCR.	Cyclic AMP	16-20	C-terminal Src kinase	Homo sapiens	31-34
12665526-1	2003	Raft-associated Csk controls signaling through the T cell receptor (TCR) and was mainly anchored to Cbp/PAG (phosphoprotein associated with glycosphingolipid-enriched membrane domains).	Glycosphingolipids	140-157	C-terminal Src kinase	Homo sapiens	16-19
12665526-2	2003	Treatment of cells with the cAMP-elevating agent prostaglandin E(2) (PGE(2)) augmented the level of Cbp/PAG phosphorylation with a concomitant increase in amounts of Csk bound to Cbp/PAG.	Cyclic AMP	28-32	C-terminal Src kinase	Homo sapiens	166-169
12665526-2	2003	Treatment of cells with the cAMP-elevating agent prostaglandin E(2) (PGE(2)) augmented the level of Cbp/PAG phosphorylation with a concomitant increase in amounts of Csk bound to Cbp/PAG.	Dinoprostone	49-67	C-terminal Src kinase	Homo sapiens	166-169
12665526-2	2003	Treatment of cells with the cAMP-elevating agent prostaglandin E(2) (PGE(2)) augmented the level of Cbp/PAG phosphorylation with a concomitant increase in amounts of Csk bound to Cbp/PAG.	Dinoprostone	69-75	C-terminal Src kinase	Homo sapiens	166-169
12665526-2	2003	Treatment of cells with the cAMP-elevating agent prostaglandin E(2) (PGE(2)) augmented the level of Cbp/PAG phosphorylation with a concomitant increase in amounts of Csk bound to Cbp/PAG.	phenylacetylglycine	183-186	C-terminal Src kinase	Homo sapiens	166-169
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	37-40
12600271-0	2003	Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.	Serine	64-70	C-terminal Src kinase	Homo sapiens	90-93
12600271-2	2003	Although isolated Csk kinase domain was phosphorylated at Ser(364) by PKA to the same stoichiometry as wild-type Csk, significant activation of the isolated Csk kinase domain by PKA was observed only in the presence of the purified Src homology 3 domain (SH3 domain).	Serine	58-61	C-terminal Src kinase	Homo sapiens	18-21
12606547-1	2003	Regulation of Src kinase activity is tightly coupled to the phosphorylation status of the C-terminal regulatory tyrosine Tyr(527), which, when phosphorylated by Csk, represses Src.	Tyrosine	112-124	C-terminal Src kinase	Homo sapiens	161-164
12606547-2	2003	Here, we demonstrate that activation of Csk through a prostaglandin E(2)-cAMP-protein kinase A (PKA) pathway inhibits Src.	Dinoprostone	54-72	C-terminal Src kinase	Homo sapiens	40-43
12606547-3	2003	This inhibitory pathway is operative in detergent-resistant membrane fractions where cAMP-elevating agents activate Csk, resulting in a concomitant decrease in Src activity.	Cyclic AMP	85-89	C-terminal Src kinase	Homo sapiens	116-119
12606547-5	2003	Furthermore, epidermal growth factor-induced activation of Src and phosphorylation of the Src substrates Cbl and focal adhesion kinase are inhibited by activation of the cAMP-PKA-Csk pathway.	Cyclic AMP	170-174	C-terminal Src kinase	Homo sapiens	179-182
12606547-6	2003	We propose a novel mechanism whereby G protein-coupled receptors inhibit Src signaling by activation of Csk in a cAMP-PKA-dependent manner.	Cyclic AMP	113-117	C-terminal Src kinase	Homo sapiens	104-107
12444928-3	2003	Tyr-568 has previously been identified as the binding site of the Src family of tyrosine kinases, the Csk-homologous kinase CHK, and the protein tyrosine phosphatase SHP-2.	Tyrosine	0-3	C-terminal Src kinase	Homo sapiens	102-105
12727858-5	2003	Inhibition of C-SRC tyrosine kinase activity also blocks PGE(2)-induced HIF-1alpha protein and VEGF mRNA expression without blocking ERK phosphorylation.	Dinoprostone	57-63	C-terminal Src kinase	Homo sapiens	14-35
12697812-2	2003	We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association.	Tyrosine	101-109	C-terminal Src kinase	Homo sapiens	128-149
12485116-2	2003	Proximal signalling pathways involve PTKs of the Src, Syk, Csk and Tec families, adapter proteins and effector enzymes in a highly organized tyrosine-phosphorylation cascade.	Tyrosine	141-149	C-terminal Src kinase	Homo sapiens	59-62
12417200-0	2002	Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS).	Hydrogen	95-103	C-terminal Src kinase	Homo sapiens	64-67
12612075-2	2003	In resting human T cells, PAG is tyrosine phosphorylated and associated with Csk, an inhibitor of Src-related protein tyrosine kinases.	phenylacetylglycine	26-29	C-terminal Src kinase	Homo sapiens	77-80
12612075-7	2003	By expressing wild-type and phosphorylation-defective (dominant-negative) PAG polypeptides in these cells, we found that the inhibitory effect of PAG is dependent on its capacity to be tyrosine phosphorylated and to associate with Csk.	phenylacetylglycine	146-149	C-terminal Src kinase	Homo sapiens	231-234
12612075-8	2003	PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk.	phenylacetylglycine	0-3	C-terminal Src kinase	Homo sapiens	238-241
12612075-8	2003	PAG-mediated inhibition was accompanied by a repression of proximal TCR signaling and was rescued by expression of a constitutively activated Src-related kinase, implying that it is due to an inactivation of Src kinases by PAG-associated Csk.	phenylacetylglycine	223-226	C-terminal Src kinase	Homo sapiens	238-241
12612075-12	2003	Taken together, these data provide firm evidence that PAG is a bona fide negative regulator of T-cell activation as a result of its capacity to recruit Csk.	phenylacetylglycine	54-57	C-terminal Src kinase	Homo sapiens	152-155
12454411-3	2003	The spatial arrangement of the CSK network was therefore studied in fixed cells probed by beads and stained for F-actin by rhodamined phalloidine.	rhodamined phalloidine	123-145	C-terminal Src kinase	Homo sapiens	31-34
12468645-2	2002	We have previously reported the activation of c-Src tyrosine kinase during ovarian steroid-induced decidualization of cultured human endometrial stromal cells.	Steroids	83-90	C-terminal Src kinase	Homo sapiens	46-67
12417200-0	2002	Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS).	Deuterium	104-113	C-terminal Src kinase	Homo sapiens	64-67
12417200-0	2002	Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS).	Dexamethasone	146-150	C-terminal Src kinase	Homo sapiens	64-67
12417200-2	2002	We have employed enhanced methods of hydrogen-deuterium exchange-mass spectrometry (DXMS) to probe conformational changes on CSK in the absence and presence of nucleotides and thereby provide a structural framework for understanding phosphorylation-driven conformational changes.	Hydrogen	37-45	C-terminal Src kinase	Homo sapiens	125-128
12417200-2	2002	We have employed enhanced methods of hydrogen-deuterium exchange-mass spectrometry (DXMS) to probe conformational changes on CSK in the absence and presence of nucleotides and thereby provide a structural framework for understanding phosphorylation-driven conformational changes.	Deuterium	46-55	C-terminal Src kinase	Homo sapiens	125-128
12417200-2	2002	We have employed enhanced methods of hydrogen-deuterium exchange-mass spectrometry (DXMS) to probe conformational changes on CSK in the absence and presence of nucleotides and thereby provide a structural framework for understanding phosphorylation-driven conformational changes.	Dexamethasone	84-88	C-terminal Src kinase	Homo sapiens	125-128
12417200-9	2002	These results imply that delivery of the gamma phosphate group of ATP induces unique local and long-range conformational changes in CSK that may influence regulatory motions in the catalytic pathway.	Phosphates	47-56	C-terminal Src kinase	Homo sapiens	132-135
12417200-9	2002	These results imply that delivery of the gamma phosphate group of ATP induces unique local and long-range conformational changes in CSK that may influence regulatory motions in the catalytic pathway.	Adenosine Triphosphate	66-69	C-terminal Src kinase	Homo sapiens	132-135
12022825-1	2002	In contrast to previous studies that have shown that the neutral phenol serves as the nucleophile for WT Csk-promoted phosphorylation of a tyrosine-containing substrate, the phenolate ion acts as primary nucleophile for the D314N Csk-catalyzed reaction.	Phenol	65-71	C-terminal Src kinase	Homo sapiens	105-108
12356311-3	2002	It was found that W352 contributed approximately 35% of the total Trp fluorescence of Csk even though seven other Trp residues were present.	Tryptophan	114-117	C-terminal Src kinase	Homo sapiens	86-89
12356311-4	2002	The enhanced contribution by W352 to Csk fluorescence was due to an interaction between its indole ring and the positively charged guanidino group of R318.	w352	29-33	C-terminal Src kinase	Homo sapiens	37-40
12356311-4	2002	The enhanced contribution by W352 to Csk fluorescence was due to an interaction between its indole ring and the positively charged guanidino group of R318.	indole	92-98	C-terminal Src kinase	Homo sapiens	37-40
12269817-7	2002	Changing all of these sites to phenylalanine resulted in a villin mutant that neither was phosphorylated in TKX1 cells nor was a substrate for c-src kinase in an in vitro kinase assay.	Phenylalanine	31-44	C-terminal Src kinase	Homo sapiens	143-155
12052863-4	2002	We show that hnRNP K and the c-Src kinase specifically interact with each other, leading to c-Src activation and tyrosine phosphorylation of hnRNP K in vivo and in vitro.	Tyrosine	113-121	C-terminal Src kinase	Homo sapiens	29-41
12356311-2	2002	The spectral properties of the intrinsic Trp fluorescence of Csk and their underlying structural features were investigated in combination with urea denaturation and site-specific mutagenesis.	Tryptophan	41-44	C-terminal Src kinase	Homo sapiens	61-64
12356311-2	2002	The spectral properties of the intrinsic Trp fluorescence of Csk and their underlying structural features were investigated in combination with urea denaturation and site-specific mutagenesis.	Urea	144-148	C-terminal Src kinase	Homo sapiens	61-64
12356311-3	2002	It was found that W352 contributed approximately 35% of the total Trp fluorescence of Csk even though seven other Trp residues were present.	w352	18-22	C-terminal Src kinase	Homo sapiens	86-89
12356311-3	2002	It was found that W352 contributed approximately 35% of the total Trp fluorescence of Csk even though seven other Trp residues were present.	Tryptophan	66-69	C-terminal Src kinase	Homo sapiens	86-89
12022825-1	2002	In contrast to previous studies that have shown that the neutral phenol serves as the nucleophile for WT Csk-promoted phosphorylation of a tyrosine-containing substrate, the phenolate ion acts as primary nucleophile for the D314N Csk-catalyzed reaction.	Tyrosine	139-147	C-terminal Src kinase	Homo sapiens	105-108
12022825-2	2002	Rate comparisons of D314N Csk-promoted phosphotransfer using a series of fluorotyrosine-containing peptide substrates reveal a near zero beta(nuc), consistent with a dissociative mechanism of phosphotransfer.	fluorotyrosine	73-87	C-terminal Src kinase	Homo sapiens	26-29
11940607-4	2002	Csk, which negatively regulates Src by phosphorylating Tyr-529, was also constitutively associated with alphaIIbbeta3.	Tyrosine	55-58	C-terminal Src kinase	Homo sapiens	0-3
11328818-5	2001	In vivo S2V was tyrosine-phosphorylated when co-expressed with exogenous c-Src kinase.	Tyrosine	16-24	C-terminal Src kinase	Homo sapiens	73-85
11552794-0	2001	Protein tyrosine kinase Csk-catalyzed phosphorylation of Src containing unnatural tyrosine analogues.	Tyrosine	8-16	C-terminal Src kinase	Homo sapiens	24-27
11451957-0	2001	Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14).	Cysteine	47-50	C-terminal Src kinase	Homo sapiens	85-106
11451957-0	2001	Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14).	Tyrosine	247-250	C-terminal Src kinase	Homo sapiens	85-106
11451957-5	2001	Here, we show that palmitoylation of caveolin-1 at a single site (Cys-156) is required for coupling caveolin-1 to the c-Src tyrosine kinase.	Cysteine	66-69	C-terminal Src kinase	Homo sapiens	118-139
11755212-7	2001	Taken together, these results demonstrate that 1,25(OH)2D3 stimulates proliferation-associated signalling pathways in skeletal muscle cells and implicate c-Src kinase as mediator of this response.	Calcitriol	47-58	C-terminal Src kinase	Homo sapiens	154-166
11685249-1	2001	C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells.	Proline	132-139	C-terminal Src kinase	Homo sapiens	0-21
11685249-1	2001	C-terminal Src kinase (Csk) takes part in a highly specific, high affinity interaction via its Src homology 3 (SH3) domain with the proline-enriched tyrosine phosphatase PEP in hematopoietic cells.	Proline	132-139	C-terminal Src kinase	Homo sapiens	23-26
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Peptides	74-81	C-terminal Src kinase	Homo sapiens	30-33
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Proline	91-94	C-terminal Src kinase	Homo sapiens	30-33
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Glutamic Acid	95-98	C-terminal Src kinase	Homo sapiens	30-33
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Serine	99-102	C-terminal Src kinase	Homo sapiens	30-33
11685249-2	2001	The solution structure of the Csk-SH3 domain in complex with a 25-residue peptide from the Pro/Glu/Ser/Thr-rich (PEST) domain of PEP reveals the basis for this specific peptide recognition motif involving an SH3 domain.	Threonine	103-106	C-terminal Src kinase	Homo sapiens	30-33
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Alanine	16-19	C-terminal Src kinase	Homo sapiens	64-67
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Threonine	0-3	C-terminal Src kinase	Homo sapiens	64-67
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Lysine	35-38	C-terminal Src kinase	Homo sapiens	64-67
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Isoleucine	117-120	C-terminal Src kinase	Homo sapiens	64-67
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Valine	129-132	C-terminal Src kinase	Homo sapiens	64-67
11685249-3	2001	Three residues, Ala 40, Thr 42 and Lys 43, in the SH3 domain of Csk specifically recognize two hydrophobic residues, Ile 625 and Val 626, in the proline-rich sequence of the PEST domain of PEP.	Proline	145-152	C-terminal Src kinase	Homo sapiens	64-67
11551213-9	2001	These findings indicate that Csk rapidly delivers the gamma-phosphate of ATP to the substrate and rapidly releases the phosphoproduct.	gamma-phosphate	54-69	C-terminal Src kinase	Homo sapiens	29-32
11551213-9	2001	These findings indicate that Csk rapidly delivers the gamma-phosphate of ATP to the substrate and rapidly releases the phosphoproduct.	Adenosine Triphosphate	73-76	C-terminal Src kinase	Homo sapiens	29-32
11408488-2	2001	In contrast to other cell types, IkappaBalpha, in bone marrow macrophages (BMMs), which are osteoclast precursors, is tyrosine-phosphorylated by c-Src kinase.	Tyrosine	118-126	C-terminal Src kinase	Homo sapiens	145-157
11390365-1	2001	In resting peripheral T cells, Csk is constitutively present in lipid rafts through an interaction with the Csk SH2-binding protein, PAG, also known as Cbp.	phenylacetylglycine	133-136	C-terminal Src kinase	Homo sapiens	31-34
11390365-1	2001	In resting peripheral T cells, Csk is constitutively present in lipid rafts through an interaction with the Csk SH2-binding protein, PAG, also known as Cbp.	phenylacetylglycine	133-136	C-terminal Src kinase	Homo sapiens	108-111
11390365-3	2001	However, tyrosine phosphorylation of PAG/Cbp resumes after 3--5 min, at which time Csk reassociates with the rafts.	Tyrosine	9-17	C-terminal Src kinase	Homo sapiens	83-86
11390365-3	2001	However, tyrosine phosphorylation of PAG/Cbp resumes after 3--5 min, at which time Csk reassociates with the rafts.	phenylacetylglycine	37-40	C-terminal Src kinase	Homo sapiens	83-86
11278729-10	2001	c-Src kinase activity correspondingly increased the tyrosine 705 phosphorylation and DNA binding affinity of Stat3 (but not Stat1, -5A, or -5B).	Tyrosine	52-60	C-terminal Src kinase	Homo sapiens	0-12
11278940-0	2001	c-Src tyrosine kinase binds the beta 2-adrenergic receptor via phospho-Tyr-350, phosphorylates G-protein-linked receptor kinase 2, and mediates agonist-induced receptor desensitization.	Tyrosine	71-74	C-terminal Src kinase	Homo sapiens	0-21
11084024-0	2001	CD44 interaction with c-Src kinase promotes cortactin-mediated cytoskeleton function and hyaluronic acid-dependent ovarian tumor cell migration.	Hyaluronic Acid	89-104	C-terminal Src kinase	Homo sapiens	22-34
11084024-3	2001	Furthermore, the binding of HA to SK-OV-3.ipl cells promotes c-Src kinase recruitment to CD44 and stimulates c-Src kinase activity, which, in turn, increases tyrosine phosphorylation of the cytoskeletal protein, cortactin.	Tyrosine	158-166	C-terminal Src kinase	Homo sapiens	109-121
11006267-2	2000	In this study, the role of this Arg (Arg-318) in the protein-tyrosine kinase C-terminal Src kinase (Csk) was investigated.	Arginine	32-35	C-terminal Src kinase	Homo sapiens	77-98
11162381-0	2001	Affinity purification of Csk protein tyrosine kinase based on its catalytic requirement for divalent metal cations.	Metals	101-106	C-terminal Src kinase	Homo sapiens	25-28
11162381-1	2001	Protein tyrosine kinase Csk requires two Mg2+ ions for activity: one magnesium is part of the ATP-Mg complex, and the second free Mg2+ ion is required as an essential activator.	magnesium ion	41-45	C-terminal Src kinase	Homo sapiens	24-27
11162381-1	2001	Protein tyrosine kinase Csk requires two Mg2+ ions for activity: one magnesium is part of the ATP-Mg complex, and the second free Mg2+ ion is required as an essential activator.	Magnesium	69-78	C-terminal Src kinase	Homo sapiens	24-27
11162381-1	2001	Protein tyrosine kinase Csk requires two Mg2+ ions for activity: one magnesium is part of the ATP-Mg complex, and the second free Mg2+ ion is required as an essential activator.	atp-mg	94-100	C-terminal Src kinase	Homo sapiens	24-27
11162381-1	2001	Protein tyrosine kinase Csk requires two Mg2+ ions for activity: one magnesium is part of the ATP-Mg complex, and the second free Mg2+ ion is required as an essential activator.	magnesium ion	130-134	C-terminal Src kinase	Homo sapiens	24-27
11162381-2	2001	Zn2+ can bind to this site to replace Mg2+, which inhibits Csk kinase activity.	Zinc	0-4	C-terminal Src kinase	Homo sapiens	59-62
11162381-2	2001	Zn2+ can bind to this site to replace Mg2+, which inhibits Csk kinase activity.	magnesium ion	38-42	C-terminal Src kinase	Homo sapiens	59-62
11162381-3	2001	The binding is reversible and removal of Zn2+ results in an active Csk apoenzyme.	Zinc	41-45	C-terminal Src kinase	Homo sapiens	67-70
11162381-5	2001	When bacterial cell lysate containing overexpressed GST-Csk was applied to a column of Zn2+-iminodiacetic acid immobilized to agarose, Csk was specifically retained by the column.	zn2+-iminodiacetic acid	87-110	C-terminal Src kinase	Homo sapiens	56-59
11162381-5	2001	When bacterial cell lysate containing overexpressed GST-Csk was applied to a column of Zn2+-iminodiacetic acid immobilized to agarose, Csk was specifically retained by the column.	zn2+-iminodiacetic acid	87-110	C-terminal Src kinase	Homo sapiens	135-138
11006267-7	2000	Imidazole is the best of these activators, enhancing phosphorylation rates by Csk R318A up to 100-fold for poly(Glu,Tyr) and significantly stimulating Csk R318A phosphorylation of the physiologic substrate Src.	Glutamic Acid	112-115	C-terminal Src kinase	Homo sapiens	78-81
11006267-7	2000	Imidazole is the best of these activators, enhancing phosphorylation rates by Csk R318A up to 100-fold for poly(Glu,Tyr) and significantly stimulating Csk R318A phosphorylation of the physiologic substrate Src.	Tyrosine	116-119	C-terminal Src kinase	Homo sapiens	78-81
11329267-0	2001	Molecular determinants for Csk-catalyzed tyrosine phosphorylation of the Src tail.	Tyrosine	41-49	C-terminal Src kinase	Homo sapiens	27-30
11329267-2	2001	The protein tyrosine kinase Csk is responsible for catalyzing the phosphorylation of this key Src tyrosine residue, but the detailed molecular basis for Src recognition and catalysis is poorly understood.	Tyrosine	12-20	C-terminal Src kinase	Homo sapiens	28-31
11181701-0	2001	Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor.	Cyclic AMP	52-56	C-terminal Src kinase	Homo sapiens	18-42
11181701-0	2001	Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor.	Cyclic AMP	52-56	C-terminal Src kinase	Homo sapiens	44-47
11181701-4	2001	Phosphorylation of residue Y505 in Lck by COOH-terminal Src kinase (Csk), which negatively regulates Lck, is essential for the inhibitory effect of cAMP on zeta chain phosphorylation.	y505	27-31	C-terminal Src kinase	Homo sapiens	42-66
11181701-4	2001	Phosphorylation of residue Y505 in Lck by COOH-terminal Src kinase (Csk), which negatively regulates Lck, is essential for the inhibitory effect of cAMP on zeta chain phosphorylation.	y505	27-31	C-terminal Src kinase	Homo sapiens	68-71
11181701-4	2001	Phosphorylation of residue Y505 in Lck by COOH-terminal Src kinase (Csk), which negatively regulates Lck, is essential for the inhibitory effect of cAMP on zeta chain phosphorylation.	Cyclic AMP	148-152	C-terminal Src kinase	Homo sapiens	42-66
11181701-4	2001	Phosphorylation of residue Y505 in Lck by COOH-terminal Src kinase (Csk), which negatively regulates Lck, is essential for the inhibitory effect of cAMP on zeta chain phosphorylation.	Cyclic AMP	148-152	C-terminal Src kinase	Homo sapiens	68-71
11181701-5	2001	PKA phosphorylates Csk at S364 in vitro and in vivo leading to a two- to fourfold increase in Csk activity that is necessary for cAMP-mediated inhibition of TCR-induced interleukin 2 secretion.	Cyclic AMP	129-133	C-terminal Src kinase	Homo sapiens	19-22
11181701-5	2001	PKA phosphorylates Csk at S364 in vitro and in vivo leading to a two- to fourfold increase in Csk activity that is necessary for cAMP-mediated inhibition of TCR-induced interleukin 2 secretion.	Cyclic AMP	129-133	C-terminal Src kinase	Homo sapiens	94-97
11181701-6	2001	Both PKA type I and Csk are targeted to lipid rafts where proximal T cell activation occurs, and phosphorylation of raft-associated Lck by Csk is increased in cells treated with forskolin.	Colforsin	178-187	C-terminal Src kinase	Homo sapiens	20-23
11181701-6	2001	Both PKA type I and Csk are targeted to lipid rafts where proximal T cell activation occurs, and phosphorylation of raft-associated Lck by Csk is increased in cells treated with forskolin.	Colforsin	178-187	C-terminal Src kinase	Homo sapiens	139-142
11162381-5	2001	When bacterial cell lysate containing overexpressed GST-Csk was applied to a column of Zn2+-iminodiacetic acid immobilized to agarose, Csk was specifically retained by the column.	Sepharose	126-133	C-terminal Src kinase	Homo sapiens	56-59
11162381-5	2001	When bacterial cell lysate containing overexpressed GST-Csk was applied to a column of Zn2+-iminodiacetic acid immobilized to agarose, Csk was specifically retained by the column.	Sepharose	126-133	C-terminal Src kinase	Homo sapiens	135-138
11162381-6	2001	Since the binding of Csk to Zn2+ is not affected by up to 200 mM NaCl, high ionic strength conditions were used in the purification procedure, minimizing nonspecific binding due to ionic interactions.	Zinc	28-32	C-terminal Src kinase	Homo sapiens	21-24
11162381-8	2001	The retained Csk enzyme was eluted with 1 M imidazole.	imidazole	44-53	C-terminal Src kinase	Homo sapiens	13-16
11162381-9	2001	The 1 M imidazole-eluted fraction contained pure Csk that had a specific activity similar to the enzyme purified by a glutathione-agarose affinity column.	imidazole	8-17	C-terminal Src kinase	Homo sapiens	49-52
11162381-9	2001	The 1 M imidazole-eluted fraction contained pure Csk that had a specific activity similar to the enzyme purified by a glutathione-agarose affinity column.	Glutathione	118-129	C-terminal Src kinase	Homo sapiens	49-52
11162381-9	2001	The 1 M imidazole-eluted fraction contained pure Csk that had a specific activity similar to the enzyme purified by a glutathione-agarose affinity column.	Sepharose	130-137	C-terminal Src kinase	Homo sapiens	49-52
11006267-2	2000	In this study, the role of this Arg (Arg-318) in the protein-tyrosine kinase C-terminal Src kinase (Csk) was investigated.	Arginine	32-35	C-terminal Src kinase	Homo sapiens	100-103
11006267-2	2000	In this study, the role of this Arg (Arg-318) in the protein-tyrosine kinase C-terminal Src kinase (Csk) was investigated.	Arginine	37-40	C-terminal Src kinase	Homo sapiens	77-98
11006267-2	2000	In this study, the role of this Arg (Arg-318) in the protein-tyrosine kinase C-terminal Src kinase (Csk) was investigated.	Arginine	37-40	C-terminal Src kinase	Homo sapiens	100-103
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	copolymer	54-63	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	copolymer	54-63	C-terminal Src kinase	Homo sapiens	168-171
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	poly	56-60	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	poly	56-60	C-terminal Src kinase	Homo sapiens	168-171
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Glutamic Acid	69-72	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Glutamic Acid	69-72	C-terminal Src kinase	Homo sapiens	168-171
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Tyrosine	73-76	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Tyrosine	73-76	C-terminal Src kinase	Homo sapiens	168-171
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Adenosine Triphosphate	201-204	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	poly	64-68	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	poly	64-68	C-terminal Src kinase	Homo sapiens	168-171
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Glutamic Acid	214-217	C-terminal Src kinase	Homo sapiens	91-94
11006267-3	2000	The observed k(cat) for phosphorylation of the random copolymer poly(Glu,Tyr) substrate by Csk R318A is approximately 3000-fold smaller compared with that of wild type Csk, whereas the K(m) values for ATP and poly(Glu,Tyr) are only mildly affected.	Tyrosine	218-221	C-terminal Src kinase	Homo sapiens	91-94
11006267-4	2000	The k(cat) value for poly(Glu,Tyr) phosphorylation by the Csk double mutant A316R,R318A is 100-fold greater than the k(cat) value for the single R318A mutant, suggesting that an Arg positioned at the alternative location fulfills a similar function as in wild type.	poly	21-25	C-terminal Src kinase	Homo sapiens	58-61
11006267-4	2000	The k(cat) value for poly(Glu,Tyr) phosphorylation by the Csk double mutant A316R,R318A is 100-fold greater than the k(cat) value for the single R318A mutant, suggesting that an Arg positioned at the alternative location fulfills a similar function as in wild type.	Glutamic Acid	26-29	C-terminal Src kinase	Homo sapiens	58-61
11006267-4	2000	The k(cat) value for poly(Glu,Tyr) phosphorylation by the Csk double mutant A316R,R318A is 100-fold greater than the k(cat) value for the single R318A mutant, suggesting that an Arg positioned at the alternative location fulfills a similar function as in wild type.	Tyrosine	30-33	C-terminal Src kinase	Homo sapiens	58-61
11006267-4	2000	The k(cat) value for poly(Glu,Tyr) phosphorylation by the Csk double mutant A316R,R318A is 100-fold greater than the k(cat) value for the single R318A mutant, suggesting that an Arg positioned at the alternative location fulfills a similar function as in wild type.	Arginine	178-181	C-terminal Src kinase	Homo sapiens	58-61
11006267-5	2000	Csk R318A kinase activity can also be partially recovered by several exogenous small molecules including guanidinium and imidazole.	Guanidine	105-116	C-terminal Src kinase	Homo sapiens	0-3
11006267-5	2000	Csk R318A kinase activity can also be partially recovered by several exogenous small molecules including guanidinium and imidazole.	imidazole	121-130	C-terminal Src kinase	Homo sapiens	0-3
11006267-7	2000	Imidazole is the best of these activators, enhancing phosphorylation rates by Csk R318A up to 100-fold for poly(Glu,Tyr) and significantly stimulating Csk R318A phosphorylation of the physiologic substrate Src.	imidazole	0-9	C-terminal Src kinase	Homo sapiens	78-81
11006267-7	2000	Imidazole is the best of these activators, enhancing phosphorylation rates by Csk R318A up to 100-fold for poly(Glu,Tyr) and significantly stimulating Csk R318A phosphorylation of the physiologic substrate Src.	imidazole	0-9	C-terminal Src kinase	Homo sapiens	151-154
11006267-7	2000	Imidazole is the best of these activators, enhancing phosphorylation rates by Csk R318A up to 100-fold for poly(Glu,Tyr) and significantly stimulating Csk R318A phosphorylation of the physiologic substrate Src.	poly	107-111	C-terminal Src kinase	Homo sapiens	78-81
11075810-2	2000	Tyrosine 14 is now thought to be the principal site for recognition by c-Src kinase; however, little is known about this phosphorylation event.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	71-83
11054667-3	2000	C-terminal Src kinase (Csk) has been demonstrated to negatively regulate Src family tyrosine kinases through tyrosine phosphorylation at the C-terminal regulatory site (Tyr-527).	Tyrosine	84-92	C-terminal Src kinase	Homo sapiens	0-21
11054667-3	2000	C-terminal Src kinase (Csk) has been demonstrated to negatively regulate Src family tyrosine kinases through tyrosine phosphorylation at the C-terminal regulatory site (Tyr-527).	Tyrosine	84-92	C-terminal Src kinase	Homo sapiens	23-26
11054667-3	2000	C-terminal Src kinase (Csk) has been demonstrated to negatively regulate Src family tyrosine kinases through tyrosine phosphorylation at the C-terminal regulatory site (Tyr-527).	Tyrosine	169-172	C-terminal Src kinase	Homo sapiens	0-21
11054667-3	2000	C-terminal Src kinase (Csk) has been demonstrated to negatively regulate Src family tyrosine kinases through tyrosine phosphorylation at the C-terminal regulatory site (Tyr-527).	Tyrosine	169-172	C-terminal Src kinase	Homo sapiens	23-26
10896106-0	2000	Tyrosine analogues as alternative substrates for protein tyrosine kinase Csk: insights into substrate selectivity and catalytic mechanism.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	73-76
10893418-4	2000	Using a heterologous expression system, we observed that co-expression of murine BK(Ca) channel and the human cSrc tyrosine kinase in HEK 293 cells led to a calcium-sensitive enhancement of BK(Ca) channel activity in excised membrane patches.	Calcium	157-164	C-terminal Src kinase	Homo sapiens	110-130
10962558-4	2000	An inhibitor specific for Src family kinase or expression of Csk reduced tyrosine phosphorylation of nectin-2delta.	Tyrosine	73-81	C-terminal Src kinase	Homo sapiens	61-64
10974196-0	2000	Biochemical and cellular effects of c-Src kinase-selective pyrido[2, 3-d]pyrimidine tyrosine kinase inhibitors.	pyrido[2, 3-d]pyrimidine	59-83	C-terminal Src kinase	Homo sapiens	36-48
10974196-3	2000	The compounds were ATP-competitive inhibitors of c-Src kinase with IC(50) values < 10 nM and from 6 to >100-fold selectivity for c-Src tyrosine kinase relative to basic fibroblast growth factor receptor (bFGFr) tyrosine kinase, platelet-derived growth factor receptor (PDGFr) tyrosine kinase, and epidermal growth factor receptor (EGFr) tyrosine kinase.	Adenosine Triphosphate	19-22	C-terminal Src kinase	Homo sapiens	49-61
10974196-3	2000	The compounds were ATP-competitive inhibitors of c-Src kinase with IC(50) values < 10 nM and from 6 to >100-fold selectivity for c-Src tyrosine kinase relative to basic fibroblast growth factor receptor (bFGFr) tyrosine kinase, platelet-derived growth factor receptor (PDGFr) tyrosine kinase, and epidermal growth factor receptor (EGFr) tyrosine kinase.	Adenosine Triphosphate	19-22	C-terminal Src kinase	Homo sapiens	135-156
10974196-8	2000	In a mitogenesis assay measuring thymidine incorporation stimulated by specific mitogens, the c-Src tyrosine kinase inhibitors reduced incorporated thymidine in a manner consistent with previously reported roles of c-Src in mitogenic signaling.	Thymidine	33-42	C-terminal Src kinase	Homo sapiens	94-115
10974196-8	2000	In a mitogenesis assay measuring thymidine incorporation stimulated by specific mitogens, the c-Src tyrosine kinase inhibitors reduced incorporated thymidine in a manner consistent with previously reported roles of c-Src in mitogenic signaling.	Thymidine	148-157	C-terminal Src kinase	Homo sapiens	94-115
10918051-1	2000	Csk (carboxyl-terminal Src kinase) is a cytoplasmic tyrosine kinase that phosphorylates a critical tyrosine residue in each of the Src family kinases (SFKs) to inhibit their activities.	Tyrosine	52-60	C-terminal Src kinase	Homo sapiens	0-3
10918051-1	2000	Csk (carboxyl-terminal Src kinase) is a cytoplasmic tyrosine kinase that phosphorylates a critical tyrosine residue in each of the Src family kinases (SFKs) to inhibit their activities.	Tyrosine	52-60	C-terminal Src kinase	Homo sapiens	5-33
10918051-7	2000	Csk was also activated by a phosphopeptide containing the tyrosine in Cbp that binds to Csk (Tyr-314).	Tyrosine	58-66	C-terminal Src kinase	Homo sapiens	0-3
10918051-7	2000	Csk was also activated by a phosphopeptide containing the tyrosine in Cbp that binds to Csk (Tyr-314).	Tyrosine	58-66	C-terminal Src kinase	Homo sapiens	88-91
10918051-7	2000	Csk was also activated by a phosphopeptide containing the tyrosine in Cbp that binds to Csk (Tyr-314).	Tyrosine	93-96	C-terminal Src kinase	Homo sapiens	0-3
10918051-7	2000	Csk was also activated by a phosphopeptide containing the tyrosine in Cbp that binds to Csk (Tyr-314).	Tyrosine	93-96	C-terminal Src kinase	Homo sapiens	88-91
10896106-2	2000	Details of tyrosine substrate specificity within the context of a short peptide were investigated for protein tyrosine kinase Csk.	Tyrosine	11-19	C-terminal Src kinase	Homo sapiens	126-129
10845713-0	2000	Tyrosine nitration of c-SRC tyrosine kinase in human pancreatic ductal adenocarcinoma.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	22-43
10788500-0	2000	Overexpression of C-terminal Src kinase blocks 14, 15-epoxyeicosatrienoic acid-induced tyrosine phosphorylation and mitogenesis.	14,15-epoxy-5,8,11-eicosatrienoic acid	47-78	C-terminal Src kinase	Homo sapiens	18-39
10788500-0	2000	Overexpression of C-terminal Src kinase blocks 14, 15-epoxyeicosatrienoic acid-induced tyrosine phosphorylation and mitogenesis.	Tyrosine	87-95	C-terminal Src kinase	Homo sapiens	18-39
10788500-7	2000	In contrast, both EGF and FBS significantly increased [(3)H]thymidine incorporation in CSK cells.	Thymidine	60-69	C-terminal Src kinase	Homo sapiens	87-90
10845713-6	2000	Immunoprecipitation coupled with Western analysis identified c-Src tyrosine kinase as a target of both tyrosine nitration and tyrosine phosphorylation.	Tyrosine	103-111	C-terminal Src kinase	Homo sapiens	61-82
10845713-7	2000	Peroxynitrite treatment of human pancreatic carcinoma cells in vitro resulted in increased tyrosine nitration and tyrosine phosphorylation of c-Src kinase, increased (>2-fold) c-Src kinase activity, and increased association between c-Src kinase and its downstream substrate cortactin.	Peroxynitrous Acid	0-13	C-terminal Src kinase	Homo sapiens	142-154
10845713-7	2000	Peroxynitrite treatment of human pancreatic carcinoma cells in vitro resulted in increased tyrosine nitration and tyrosine phosphorylation of c-Src kinase, increased (>2-fold) c-Src kinase activity, and increased association between c-Src kinase and its downstream substrate cortactin.	Peroxynitrous Acid	0-13	C-terminal Src kinase	Homo sapiens	179-191
10845713-7	2000	Peroxynitrite treatment of human pancreatic carcinoma cells in vitro resulted in increased tyrosine nitration and tyrosine phosphorylation of c-Src kinase, increased (>2-fold) c-Src kinase activity, and increased association between c-Src kinase and its downstream substrate cortactin.	Peroxynitrous Acid	0-13	C-terminal Src kinase	Homo sapiens	179-191
10845713-8	2000	Collectively, these observations suggest that peroxynitrite-mediated tyrosine nitration and tyrosine phosphorylation of c-Src kinase may lead to enhanced tyrosine kinase signaling observed during pancreatic ductal adenocarcinoma growth and metastasis.	Peroxynitrous Acid	46-59	C-terminal Src kinase	Homo sapiens	120-132
10845713-8	2000	Collectively, these observations suggest that peroxynitrite-mediated tyrosine nitration and tyrosine phosphorylation of c-Src kinase may lead to enhanced tyrosine kinase signaling observed during pancreatic ductal adenocarcinoma growth and metastasis.	Tyrosine	69-77	C-terminal Src kinase	Homo sapiens	120-132
10845713-8	2000	Collectively, these observations suggest that peroxynitrite-mediated tyrosine nitration and tyrosine phosphorylation of c-Src kinase may lead to enhanced tyrosine kinase signaling observed during pancreatic ductal adenocarcinoma growth and metastasis.	Tyrosine	92-100	C-terminal Src kinase	Homo sapiens	120-132
10803607-9	2000	In c-Src kinase reactions, polarization decreased with time as reaction products displaced the fluorescein-labeled phosphopeptide from the anti-phosphotyrosine antibodies.	Fluorescein	95-106	C-terminal Src kinase	Homo sapiens	3-15
10790433-0	2000	Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation.	Glycosphingolipids	31-48	C-terminal Src kinase	Homo sapiens	174-177
10790433-6	2000	Expression of PAG in COS cells results in recruitment of endogenous Csk, altered Src kinase activity, and impaired phosphorylation of Src-specific substrates.	carbonyl sulfide	21-24	C-terminal Src kinase	Homo sapiens	68-71
10801129-2	2000	The activity of Src-PTKs in cells of different types is negatively controlled by Csk, which specifically phosphorylates a conserved regulatory tyrosine residue at the carboxy-terminal tail of the Src-PTKs.	Tyrosine	143-151	C-terminal Src kinase	Homo sapiens	81-84
10803607-9	2000	In c-Src kinase reactions, polarization decreased with time as reaction products displaced the fluorescein-labeled phosphopeptide from the anti-phosphotyrosine antibodies.	Phosphotyrosine	144-159	C-terminal Src kinase	Homo sapiens	3-15
10441393-1	1999	We screened 1680 spatially separated compounds of a diverse combinatorial library of 1,4-benzodiazepines for their ability to inhibit the kinase activity of protein tyrosine kinases Src, Yes, Abl, Lck, Csk, and fibroblast growth factor receptor.	Bz-423	85-104	C-terminal Src kinase	Homo sapiens	202-205
10601992-1	1999	The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells.	Proline	4-11	C-terminal Src kinase	Homo sapiens	256-259
10601992-1	1999	The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells.	Serine	30-36	C-terminal Src kinase	Homo sapiens	256-259
10601992-1	1999	The proline-, glutamic acid-, serine- and threonine-enriched protein tyrosine phosphatase PEP, which is expressed primarily in hematopoietic cells, was recently discovered to be physically associated with the 50-kDa cytosolic protein tyrosine kinase (PTK) Csk, an important suppressor of Src family PTK, including Lck and Fyn in T cells.	Threonine	42-51	C-terminal Src kinase	Homo sapiens	256-259
10508617-4	1999	Src kinase activity is downregulated by the carboxy-terminal Src kinase (Csk), a tyrosine kinase that phosphorylates a conserved tyrosine residue in the carboxy-terminal tail of Src [7] [8].	Tyrosine	81-89	C-terminal Src kinase	Homo sapiens	73-76
10026153-6	1999	We found that the SH2 domain of CSK binds to the tyrosine-phosphorylated form of IGF-IR and IR.	Tyrosine	49-57	C-terminal Src kinase	Homo sapiens	32-35
10364466-1	1999	The Csk Homologous Kinase (CHK) has been shown to have an enzymatic activity similar to the tyrosine kinase Csk in that it down-regulates Src family kinase activity by causing phosphorylation of the Src C-terminal tyrosine residue.	Tyrosine	92-100	C-terminal Src kinase	Homo sapiens	4-7
10233937-5	1999	Analysis of LMP2A deletion mutants demonstrated that tyrosines implicated in interacting with Src family kinase SH2 domains and the SH2 domain of Csk, as well as the LMP2A immunoreceptor tyrosine-based activation motif, are important for its phosphorylation in epithelial cells.	Tyrosine	53-62	C-terminal Src kinase	Homo sapiens	146-149
10233937-5	1999	Analysis of LMP2A deletion mutants demonstrated that tyrosines implicated in interacting with Src family kinase SH2 domains and the SH2 domain of Csk, as well as the LMP2A immunoreceptor tyrosine-based activation motif, are important for its phosphorylation in epithelial cells.	Tyrosine	53-61	C-terminal Src kinase	Homo sapiens	146-149
10220355-0	1999	Substitution studies of the second divalent metal cation requirement of protein tyrosine kinase CSK.	Metals	44-49	C-terminal Src kinase	Homo sapiens	96-99
10220355-1	1999	In addition to a magnesium ion needed to form the ATP-Mg complex, we have previously determined that at least one more free Mg2+ ion is essential for the activation of the protein tyrosine kinase, Csk [Sun, G., and Budde, R. J.	Magnesium	17-26	C-terminal Src kinase	Homo sapiens	197-200
10220355-1	1999	In addition to a magnesium ion needed to form the ATP-Mg complex, we have previously determined that at least one more free Mg2+ ion is essential for the activation of the protein tyrosine kinase, Csk [Sun, G., and Budde, R. J.	Adenosine Triphosphate	50-53	C-terminal Src kinase	Homo sapiens	197-200
10220355-1	1999	In addition to a magnesium ion needed to form the ATP-Mg complex, we have previously determined that at least one more free Mg2+ ion is essential for the activation of the protein tyrosine kinase, Csk [Sun, G., and Budde, R. J.	Magnesium	54-56	C-terminal Src kinase	Homo sapiens	197-200
10220355-1	1999	In addition to a magnesium ion needed to form the ATP-Mg complex, we have previously determined that at least one more free Mg2+ ion is essential for the activation of the protein tyrosine kinase, Csk [Sun, G., and Budde, R. J.	magnesium ion	124-128	C-terminal Src kinase	Homo sapiens	197-200
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Metals	47-52	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Manganese(2+)	70-74	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Cobalt(2+)	76-80	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Nickel(2+)	82-86	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	Zinc	92-96	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	magnesium ion	116-120	C-terminal Src kinase	Homo sapiens	137-140
10220355-4	1999	In this paper, we report that several divalent metal cations, such as Mn2+, Co2+, Ni2+, and Zn2+ bind to the second Mg2+-binding site of Csk with up to 13200-fold higher affinity than Mg2+.	magnesium ion	184-188	C-terminal Src kinase	Homo sapiens	137-140
10220355-6	1999	Substitution by these divalent metal cations resulted in varied levels of Csk activity, with Mn2+ even more effective than Mg2+.	Metals	31-36	C-terminal Src kinase	Homo sapiens	74-77
10220355-6	1999	Substitution by these divalent metal cations resulted in varied levels of Csk activity, with Mn2+ even more effective than Mg2+.	Manganese(2+)	93-97	C-terminal Src kinase	Homo sapiens	74-77
10220355-6	1999	Substitution by these divalent metal cations resulted in varied levels of Csk activity, with Mn2+ even more effective than Mg2+.	magnesium ion	123-127	C-terminal Src kinase	Homo sapiens	74-77
10220355-7	1999	Co2+ and Ni2+ supports reduced levels of Csk activity compared to Mg2+.	Cobalt(2+)	0-4	C-terminal Src kinase	Homo sapiens	41-44
10220355-7	1999	Co2+ and Ni2+ supports reduced levels of Csk activity compared to Mg2+.	Nickel(2+)	9-13	C-terminal Src kinase	Homo sapiens	41-44
10220355-8	1999	Zn2+ has the highest affinity for the second Mg2+-binding site of Csk at 0.65 microM, but supports no kinase activity, acting as a dead-end inhibitor.	Zinc	0-4	C-terminal Src kinase	Homo sapiens	66-69
10220355-8	1999	Zn2+ has the highest affinity for the second Mg2+-binding site of Csk at 0.65 microM, but supports no kinase activity, acting as a dead-end inhibitor.	magnesium ion	45-49	C-terminal Src kinase	Homo sapiens	66-69
10220355-11	1999	These results suggest that the divalent metal activator is an important element in determining the affinity between Csk and the phosphate-accepting substrate.	Metals	40-45	C-terminal Src kinase	Homo sapiens	116-119
10220355-11	1999	These results suggest that the divalent metal activator is an important element in determining the affinity between Csk and the phosphate-accepting substrate.	Phosphates	128-137	C-terminal Src kinase	Homo sapiens	116-119
9988270-3	1999	Studies of the mechanism of c-Src regulation have suggested that c-Src kinase activity is downregulated by phosphorylation of a critical carboxy-terminal tyrosine (Tyr 530 in human c-Src, equivalent to Tyr 527 in chicken Src) and have implied the existence of activating mutations in this C-terminal regulatory region.	Tyrosine	154-162	C-terminal Src kinase	Homo sapiens	65-77
10069568-0	1999	Effects of c-Src tyrosine kinase on ethanol sensitivity of recombinant NMDA receptors expressed in HEK 293 cells.	Ethanol	36-43	C-terminal Src kinase	Homo sapiens	11-32
10069568-13	1999	These results indicate that, although NMDA receptors can be a target of c-Src tyrosine kinase, tyrosine phosphorylation by this enzyme does not modulate the inhibitory effects of ethanol on NMDA-activated currents.	N-Methylaspartate	38-42	C-terminal Src kinase	Homo sapiens	72-93
9988270-3	1999	Studies of the mechanism of c-Src regulation have suggested that c-Src kinase activity is downregulated by phosphorylation of a critical carboxy-terminal tyrosine (Tyr 530 in human c-Src, equivalent to Tyr 527 in chicken Src) and have implied the existence of activating mutations in this C-terminal regulatory region.	Tyrosine	164-167	C-terminal Src kinase	Homo sapiens	65-77
9988270-3	1999	Studies of the mechanism of c-Src regulation have suggested that c-Src kinase activity is downregulated by phosphorylation of a critical carboxy-terminal tyrosine (Tyr 530 in human c-Src, equivalent to Tyr 527 in chicken Src) and have implied the existence of activating mutations in this C-terminal regulatory region.	Tyrosine	202-205	C-terminal Src kinase	Homo sapiens	65-77
9794236-4	1998	First, pre-incubation of Src with ATP-Mg led to time-dependent autophosphorylation of Src, activation of its kinase activity and loss of its ability to be inactivated by Csk.	Adenosine Triphosphate	34-37	C-terminal Src kinase	Homo sapiens	170-173
9890993-5	1999	On the other hand, overexpression of Csk-DeltaK induced tyrosine phosphorylation of cellular proteins, including the paxillin and focal adhesion kinase (FAK) and enhanced to some extent the cytoskeletal organization and the rate of cell spreading on fibronectin, indicating that Src or its relatives was functionally activated in the cells.	Tyrosine	56-64	C-terminal Src kinase	Homo sapiens	37-47
9890993-6	1999	Paxillin was also tyrosine-phosphorylated in Csk-overexpressing cells, indicating that it can serve as a substrate of Csk.	Tyrosine	18-26	C-terminal Src kinase	Homo sapiens	45-48
9890993-8	1999	In contrast, tyrosine phosphorylation of FAK and its in vitro autophosphorylation activity were increased only in cells expressing Csk-DeltaK.	Tyrosine	13-21	C-terminal Src kinase	Homo sapiens	131-141
9890993-10	1999	These findings suggest that Csk regulates Src family tyrosine kinases that play essential roles in the regulation of cell adhesion via a FAK-dependent mechanism and that the tyrosine phosphorylation of paxillin alone may not be sufficient for the regulation of the cell adhesion mechanism in astrocytes.	Tyrosine	53-61	C-terminal Src kinase	Homo sapiens	28-31
9878439-0	1999	Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine.	Staurosporine	95-108	C-terminal Src kinase	Homo sapiens	51-72
9878439-0	1999	Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine.	Staurosporine	95-108	C-terminal Src kinase	Homo sapiens	74-77
9878439-1	1999	The crystal structure of the kinase domain of C-terminal Src kinase (CSK) has been determined by molecular replacement, co-complexed with the protein kinase inhibitor staurosporine (crystals belong to the space group P21212 with a=44.5 A, b=120.6 A, c=48.3 A).	Staurosporine	167-180	C-terminal Src kinase	Homo sapiens	46-67
9878439-1	1999	The crystal structure of the kinase domain of C-terminal Src kinase (CSK) has been determined by molecular replacement, co-complexed with the protein kinase inhibitor staurosporine (crystals belong to the space group P21212 with a=44.5 A, b=120.6 A, c=48.3 A).	Staurosporine	167-180	C-terminal Src kinase	Homo sapiens	69-72
9794236-1	1998	Csk phosphorylates Src family protein tyrosine kinases on a tyrosine residue near their C-terminus and downregulates their activity.	Tyrosine	38-46	C-terminal Src kinase	Homo sapiens	0-3
9794236-10	1998	Mutation of the tyrosine autophosphorylation site of Yes to a phenylalanine resulted in a mutant Yes enzyme that can be fully inactivated by a sub-stoichiometric amount of Csk in a time-dependent manner.	Tyrosine	16-24	C-terminal Src kinase	Homo sapiens	172-175
9794236-10	1998	Mutation of the tyrosine autophosphorylation site of Yes to a phenylalanine resulted in a mutant Yes enzyme that can be fully inactivated by a sub-stoichiometric amount of Csk in a time-dependent manner.	Phenylalanine	62-75	C-terminal Src kinase	Homo sapiens	172-175
9618476-2	1998	This method was used to ligate a phosphotyrosine peptide to the C terminus of the protein tyrosine kinase C-terminal Src kinase (Csk).	phosphotyrosine peptide	33-56	C-terminal Src kinase	Homo sapiens	106-127
9735325-4	1998	Activation of c-src appeared to be dependent on active ErbB2 tyrosine kinase, as the ErbB2 inhibitor tyrphostin AG 825 blocked the induction of c-src kinase activity, as well as the ability of transformed cells to grow on soft agar, but not plastic.	tyrphostin AG825	101-118	C-terminal Src kinase	Homo sapiens	144-156
9707505-8	1998	A marked increase in the protein amount of H-Ras and a significant increase in the activity of c-Src kinase, PTK, and Erk2 were found in cells from TCDD-treated animals.	Polychlorinated Dibenzodioxins	148-152	C-terminal Src kinase	Homo sapiens	95-107
9707505-12	1998	(1) A structure-activity relationship study with TCDD and three dioxin congeners revealed a rank order for their potency in activation of AhR-associated c-Src kinase from cervical cells which was identical to that of previously determined toxicity indices.	Polychlorinated Dibenzodioxins	49-53	C-terminal Src kinase	Homo sapiens	153-165
9707505-12	1998	(1) A structure-activity relationship study with TCDD and three dioxin congeners revealed a rank order for their potency in activation of AhR-associated c-Src kinase from cervical cells which was identical to that of previously determined toxicity indices.	Dioxins	64-70	C-terminal Src kinase	Homo sapiens	153-165
9707505-13	1998	(2) TCDD-induced, AhR-associated c-Src kinase activity was abolished when an AhR immunoprecipitate from cervical cells was preincubated with alpha-naphthoflavone (AhR blocker) or geldanamycin (Src kinase inhibitor) prior to the addition of TCDD.	Polychlorinated Dibenzodioxins	4-8	C-terminal Src kinase	Homo sapiens	33-45
9707505-13	1998	(2) TCDD-induced, AhR-associated c-Src kinase activity was abolished when an AhR immunoprecipitate from cervical cells was preincubated with alpha-naphthoflavone (AhR blocker) or geldanamycin (Src kinase inhibitor) prior to the addition of TCDD.	alpha-naphthoflavone	141-161	C-terminal Src kinase	Homo sapiens	33-45
9707505-13	1998	(2) TCDD-induced, AhR-associated c-Src kinase activity was abolished when an AhR immunoprecipitate from cervical cells was preincubated with alpha-naphthoflavone (AhR blocker) or geldanamycin (Src kinase inhibitor) prior to the addition of TCDD.	geldanamycin	179-191	C-terminal Src kinase	Homo sapiens	33-45
9707505-13	1998	(2) TCDD-induced, AhR-associated c-Src kinase activity was abolished when an AhR immunoprecipitate from cervical cells was preincubated with alpha-naphthoflavone (AhR blocker) or geldanamycin (Src kinase inhibitor) prior to the addition of TCDD.	Polychlorinated Dibenzodioxins	240-244	C-terminal Src kinase	Homo sapiens	33-45
9647655-9	1998	Microinjection of either anti-Cst.1 antibody or recombinant CSK, both of which prevent activation of Src family kinase, significantly decreases ATP-induced activation of AE.	Adenosine Triphosphate	144-147	C-terminal Src kinase	Homo sapiens	60-63
9618476-2	1998	This method was used to ligate a phosphotyrosine peptide to the C terminus of the protein tyrosine kinase C-terminal Src kinase (Csk).	phosphotyrosine peptide	33-56	C-terminal Src kinase	Homo sapiens	129-132
9618476-4	1998	The semisynthetic tail-phosphorylated Csk showed evidence of an intramolecular phosphotyrosine-Src homology 2 interaction and an unexpected increase in catalytic phosphoryl transfer efficiency toward a physiologically relevant substrate compared with the non-tail-phosphorylated control.	Phosphotyrosine	79-94	C-terminal Src kinase	Homo sapiens	38-41
9736341-0	1998	Stimulation of the high-affinity IgE receptor results in the tyrosine phosphorylation of a 60 kD protein which is associated with the protein-tyrosine kinase, Csk.	Tyrosine	61-69	C-terminal Src kinase	Homo sapiens	159-162
9603960-6	1998	PD158780 potently inhibited the LPA-stimulated MAP kinase kinase 1/2 (MKK1/2) activation and EGF receptor tyrosine phosphorylation in HeLa cells, while it had no detectable effect on c-Src kinase activity.	6-(methylamino)pyrido(3,4-d)pyrimidine	0-8	C-terminal Src kinase	Homo sapiens	183-195
9603960-6	1998	PD158780 potently inhibited the LPA-stimulated MAP kinase kinase 1/2 (MKK1/2) activation and EGF receptor tyrosine phosphorylation in HeLa cells, while it had no detectable effect on c-Src kinase activity.	lysophosphatidic acid	32-35	C-terminal Src kinase	Homo sapiens	183-195
9582365-2	1998	This interaction was shown to involve the Src homology 3 (SH3) region of Csk and a proline-rich sequence of PEP termed P1 (SRRTDDEIPPPLPERTPESFIVVEE).	Proline	83-90	C-terminal Src kinase	Homo sapiens	73-76
9736341-3	1998	Using anti-Csk antibodies and recombinant fusion proteins we detected a single tyrosine-phosphorylated protein of 60 kD (herein referred to as "p60") that associates with the SH2 domain of Csk after stimulation of the FcepsilonRI.	Tyrosine	79-87	C-terminal Src kinase	Homo sapiens	11-14
9736341-3	1998	Using anti-Csk antibodies and recombinant fusion proteins we detected a single tyrosine-phosphorylated protein of 60 kD (herein referred to as "p60") that associates with the SH2 domain of Csk after stimulation of the FcepsilonRI.	Tyrosine	79-87	C-terminal Src kinase	Homo sapiens	189-192
9477973-1	1998	Two tyrosyl residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family: autophosphorylation of Tyr416 (c-Src numbering) located in the catalytic domain correlates with enzyme activation, while Csk-mediated phosphorylation of the C-terminal tyrosine Tyr527 (c-Src numbering) gives rise to inactive forms of Src kinases.	cyclo(tyrosyl-tyrosyl)	4-11	C-terminal Src kinase	Homo sapiens	249-252
9461599-2	1998	The Csk homologous kinase (CHK) is a recently identified tyrosine kinase which, like Csk, phosphorylates the C-terminal tyrosine of Src kinases, resulting in inactivation of these enzymes.	Tyrosine	57-65	C-terminal Src kinase	Homo sapiens	4-7
9477973-1	1998	Two tyrosyl residues have been reported to play a crucial role in the regulation of protein tyrosine kinases of the Src family: autophosphorylation of Tyr416 (c-Src numbering) located in the catalytic domain correlates with enzyme activation, while Csk-mediated phosphorylation of the C-terminal tyrosine Tyr527 (c-Src numbering) gives rise to inactive forms of Src kinases.	Tyrosine	92-100	C-terminal Src kinase	Homo sapiens	249-252
9425036-11	1998	The lack of a significant impact of increased salt on the Km for Lck phosphorylation differs from Csk-mediated poly(Glu,Tyr) phosphorylation, and argues against the importance of electrostatic effects in the Csk-Lck binding interaction.	poly	111-115	C-terminal Src kinase	Homo sapiens	98-101
9425036-12	1998	The failure of the Lck phosphorylation product (phosphotyrosine-505) to significantly inhibit Csk phosphorylation of Lck is consistent with a catalytic model involving multidomain structural interactions between substrate and enzyme.	Phosphotyrosine	48-63	C-terminal Src kinase	Homo sapiens	94-97
9221755-2	1997	Because the tyrosine kinase Csk is a potential negative regulator of lymphocyte activation, we examined the effects of BCR and FcgammaRIIB1 engagement on the binding of Csk to phosphotyrosine-containing proteins.	Phosphotyrosine	176-191	C-terminal Src kinase	Homo sapiens	169-172
9405393-7	1997	The ITAMs of the A74 protein are tyrosine-phosphorylated by a c-Src kinase in vitro.	Tyrosine	33-41	C-terminal Src kinase	Homo sapiens	62-74
9281320-9	1997	Finally, we show that the enzyme is inactivated by incubation with protein tyrosine kinase Csk in an ATP-Mg-dependent manner, indicating that cellular Yes can be regulated by Csk phosphorylation.	Adenosine Triphosphate	101-104	C-terminal Src kinase	Homo sapiens	91-94
9281320-9	1997	Finally, we show that the enzyme is inactivated by incubation with protein tyrosine kinase Csk in an ATP-Mg-dependent manner, indicating that cellular Yes can be regulated by Csk phosphorylation.	Adenosine Triphosphate	101-104	C-terminal Src kinase	Homo sapiens	175-178
9276617-3	1997	One of them, soluble tyrosine kinase-1 (STK-1), represents a soluble form of the c-Src protein, which is apparently underphosphorylated on its C-terminal tyrosine residue whereas the other (STK-2) is a 48-kDa protein tyrosine kinase (PTK), which is molecularly and functionally related to the C-terminal Src kinase (Csk).	Tyrosine	21-29	C-terminal Src kinase	Homo sapiens	293-314
9276617-3	1997	One of them, soluble tyrosine kinase-1 (STK-1), represents a soluble form of the c-Src protein, which is apparently underphosphorylated on its C-terminal tyrosine residue whereas the other (STK-2) is a 48-kDa protein tyrosine kinase (PTK), which is molecularly and functionally related to the C-terminal Src kinase (Csk).	Tyrosine	21-29	C-terminal Src kinase	Homo sapiens	316-319
8995444-5	1997	Like p50csk, Chk reduced the elevated phosphotyrosine levels and the augmented activity of Src family kinases in Csk-deficient fibroblasts.	Phosphotyrosine	38-53	C-terminal Src kinase	Homo sapiens	5-11
9224730-5	1997	Csk phosphorylation in vitro by PKA is on a serine residue(s) and can reach a stoichiometry of approximately 0.6 mol phosphate per mole of enzyme.	Serine	44-50	C-terminal Src kinase	Homo sapiens	0-3
9224730-5	1997	Csk phosphorylation in vitro by PKA is on a serine residue(s) and can reach a stoichiometry of approximately 0.6 mol phosphate per mole of enzyme.	Phosphates	117-126	C-terminal Src kinase	Homo sapiens	0-3
9224730-6	1997	Furthermore, incubation with PKA in the presence of ATP and magnesium ion results in a time-dependent decrease in Csk kinase activity.	Adenosine Triphosphate	52-55	C-terminal Src kinase	Homo sapiens	114-117
9224730-6	1997	Furthermore, incubation with PKA in the presence of ATP and magnesium ion results in a time-dependent decrease in Csk kinase activity.	Magnesium	60-69	C-terminal Src kinase	Homo sapiens	114-117
9224730-7	1997	A six-fold decrease in Csk activity (expressed as Vmax/Km ratio) was achieved due to a threefold increase in its Km and a twofold decrease in its Vmax value within 1 h of incubation with the catalytic subunit of PKA and ATP-Mg.	atp-mg	220-226	C-terminal Src kinase	Homo sapiens	23-26
9148770-0	1997	Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure.	Tyrosine	22-30	C-terminal Src kinase	Homo sapiens	18-21
9148770-1	1997	The lack of a conserved tyrosine autophosphorylation site is a unique feature of the C-terminal Src-kinase, Csk, although this protein tyrosine kinase can be autophosphorylated on tyrosine residues in vitro and in bacteria.	Tyrosine	24-32	C-terminal Src kinase	Homo sapiens	108-111
9148770-1	1997	The lack of a conserved tyrosine autophosphorylation site is a unique feature of the C-terminal Src-kinase, Csk, although this protein tyrosine kinase can be autophosphorylated on tyrosine residues in vitro and in bacteria.	Tyrosine	135-143	C-terminal Src kinase	Homo sapiens	108-111
9148770-2	1997	Here we show that human Csk is tyrosine phosphorylated in HeLa cells treated with sodium pervanadate.	Tyrosine	31-39	C-terminal Src kinase	Homo sapiens	24-27
9148770-2	1997	Here we show that human Csk is tyrosine phosphorylated in HeLa cells treated with sodium pervanadate.	Sodium orthovanadate	82-100	C-terminal Src kinase	Homo sapiens	24-27
9148770-5	1997	A catalytically inactive form of Csk was also phosphorylated on Tyr-184 in vivo, suggesting that this is not a site of autophosphorylation.	Tyrosine	64-67	C-terminal Src kinase	Homo sapiens	33-36
9148770-7	1997	Three-dimensional modelling of the Csk kinase domain indicated that the Y304F mutation abolishes one of two conserved hydrogen bonds between the upper and the lower lobes in the open conformation of the kinase domain.	Hydrogen	118-126	C-terminal Src kinase	Homo sapiens	35-38
9148770-10	1997	Taken together these results indicate that Csk can be phosphorylated in vivo at Tyr-184 by an as yet unknown tyrosine kinase, and that autophosphorylation of Tyr-304 occurs only at abnormally high Csk concentrations in vitro.	Tyrosine	80-83	C-terminal Src kinase	Homo sapiens	43-46
9148770-11	1997	Furthermore, Tyr-304 is required for the maintenance of the structure of the Csk kinase domain.	Tyrosine	13-16	C-terminal Src kinase	Homo sapiens	77-80
9047313-5	1997	(3) The free magnesium ion activates Csk and Src kinase activity by increasing the Vmax but does not change their apparent Km(ATP-Mg).	Magnesium	13-22	C-terminal Src kinase	Homo sapiens	37-40
9048573-1	1997	Csk (C-terminal Src kinase) is a protein tyrosine kinase which catalyzes the transfer of the gamma-phosphoryl group of ATP to the tyrosine hydroxyl of proteins in the presence of a divalent ion.	Adenosine Triphosphate	119-122	C-terminal Src kinase	Homo sapiens	0-3
9048573-1	1997	Csk (C-terminal Src kinase) is a protein tyrosine kinase which catalyzes the transfer of the gamma-phosphoryl group of ATP to the tyrosine hydroxyl of proteins in the presence of a divalent ion.	Adenosine Triphosphate	119-122	C-terminal Src kinase	Homo sapiens	5-26
9048573-1	1997	Csk (C-terminal Src kinase) is a protein tyrosine kinase which catalyzes the transfer of the gamma-phosphoryl group of ATP to the tyrosine hydroxyl of proteins in the presence of a divalent ion.	tyrosine hydroxyl	130-147	C-terminal Src kinase	Homo sapiens	0-3
9048573-1	1997	Csk (C-terminal Src kinase) is a protein tyrosine kinase which catalyzes the transfer of the gamma-phosphoryl group of ATP to the tyrosine hydroxyl of proteins in the presence of a divalent ion.	tyrosine hydroxyl	130-147	C-terminal Src kinase	Homo sapiens	5-26
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	Cobalt	52-54	C-terminal Src kinase	Homo sapiens	33-36
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	Cobalt	52-54	C-terminal Src kinase	Homo sapiens	110-113
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	Magnesium	77-79	C-terminal Src kinase	Homo sapiens	110-113
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	Adenosine Triphosphate	119-122	C-terminal Src kinase	Homo sapiens	33-36
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	Adenosine Triphosphate	119-122	C-terminal Src kinase	Homo sapiens	110-113
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	adenosine 5'-O-(3-thiotriphosphate)	127-138	C-terminal Src kinase	Homo sapiens	33-36
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	adenosine 5'-O-(3-thiotriphosphate)	127-138	C-terminal Src kinase	Homo sapiens	110-113
9048573-11	1997	Steady-state kinetic analyses of Csk reactions with Co and Ni in addition to Mg and Mn on wild-type and D314E Csk with ATP and ATP gamma S [adenosine 5"-O-(3-thiotriphosphate)] as substrates were performed.	adenosine 5'-O-(3-thiotriphosphate)	140-175	C-terminal Src kinase	Homo sapiens	33-36
9048573-12	1997	The Kcat thio effects [Kcat(ATP)/Kcat(ATP gamma S)] were inversely correlated with metal thiophilicity in both wild-type and D314E mutant Csk reactions, although the relationship was less pronounced in the latter.	thio	9-13	C-terminal Src kinase	Homo sapiens	138-141
9048573-12	1997	The Kcat thio effects [Kcat(ATP)/Kcat(ATP gamma S)] were inversely correlated with metal thiophilicity in both wild-type and D314E mutant Csk reactions, although the relationship was less pronounced in the latter.	Adenosine Triphosphate	28-31	C-terminal Src kinase	Homo sapiens	138-141
9048573-12	1997	The Kcat thio effects [Kcat(ATP)/Kcat(ATP gamma S)] were inversely correlated with metal thiophilicity in both wild-type and D314E mutant Csk reactions, although the relationship was less pronounced in the latter.	Adenosine Triphosphate	38-41	C-terminal Src kinase	Homo sapiens	138-141
9048573-12	1997	The Kcat thio effects [Kcat(ATP)/Kcat(ATP gamma S)] were inversely correlated with metal thiophilicity in both wild-type and D314E mutant Csk reactions, although the relationship was less pronounced in the latter.	Metals	83-88	C-terminal Src kinase	Homo sapiens	138-141
9048573-13	1997	These results appear to underscore the role of gamma-phosphoryl hydrogen bonding/salt bridging in the wild-type Csk reaction transition state, which is somewhat perturbed in the D314E Csk reaction.	Hydrogen	64-72	C-terminal Src kinase	Homo sapiens	112-115
9048573-13	1997	These results appear to underscore the role of gamma-phosphoryl hydrogen bonding/salt bridging in the wild-type Csk reaction transition state, which is somewhat perturbed in the D314E Csk reaction.	Hydrogen	64-72	C-terminal Src kinase	Homo sapiens	184-187
9048573-13	1997	These results appear to underscore the role of gamma-phosphoryl hydrogen bonding/salt bridging in the wild-type Csk reaction transition state, which is somewhat perturbed in the D314E Csk reaction.	Salts	81-85	C-terminal Src kinase	Homo sapiens	112-115
9048573-13	1997	These results appear to underscore the role of gamma-phosphoryl hydrogen bonding/salt bridging in the wild-type Csk reaction transition state, which is somewhat perturbed in the D314E Csk reaction.	Salts	81-85	C-terminal Src kinase	Homo sapiens	184-187
9048573-14	1997	In the case of the Ni reaction, the Kcat thio effect was reduced to about 2 in the wild-type and D314E mutant Csk reactions.	thio	41-45	C-terminal Src kinase	Homo sapiens	110-113
8621646-0	1996	Csk is constitutively associated with a 60-kDa tyrosine-phosphorylated protein in human T cells.	Tyrosine	47-55	C-terminal Src kinase	Homo sapiens	0-3
9172452-2	1996	Csk is probably involved in the downregulation of TCR signaling by C-terminal tyrosine phosphorylation of Lck and Fyn, but the mechanism whereby Csk targets these Src family members is not known.	Tyrosine	78-86	C-terminal Src kinase	Homo sapiens	0-3
8756634-4	1996	We show here that C-terminal Src kinase (Csk), which phosphorylates C-terminal tyrosine residues of Src family protein tyrosine kinases and suppresses their kinase activities, is involved in this insulin-stimulated dephosphorylation of focal adhesion proteins.	Tyrosine	79-87	C-terminal Src kinase	Homo sapiens	18-39
8756634-4	1996	We show here that C-terminal Src kinase (Csk), which phosphorylates C-terminal tyrosine residues of Src family protein tyrosine kinases and suppresses their kinase activities, is involved in this insulin-stimulated dephosphorylation of focal adhesion proteins.	Tyrosine	79-87	C-terminal Src kinase	Homo sapiens	41-44
8756634-7	1996	Although we have shown that the Csk Src homology 2 domain can bind to several tyrosine-phosphorylated proteins, including pp125FAK and paxillin, a majority of protein which bound to Csk was IRS-1 when cells were stimulated by insulin.	Tyrosine	78-86	C-terminal Src kinase	Homo sapiens	32-35
8979366-0	1996	The C-terminal Src kinase (Csk) is widely expressed, active in HT-29 cells that contain activated Src, and its expression is downregulated in butyrate-treated SW620 cells.	Butyrates	142-150	C-terminal Src kinase	Homo sapiens	4-25
8979366-0	1996	The C-terminal Src kinase (Csk) is widely expressed, active in HT-29 cells that contain activated Src, and its expression is downregulated in butyrate-treated SW620 cells.	Butyrates	142-150	C-terminal Src kinase	Homo sapiens	27-30
8979366-5	1996	The expression of Csk was downregulated upon chemical-induced differentiation of SW620 human colon cells by treatment with sodium butyrate.	Butyric Acid	123-138	C-terminal Src kinase	Homo sapiens	18-21
8807585-10	1996	The c-src phosphorylation was associated with an inhibition of c-src kinase activity, suggesting phosphorylation of tyrosine 527 in the c-src regulatory domain.	Tyrosine	116-124	C-terminal Src kinase	Homo sapiens	63-75
8621646-2	1996	Csk may be involved in the down-regulation of T cell receptor (TCR) signaling by C-terminal tyrosine phosphorylation of Lck and Fyn; however, it is not known how Csk activity is regulated or how it targets these Src family members.	Tyrosine	92-100	C-terminal Src kinase	Homo sapiens	0-3
8621646-4	1996	In both Jurkat and normal T cells, the Src homology 2 (SH2) domain of Csk bound constitutively to a tyrosine-phosphorylated protein of 60 kDa (p60).	Tyrosine	100-108	C-terminal Src kinase	Homo sapiens	70-73
8621646-8	1996	Our data demonstrate that the SH2 domain of Csk specifically associates with at least two tyrosine-phosphorylated proteins in normal human T cells, that this association is independent of TCR/CD3 activation, and that Csk may be a part of a multiprotein complex containing GAP.	Tyrosine	90-98	C-terminal Src kinase	Homo sapiens	44-47
8631775-0	1996	Detection of a physical and functional interaction between Csk and Lck which involves the SH2 domain of Csk and is mediated by autophosphorylation of Lck on tyrosine 394.	Tyrosine	157-165	C-terminal Src kinase	Homo sapiens	59-62
8621432-1	1996	Phosphorylation and dephosphorylation of Tyr-530 in human c-Src (Tyr-527 in avian c-Src) is critical in regulating c-Src kinase activity.	Tyrosine	41-44	C-terminal Src kinase	Homo sapiens	115-127
8621432-1	1996	Phosphorylation and dephosphorylation of Tyr-530 in human c-Src (Tyr-527 in avian c-Src) is critical in regulating c-Src kinase activity.	Tyrosine	65-68	C-terminal Src kinase	Homo sapiens	115-127
8631775-0	1996	Detection of a physical and functional interaction between Csk and Lck which involves the SH2 domain of Csk and is mediated by autophosphorylation of Lck on tyrosine 394.	Tyrosine	157-165	C-terminal Src kinase	Homo sapiens	104-107
8631775-1	1996	The COOH-terminal Src kinase (Csk) is responsible for the phosphorylation of the conserved, negative regulatory, carboxyl-terminal tyrosine of most of the Src family protein tyrosine kinases.	Tyrosine	131-139	C-terminal Src kinase	Homo sapiens	4-28
8631775-1	1996	The COOH-terminal Src kinase (Csk) is responsible for the phosphorylation of the conserved, negative regulatory, carboxyl-terminal tyrosine of most of the Src family protein tyrosine kinases.	Tyrosine	131-139	C-terminal Src kinase	Homo sapiens	30-33
8631775-6	1996	This interaction requires the autophosphorylation of Lck on tyrosine 394 (the phosphorylation of which is correlated with an increase of the kinase activity) and involves a functional Csk SH2 domain.	Tyrosine	60-68	C-terminal Src kinase	Homo sapiens	184-187
8631775-8	1996	Furthermore, in vitro we showed that autophosphorylation of Lck on tyrosine 394 enhances the phosphorylation of Lck by Csk on the negative regulatory site, tyrosine 505, suggesting that activated Lck serves preferentially as substrate for Csk.	Tyrosine	67-75	C-terminal Src kinase	Homo sapiens	119-122
8631775-8	1996	Furthermore, in vitro we showed that autophosphorylation of Lck on tyrosine 394 enhances the phosphorylation of Lck by Csk on the negative regulatory site, tyrosine 505, suggesting that activated Lck serves preferentially as substrate for Csk.	Tyrosine	67-75	C-terminal Src kinase	Homo sapiens	239-242
8631775-8	1996	Furthermore, in vitro we showed that autophosphorylation of Lck on tyrosine 394 enhances the phosphorylation of Lck by Csk on the negative regulatory site, tyrosine 505, suggesting that activated Lck serves preferentially as substrate for Csk.	Tyrosine	156-164	C-terminal Src kinase	Homo sapiens	119-122
8631775-8	1996	Furthermore, in vitro we showed that autophosphorylation of Lck on tyrosine 394 enhances the phosphorylation of Lck by Csk on the negative regulatory site, tyrosine 505, suggesting that activated Lck serves preferentially as substrate for Csk.	Tyrosine	156-164	C-terminal Src kinase	Homo sapiens	239-242
8522345-3	1995	Five of the clones were analyzed for their ability to recognize native and denatured p50csk protein after undergoing native and denaturing polyacrylamide gel electrophoresis followed by western blotting.	polyacrylamide	139-153	C-terminal Src kinase	Homo sapiens	85-91
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	unnatural	53-62	C-terminal Src kinase	Homo sapiens	166-169
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	unnatural	53-62	C-terminal Src kinase	Homo sapiens	171-192
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	amino acid trifluorotyrosine	63-91	C-terminal Src kinase	Homo sapiens	166-169
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	amino acid trifluorotyrosine	63-91	C-terminal Src kinase	Homo sapiens	171-192
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	Tyrosine	83-91	C-terminal Src kinase	Homo sapiens	166-169
7673185-2	1995	In this study, we show that a peptide containing the unnatural amino acid trifluorotyrosine shows remarkably similar efficiency as a substrate of the tyrosine kinase Csk (C-terminal Src kinase) compared with the corresponding tyrosine-containing peptide despite a 4-unit change in the phenolic pKa.	Tyrosine	83-91	C-terminal Src kinase	Homo sapiens	171-192
7673185-6	1995	Examination of the thio effect (kcat-ATP/kcat-adenosine 5"-O-(thiotriphosphate)) for D314E Csk led to the suggestion that a role of aspartate 314 may be to enhance the reactivity of the gamma-phosphate of ATP toward electrophilic attack.	thio	19-23	C-terminal Src kinase	Homo sapiens	91-94
7673185-6	1995	Examination of the thio effect (kcat-ATP/kcat-adenosine 5"-O-(thiotriphosphate)) for D314E Csk led to the suggestion that a role of aspartate 314 may be to enhance the reactivity of the gamma-phosphate of ATP toward electrophilic attack.	adenosine 5'-O-(3-thiotriphosphate)	46-78	C-terminal Src kinase	Homo sapiens	91-94
7592753-2	1995	Previous studies have indicated that c-Src preferentially autophosphorylates Tyr-416, a residue in the middle of the catalytic domain, in vitro, and that Tyr-527 is phosphorylated by the carboxyl-terminal Src kinase, Csk.	Tyrosine	154-157	C-terminal Src kinase	Homo sapiens	217-220
7537852-5	1995	Phosphorylation of paxillin on tyrosine creates binding sites for the SH2 domains of Crk, Csk, and Src.	Tyrosine	31-39	C-terminal Src kinase	Homo sapiens	90-93
8520026-3	1995	The catalytic function of Src-like products is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue, which is mediated by another cellular tyrosine protein kinase, p50csk.	Tyrosine	108-116	C-terminal Src kinase	Homo sapiens	189-195
7786302-2	1995	Nanomolar concentrations of hypericin inhibit the protein tyrosine kinase activities (PTK) of the epidermal growth factor receptor and the insulin receptor, while being ineffective towards the cytosolic protein tyrosine kinases Lyn, Fgr, TPK-IIB and CSK.	hypericin	28-37	C-terminal Src kinase	Homo sapiens	250-253
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	pervanadate	71-82	C-terminal Src kinase	Homo sapiens	31-34
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	Tritium	141-143	C-terminal Src kinase	Homo sapiens	31-34
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	Tyrosine	100-108	C-terminal Src kinase	Homo sapiens	31-34
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	Inositol 1,4,5-Trisphosphate	144-147	C-terminal Src kinase	Homo sapiens	31-34
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	Tritium	129-131	C-terminal Src kinase	Homo sapiens	31-34
7862136-10	1995	When yeast coexpressing c-Src, Csk, and PLC gamma 2 was incubated with pervanadate, PLC gamma 2 was tyrosine phosphorylated and [3H]IP2 and [3H]IP3 production increased 11.0- and 7.0-fold, respectively.	1D-myo-inositol 4,5-bisphosphate	132-135	C-terminal Src kinase	Homo sapiens	31-34
7527038-5	1994	Both ATP and poly(Glu,Tyr) were shown to be well behaved saturable substrates for recombinant Csk, with Km values that were in reasonable agreement with literature values reported for the non-recombinant enzyme and with kcat about 40 min-1.	Adenosine Triphosphate	5-8	C-terminal Src kinase	Homo sapiens	94-97
7862631-3	1995	Analysis of the purified protein by SDS/polyacrylamide gel electrophoresis reveals a single band with an apparent molecular mass of 50 kDa, indicating that recombinant human p50csk has been purified to near homogeneity.	Sodium Dodecyl Sulfate	36-39	C-terminal Src kinase	Homo sapiens	174-180
7862631-3	1995	Analysis of the purified protein by SDS/polyacrylamide gel electrophoresis reveals a single band with an apparent molecular mass of 50 kDa, indicating that recombinant human p50csk has been purified to near homogeneity.	polyacrylamide	40-54	C-terminal Src kinase	Homo sapiens	174-180
7529872-4	1995	Immunofluorescence for the induced p50csk was localized in the cytoplasm and distinctly in focal adhesions, in which the amount of phosphotyrosine containing proteins was also increased.	Phosphotyrosine	131-146	C-terminal Src kinase	Homo sapiens	35-41
7529872-9	1995	Our results thus show that a fraction of cellular Csk is targeted to focal adhesions via its SH2 and SH3 domains, probably interacting with tyrosyl-phosphorylated focal adhesion proteins.	cyclo(tyrosyl-tyrosyl)	140-147	C-terminal Src kinase	Homo sapiens	50-53
7527029-0	1994	Signaling-induced association of a tyrosine-phosphorylated 36-kDa protein with p50csk.	Tyrosine	35-43	C-terminal Src kinase	Homo sapiens	79-85
7527029-1	1994	The protein-tyrosine kinase, p50csk, is thought to participate in the regulation of signal transduction pathways by catalyzing the phosphorylation of the Src-related protein-tyrosine kinases on a negative regulatory tyrosine residue located near the COOH terminus.	Tyrosine	12-20	C-terminal Src kinase	Homo sapiens	29-35
7527029-1	1994	The protein-tyrosine kinase, p50csk, is thought to participate in the regulation of signal transduction pathways by catalyzing the phosphorylation of the Src-related protein-tyrosine kinases on a negative regulatory tyrosine residue located near the COOH terminus.	Carbonic Acid	250-254	C-terminal Src kinase	Homo sapiens	29-35
7527029-3	1994	We found that in response to the treatment of cells with pervanadate, a potent inhibitor of protein tyrosine phosphatases, or to the cross-linking of Fc gamma RIIA receptors, p50csk becomes tightly associated with a 36-kDa protein (p36).	pervanadate	57-68	C-terminal Src kinase	Homo sapiens	175-181
7527029-4	1994	This association is dependent on the tyrosine phosphorylation of p36 and involves its interaction with the SH2 domain of p50csk.p36 can be phosphorylated in vitro by p50csk or by a full-length GST-Csk fusion protein expressed in Escherichia coli.	Tyrosine	37-45	C-terminal Src kinase	Homo sapiens	121-127
7527029-4	1994	This association is dependent on the tyrosine phosphorylation of p36 and involves its interaction with the SH2 domain of p50csk.p36 can be phosphorylated in vitro by p50csk or by a full-length GST-Csk fusion protein expressed in Escherichia coli.	Tyrosine	37-45	C-terminal Src kinase	Homo sapiens	166-172
7527038-5	1994	Both ATP and poly(Glu,Tyr) were shown to be well behaved saturable substrates for recombinant Csk, with Km values that were in reasonable agreement with literature values reported for the non-recombinant enzyme and with kcat about 40 min-1.	poly	13-17	C-terminal Src kinase	Homo sapiens	94-97
7527038-5	1994	Both ATP and poly(Glu,Tyr) were shown to be well behaved saturable substrates for recombinant Csk, with Km values that were in reasonable agreement with literature values reported for the non-recombinant enzyme and with kcat about 40 min-1.	Glutamic Acid	18-21	C-terminal Src kinase	Homo sapiens	94-97
7527038-5	1994	Both ATP and poly(Glu,Tyr) were shown to be well behaved saturable substrates for recombinant Csk, with Km values that were in reasonable agreement with literature values reported for the non-recombinant enzyme and with kcat about 40 min-1.	Tyrosine	22-25	C-terminal Src kinase	Homo sapiens	94-97
7527038-9	1994	Csk utilized adenosine 5"-O-(3-thiotriphosphate) in place of ATP.	adenosine 5'-O-(3-thiotriphosphate)	13-48	C-terminal Src kinase	Homo sapiens	0-3
7527038-9	1994	Csk utilized adenosine 5"-O-(3-thiotriphosphate) in place of ATP.	Adenosine Triphosphate	61-64	C-terminal Src kinase	Homo sapiens	0-3
7696183-3	1994	Biochemical and site-directed mutagenesis analyses revealed that a carboxy-terminal peptide of p54rak was phosphorylated by a cytoplasmic tyrosine kinase (CSK) and that, as in the Src family, it is the COOH-terminal tyrosine that is phosphorylated by CSK.	Carbonic Acid	202-206	C-terminal Src kinase	Homo sapiens	155-158
7696183-3	1994	Biochemical and site-directed mutagenesis analyses revealed that a carboxy-terminal peptide of p54rak was phosphorylated by a cytoplasmic tyrosine kinase (CSK) and that, as in the Src family, it is the COOH-terminal tyrosine that is phosphorylated by CSK.	Tyrosine	138-146	C-terminal Src kinase	Homo sapiens	155-158
7518562-1	1994	Csk phosphorylates Src family members at a key regulatory tyrosine in the C-terminal tail and suppresses their activities.	Tyrosine	58-66	C-terminal Src kinase	Homo sapiens	0-3
7929427-6	1994	Moreover, phosphorylation of Csk-treated pp60c-src by Cdc2 also facilitated complete reactivation by the protein-tyrosine phosphatase CD45 or by a synthetic phosphopeptide corresponding to the C-terminal, regulatory phosphorylation site (Tyr-527).	Tyrosine	238-241	C-terminal Src kinase	Homo sapiens	29-32
7929427-7	1994	These data indicate that the Src homology 2 domain of Csk-phosphorylated pp60c-src was more accessible for intermolecular interactions and that Tyr-527 was more readily dephosphorylated after treatment with Cdc2.	Tyrosine	144-147	C-terminal Src kinase	Homo sapiens	54-57
7525268-4	1994	In cells lacking the regulatory kinase (CSK) that phosphorylates tyrosine 527, c-Src is also found predominantly in focal adhesions, confirming that phosphorylation of tyrosine 527 affects the location of c-Src inside the cell.	Tyrosine	65-73	C-terminal Src kinase	Homo sapiens	40-43
7525268-4	1994	In cells lacking the regulatory kinase (CSK) that phosphorylates tyrosine 527, c-Src is also found predominantly in focal adhesions, confirming that phosphorylation of tyrosine 527 affects the location of c-Src inside the cell.	Tyrosine	168-176	C-terminal Src kinase	Homo sapiens	40-43
7524477-7	1994	Repression of Fyn activity by Csk reduced binding of Fyn to phosphopeptides to undetectable levels, supporting the model that predicts an intramolecular interaction of the Fyn SH2 domain with a C-terminal phosphotyrosine residue.	Phosphotyrosine	205-220	C-terminal Src kinase	Homo sapiens	30-33
7518562-9	1994	Csk also localizes to podosomes of cells transformed by an activated Src that lacks the major tyrosine autophosphorylation site, suggesting that the relocalization of Csk is not a consequence of the binding of the Csk SH2 domain to phosphorylated Src.	Tyrosine	94-102	C-terminal Src kinase	Homo sapiens	0-3
7516063-4	1994	Like p50csk, the deduced protein sequence of this novel cDNA includes a tyrosine kinase catalytic domain, SH2 and SH3 domains, a short amino terminus, and no autophosphorylation or carboxyl-terminal tyrosine residues.	Tyrosine	72-80	C-terminal Src kinase	Homo sapiens	5-11
7515063-2	1994	CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416.	Tyrosine	38-41	C-terminal Src kinase	Homo sapiens	0-3
8145772-5	1993	This inhibitory activity copurifies with the IR on insulin-Sepharose affinity chromatography and is also effective against the tyrosine kinase activity of the IR-related insulin-like growth factor-I receptor and the oncoprotein v-abl but is ineffective against c-src tyrosine kinase activity.	Sepharose	59-68	C-terminal Src kinase	Homo sapiens	261-282
7515063-2	1994	CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416.	Tyrosine	70-73	C-terminal Src kinase	Homo sapiens	0-3
7515063-2	1994	CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416.	Tyrosine	70-73	C-terminal Src kinase	Homo sapiens	0-3
7515063-2	1994	CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416.	Tyrosine	70-73	C-terminal Src kinase	Homo sapiens	0-3
7515063-5	1994	Previous autophosphorylation (at Tyr-400) reduces c-Fgr susceptibility to down-regulation by CSK, although Tyr-511 can be still phosphorylated by it.	Tyrosine	33-36	C-terminal Src kinase	Homo sapiens	93-96
8183556-4	1994	Recently, we found that p50csk specifically phosphorylates the negative regulatory Tyr-505 of the T cell-specific src-family kinase p56lck, and thereby suppresses its catalytic activity.	Tyrosine	83-86	C-terminal Src kinase	Homo sapiens	24-30
8183556-6	1994	In parallel with this activation, p50csk formed a stable complex with one major 72 kDa tyrosine phosphorylated protein and minor polypeptides at 90 and 110 kDa.	Tyrosine	87-95	C-terminal Src kinase	Homo sapiens	34-40
7513429-0	1994	Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.	Tyrosine	63-71	C-terminal Src kinase	Homo sapiens	56-59
7513429-1	1994	Csk (C-terminal Src kinase), a protein-tyrosine kinase, bearing the Src homology 2 and 3 (SH2 and SH3) domains, has been implicated in phosphorylation of c-Src Tyr-527, resulting in suppression of c-Src kinase activity.	Tyrosine	160-163	C-terminal Src kinase	Homo sapiens	0-3
7513429-1	1994	Csk (C-terminal Src kinase), a protein-tyrosine kinase, bearing the Src homology 2 and 3 (SH2 and SH3) domains, has been implicated in phosphorylation of c-Src Tyr-527, resulting in suppression of c-Src kinase activity.	Tyrosine	160-163	C-terminal Src kinase	Homo sapiens	5-26
7513429-1	1994	Csk (C-terminal Src kinase), a protein-tyrosine kinase, bearing the Src homology 2 and 3 (SH2 and SH3) domains, has been implicated in phosphorylation of c-Src Tyr-527, resulting in suppression of c-Src kinase activity.	Tyrosine	160-163	C-terminal Src kinase	Homo sapiens	197-209
7513429-3	1994	In normal fibroblasts, tyrosine-phosphorylated paxillin and focal adhesion kinase pp125FAK, which colocalize at focal adhesion plaques, were the major proteins to which the Csk SH2 domain bound.	Tyrosine	23-31	C-terminal Src kinase	Homo sapiens	173-176
8197166-1	1994	The activity of Src-related protein-tyrosine kinases is repressed by the phosphorylation of a conserved carboxyl-terminal tyrosine by another cytoplasmic protein-tyrosine kinase termed p50csk.	Tyrosine	36-44	C-terminal Src kinase	Homo sapiens	185-191
8197166-6	1994	Firm evidence that Ntk is a Csk-related enzyme was provided by the observation that it phosphorylated a Src-related polypeptide on the inhibitory carboxyl-terminal tyrosine.	Tyrosine	164-172	C-terminal Src kinase	Homo sapiens	28-31
8262983-8	1993	Csk, which phosphorylates tyrosine residues in the negative regulatory sites of Src family kinases, down-regulated Fyn- and Lck-mediated stimulation of the serum response element and Fyn-mediated enhancement of IL-2 promoter activity.	Tyrosine	26-34	C-terminal Src kinase	Homo sapiens	0-3
8246968-1	1993	We have previously shown that the c-Src tyrosine kinase is activated four- to fivefold when cultured keratinocytes differentiate following the elevation of intracellular calcium levels.	Calcium	170-177	C-terminal Src kinase	Homo sapiens	34-55
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Heparin	49-56	C-terminal Src kinase	Homo sapiens	0-3
7692368-2	1993	Current models predict that inhibition of c-Src kinase activity results from an interaction of phosphorylated Tyr-527 with the amino terminal SH2 domain.	Tyrosine	110-113	C-terminal Src kinase	Homo sapiens	42-54
7683128-3	1993	Since SH2 domains recognize phosphotyrosine, it is possible that these two non-catalytic domains associate, and thereby repress c-Src kinase activity.	Phosphotyrosine	28-43	C-terminal Src kinase	Homo sapiens	128-140
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Sepharose	57-66	C-terminal Src kinase	Homo sapiens	0-3
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Peptides	140-148	C-terminal Src kinase	Homo sapiens	0-3
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Tyrosine	237-240	C-terminal Src kinase	Homo sapiens	0-3
1280230-3	1992	CSK and TPK-IIB once resolved from each other by heparin-Sepharose affinity chromatography, display opposite specificities toward synthetic peptides reproducing the sequences around the main phosphoacceptor residues of pp60c-src, namely Tyr-416 and Tyr-527.	Tyrosine	249-252	C-terminal Src kinase	Homo sapiens	0-3
1639064-0	1992	The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity.	Tyrosine	58-61	C-terminal Src kinase	Homo sapiens	10-16
1381508-2	1992	Activation of c-Src kinase was accompanied by tyrosine dephosphorylation, which might be explained by a rapid increase in intracellular protein-tyrosine phosphatase activity.	Tyrosine	46-54	C-terminal Src kinase	Homo sapiens	14-26
1323290-2	1992	The tyrosine residue at 845 in EGF-R corresponds to Y416 of v/c-src kinase, which is highly conserved and functionally important in many tyrosine kinases.	Tyrosine	4-12	C-terminal Src kinase	Homo sapiens	62-74
1639064-4	1992	Here we characterize a human cytosolic 50 kDa protein tyrosine kinase, p50csk, which specifically phosphorylates Tyr-505 of p56lck and a synthetic peptide containing this site.	Tyrosine	113-116	C-terminal Src kinase	Homo sapiens	71-77
34632931-5	2021	identified that ibrutinib-mediated atrial fibrillation is likely due to off-target CSK inhibition.	ibrutinib	16-25	C-terminal Src kinase	Homo sapiens	83-86
1722201-6	1991	The putative regulatory site, tyrosine 508, was found to be essential for phosphorylation in p56lyn, and the kinase activities of these src family kinases were repressed by phosphorylation with CSK.	Tyrosine	30-38	C-terminal Src kinase	Homo sapiens	194-197
34688667-7	2021	Treg induction potentiates the formation of the canonical SMAD3/4 trimer to activate a negative feedback loop through kinases PKA and CSK to suppress TCR signaling, phosphatidylinositol metabolism, and mTOR signaling.	treg	0-4	C-terminal Src kinase	Homo sapiens	134-137
34668699-6	2021	In the end, the covalent inhibitor DC-Srci-6668 targeting the PTM pocket in c-Src kinase was identified, which inhibited the phosphorylation and locked c-Src in the inactive state.	dc-srci-6668	35-47	C-terminal Src kinase	Homo sapiens	76-88
34472425-0	2021	Complete reconstruction of dasatinib unbinding pathway from c-Src kinase by supervised molecular dynamics simulation method; assessing efficiency and trustworthiness of the method.	Dasatinib	27-36	C-terminal Src kinase	Homo sapiens	60-72
34472425-4	2021	In this work, we utilized this strategy to reconstruct the unbinding pathway of the anticancer drug dasatinib from its target protein, the c-Src kinase.	Dasatinib	100-109	C-terminal Src kinase	Homo sapiens	139-151
34399705-7	2021	RESULTS: We found that loss of function of CSK or PTEN conferred lapatinib resistance in HER2-amplified GC cell lines NCI-N87 and OE19, respectively.	Lapatinib	65-74	C-terminal Src kinase	Homo sapiens	43-46
34399705-9	2021	Furthermore, in vitro and in vivo pharmacological study has shown that lapatinib resistance by the loss of function of CSK or PTEN, could be overcome by lapatinib combined with the PI3K inhibitor copanlisib and MEK inhibitor trametinib.	Lapatinib	71-80	C-terminal Src kinase	Homo sapiens	119-122
34399705-10	2021	CONCLUSIONS: Our study suggests that loss-of-function mutations of CSK and PTEN cause lapatinib resistance by re-activating MAPK and PI3K pathways, and further proved these two pathways are druggable targets.	Lapatinib	86-95	C-terminal Src kinase	Homo sapiens	67-70
34399705-9	2021	Furthermore, in vitro and in vivo pharmacological study has shown that lapatinib resistance by the loss of function of CSK or PTEN, could be overcome by lapatinib combined with the PI3K inhibitor copanlisib and MEK inhibitor trametinib.	Lapatinib	153-162	C-terminal Src kinase	Homo sapiens	119-122
34399705-9	2021	Furthermore, in vitro and in vivo pharmacological study has shown that lapatinib resistance by the loss of function of CSK or PTEN, could be overcome by lapatinib combined with the PI3K inhibitor copanlisib and MEK inhibitor trametinib.	copanlisib	196-206	C-terminal Src kinase	Homo sapiens	119-122
34399705-9	2021	Furthermore, in vitro and in vivo pharmacological study has shown that lapatinib resistance by the loss of function of CSK or PTEN, could be overcome by lapatinib combined with the PI3K inhibitor copanlisib and MEK inhibitor trametinib.	trametinib	225-235	C-terminal Src kinase	Homo sapiens	119-122
35393453-1	2022	The kinase Csk is the primary negative regulator of the Src-family kinases (SFKs, e.g., Lck, Fyn, Lyn, Hck, Fgr, Blk, Yes), phosphorylating a tyrosine on the SFK C-terminal tail that mediates autoinhibition.	Tyrosine	142-150	C-terminal Src kinase	Homo sapiens	11-14
34215742-4	2021	The populations of the inhibitor, 4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo(3,4-d)pyrimidine (PP1), in bulk solution and on the surface of c-Src kinase are reduced as the concentration of crowder bovine serum albumins (BSAs) increases.	4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo(3,4-d)pyrimidine	34-97	C-terminal Src kinase	Homo sapiens	144-156
34215742-4	2021	The populations of the inhibitor, 4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo(3,4-d)pyrimidine (PP1), in bulk solution and on the surface of c-Src kinase are reduced as the concentration of crowder bovine serum albumins (BSAs) increases.	PP1	99-102	C-terminal Src kinase	Homo sapiens	144-156
35504181-2	2022	In this study, we developed a macrophage-modulated and injectable "building block" drug delivery system comprised of porous chitosan (CS) microspheres and hydroxypropyl chitin (HPCH) hydrogel, where the dimethyloxallyl glycine (DMOG) was encapsulated in the thermosensitive HPCH hydrogel (HD) while kartogenin (KGN) was conjugated on the porous CS microspheres (CSK-PMS).	porous chitosan	117-132	C-terminal Src kinase	Homo sapiens	362-365
35504181-2	2022	In this study, we developed a macrophage-modulated and injectable "building block" drug delivery system comprised of porous chitosan (CS) microspheres and hydroxypropyl chitin (HPCH) hydrogel, where the dimethyloxallyl glycine (DMOG) was encapsulated in the thermosensitive HPCH hydrogel (HD) while kartogenin (KGN) was conjugated on the porous CS microspheres (CSK-PMS).	hydroxypropyl-chitin	155-175	C-terminal Src kinase	Homo sapiens	362-365
35504181-2	2022	In this study, we developed a macrophage-modulated and injectable "building block" drug delivery system comprised of porous chitosan (CS) microspheres and hydroxypropyl chitin (HPCH) hydrogel, where the dimethyloxallyl glycine (DMOG) was encapsulated in the thermosensitive HPCH hydrogel (HD) while kartogenin (KGN) was conjugated on the porous CS microspheres (CSK-PMS).	dimethyloxallyl glycine	203-226	C-terminal Src kinase	Homo sapiens	362-365
2479412-4	1989	Synthetic (4E)-D-erythro-sphingenine and several samples of natural sphingosine inhibited v-src or c-src tyrosine kinase activity measured with polyglutamate-tyrosine (4:1) as substrate.	(4e)-d-erythro-sphingenine	10-36	C-terminal Src kinase	Homo sapiens	99-120
35059869-3	2022	Tyrosine phosphorylated SGK223 at Y411 enables to interact with CSK resulting up regulation of c-Src activity and promotion of the cell migration.	Tyrosine	0-8	C-terminal Src kinase	Homo sapiens	64-67
2479412-4	1989	Synthetic (4E)-D-erythro-sphingenine and several samples of natural sphingosine inhibited v-src or c-src tyrosine kinase activity measured with polyglutamate-tyrosine (4:1) as substrate.	Sphingosine	68-79	C-terminal Src kinase	Homo sapiens	99-120
2479412-4	1989	Synthetic (4E)-D-erythro-sphingenine and several samples of natural sphingosine inhibited v-src or c-src tyrosine kinase activity measured with polyglutamate-tyrosine (4:1) as substrate.	polyglutamate-tyrosine	144-166	C-terminal Src kinase	Homo sapiens	99-120
33113518-6	2021	Molecular docking studies against the identified targets in HepG2 cells showed that the capsaicin is able to bind Abelson tyrosine-protein kinase, c-Src kinase, p38 MAP kinase and VEGF-receptor.	Capsaicin	88-97	C-terminal Src kinase	Homo sapiens	114-159
2434223-12	1987	Immune complex kinase assays of K562 cells with an anti-src serum (GD-11) yielded active c-src kinase and a Mr 50,000 phosphorylated protein, both of which were resistant to alkaline hydrolysis.	gd-11	67-72	C-terminal Src kinase	Homo sapiens	89-101
33387392-9	2021	Serum creatinine, uric acid, total cholesterol levels, ABPM parameters, cBP levels, and PWV values were significantly higher, and eGFR levels were significantly lower in the CSK group.	Cholesterol	35-46	C-terminal Src kinase	Homo sapiens	174-177
31756921-3	2019	Four major classes of enzymes that attenuate TCR signaling include E3 ubiquitin kinases such as the Casitas B-lineage lymphoma proteins (Cbl-b and c-Cbl), and Itchy (Itch), inhibitory tyrosine phosphatases, such as Src homology region 2 domain-containing phosphatases (SHP-1 and SHP-2), inhibitory protein kinases, such as C-terminal Src kinase (Csk), and inhibitory lipid kinases such as Src homology 2 (SH2) domain-containing inositol polyphosphate 5-phosphatase (SHIP) and Diacylglycerol kinases (DGKs).	Carbon	46-47	C-terminal Src kinase	Homo sapiens	346-349
32224253-2	2020	It has been shown previously that the activity of cSrc kinase is upregulated by substitution of 3 residues by glycine in the SH3-SH2 connector.	Glycine	110-117	C-terminal Src kinase	Homo sapiens	50-61
32358062-6	2020	Additionally, TGFbetaR signaling potentiated CSK phosphorylation of the P85 subunit in the P85-P110 phosphoinositide 3-kinase (PI3K) heterodimer, which reduced PI3K activity and down-regulated the activation of proteins that require phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) for their activation.	phosphatidylinositol 3,4,5-triphosphate	233-275	C-terminal Src kinase	Homo sapiens	45-48
32358062-6	2020	Additionally, TGFbetaR signaling potentiated CSK phosphorylation of the P85 subunit in the P85-P110 phosphoinositide 3-kinase (PI3K) heterodimer, which reduced PI3K activity and down-regulated the activation of proteins that require phosphatidylinositol (3,4,5)-trisphosphate (PtdIns(3,4,5)P3) for their activation.	phosphatidylinositol 3,4,5-triphosphate	277-292	C-terminal Src kinase	Homo sapiens	45-48
31872783-6	2021	We purposed a new mechanism that the protein context is primarily responsible for the atypical intramolecular SH3-fSBP recognition in c-Src kinase, which can promote the tight packing of segment against domain surface, support the segment polyproline-II (PPII) conformation in unbound state, and avoid unfavorable segment interactions with SH3 charged region by forming a C-terminal t-turn.	polyproline	239-253	C-terminal Src kinase	Homo sapiens	134-146
31872783-6	2021	We purposed a new mechanism that the protein context is primarily responsible for the atypical intramolecular SH3-fSBP recognition in c-Src kinase, which can promote the tight packing of segment against domain surface, support the segment polyproline-II (PPII) conformation in unbound state, and avoid unfavorable segment interactions with SH3 charged region by forming a C-terminal t-turn.	polyproline	255-259	C-terminal Src kinase	Homo sapiens	134-146
31872783-6	2021	We purposed a new mechanism that the protein context is primarily responsible for the atypical intramolecular SH3-fSBP recognition in c-Src kinase, which can promote the tight packing of segment against domain surface, support the segment polyproline-II (PPII) conformation in unbound state, and avoid unfavorable segment interactions with SH3 charged region by forming a C-terminal t-turn.	Carbon	372-373	C-terminal Src kinase	Homo sapiens	134-146
31872783-7	2021	In addition, the only proline residue Pro250 of fSBP segment is also required for the segment recognition by SH3 domain in c-Src kinase context; lack of Pro250 residue the segment exhibits considerable disorder and cannot maintain in PPII helical conformation, thus largely impairing the domain-segment binding capability.	isoleucyl-prolyl-proline	22-29	C-terminal Src kinase	Homo sapiens	123-135
32794043-3	2020	The balance of phosphorylation at the inhibitory and activating Tyr residues is maintained by a balance between CD45 and Csk and is dependent upon intact intracellular trafficking machinery.	Tyrosine	64-67	C-terminal Src kinase	Homo sapiens	121-124
32916637-6	2020	Conversely, increasing cytosolic [Ca2+] in crt-/- cells with ionomycin deactivated c-Src kinase and restored osteogenesis.	Ionomycin	61-70	C-terminal Src kinase	Homo sapiens	83-95
32525544-7	2020	Here, we have described a dynamical binding"s process of an anticancer drug, the dasatinib, to the c-Src kinase in full atomistic details for the first time, without applying any biasing force or potential which may lead the drug to artificial interactions with the protein.	Dasatinib	81-90	C-terminal Src kinase	Homo sapiens	99-111
31981897-6	2020	Significantly, Ectopic expression of wild-type AGO2, but not the three tyrosine site mutants, has an obvious tumor-promoting effect in vitro and in vivo, which function could be blocked thoroughly by treatment with c-Src kinase inhibitor, Saracatinib.	saracatinib	239-250	C-terminal Src kinase	Homo sapiens	215-227
31703690-8	2019	RESULTS: Activity of c-Src kinase, which causes the expression of p-Src418, was upregulated by different inflammatory factors and high glucose in HLE-B3 cells.	Glucose	135-142	C-terminal Src kinase	Homo sapiens	21-33
30601014-0	2019	Synthesis of CSK-DEX-PLGA Nanoparticles for the Oral Delivery of Exenatide to Improve Its Mucus Penetration and Intestinal Absorption.	Exenatide	65-74	C-terminal Src kinase	Homo sapiens	13-16
31125786-4	2019	Here we report that Csk is covalently modified by SUMO1 at lysine 53 (K53) both in vitro and in vivo.	Lysine	59-65	C-terminal Src kinase	Homo sapiens	20-23
31125786-5	2019	Treatment with hydrogen peroxide inhibited this modification to a certain extent, but PIAS3, identified as the main specific SUMO E3 ligase for Csk, could significantly enhance SUMO1-Csk level.	Hydrogen Peroxide	15-32	C-terminal Src kinase	Homo sapiens	144-147
31125786-5	2019	Treatment with hydrogen peroxide inhibited this modification to a certain extent, but PIAS3, identified as the main specific SUMO E3 ligase for Csk, could significantly enhance SUMO1-Csk level.	Hydrogen Peroxide	15-32	C-terminal Src kinase	Homo sapiens	183-186
31125786-9	2019	Our results suggest that SUMOylation of Csk mainly at lysine 53 negatively modulates its tumor suppressor function by reducing its binding with Cbp and consequently, inducing c-Src activation.	Lysine	54-60	C-terminal Src kinase	Homo sapiens	40-43
31140197-5	2019	Further investigation revealed that activation of Galphai2 by MTNR1B upon melatonin stimulation could inhibit SRC kinase activity via recruiting CSK and SRC, increasing SRC Y530 phosphorylation, and decreasing SRC Y419 phosphorylation.	Melatonin	74-83	C-terminal Src kinase	Homo sapiens	145-148
30601014-2	2019	To improve the mucus penetration and intestinal absorption of exenatide, we designed a block copolymer, CSKSSDYQC-dextran-poly(lactic-co-glycolic acid) (CSK-DEX-PLGA), and used it for the preparation of exenatide-loaded NPs.	Exenatide	62-71	C-terminal Src kinase	Homo sapiens	104-107
30601014-2	2019	To improve the mucus penetration and intestinal absorption of exenatide, we designed a block copolymer, CSKSSDYQC-dextran-poly(lactic-co-glycolic acid) (CSK-DEX-PLGA), and used it for the preparation of exenatide-loaded NPs.	dextran-poly(lactic-co-glycolic acid)	114-151	C-terminal Src kinase	Homo sapiens	104-107
30601014-2	2019	To improve the mucus penetration and intestinal absorption of exenatide, we designed a block copolymer, CSKSSDYQC-dextran-poly(lactic-co-glycolic acid) (CSK-DEX-PLGA), and used it for the preparation of exenatide-loaded NPs.	Exenatide	203-212	C-terminal Src kinase	Homo sapiens	104-107
30601014-3	2019	The functionalized exenatide-loaded NPs composed of CSK-DEX-PLGA were able to target intestinal epithelial cells and reduce the mucus-blocking effect of the intestine.	Exenatide	19-28	C-terminal Src kinase	Homo sapiens	52-55
30601014-5	2019	Compared to DEX-PLGA-NPs (DPs), the absorption of CSK-DEX-PLGA-NPs (CDPs) was increased in the villi, allowing the drug to act on gobletlike Caco-2 cells through clathrin-, caveolin-, and gap-mediated endocytosis.	cdps	68-72	C-terminal Src kinase	Homo sapiens	50-53
29723216-0	2018	c-Src kinase is involved in the tyrosine phosphorylation and activity of SLC11A1 in differentiating macrophages.	Tyrosine	32-40	C-terminal Src kinase	Homo sapiens	0-12
29923425-0	2018	Introducing novel potent anticancer agents of 1H-benzo[f]chromene scaffolds, targeting c-Src kinase enzyme with MDA-MB-231 cell line anti-invasion effect.	1h-benzo[f]chromene	46-65	C-terminal Src kinase	Homo sapiens	87-99
30100205-4	2018	Here, we demonstrated that TRIM25 interacted with c-Src and underwent tyrosine phosphorylation by c-Src kinase upon viral infection and the phosphorylation is required for the complete activation of RIG-I signaling.	Tyrosine	70-78	C-terminal Src kinase	Homo sapiens	98-110
30116401-0	2018	Regulation of transforming growth factor beta-mediated epithelial-mesenchymal transition of lens epithelial cells by c-Src kinase under high glucose conditions.	Glucose	141-148	C-terminal Src kinase	Homo sapiens	117-129
30116401-1	2018	Recent studies have reported that high glucose (HG) conditions may contribute to the acceleration of renal cell apoptosis and renal fibrosis by inducing epithelial-mesenchymal transition (EMT) of tubular epithelial cells, in which c-Src kinase and transforming growth factor (TGF)-beta are key modulators.	Glucose	39-46	C-terminal Src kinase	Homo sapiens	231-243
29723216-5	2018	Furthermore, we found that SLC11A1 is a direct substrate for active c-Src kinase and siRNA-mediated knockdown of cellular Src (c-Src) expression results in a significant decrease in tyrosine phosphorylation.	Tyrosine	182-190	C-terminal Src kinase	Homo sapiens	68-80
29723216-6	2018	We found that PMA induces the interaction of SLC11A1 with c-Src kinase.	Tetradecanoylphorbol Acetate	14-17	C-terminal Src kinase	Homo sapiens	58-70
29026535-1	2017	BACKGROUND: To analyze the clinical characteristics and outcomes of carbapenem-resistant Klebsiella pneumoniae (CRKp) and carbapenem-susceptible K. pneumoniae (CSKp) bloodstream infections (BSIs), and to study the risk factors for development of CRKp BSI and K. pneumoniae BSI-related mortality.	Carbapenems	122-132	C-terminal Src kinase	Homo sapiens	160-164
29725363-4	2018	Overexpression of CBP/PAG suppressed the growth of Jurkat cells by recruiting c-Src and its negative regulator, C-terminal Src kinase (CSK), to lipid rafts.	phenylacetylglycine	22-25	C-terminal Src kinase	Homo sapiens	112-133
29725363-4	2018	Overexpression of CBP/PAG suppressed the growth of Jurkat cells by recruiting c-Src and its negative regulator, C-terminal Src kinase (CSK), to lipid rafts.	phenylacetylglycine	22-25	C-terminal Src kinase	Homo sapiens	135-138
29503074-4	2018	By proteomics, we discovered that this pseudo-kinase uses the tyrosine kinase CSK to induce protein tyrosine phosphorylation in human cells.	Tyrosine	62-70	C-terminal Src kinase	Homo sapiens	78-81
29410316-3	2018	The potential of mean force computations predict that a specific double mutant can stabilize c-Src kinase into an active-like conformation while disabling the binding of ATP in the catalytic active site.	Adenosine Triphosphate	170-173	C-terminal Src kinase	Homo sapiens	93-105
30381668-9	2018	Nevertheless, L-theanine significantly lowered Ang II-prompted phosphorylation of Janus kinase 2 (JAK2), c-Src tyrosine kinase, and signal transducer and activators of transcription 3 (STAT3).	theanine	14-24	C-terminal Src kinase	Homo sapiens	105-126
29026535-7	2017	CSKp infection was associated with more severe clinical symptoms, particularly a higher serum creatinine level (165.06 +- 127.01 in the CSKp group vs. 93.77 +- 84.35 mumol/L in the CRKp group, p = 0.039), but there was no significant difference in prognosis between the CSKp and CRKp groups.	Creatinine	94-104	C-terminal Src kinase	Homo sapiens	0-4
28768887-6	2017	Biochemical analyses of premetazoan pTyr signalling components have further revealed the premetazoan origin of many key features of metazoan pTyr signalling, and the metazoan establishment of others, including the Csk-mediated negative regulation of the activity of Src, a conserved tyrosine kinase in the Holozoa.	premetazoan	24-35	C-terminal Src kinase	Homo sapiens	214-217
28768887-6	2017	Biochemical analyses of premetazoan pTyr signalling components have further revealed the premetazoan origin of many key features of metazoan pTyr signalling, and the metazoan establishment of others, including the Csk-mediated negative regulation of the activity of Src, a conserved tyrosine kinase in the Holozoa.	Phosphotyrosine	36-40	C-terminal Src kinase	Homo sapiens	214-217
28580424-2	2017	We report the unbinding dynamics of the anticancer drug dasatinib from c-Src kinase in full atomistic resolution using enhanced sampling molecular dynamics simulations.	Dasatinib	56-65	C-terminal Src kinase	Homo sapiens	71-83
28784162-12	2017	RESULTS: Our results revealed Csk as a robust enzyme catalysing phosphorylation of the C-terminal tail tyrosine of SFKs but a weak non-catalytic inhibitor of SFKs.	Tyrosine	103-111	C-terminal Src kinase	Homo sapiens	30-33
28178691-5	2017	Moreover, we demonstrated that P-gp can not only interact with Cbp and Src but also enhance the formation of inhibitory C-terminal Src kinase (Csk)-Cbp complexes that reduce phosphorylation of the Src activation residue Y416 and increase phosphorylation of the Src negative regulatory residue Y527.	y416	220-224	C-terminal Src kinase	Homo sapiens	120-141
28178691-5	2017	Moreover, we demonstrated that P-gp can not only interact with Cbp and Src but also enhance the formation of inhibitory C-terminal Src kinase (Csk)-Cbp complexes that reduce phosphorylation of the Src activation residue Y416 and increase phosphorylation of the Src negative regulatory residue Y527.	y416	220-224	C-terminal Src kinase	Homo sapiens	143-146
28273873-6	2017	CSK rs1378942 and CSK-MIR4513 rs3784789 were significantly modified by urinary sodium-potassium excretion ratio.	Sodium	79-85	C-terminal Src kinase	Homo sapiens	0-3
28317151-2	2017	Among the various synthesized amides, compound 20, a cyclic amide/pyridin-2(1H)-one derivative, exhibited an IC50 value comparable to that of the drug imatinib against c-Src kinase, and another compound (14) containing a 2-((4-methyl-2-oxo-2H-chromen-6-yl)oxy)acetamide demonstrated an IC50 value of 8.39 muM.	Amides	30-36	C-terminal Src kinase	Homo sapiens	168-180
28273873-6	2017	CSK rs1378942 and CSK-MIR4513 rs3784789 were significantly modified by urinary sodium-potassium excretion ratio.	Sodium	79-85	C-terminal Src kinase	Homo sapiens	18-21
28273873-6	2017	CSK rs1378942 and CSK-MIR4513 rs3784789 were significantly modified by urinary sodium-potassium excretion ratio.	Potassium	86-95	C-terminal Src kinase	Homo sapiens	0-3
28273873-6	2017	CSK rs1378942 and CSK-MIR4513 rs3784789 were significantly modified by urinary sodium-potassium excretion ratio.	Potassium	86-95	C-terminal Src kinase	Homo sapiens	18-21
28273873-8	2017	The present study results indicated that the mutant alleles of CSK rs1378942 and CSK-MIR4513 rs3784789 had the strongest protective effects against hypertension in the middle group of 24 h estimated urinary sodium-potassium excretion ratio.	Sodium	207-213	C-terminal Src kinase	Homo sapiens	63-66
28273873-8	2017	The present study results indicated that the mutant alleles of CSK rs1378942 and CSK-MIR4513 rs3784789 had the strongest protective effects against hypertension in the middle group of 24 h estimated urinary sodium-potassium excretion ratio.	Sodium	207-213	C-terminal Src kinase	Homo sapiens	81-84
28273873-8	2017	The present study results indicated that the mutant alleles of CSK rs1378942 and CSK-MIR4513 rs3784789 had the strongest protective effects against hypertension in the middle group of 24 h estimated urinary sodium-potassium excretion ratio.	Potassium	214-223	C-terminal Src kinase	Homo sapiens	63-66
28273873-8	2017	The present study results indicated that the mutant alleles of CSK rs1378942 and CSK-MIR4513 rs3784789 had the strongest protective effects against hypertension in the middle group of 24 h estimated urinary sodium-potassium excretion ratio.	Potassium	214-223	C-terminal Src kinase	Homo sapiens	81-84
28098256-0	2017	Dopamine promotes NMDA receptor hypofunction in the retina through D1 receptor-mediated Csk activation, Src inhibition and decrease of GluN2B phosphorylation.	Dopamine	0-8	C-terminal Src kinase	Homo sapiens	88-91
28098256-5	2017	This dopamine effect was dependent on upregulation of the canonical D1R/adenylyl cyclase/cAMP/PKA pathway, of PKA-induced activation of C-terminal Src kinase (Csk) and of Src inhibition.	Dopamine	5-13	C-terminal Src kinase	Homo sapiens	136-157
28098256-6	2017	Accordingly, knocking down Csk or overexpressing a Csk phosphoresistant Src mutant abrogated the dopamine-induced NMDAR hypofunction.	nmdar	114-119	C-terminal Src kinase	Homo sapiens	27-30
28098256-5	2017	This dopamine effect was dependent on upregulation of the canonical D1R/adenylyl cyclase/cAMP/PKA pathway, of PKA-induced activation of C-terminal Src kinase (Csk) and of Src inhibition.	Dopamine	5-13	C-terminal Src kinase	Homo sapiens	159-162
28098256-6	2017	Accordingly, knocking down Csk or overexpressing a Csk phosphoresistant Src mutant abrogated the dopamine-induced NMDAR hypofunction.	nmdar	114-119	C-terminal Src kinase	Homo sapiens	51-54
28098256-6	2017	Accordingly, knocking down Csk or overexpressing a Csk phosphoresistant Src mutant abrogated the dopamine-induced NMDAR hypofunction.	Dopamine	97-105	C-terminal Src kinase	Homo sapiens	27-30
28098256-7	2017	Overall, the interplay between dopamine and NMDAR hypofunction, through the D1R/Csk/Src/GluN2B pathway, might impact on light-regulated synaptic activity in retinal neurons.	Dopamine	31-39	C-terminal Src kinase	Homo sapiens	80-83
28098256-7	2017	Overall, the interplay between dopamine and NMDAR hypofunction, through the D1R/Csk/Src/GluN2B pathway, might impact on light-regulated synaptic activity in retinal neurons.	nmdar	44-49	C-terminal Src kinase	Homo sapiens	80-83
28098256-6	2017	Accordingly, knocking down Csk or overexpressing a Csk phosphoresistant Src mutant abrogated the dopamine-induced NMDAR hypofunction.	Dopamine	97-105	C-terminal Src kinase	Homo sapiens	51-54
27391443-3	2016	The inhibition of c-Src requires phosphorylation at tyrosine 527 mediated by C-terminal Src kinase (Csk) and dephosphorylation at tyrosine 416 mediated by phosphatases, such as phosphatase and tensin homolog (PTEN).	Tyrosine	52-60	C-terminal Src kinase	Homo sapiens	77-98
27875633-2	2017	The dasatinib-l-arginine derivative (Das-R, 7) was found to be the most potent of the inhibitors tested, with IC50 values of 4.4, <0.25, and <0.45 nm against Csk, Src, and Abl kinases, respectively.	dasatinib-l-arginine	4-24	C-terminal Src kinase	Homo sapiens	164-167
27391443-3	2016	The inhibition of c-Src requires phosphorylation at tyrosine 527 mediated by C-terminal Src kinase (Csk) and dephosphorylation at tyrosine 416 mediated by phosphatases, such as phosphatase and tensin homolog (PTEN).	Tyrosine	52-60	C-terminal Src kinase	Homo sapiens	100-103
27819029-7	2016	This work employed NMR, X-ray cryptography, and other biophysical methods to study a disulfide bond in Csk SH2 domain.	Disulfides	85-94	C-terminal Src kinase	Homo sapiens	103-106
27116701-4	2016	In the present study, we found that Pragmin directly binds to Csk by the tyrosine-phosphorylated EPIYA motif.	Tyrosine	73-81	C-terminal Src kinase	Homo sapiens	62-65
27116701-5	2016	The complex formation potentiates kinase activity of Csk, which in turn phosphorylates Pragmin on tyrosine-238 (Y238), Y343, and Y391.	Tyrosine	98-106	C-terminal Src kinase	Homo sapiens	53-56
27375620-3	2016	In the immune system, cAMP is a potent negative regulator of T cell receptor-mediated activation of effector T cells (Teff) acting through a proximal PKA/Csk/Lck pathway anchored via a scaffold consisting of the AKAP Ezrin holding PKA, the linker protein EBP50, and the anchoring protein phosphoprotein associated with glycosphingolipid-enriched microdomains holding Csk.	Cyclic AMP	22-26	C-terminal Src kinase	Homo sapiens	154-157
27375620-3	2016	In the immune system, cAMP is a potent negative regulator of T cell receptor-mediated activation of effector T cells (Teff) acting through a proximal PKA/Csk/Lck pathway anchored via a scaffold consisting of the AKAP Ezrin holding PKA, the linker protein EBP50, and the anchoring protein phosphoprotein associated with glycosphingolipid-enriched microdomains holding Csk.	Cyclic AMP	22-26	C-terminal Src kinase	Homo sapiens	367-370
27375620-4	2016	As PKA activates Csk and Csk inhibits Lck, this pathway in response to cAMP shuts down proximal T cell activation.	Cyclic AMP	71-75	C-terminal Src kinase	Homo sapiens	17-20
27375620-4	2016	As PKA activates Csk and Csk inhibits Lck, this pathway in response to cAMP shuts down proximal T cell activation.	Cyclic AMP	71-75	C-terminal Src kinase	Homo sapiens	25-28
27038655-6	2016	In the endometriotic lesions, prostaglandin E2 (PGE2) produced by cyclooxygenase-2 (COX-2), binds to its EP4 receptor (EP4), and via c-Src kinase induces MMPs activation, promoting endometriosis.	Dinoprostone	30-46	C-terminal Src kinase	Homo sapiens	133-145
27038655-6	2016	In the endometriotic lesions, prostaglandin E2 (PGE2) produced by cyclooxygenase-2 (COX-2), binds to its EP4 receptor (EP4), and via c-Src kinase induces MMPs activation, promoting endometriosis.	Dinoprostone	48-52	C-terminal Src kinase	Homo sapiens	133-145
27038655-11	2016	HCB enhanced COX-2 and EP4 expression, PGE2 secretion and the c-Src kinase activation in T-HESC.	Hexachlorobenzene	0-3	C-terminal Src kinase	Homo sapiens	62-74
26755576-8	2016	Further mechanistic analyses reveal that GOF mutant Shp2 hyperactivates the Polo-like kinase 1 (Plk1) kinase by enhancing c-Src kinase-mediated tyrosine phosphorylation of Plk1.	Tyrosine	144-152	C-terminal Src kinase	Homo sapiens	122-134
26527736-8	2016	Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SHP2 [SH2 (Src homology 2) domain-containing protein tyrosine phosphatase 2] and their roles in stabilizing the phosphorylation and activation of CSK (c-Src tyrosine kinase).	Tyrosine	24-32	C-terminal Src kinase	Homo sapiens	346-349
26527736-8	2016	Phosphorylation of this tyrosine residue of TXNIP diminished the binding capability of PPxY motifs of TXNIP to Itch, whereas this phosphorylation is a prerequisite to the binding activity of TXNIP to SHP2 [SH2 (Src homology 2) domain-containing protein tyrosine phosphatase 2] and their roles in stabilizing the phosphorylation and activation of CSK (c-Src tyrosine kinase).	Tyrosine	24-32	C-terminal Src kinase	Homo sapiens	351-372
26996624-7	2016	First, 17beta-estradiol (E2), through c-Src kinase, is able to enhance tyrosine phosphorylation levels of aromatase protein and increases its enzymatic activity and estrogen biosynthesis.	Estradiol	7-23	C-terminal Src kinase	Homo sapiens	38-50
27819029-0	2016	Combining biophysical methods to analyze the disulfide bond in SH2 domain of C-terminal Src kinase.	Disulfides	45-54	C-terminal Src kinase	Homo sapiens	77-98
27819029-2	2016	The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains.	Disulfides	64-73	C-terminal Src kinase	Homo sapiens	18-39
27819029-2	2016	The SH2 domain of C-terminal Src kinase (Csk) contains a single disulfide bond, which is unusual for most SH2 domains.	Disulfides	64-73	C-terminal Src kinase	Homo sapiens	41-44
26996624-7	2016	First, 17beta-estradiol (E2), through c-Src kinase, is able to enhance tyrosine phosphorylation levels of aromatase protein and increases its enzymatic activity and estrogen biosynthesis.	Tyrosine	71-79	C-terminal Src kinase	Homo sapiens	38-50
26617519-10	2015	It was hypothesized that inhibition of c-Src kinase activity may explain CS in EGFR-transfected cells.	Cesium	73-75	C-terminal Src kinase	Homo sapiens	39-51
26304753-10	2015	Simvastatin evoked epidermal growth factor receptor-c-Src-increased Tyr phosphorylation of sEH and formation of an sEH-Akt-AMPK-eNOS complex, which was abolished by the c-Src kinase inhibitor PP1 or c-Src dominant-negative mutant K298M.	Simvastatin	0-11	C-terminal Src kinase	Homo sapiens	169-181
26234813-0	2015	Csk-Induced Phosphorylation of Src at Tyrosine 530 is Essential for H2O2-Mediated Suppression of ERK1/2 in Human Umbilical Vein Endothelial Cells.	Tyrosine	38-46	C-terminal Src kinase	Homo sapiens	0-3
26234813-0	2015	Csk-Induced Phosphorylation of Src at Tyrosine 530 is Essential for H2O2-Mediated Suppression of ERK1/2 in Human Umbilical Vein Endothelial Cells.	Hydrogen Peroxide	68-72	C-terminal Src kinase	Homo sapiens	0-3
26234813-5	2015	Using siRNA, it was found that H2O2-induced suppression of ERK1/2 was dependent on Csk.	Hydrogen Peroxide	31-35	C-terminal Src kinase	Homo sapiens	83-86
26234813-7	2015	In conclusion, H2O2-induced Csk translocation to the plasma membrane leads to phosphorylation of Src at the tyrosine 530 residue resulting in a reduction of ERK1/2 phosphorylation.	Hydrogen Peroxide	15-19	C-terminal Src kinase	Homo sapiens	28-31
26234813-7	2015	In conclusion, H2O2-induced Csk translocation to the plasma membrane leads to phosphorylation of Src at the tyrosine 530 residue resulting in a reduction of ERK1/2 phosphorylation.	Tyrosine	108-116	C-terminal Src kinase	Homo sapiens	28-31
25376742-3	2015	Using assay conditions where c-Src kinase activity required binding to a tyrosine phosphopeptide based on the focal adhesion kinase SH3-SH2 docking sequence, we screened a kinase-biased library for selective inhibitors of the Src/focal adhesion kinase peptide complex versus c-Src alone.	Tyrosine	73-81	C-terminal Src kinase	Homo sapiens	29-41
26286460-3	2015	Enzyme-templated screening was performed to identify acrylamides that assemble into bivalent inhibitors of c-Src kinase.	Acrylamides	53-64	C-terminal Src kinase	Homo sapiens	107-119
26304753-10	2015	Simvastatin evoked epidermal growth factor receptor-c-Src-increased Tyr phosphorylation of sEH and formation of an sEH-Akt-AMPK-eNOS complex, which was abolished by the c-Src kinase inhibitor PP1 or c-Src dominant-negative mutant K298M.	Tyrosine	68-71	C-terminal Src kinase	Homo sapiens	169-181
25897081-8	2015	In contrast, PTP1B potentiated SRC activity, but not by dephosphorylating SRC itself directly; instead, PTP1B regulated the interaction between CBP/PAG and CSK.	phenylacetylglycine	148-151	C-terminal Src kinase	Homo sapiens	156-159
25897081-9	2015	SRC associated with, and phosphorylated, the transmembrane protein CBP/PAG at Tyr-317, resulting in CSK recruitment.	phenylacetylglycine	71-74	C-terminal Src kinase	Homo sapiens	100-103
25897081-9	2015	SRC associated with, and phosphorylated, the transmembrane protein CBP/PAG at Tyr-317, resulting in CSK recruitment.	Tyrosine	78-81	C-terminal Src kinase	Homo sapiens	100-103
25897081-10	2015	We identified PAG as a substrate of PTP1B, and dephosphorylation abolished recruitment of the inhibitory kinase CSK.	phenylacetylglycine	14-17	C-terminal Src kinase	Homo sapiens	112-115
25447713-1	2015	OBJECTIVE: To study the characteristics, risk factors and outcomes of intensive care unit (ICU) patients with carbapenem-resistant (CRKp) and carbapenem-susceptible (CSKp) Klebsiella pneumoniae infections.	Carbapenems	142-152	C-terminal Src kinase	Homo sapiens	166-170
25505610-7	2014	The signaling properties of COA-Cl showed significant similarities to those of sphingosine 1-phosphate, an endogenous S1P1 ligand, in that both induced responses sensitive to pertussis toxin (Galpha i/o inhibitor), 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid tetrakis (acetoxymethyl ester) (BAPTA-AM), (calcium chelator), and PP2 (c-Src tyrosine kinase inhibitor).	coa-cl	28-34	C-terminal Src kinase	Homo sapiens	344-365
25302671-7	2014	Most notably, a dampened allosteric connection between the SH3 domain and alphaC helix leads to greater autoinhibitory phosphorylation by Csk, illustrating the complex effects of SH2-CD linker sequence on cellular function.	sh2-cd	179-185	C-terminal Src kinase	Homo sapiens	138-141
25292214-4	2014	We found that activation of FGFR1 led to activation of c-Src kinase-dependent tyrosine phosphorylation of NEDD4, enhancing the ubiquitin ligase activity of NEDD4.	Tyrosine	78-86	C-terminal Src kinase	Homo sapiens	55-67
26380301-4	2015	On contrary, direct relation was observed between percent drug release and polymer concentrations of Kollidon VA 64/Soluplus (CSK, CSS).	poly(vinylpyrrolidone-co-vinyl-acetate)	101-115	C-terminal Src kinase	Homo sapiens	126-129
25447263-2	2015	We have crystallized the complex between the SH3 domain of the c-Src tyrosine kinase and the C-terminal proline rich motif of the NS5A protein (A349PPIPPPRRKR359).	Proline	104-111	C-terminal Src kinase	Homo sapiens	63-84
25447263-6	2015	Our results show the interaction of the SH3 domain of the c-Src tyrosine kinase with a proline rich motif in the NS5A protein and point to their potential interaction in vivo.	Proline	87-94	C-terminal Src kinase	Homo sapiens	58-79
25505610-7	2014	The signaling properties of COA-Cl showed significant similarities to those of sphingosine 1-phosphate, an endogenous S1P1 ligand, in that both induced responses sensitive to pertussis toxin (Galpha i/o inhibitor), 1,2-bis(2-aminophenoxy)ethane-N,N,N",N"-tetraacetic acid tetrakis (acetoxymethyl ester) (BAPTA-AM), (calcium chelator), and PP2 (c-Src tyrosine kinase inhibitor).	sphingosine 1-phosphate	79-102	C-terminal Src kinase	Homo sapiens	344-365
25015208-7	2014	Importantly, we revealed that SA stimulates elastogenesis only after intracellular influx of non-oxidized ascorbate anions (facilitated by the sodium-dependent ascorbate transporter), that causes reduction of intracellular ROS, activation of c-Src tyrosine kinase and the enhancement of IGF-1-induced phosphorylation of the IGF-1 receptor that ultimately triggers elastogenic signalling pathway.	Ascorbic Acid	30-32	C-terminal Src kinase	Homo sapiens	242-263
24632723-0	2014	SHP-2 binds to caveolin-1 and regulates Src activity via competitive inhibition of CSK in response to H2O2 in astrocytes.	Hydrogen Peroxide	102-106	C-terminal Src kinase	Homo sapiens	83-86
24902122-8	2014	Csk was identified as the predominant mammalian protein interacting with YL2, and a dominant-negative Csk rescued phagocytosis in the presence of YL2.	CHEMBL3087937	73-76	C-terminal Src kinase	Homo sapiens	0-3
24902122-9	2014	Purified Csk phosphorylated the tyrosines in the YL2 EPIYG motifs.	Tyrosine	32-41	C-terminal Src kinase	Homo sapiens	9-12
24902122-10	2014	Phosphorylated YL2 increased Csk catalytic activity, resulting in positive feedback, such that YL2 can be phosphorylated by the same kinase that it activates.	CHEMBL3087937	15-18	C-terminal Src kinase	Homo sapiens	29-32
24902122-10	2014	Phosphorylated YL2 increased Csk catalytic activity, resulting in positive feedback, such that YL2 can be phosphorylated by the same kinase that it activates.	CHEMBL3087937	95-98	C-terminal Src kinase	Homo sapiens	29-32
23901911-2	2014	RECENT ADVANCES: Several recent insights have reported that, alongside the well-known phosphorylation/dephosphorylation control, cysteine oxidation is a further mechanism of enzyme activation for both c-Src kinase and its oncogenic counterparts.	Cysteine	129-137	C-terminal Src kinase	Homo sapiens	201-213
24632506-0	2014	Synthesis and evaluation of c-Src kinase inhibitory activity of pyridin-2(1H)-one derivatives.	2-hydroxypyridine	64-81	C-terminal Src kinase	Homo sapiens	28-40
24632506-2	2014	In this perspective, a series of eighteen 2-pyridone derivatives were synthesized and evaluated for their c-Src kinase inhibitory activity.	2-hydroxypyridine	42-52	C-terminal Src kinase	Homo sapiens	106-118
24632723-7	2014	Our results collectively indicate that SHP-2 alters Src kinase activity by interfering with the complex formation between CSK and phosphotyrosine caveolin-1 in the presence of H2O2, thus functions as a positive regulator in Src signaling under oxidative stress in brain astrocytes.	Phosphotyrosine	130-145	C-terminal Src kinase	Homo sapiens	122-125
24632723-7	2014	Our results collectively indicate that SHP-2 alters Src kinase activity by interfering with the complex formation between CSK and phosphotyrosine caveolin-1 in the presence of H2O2, thus functions as a positive regulator in Src signaling under oxidative stress in brain astrocytes.	Hydrogen Peroxide	176-180	C-terminal Src kinase	Homo sapiens	122-125
24632723-5	2014	In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419.	Hydrogen Peroxide	83-87	C-terminal Src kinase	Homo sapiens	19-22
24632723-5	2014	In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419.	Tyrosine	143-151	C-terminal Src kinase	Homo sapiens	19-22
24632723-5	2014	In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419.	Tyrosine	153-156	C-terminal Src kinase	Homo sapiens	19-22
24632723-5	2014	In the presence of CSK siRNA, binding between caveolin-1 and SHP-2 was enhanced by H2O2 treatment, which led to reduced Src phosphorylation at tyrosine (Tyr) 530 and enhanced Src phosphorylation at Tyr 419.	Tyrosine	198-201	C-terminal Src kinase	Homo sapiens	19-22
24632723-6	2014	In contrast, siRNA targeting of SHP-2 facilitated H2O2-mediated interaction between caveolin-1 and CSK and enhanced Src phosphorylation at Tyr 530, leading to subsequent decrease in Src downstream signaling, such as focal adhesion kinase (FAK) and extracellular signal-related kinase (ERK).	Hydrogen Peroxide	50-54	C-terminal Src kinase	Homo sapiens	99-102
24314082-4	2013	Between the two distinct populations of CD11b/CD18:ICAM-1 complex that participate in cell adhesion, the cytoskeleton(CSK)-anchored elastic elements and the membrane tethers, we found that LA1 enhanced binding of CD11b/CD18 on K562 cells to ICAM-1 via the formation of long membrane tethers, whereas Mn(2+) additionally increased ICAM-1 binding via CSK-anchored bonds.	leukadherin-1	189-192	C-terminal Src kinase	Homo sapiens	118-121
24405902-8	2014	We used tyrosine-specific mAbs and Western blot analysis to show that a deregulation of the Csk/PAG loop in activated T cells from elderly individuals favored the inactive form of tyrosine-phosphorylated Lck (Y505).	Tyrosine	8-16	C-terminal Src kinase	Homo sapiens	92-95
24405902-8	2014	We used tyrosine-specific mAbs and Western blot analysis to show that a deregulation of the Csk/PAG loop in activated T cells from elderly individuals favored the inactive form of tyrosine-phosphorylated Lck (Y505).	Tyrosine	180-188	C-terminal Src kinase	Homo sapiens	92-95
24300854-6	2014	C-terminal Src kinase (Csk) binds to tyrosine phosphorylated JAM-A through its Src homology 2 domain.	Tyrosine	37-45	C-terminal Src kinase	Homo sapiens	0-21
24300854-6	2014	C-terminal Src kinase (Csk) binds to tyrosine phosphorylated JAM-A through its Src homology 2 domain.	Tyrosine	37-45	C-terminal Src kinase	Homo sapiens	23-26
24300854-10	2014	Our results strongly suggest that tyrosine-phosphorylated JAM-A is a Csk-binding protein and functions as an endogenous inhibitor of integrin signaling.	Tyrosine	34-42	C-terminal Src kinase	Homo sapiens	69-72
24300854-12	2014	Upon agonist stimulation, JAM-A is dephosphorylated on the tyrosine, allowing the dissociation of Csk from the integrin complex, and thus facilitating outside-in signaling.	Tyrosine	59-67	C-terminal Src kinase	Homo sapiens	98-101
24145190-8	2014	Finally, we discovered that c-Src kinase activity was required for the downregulation of miR-203 in HCT-15 cells, which was stimulated by the interaction between hyaluronan (HA) and CD44.	Hyaluronic Acid	162-172	C-terminal Src kinase	Homo sapiens	28-40
24145190-8	2014	Finally, we discovered that c-Src kinase activity was required for the downregulation of miR-203 in HCT-15 cells, which was stimulated by the interaction between hyaluronan (HA) and CD44.	Hyaluronic Acid	174-176	C-terminal Src kinase	Homo sapiens	28-40
24314082-4	2013	Between the two distinct populations of CD11b/CD18:ICAM-1 complex that participate in cell adhesion, the cytoskeleton(CSK)-anchored elastic elements and the membrane tethers, we found that LA1 enhanced binding of CD11b/CD18 on K562 cells to ICAM-1 via the formation of long membrane tethers, whereas Mn(2+) additionally increased ICAM-1 binding via CSK-anchored bonds.	leukadherin-1	189-192	C-terminal Src kinase	Homo sapiens	349-352
23698767-7	2013	In addition, D-pinitol exerted its inhibitory effects by reducing focal adhesion kinase (FAK) phosphorylation, c-Src kinase activity and NF-kB activation.	pinitol	13-22	C-terminal Src kinase	Homo sapiens	111-123
23824743-5	2013	Isorhamnetin inhibited AOM/DSS-induced oncogenic c-Src activation and beta-catenin nuclear translocation, while promoting the expression of C-terminal Src kinase (CSK), a negative regulator of Src family of tyrosine kinases.	3-methylquercetin	0-12	C-terminal Src kinase	Homo sapiens	140-161
23824743-5	2013	Isorhamnetin inhibited AOM/DSS-induced oncogenic c-Src activation and beta-catenin nuclear translocation, while promoting the expression of C-terminal Src kinase (CSK), a negative regulator of Src family of tyrosine kinases.	3-methylquercetin	0-12	C-terminal Src kinase	Homo sapiens	163-166
23824743-6	2013	Similarly, in HT-29 colon cancer cells, isorhamnetin inhibited oncogenic Src activity and beta-catenin nuclear translocation by inducing expression of csk, as verified by RNA interference knockdown of csk.	3-methylquercetin	40-52	C-terminal Src kinase	Homo sapiens	151-154
23824743-6	2013	Similarly, in HT-29 colon cancer cells, isorhamnetin inhibited oncogenic Src activity and beta-catenin nuclear translocation by inducing expression of csk, as verified by RNA interference knockdown of csk.	3-methylquercetin	40-52	C-terminal Src kinase	Homo sapiens	201-204
23824743-7	2013	Our observations suggest the chemoprotective effects of isorhamnetin in colon cancer are linked to its anti-inflammatory activities and its inhibition of oncogenic Src activity and consequential loss of nuclear beta-catenin, activities that are dependent on CSK expression.	3-methylquercetin	56-68	C-terminal Src kinase	Homo sapiens	258-261
23670194-4	2013	TLR3 induction led to a rapid increase in ROS generation and a physical association between components of the NADPH oxidase (NOX) enzyme complex (NOX2 and p47(phox)) and TLR3 via a Ca(2+)-c-Src tyrosine kinase-dependent pathway.	Reactive Oxygen Species	42-45	C-terminal Src kinase	Homo sapiens	188-209
23548896-0	2013	Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains.	Glycosphingolipids	161-178	C-terminal Src kinase	Homo sapiens	78-99
23548896-0	2013	Identification of a new interaction mode between the Src homology 2 domain of C-terminal Src kinase (Csk) and Csk-binding protein/phosphoprotein associated with glycosphingolipid microdomains.	Glycosphingolipids	161-178	C-terminal Src kinase	Homo sapiens	101-104
23593342-0	2013	Fulvestrant-induced cell death and proteasomal degradation of estrogen receptor alpha protein in MCF-7 cells require the CSK c-Src tyrosine kinase.	Fulvestrant	0-11	C-terminal Src kinase	Homo sapiens	121-124
23471971-5	2013	In search of a potential downstream mechanism, we found that TI-VAMP is phosphorylated in vitro by c-Src kinase on tyrosine 45 of the Longin domain.	Tyrosine	115-123	C-terminal Src kinase	Homo sapiens	99-111
23593342-6	2013	MCF-7 cell sensitivities to fulvestrant-induced cell death or ERalpha protein degradation was not affected by small-molecular-weight inhibitors of the tyrosine kinase activity of c-Src, suggesting possible involvement of other signaling molecules in CSK-dependent MCF-7 cell death induced by fulvestrant.	Fulvestrant	28-39	C-terminal Src kinase	Homo sapiens	250-253
23593342-4	2013	Whereas RNAi knockdown of CSK in MCF-7 cells by shRNA-expressing lentiviruses strongly suppressed fulvestrant-induced cell death, CSK knockdown did not affect cytocidal actions of 4-hydroxytamoxifen or paclitaxel, a chemotherapeutic agent.	Fulvestrant	98-109	C-terminal Src kinase	Homo sapiens	26-29
23593342-5	2013	In the absence of CSK, fulvestrant-induced proteasomal degradation of ERalpha protein was suppressed in both MCF-7 and T47D estrogen-dependent breast cancer cells whereas the TP53-mutated T47D cells were resistant to the cytocidal action of fulvestrant in the presence or absence of CSK.	Fulvestrant	23-34	C-terminal Src kinase	Homo sapiens	18-21
23593342-5	2013	In the absence of CSK, fulvestrant-induced proteasomal degradation of ERalpha protein was suppressed in both MCF-7 and T47D estrogen-dependent breast cancer cells whereas the TP53-mutated T47D cells were resistant to the cytocidal action of fulvestrant in the presence or absence of CSK.	Fulvestrant	23-34	C-terminal Src kinase	Homo sapiens	283-286
22928736-0	2012	Irreversible inhibitors of c-Src kinase that target a nonconserved cysteine.	Cysteine	67-75	C-terminal Src kinase	Homo sapiens	27-39
23333462-6	2013	Cbp over-expression in T-FGM AhR-/- cells enhanced the formation of inhibitory Csk-Cbp complexes which in turn reduced c-Src p-Tyr(416) activation and focal adhesion kinase (FAK) phosphorylation at the c-Src-responsive residues p-Tyr(576) and p-Tyr(577).	Tyrosine	127-130	C-terminal Src kinase	Homo sapiens	79-82
23333462-6	2013	Cbp over-expression in T-FGM AhR-/- cells enhanced the formation of inhibitory Csk-Cbp complexes which in turn reduced c-Src p-Tyr(416) activation and focal adhesion kinase (FAK) phosphorylation at the c-Src-responsive residues p-Tyr(576) and p-Tyr(577).	Tyrosine	230-233	C-terminal Src kinase	Homo sapiens	79-82
23333462-6	2013	Cbp over-expression in T-FGM AhR-/- cells enhanced the formation of inhibitory Csk-Cbp complexes which in turn reduced c-Src p-Tyr(416) activation and focal adhesion kinase (FAK) phosphorylation at the c-Src-responsive residues p-Tyr(576) and p-Tyr(577).	Tyrosine	230-233	C-terminal Src kinase	Homo sapiens	79-82
23271210-1	2013	BACKGROUND: The objective of this study was to evaluate the mortality of and risk factors for bacteriuria due to carbapenem-resistant Klebsiella pneumoniae (CRKp) versus carbapenem-susceptible K. pneumoniae (CSKp) producing extended spectrum beta lactamase (ESBL).	Carbapenems	113-123	C-terminal Src kinase	Homo sapiens	208-212
24039559-5	2013	A unique feature of the SH2 domain of Csk is the tight turn in place of the canonical CD loop in a surface site far removed from kinase domain interactions.	Cadmium	86-88	C-terminal Src kinase	Homo sapiens	38-41
24039559-6	2013	In this study, we used a combination of experimental and computational methods to probe the importance of this difference by constructing a Csk variant with a longer SH2 CD loop to mimic the flexibility found in homologous kinase SH2 domains.	Cadmium	170-172	C-terminal Src kinase	Homo sapiens	140-143
22943437-0	2012	Biological effects of AL622, a molecule rationally designed to release an EGFR and a c-Src kinase inhibitor.	AL622	22-27	C-terminal Src kinase	Homo sapiens	85-97
22962253-2	2012	We have previously shown that 17-beta estradiol (E(2)) rapidly enhances aromatase enzymatic activity through an increase of tyrosine protein phosphorylation controlled by the activity of the c-Src kinase in breast cancer cells.	Estradiol	30-47	C-terminal Src kinase	Homo sapiens	191-203
22962253-2	2012	We have previously shown that 17-beta estradiol (E(2)) rapidly enhances aromatase enzymatic activity through an increase of tyrosine protein phosphorylation controlled by the activity of the c-Src kinase in breast cancer cells.	Tyrosine	124-132	C-terminal Src kinase	Homo sapiens	191-203
22777522-3	2012	We show that the hyperresponsive phenotype of B cells lacking Lyn is predicated on significantly increased basal and inducible PI3K activity that correlates with the constitutive hypophosphorylation of PAG/Cbp (phosphoprotein associated with glycosphingolipid-enriched microdomains/Csk-binding protein), a concomitant reduction in bound Csk in Lyn(-/-) B cells and elevated levels of active Fyn.	phenylacetylglycine	202-205	C-terminal Src kinase	Homo sapiens	282-285
22141738-3	2012	The PKA-Csk immunoregulatory pathway is scaffolded by the A kinase anchoring protein ezrin, the Csk binding protein phosphoprotein associated with glycosphingolipid-enriched membrane microdomains and the linker protein ezrin/radixin/moesin binding protein of 50 kDa.	Glycosphingolipids	147-164	C-terminal Src kinase	Homo sapiens	8-11
22659621-1	2012	The transmembrane protein Cbp/PAG (Csk binding protein/phospho-protein associated with glycosphingolipid-enriched microdomains) has a negative regulatory role in T cell activation as an adapter for C-terminal Src kinase, Csk.	Glycosphingolipids	87-104	C-terminal Src kinase	Homo sapiens	35-38
22659621-1	2012	The transmembrane protein Cbp/PAG (Csk binding protein/phospho-protein associated with glycosphingolipid-enriched microdomains) has a negative regulatory role in T cell activation as an adapter for C-terminal Src kinase, Csk.	Glycosphingolipids	87-104	C-terminal Src kinase	Homo sapiens	221-224
22659621-2	2012	In T cells, membrane docking of Csk is promoted by binding to FynT-phosphorylated Cbp/PAG (pTyr317) to allow targeting of substrates residing in lipid rafts.	phenylacetylglycine	86-89	C-terminal Src kinase	Homo sapiens	32-35
22659621-2	2012	In T cells, membrane docking of Csk is promoted by binding to FynT-phosphorylated Cbp/PAG (pTyr317) to allow targeting of substrates residing in lipid rafts.	ptyr317	91-98	C-terminal Src kinase	Homo sapiens	32-35
22544307-5	2012	Differential blocking of Src kinase family members (despite c-Src) by PP2 increased the activity of c-Src and the tyrosine phosphorylation of PTPIP51 at position 176, which is the substrate of c-Src kinase.	Tyrosine	114-122	C-terminal Src kinase	Homo sapiens	193-205
22935373-2	2012	The peptides with a sequence specific to c-Src tyrosine kinase and protein tyrosine phosphatase 1B (PTP1B) were first validated with ELISA-based protein tyrosine kinase assay and then functionalized on vertically aligned carbon nanofiber (VACNF) nanoelectrode arrays (NEAs).	Carbon	221-227	C-terminal Src kinase	Homo sapiens	41-62
22141738-3	2012	The PKA-Csk immunoregulatory pathway is scaffolded by the A kinase anchoring protein ezrin, the Csk binding protein phosphoprotein associated with glycosphingolipid-enriched membrane microdomains and the linker protein ezrin/radixin/moesin binding protein of 50 kDa.	Glycosphingolipids	147-164	C-terminal Src kinase	Homo sapiens	96-99
21551129-4	2011	Here, we demonstrate that aspirin activates the c-Src tyrosine kinase pathway in CRC cells.	Aspirin	26-33	C-terminal Src kinase	Homo sapiens	48-69
21418517-5	2012	Several signalling inhibitors interfered with progesterone-induced FAK activation, including progesterone receptor (PR) antagonist ORG 31710, specific c-Src kinase inhibitor PP2, phosphatidylinosital-3 kinase (PI3K) inhibitor wortmannin as well as rho-associated kinase (ROCK-2) inhibitor Y27632.	Progesterone	46-58	C-terminal Src kinase	Homo sapiens	151-163
22119472-2	2012	The synthesized tetrahydroindazolones were evaluated for inhibition of cell proliferation of human colon carcinoma (HT-29), human ovarian adenocarcinoma (SK-OV-3), and c-Src kinase activity.	tetrahydroindazolones	16-37	C-terminal Src kinase	Homo sapiens	168-180
22119472-5	2012	In general, the tetrahydroindazolones showed modest inhibition of c-Src kinase where 4-tertbutylphenyl- and 3,4-dichlorophenyl- derivatives showed the inhibition of c-Src kinase with IC(50) values of 35.1 and 50.7 muM, respectively.	tetrahydroindazolones	16-37	C-terminal Src kinase	Homo sapiens	66-78
22119472-5	2012	In general, the tetrahydroindazolones showed modest inhibition of c-Src kinase where 4-tertbutylphenyl- and 3,4-dichlorophenyl- derivatives showed the inhibition of c-Src kinase with IC(50) values of 35.1 and 50.7 muM, respectively.	tetrahydroindazolones	16-37	C-terminal Src kinase	Homo sapiens	165-177
22119472-5	2012	In general, the tetrahydroindazolones showed modest inhibition of c-Src kinase where 4-tertbutylphenyl- and 3,4-dichlorophenyl- derivatives showed the inhibition of c-Src kinase with IC(50) values of 35.1 and 50.7 muM, respectively.	3,4-dichlorophenyl	108-126	C-terminal Src kinase	Homo sapiens	165-177
23028292-6	2012	Here, we investigated whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of Csk in solution using a combination of small angle x-ray scattering and molecular dynamics simulations.	Adenosine Triphosphate	52-55	C-terminal Src kinase	Homo sapiens	120-123
23028292-6	2012	Here, we investigated whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of Csk in solution using a combination of small angle x-ray scattering and molecular dynamics simulations.	Adenylyl Imidodiphosphate	63-70	C-terminal Src kinase	Homo sapiens	120-123
23028292-6	2012	Here, we investigated whether interactions with the ATP analog AMP-PNP and ADP can shift the conformational ensemble of Csk in solution using a combination of small angle x-ray scattering and molecular dynamics simulations.	Adenosine Diphosphate	75-78	C-terminal Src kinase	Homo sapiens	120-123
21708247-6	2011	The critical role of NADPH-oxidase-dependent superoxide generation in this cross-talk mechanism is corroborated by the finding that apocynin or a siRNA against p22(phox) prevents EGFR transactivation and c-Src kinase activity.	Superoxides	45-55	C-terminal Src kinase	Homo sapiens	204-216
21873224-4	2011	Here we show that mammalian Pragmin/SgK223 undergoes tyrosine phosphorylation at the EPIYA motif by SFKs and thereby acquires the ability to interact with the SH2 domain of the C-terminal Src kinase (Csk), a negative regulator of SFKs.	Tyrosine	53-61	C-terminal Src kinase	Homo sapiens	177-198
21130867-7	2011	Thus, the cAMP-type I PKA-Csk pathway emerges as a putative target for therapeutic intervention in autoimmune disorders as well as in cancer, where T(R) cell-mediated suppression contributes to suboptimal local immune responses.	Cyclic AMP	10-14	C-terminal Src kinase	Homo sapiens	26-29
20457609-7	2010	SH2 profiling revealed that Shc, Csk, Abl, and Sap associate with Tyr-826, whereas SH2-B, Src, Brk, GTPase-activating protein, and phospholipase C-gamma associate with Tyr-841.	Tyrosine	66-69	C-terminal Src kinase	Homo sapiens	33-36
21367918-12	2011	Imatinib suppressed the albumin-induced EMT and ER stress via inhibition of ROS and c-Src kinase.	Imatinib Mesylate	0-8	C-terminal Src kinase	Homo sapiens	84-96
21367918-14	2011	In conclusion, the ROS-c-Src kinase-mTOR pathway played a central role in the signaling pathway that linked albumin to EMT and ER stress.	Reactive Oxygen Species	19-22	C-terminal Src kinase	Homo sapiens	23-35
21113815-1	2011	Previous studies have shown that Csk plays critical roles in the regulation of neural development, differentiation and glutamate-mediated synaptic plasticity.	Glutamic Acid	119-128	C-terminal Src kinase	Homo sapiens	33-36
21113815-5	2011	The truncation of the NR1 subunit C-tail which contains only one tyrosine (Y837) significantly reduced the Csk association with the NR1-1a/NR2A receptor complex.	Tyrosine	65-73	C-terminal Src kinase	Homo sapiens	107-110
21113815-6	2011	Furthermore, we found that either the truncation of NR2A C-tail at aa 857 or the mutation of Y837 in the NR1-1a subunit to phenylalanine blocked the inhibition of NR1-1a/NR2A receptors induced by intracellular application of Csk.	Phenylalanine	123-136	C-terminal Src kinase	Homo sapiens	225-228
21695648-5	2011	However, engagement of the TCR in primary T cells is followed by rapid cAMP production in lipid rafts and activation of the cAMP- PKA-Csk pathway inhibiting proximal T-cell signaling.	Cyclic AMP	124-128	C-terminal Src kinase	Homo sapiens	134-137
20843787-3	2010	In this study, we investigated hyaluronan (HA)-induced CD44 (a primary HA receptor) interaction with c-Src kinase and the transcriptional factor, Twist, in breast tumor cells (MDA-MB-231 cells).	Hyaluronic Acid	31-41	C-terminal Src kinase	Homo sapiens	101-113
20843787-3	2010	In this study, we investigated hyaluronan (HA)-induced CD44 (a primary HA receptor) interaction with c-Src kinase and the transcriptional factor, Twist, in breast tumor cells (MDA-MB-231 cells).	Hyaluronic Acid	43-45	C-terminal Src kinase	Homo sapiens	101-113
21145940-1	2011	BACKGROUND: Activation of the protein tyrosine kinase c-Src (c-Src kinase) induced by the exposure to the environmental pollutant 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) has been shown in various cell types.	Polychlorinated Dibenzodioxins	130-165	C-terminal Src kinase	Homo sapiens	61-73
21145940-1	2011	BACKGROUND: Activation of the protein tyrosine kinase c-Src (c-Src kinase) induced by the exposure to the environmental pollutant 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) has been shown in various cell types.	Polychlorinated Dibenzodioxins	167-171	C-terminal Src kinase	Homo sapiens	61-73
21145940-5	2011	Data from FRET assay visualized and quantified the activation of c-Src kinase induced by TCDD in living cells of both cell types.	Polychlorinated Dibenzodioxins	89-93	C-terminal Src kinase	Homo sapiens	65-77
22022425-0	2011	Barium promotes anchorage-independent growth and invasion of human HaCaT keratinocytes via activation of c-SRC kinase.	Barium	0-6	C-terminal Src kinase	Homo sapiens	105-117
22022425-8	2011	Barium (2.5-5 microM) also promoted anchorage-independent growth and invasion of fibroblasts (NIH3T3) and immortalized nontumorigenic melanocytes (melan-a), but not transformed cutaneous squamous cell carcinoma (HSC5 and A431) and malignant melanoma (Mel-ret) cells, with activation of c-SRC kinase.	Barium	0-6	C-terminal Src kinase	Homo sapiens	286-298
20570525-0	2010	Discovery of novel purine derivatives with potent and selective inhibitory activity against c-Src tyrosine kinase.	purine	19-25	C-terminal Src kinase	Homo sapiens	92-113
20570525-1	2010	We report here the discovery of novel purine derivatives with potent and selective inhibitory activity against c-Src tyrosine kinase by adopting a strategy integrating focused combinatorial library design, virtual screening, chemical synthesis, and bioassay.	purine	38-44	C-terminal Src kinase	Homo sapiens	111-132
20346773-1	2010	The kinase-phosphatase pair Csk and CD45 reciprocally regulate phosphorylation of the inhibitory tyrosine of the Src family kinases Lck and Fyn.	Tyrosine	97-105	C-terminal Src kinase	Homo sapiens	28-31
20420835-0	2010	Spatiotemporal control of cyclic AMP immunomodulation through the PKA-Csk inhibitory pathway is achieved by anchoring to an Ezrin-EBP50-PAG scaffold in effector T cells.	Cyclic AMP	26-36	C-terminal Src kinase	Homo sapiens	70-73
20420835-4	2010	The A kinase anchoring protein Ezrin colocalizes PKA and Csk by forming a supramolecular signaling complex consisting of PKA, Ezrin, Ezrin/radixin/moesin (ERM) binding protein of 50 kDa (EBP50), phosphoprotein associated with glycosphingolipid-enriched membrane microdomains (GEMs) (PAG) and Csk.	Glycosphingolipids	226-243	C-terminal Src kinase	Homo sapiens	57-60
20420835-4	2010	The A kinase anchoring protein Ezrin colocalizes PKA and Csk by forming a supramolecular signaling complex consisting of PKA, Ezrin, Ezrin/radixin/moesin (ERM) binding protein of 50 kDa (EBP50), phosphoprotein associated with glycosphingolipid-enriched membrane microdomains (GEMs) (PAG) and Csk.	phenylacetylglycine	283-286	C-terminal Src kinase	Homo sapiens	57-60
20086095-1	2010	Engagement of the T-cell receptor (TCR) in human primary T cells activates a cyclic AMP (cAMP)-protein kinase A (PKA)-Csk inhibitory pathway that prevents full T-cell activation in the absence of a coreceptor stimulus.	Cyclic AMP	77-87	C-terminal Src kinase	Homo sapiens	118-121
20086095-1	2010	Engagement of the T-cell receptor (TCR) in human primary T cells activates a cyclic AMP (cAMP)-protein kinase A (PKA)-Csk inhibitory pathway that prevents full T-cell activation in the absence of a coreceptor stimulus.	Cyclic AMP	89-93	C-terminal Src kinase	Homo sapiens	118-121
20048167-3	2010	Activation of SFK by overexpression of dominant negative Csk induced VE-cadherin phosphorylation at tyrosines 658, 685, and 731.	Tyrosine	100-109	C-terminal Src kinase	Homo sapiens	57-60
20197690-0	2010	Fatty acid-bearing albumin induces VCAM-1 expression through c-Src kinase-AP-1/NF-kB pathways: effect of L-carnitine.	Fatty Acids	0-10	C-terminal Src kinase	Homo sapiens	61-73
19948721-0	2010	S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion.	Cysteine	19-27	C-terminal Src kinase	Homo sapiens	35-56
19948721-0	2010	S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion.	Nitric Oxide	67-79	C-terminal Src kinase	Homo sapiens	35-56
19818398-3	2010	Recently, biochemical evidence indicated that the c-Abl and Csk kinases were able to phosphorylate the tyrosine 170 (Y170) residue of c-Jun - which lies within the recognition motif of the Itch ubiquitin ligase - and also regulate its stability independent of the JNK phosphorylation sites.	Tyrosine	103-111	C-terminal Src kinase	Homo sapiens	60-63
20197690-8	2010	Inhibitors of protein kinase C and tyrosine kinase, anti-oxidants and intracellular calcium chelator suppressed the FA(+) albumin-induced activation of c-Src kinase.	Calcium	84-91	C-terminal Src kinase	Homo sapiens	152-164
20197690-9	2010	L-Carnitine suppressed the FA(+) albumin-induced VCAM-1 expression via inhibition of c-Src kinase.	Carnitine	0-11	C-terminal Src kinase	Homo sapiens	85-97
19350053-10	2009	Furthermore, Crk induced the phosphorylation of Src-Y416; accordingly the interaction between Crk and Csk was increased.	y416	52-56	C-terminal Src kinase	Homo sapiens	102-105
19808673-5	2009	In addition, unlike PIP(2), LPA dramatically stimulates the tyrosine phosphorylation of villin by c-Src kinase.	lysophosphatidic acid	28-31	C-terminal Src kinase	Homo sapiens	98-110
19808673-5	2009	In addition, unlike PIP(2), LPA dramatically stimulates the tyrosine phosphorylation of villin by c-Src kinase.	Tyrosine	60-68	C-terminal Src kinase	Homo sapiens	98-110
19822664-6	2009	In contrast, disruption of the microdomain by depleting cholesterol could induce a robust transformation in Csk-deficient fibroblasts in which only a limited amount of activated SFKs was expressed.	Cholesterol	56-67	C-terminal Src kinase	Homo sapiens	108-111
19632164-5	2009	Using SILAC, we were able to detect changes in tyrosine phosphorylation patterns of 43 potential c-Src kinase substrates in PDGF receptor signaling.	Tyrosine	47-55	C-terminal Src kinase	Homo sapiens	97-109
19887846-8	2010	Inhibitors of protein kinase C and tyrosine kinase, antioxidants and intracellular calcium chelator suppressed myoglobin-induced activation of c-Src kinase.	Calcium	83-90	C-terminal Src kinase	Homo sapiens	143-155
19887846-9	2010	Losartan and simvastatin suppressed myoglobin-induced VCAM-1 expression via inhibition of c-Src kinase.	Losartan	0-8	C-terminal Src kinase	Homo sapiens	90-102
19887846-9	2010	Losartan and simvastatin suppressed myoglobin-induced VCAM-1 expression via inhibition of c-Src kinase.	Simvastatin	13-24	C-terminal Src kinase	Homo sapiens	90-102
18586953-7	2008	In excised inside-out membrane patches CACC were activated by exposure of the cytoplasmic face of the channels to the human recombinant Src(p60(c-src)) kinase with endogenous or exogenous ATP and inhibited by lambda-protein phosphatase.	Adenosine Triphosphate	188-191	C-terminal Src kinase	Homo sapiens	144-158
19026486-0	2009	Mislocalization of cell-cell adhesion complexes in tamoxifen-resistant breast cancer cells with elevated c-Src tyrosine kinase activity.	Tamoxifen	51-60	C-terminal Src kinase	Homo sapiens	105-126
19185573-0	2009	Intertwined dimeric structure for the SH3 domain of the c-Src tyrosine kinase induced by polyethylene glycol binding.	Polyethylene Glycols	89-108	C-terminal Src kinase	Homo sapiens	56-77
18948260-7	2008	Finally, RPTPalpha-induced phosphorylation of Paxillin and Cbp/PAG induces recruitment of the SFK inhibitory kinase Csk, indicative of negative feedback loops limiting SFK activation by RPTPalpha.	phenylacetylglycine	63-66	C-terminal Src kinase	Homo sapiens	116-119
19260709-3	2009	Prior studies on protein tyrosine kinases Csk and Src revealed the potential for chemical rescue of catalytically deficient mutant kinases (Arg to Ala mutations) by small diamino compounds, particularly imidazole; however, the potency and efficiency of rescue was greater for Src.	Arginine	140-143	C-terminal Src kinase	Homo sapiens	42-45
19260709-3	2009	Prior studies on protein tyrosine kinases Csk and Src revealed the potential for chemical rescue of catalytically deficient mutant kinases (Arg to Ala mutations) by small diamino compounds, particularly imidazole; however, the potency and efficiency of rescue was greater for Src.	Alanine	147-150	C-terminal Src kinase	Homo sapiens	42-45
19260709-3	2009	Prior studies on protein tyrosine kinases Csk and Src revealed the potential for chemical rescue of catalytically deficient mutant kinases (Arg to Ala mutations) by small diamino compounds, particularly imidazole; however, the potency and efficiency of rescue was greater for Src.	diamino	171-178	C-terminal Src kinase	Homo sapiens	42-45
19260709-3	2009	Prior studies on protein tyrosine kinases Csk and Src revealed the potential for chemical rescue of catalytically deficient mutant kinases (Arg to Ala mutations) by small diamino compounds, particularly imidazole; however, the potency and efficiency of rescue was greater for Src.	imidazole	203-212	C-terminal Src kinase	Homo sapiens	42-45
19291104-2	2009	Three dimensional quantitative structure-activity relationship (3D-QSAR) studies were carried out on quinazolin derivatives inhibiting c-Src kinase.	quinazolin	101-111	C-terminal Src kinase	Homo sapiens	135-147
19111446-12	2009	CONCLUSION: Mechanical wounding induces significant ROS generation at the wound edge which, in turn, induced ligand-independent KGFR and FRS2 activation via c-Src kinase signaling.	Reactive Oxygen Species	52-55	C-terminal Src kinase	Homo sapiens	157-169
18721137-1	2008	Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched domains is a transmembrane adaptor protein primarily involved in negative regulation of T-cell activation by recruitment of C-terminal Src kinase (Csk), a protein tyrosine kinase which represses Src kinase activity through C-terminal phosphorylation.	Glycosphingolipids	51-68	C-terminal Src kinase	Homo sapiens	202-223
18721137-1	2008	Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched domains is a transmembrane adaptor protein primarily involved in negative regulation of T-cell activation by recruitment of C-terminal Src kinase (Csk), a protein tyrosine kinase which represses Src kinase activity through C-terminal phosphorylation.	Glycosphingolipids	51-68	C-terminal Src kinase	Homo sapiens	0-3
18721137-2	2008	Recruitment of Csk occurs via SH2-domain binding to PAG pTyr317, thus, the interaction is highly dependent on phosphorylation performed by the Src family kinase Fyn, which docks onto PAG using a dual-domain binding mode involving both SH3- and SH2-domains of Fyn.	phenylacetylglycine	52-55	C-terminal Src kinase	Homo sapiens	15-18
18721137-2	2008	Recruitment of Csk occurs via SH2-domain binding to PAG pTyr317, thus, the interaction is highly dependent on phosphorylation performed by the Src family kinase Fyn, which docks onto PAG using a dual-domain binding mode involving both SH3- and SH2-domains of Fyn.	ptyr317	56-63	C-terminal Src kinase	Homo sapiens	15-18
18721137-2	2008	Recruitment of Csk occurs via SH2-domain binding to PAG pTyr317, thus, the interaction is highly dependent on phosphorylation performed by the Src family kinase Fyn, which docks onto PAG using a dual-domain binding mode involving both SH3- and SH2-domains of Fyn.	phenylacetylglycine	183-186	C-terminal Src kinase	Homo sapiens	15-18
18783823-9	2008	Moreover, the kinase activity of SFK is negatively regulated by the phosphorylation of their carboxy (C)-terminal regulatory tyrosines by specific proteins called carboxyl-terminal Src kinase (Csk) and Csk homologous kinase (CHK).	Tyrosine	125-134	C-terminal Src kinase	Homo sapiens	163-191
18783823-9	2008	Moreover, the kinase activity of SFK is negatively regulated by the phosphorylation of their carboxy (C)-terminal regulatory tyrosines by specific proteins called carboxyl-terminal Src kinase (Csk) and Csk homologous kinase (CHK).	Tyrosine	125-134	C-terminal Src kinase	Homo sapiens	193-196
18451158-4	2008	In one such cell line, SUM229, inhibiting c-Src kinase activity with either a dominant-negative c-Src or a c-Src TKI decreased EGFR phosphorylation on Tyr(845), Tyr(992), and Tyr(1086) in the presence of EGFR TKIs.	Tyrosine	161-164	C-terminal Src kinase	Homo sapiens	42-54
18614016-1	2008	The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk).	Tyrosine	44-52	C-terminal Src kinase	Homo sapiens	186-207
18614016-1	2008	The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk).	Tyrosine	44-52	C-terminal Src kinase	Homo sapiens	209-212
18614016-1	2008	The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk).	Tyrosine	145-148	C-terminal Src kinase	Homo sapiens	186-207
18614016-1	2008	The catalytic activity of the Src family of tyrosine kinases is suppressed by phosphorylation on a tyrosine residue located near the C terminus (Tyr 527 in c-Src), which is catalyzed by C-terminal Src Kinase (Csk).	Tyrosine	145-148	C-terminal Src kinase	Homo sapiens	209-212
18485715-0	2008	Design and synthesis of 7-alkoxy-4-heteroarylamino-3-quinolinecarbonitriles as dual inhibitors of c-Src kinase and nitric oxide synthase.	7-alkoxy-4-heteroarylamino-3-quinolinecarbonitriles	24-75	C-terminal Src kinase	Homo sapiens	98-110
18451158-4	2008	In one such cell line, SUM229, inhibiting c-Src kinase activity with either a dominant-negative c-Src or a c-Src TKI decreased EGFR phosphorylation on Tyr(845), Tyr(992), and Tyr(1086) in the presence of EGFR TKIs.	Tyrosine	151-154	C-terminal Src kinase	Homo sapiens	42-54
18331839-6	2008	Two example protein domains (Csk and Abl tyrosine kinase domain) with N-terminal Cys are demonstrated using this method.	Cysteine	81-84	C-terminal Src kinase	Homo sapiens	29-32
18644992-4	2008	Sulindac-mediated Csk induction was replicated in the human colorectal cancer cell line HT-29, with a corresponding suppression of both Src kinase activity (63% of vehicle; P < 0.05) and E-cadherin tyrosine phosphorylation (an in vivo Src target).	Sulindac	0-8	C-terminal Src kinase	Homo sapiens	18-21
18644992-4	2008	Sulindac-mediated Csk induction was replicated in the human colorectal cancer cell line HT-29, with a corresponding suppression of both Src kinase activity (63% of vehicle; P < 0.05) and E-cadherin tyrosine phosphorylation (an in vivo Src target).	Tyrosine	201-209	C-terminal Src kinase	Homo sapiens	18-21
18644992-5	2008	To determine the importance of Csk in NSAID antiproliferative activity, we stably transfected a Csk-specific short hairpin RNA (shRNA) vector into HT-29 cells, thereby blunting the sulindac-mediated Csk induction.	Sulindac	181-189	C-terminal Src kinase	Homo sapiens	96-99
18644992-5	2008	To determine the importance of Csk in NSAID antiproliferative activity, we stably transfected a Csk-specific short hairpin RNA (shRNA) vector into HT-29 cells, thereby blunting the sulindac-mediated Csk induction.	Sulindac	181-189	C-terminal Src kinase	Homo sapiens	96-99
18644992-8	2008	Moreover, although sulindac-mediated induction of p21(cip/waf1) was 113% in wild-type HT-29, this induction was alleviated in the Csk shRNA transfectants (65% induction; P < 0.01).	Sulindac	19-27	C-terminal Src kinase	Homo sapiens	130-133
18180373-0	2008	Inhibitory phosphorylation of soluble guanylyl cyclase by muscarinic m2 receptors via Gbetagamma-dependent activation of c-Src kinase.	gbetagamma	86-96	C-terminal Src kinase	Homo sapiens	121-133
18451158-4	2008	In one such cell line, SUM229, inhibiting c-Src kinase activity with either a dominant-negative c-Src or a c-Src TKI decreased EGFR phosphorylation on Tyr(845), Tyr(992), and Tyr(1086) in the presence of EGFR TKIs.	Tyrosine	161-164	C-terminal Src kinase	Homo sapiens	42-54
17905674-8	2008	Lyn also phosphorylates Y314, which recruits Csk/Ctk to phosphorylate Lyn at its Y508 negative site, allowing an inactive conformation to form.	y314	24-28	C-terminal Src kinase	Homo sapiens	45-48
18086565-1	2008	To elucidate the regulatory mechanism of cell transformation induced by c-Src tyrosine kinase, we performed a proteomic analysis of tyrosine phosphorylated proteins that interact with c-Src and/or its negative regulator Csk.	Tyrosine	78-86	C-terminal Src kinase	Homo sapiens	220-223
18056706-2	2008	PAG has a role in negative regulation of Src family kinases in T-cells by recruitment of Csk (C-terminal Src kinase) to the membrane via binding to PAG phosphotyrosine 317.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	89-92
18056706-2	2008	PAG has a role in negative regulation of Src family kinases in T-cells by recruitment of Csk (C-terminal Src kinase) to the membrane via binding to PAG phosphotyrosine 317.	Phosphotyrosine	152-167	C-terminal Src kinase	Homo sapiens	94-115
17918184-7	2008	Treatment with the dual specific Abl/c-Src kinase inhibitor AZD0530 significantly reduces the growth inhibitory effect of high EGF concentrations, signifying that EGFR induced IRF-1 is responsible for the observed growth inhibition.	saracatinib	60-67	C-terminal Src kinase	Homo sapiens	37-49
18212280-8	2008	These effects of salusins were abolished by G-protein, c-Src tyrosine kinase, protein kinase C, and mitogen-activated protein kinase kinase inhibitors.	salusins	17-25	C-terminal Src kinase	Homo sapiens	55-76
17905674-8	2008	Lyn also phosphorylates Y314, which recruits Csk/Ctk to phosphorylate Lyn at its Y508 negative site, allowing an inactive conformation to form.	y508	81-85	C-terminal Src kinase	Homo sapiens	45-48
18491059-6	2008	One immunomodulating pathway is the cAMP-protein kinase A-Csk pathway scaffolded by a supramolecular complex residing in lipid rafts with the A kinase-anchoring protein (AKAP) ezrin, the Csk-binding protein PAG and a linker between the two, EBP50.	phenylacetylglycine	207-210	C-terminal Src kinase	Homo sapiens	58-61
18491059-6	2008	One immunomodulating pathway is the cAMP-protein kinase A-Csk pathway scaffolded by a supramolecular complex residing in lipid rafts with the A kinase-anchoring protein (AKAP) ezrin, the Csk-binding protein PAG and a linker between the two, EBP50.	phenylacetylglycine	207-210	C-terminal Src kinase	Homo sapiens	187-190
17490855-7	2007	Oligo(dT)18 primed cDNA was synthesized from HepG2 and HT29 total RNA to amplify IR and cSRC kinase ORFs, respectively.	oligo(dt)18	0-11	C-terminal Src kinase	Homo sapiens	88-99
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	phenylacetylglycine	0-3	C-terminal Src kinase	Homo sapiens	141-162
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	phenylacetylglycine	0-3	C-terminal Src kinase	Homo sapiens	164-167
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	phenylacetylglycine	0-3	C-terminal Src kinase	Homo sapiens	192-195
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	Glycosphingolipids	40-57	C-terminal Src kinase	Homo sapiens	164-167
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	Glycosphingolipids	40-57	C-terminal Src kinase	Homo sapiens	192-195
18085663-1	2008	PAG, the phosphoprotein associated with glycosphingolipid-enriched microdomains (GEM), negatively regulates Src family kinases by recruiting C-terminal Src kinase (Csk) to the membrane, where Csk phosphorylates the inhibitory tyrosine of the Src kinases.	Tyrosine	226-234	C-terminal Src kinase	Homo sapiens	164-167
18085663-5	2008	Despite being displaced, the mutant PAG molecule still binds the Src kinase Fyn and the cytoskeletal adaptor ezrin-radixin-moesin-binding phosphoprotein of 50 kDa, becomes tyrosine-phosphorylated, and recruits Csk to the membrane.	phenylacetylglycine	36-39	C-terminal Src kinase	Homo sapiens	210-213
17897955-4	2007	The mutants differed from wild-type Lck only in one to three amino acid residues following the negative regulatory tyrosine 505, which was normally phosphorylated by Csk and dephosphorylated by CD45 in the mutants.	Tyrosine	115-123	C-terminal Src kinase	Homo sapiens	166-169
17942635-2	2007	Potential protein-protein interaction sites within the COOH terminus of the L-type calcium channel include those for the SH3 and SH2 binding domains of c-Src kinase that regulates calcium currents in smooth muscle.	Calcium	83-90	C-terminal Src kinase	Homo sapiens	152-164
18056464-5	2007	The cysteine replacement of the highly conserved Y367 residue in fibroblast growth factor receptor 4 or the Q26X nonsense mutation in the tumor-suppressor kinase CSK are examples, and may contribute to cell line-specific signaling characteristics and tumor progression.	Cysteine	4-12	C-terminal Src kinase	Homo sapiens	162-165
18056464-5	2007	The cysteine replacement of the highly conserved Y367 residue in fibroblast growth factor receptor 4 or the Q26X nonsense mutation in the tumor-suppressor kinase CSK are examples, and may contribute to cell line-specific signaling characteristics and tumor progression.	y367	49-53	C-terminal Src kinase	Homo sapiens	162-165
17911601-1	2007	cAMP negatively regulates T cell immune responses by activation of type I protein kinase A (PKA), which in turn phosphorylates and activates C-terminal Src kinase (Csk) in T cell lipid rafts.	Cyclic AMP	0-4	C-terminal Src kinase	Homo sapiens	141-162
17911601-1	2007	cAMP negatively regulates T cell immune responses by activation of type I protein kinase A (PKA), which in turn phosphorylates and activates C-terminal Src kinase (Csk) in T cell lipid rafts.	Cyclic AMP	0-4	C-terminal Src kinase	Homo sapiens	164-167
17911601-3	2007	Furthermore, Ezrin brings PKA in proximity to its downstream substrate Csk in lipid rafts by forming a multiprotein complex consisting of PKA/Ezrin/Ezrin-binding protein 50, Csk, and Csk-binding protein/phosphoprotein associated with glycosphingolipid-enriched microdomains.	Glycosphingolipids	234-251	C-terminal Src kinase	Homo sapiens	71-74
18085663-7	2008	The mutant functions by depleting Csk from the GEM fractions, as apparent by changes in the phosphorylation of the inhibitory tyrosines within the Src kinases.	Tyrosine	126-135	C-terminal Src kinase	Homo sapiens	34-37
17691821-3	2007	First, both Csk and Src phosphorylate Src as a common substrate, but on different Tyr residues.	Tyrosine	82-85	C-terminal Src kinase	Homo sapiens	12-15
17186241-0	2007	Targeting c-Src kinase enhances tamoxifen"s inhibitory effect on cell growth by modulating expression of cell cycle and survival proteins.	Tamoxifen	32-41	C-terminal Src kinase	Homo sapiens	10-22
17186241-7	2007	Nevertheless, blocking c-Src kinase in tamoxifen-treated MCF-7 cells led to apoptosis.	Tamoxifen	39-48	C-terminal Src kinase	Homo sapiens	23-35
17186241-10	2007	This inactivation of Bad upon ER blockade seemed to depend on c-Src function as chemical inhibition of c-Src kinase reduced BadpS112 levels in cells with impaired ER function but not in estrogen-treated cells.	badps112	124-132	C-terminal Src kinase	Homo sapiens	103-115
17530729-2	2007	A series of PhPP-peptide conjugates were synthesized using PhPP as an ATP mimic and CIYKYY or YIYGSFK as a peptide substrate to improve the inhibitory potency against active c-Src kinase.	phpp	12-16	C-terminal Src kinase	Homo sapiens	174-186
17349748-0	2007	Sphingosine 1-phosphate stimulation of NADPH oxidase activity: relationship with platelet-derived growth factor receptor and c-Src kinase.	sphingosine 1-phosphate	0-23	C-terminal Src kinase	Homo sapiens	125-137
17389760-2	2007	Because Fyn is the kinase primarily responsible for the phosphorylation of PAG (the phosphoprotein associated with glycosphingolipid-enriched microdomains), which negatively regulates Src-kinase activity by recruiting Csk (the C-terminal Src kinase) to the membrane, we investigated whether anergy induction also affects PAG.	Glycosphingolipids	115-132	C-terminal Src kinase	Homo sapiens	218-221
17389760-2	2007	Because Fyn is the kinase primarily responsible for the phosphorylation of PAG (the phosphoprotein associated with glycosphingolipid-enriched microdomains), which negatively regulates Src-kinase activity by recruiting Csk (the C-terminal Src kinase) to the membrane, we investigated whether anergy induction also affects PAG.	Glycosphingolipids	115-132	C-terminal Src kinase	Homo sapiens	227-248
17389760-3	2007	Analysis of anergic T cells revealed that PAG is hyperphosphorylated at the Csk binding site, leading to enhanced Csk recruitment and inhibitory tyrosine phosphorylation within Fyn.	Tyrosine	145-153	C-terminal Src kinase	Homo sapiens	76-79
17498653-5	2007	Cholesterol depletion attenuated integrin-dependent caveolin-1 phosphorylation, Src activation and Csk association with beta1 integrin.	Cholesterol	0-11	C-terminal Src kinase	Homo sapiens	99-102
17349748-2	2007	The results demonstrate also that both platelet-derived growth factor (PDGF) and S1P-mediated NADPH oxidase activation and H2O2 production by Gi-protein coupled receptors (GPCRs) and c-Src kinase.	Hydrogen Peroxide	123-127	C-terminal Src kinase	Homo sapiens	183-195
17349748-5	2007	However, a different time course of H2O2 production in S1P-stimulated cells compared to that obtained in PDGF-stimulated cells has been observed, and this seems to be related to the different activation behavior of c-Src kinase induced after S1P or PDGF stimulation.	Hydrogen Peroxide	36-40	C-terminal Src kinase	Homo sapiens	215-227
17349748-6	2007	Finally, these data demonstrate that S1P-induced H2O2 production is necessary to maximize c-Src kinase activation, confirming that this is a redox regulated kinase.	Hydrogen Peroxide	49-53	C-terminal Src kinase	Homo sapiens	90-102
17233630-2	2007	SFK activity is controlled by Csk (C-terminal Src kinase), which phosphorylates a C-terminal tyrosine residue on SFKs, resulting in inhibition of SFK activity.	Tyrosine	93-101	C-terminal Src kinase	Homo sapiens	30-33
17325034-3	2007	CSK overexpression inhibited RA-mediated neurite outgrowth, a result which correlated with the inhibition of the SFK c-SRC.	Tretinoin	29-31	C-terminal Src kinase	Homo sapiens	0-3
17325034-11	2007	We have elucidated a nongenomic extranuclear signal mediated by the RAR-SRC interaction that is negatively regulated by CSK and is required for RA-induced neuronal differentiation.	Tretinoin	68-70	C-terminal Src kinase	Homo sapiens	120-123
17233630-2	2007	SFK activity is controlled by Csk (C-terminal Src kinase), which phosphorylates a C-terminal tyrosine residue on SFKs, resulting in inhibition of SFK activity.	Tyrosine	93-101	C-terminal Src kinase	Homo sapiens	35-56
17233630-3	2007	Csk is recruited to sites of SFK activity by tyrosine-phosphorylated Csk-binding proteins.	Tyrosine	45-53	C-terminal Src kinase	Homo sapiens	0-3
17233630-3	2007	Csk is recruited to sites of SFK activity by tyrosine-phosphorylated Csk-binding proteins.	Tyrosine	45-53	C-terminal Src kinase	Homo sapiens	69-72
17409508-5	2007	It was found that 3-(substituted-benzylidene)-1,3-dihydro-indolin-2-thione derivatives are more effective than indolin-2-one congeners for the inhibition of CK2 and p60(c-Src) tyrosine kinase.	3-(substituted-benzylidene)-1,3-dihydro-indolin-2-thione	18-74	C-terminal Src kinase	Homo sapiens	169-191
17409508-5	2007	It was found that 3-(substituted-benzylidene)-1,3-dihydro-indolin-2-thione derivatives are more effective than indolin-2-one congeners for the inhibition of CK2 and p60(c-Src) tyrosine kinase.	indolin-2-one	111-124	C-terminal Src kinase	Homo sapiens	169-191
17223712-8	2007	Interestingly, such a role of cdc37 in mediating the action of TCDD appears to be limited to activation of c-Src kinase, but not kinases associated with activation of NFkB, C/EBPalpha, or ERK.	Polychlorinated Dibenzodioxins	63-67	C-terminal Src kinase	Homo sapiens	107-119
17137590-0	2007	A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity.	Disulfides	8-17	C-terminal Src kinase	Homo sapiens	48-69
17137590-1	2007	The SH2 domain of the C-terminal Src kinase [Csk] contains a unique disulfide bond that is not present in other known SH2 domains.	Disulfides	68-77	C-terminal Src kinase	Homo sapiens	22-43
17137590-1	2007	The SH2 domain of the C-terminal Src kinase [Csk] contains a unique disulfide bond that is not present in other known SH2 domains.	Disulfides	68-77	C-terminal Src kinase	Homo sapiens	45-48
17137590-3	2007	The kinase activity of full-length Csk decreases by an order of magnitude upon formation of the disulfide bond in the distal SH2 domain.	Disulfides	96-105	C-terminal Src kinase	Homo sapiens	35-38
17137590-8	2007	Overall, the data indicate that reversible cross-linking of two cysteine residues in the SH2 domain greatly impacts catalytic function and interdomain communication in Csk.	Cysteine	64-72	C-terminal Src kinase	Homo sapiens	168-171
17149882-3	2006	Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase.	hydroxamates	52-64	C-terminal Src kinase	Homo sapiens	102-123
17149882-3	2006	Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase.	hydroxamates	52-64	C-terminal Src kinase	Homo sapiens	125-128
17149882-3	2006	Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase.	Metals	68-73	C-terminal Src kinase	Homo sapiens	102-123
17149882-3	2006	Taking advantage of this high affinity, we examined hydroxamates as metal-mediated inhibitors against C-terminal Src kinase (Csk), a protein tyrosine kinase.	Metals	68-73	C-terminal Src kinase	Homo sapiens	125-128
17149882-4	2006	Of a small group of amino acid hydroxamates, tyrosine and phenylalanine hydroxamates inhibited Csk activity only in the presence of Co(2+).	amino acid hydroxamates	20-43	C-terminal Src kinase	Homo sapiens	95-98
17149882-4	2006	Of a small group of amino acid hydroxamates, tyrosine and phenylalanine hydroxamates inhibited Csk activity only in the presence of Co(2+).	Tyrosine	45-53	C-terminal Src kinase	Homo sapiens	95-98
17149882-4	2006	Of a small group of amino acid hydroxamates, tyrosine and phenylalanine hydroxamates inhibited Csk activity only in the presence of Co(2+).	phenylalanine hydroxamates	58-84	C-terminal Src kinase	Homo sapiens	95-98
17149882-4	2006	Of a small group of amino acid hydroxamates, tyrosine and phenylalanine hydroxamates inhibited Csk activity only in the presence of Co(2+).	Cobalt(2+)	132-138	C-terminal Src kinase	Homo sapiens	95-98
17149882-5	2006	Four classes of phenylalanine and tyrosine hydroxamate derivatives were synthesized and evaluated as metal-mediated inhibitors of Csk, leading to improved inhibition and a better understanding of the structure-activity relationships.	Phenylalanine	16-29	C-terminal Src kinase	Homo sapiens	130-133
17149882-5	2006	Four classes of phenylalanine and tyrosine hydroxamate derivatives were synthesized and evaluated as metal-mediated inhibitors of Csk, leading to improved inhibition and a better understanding of the structure-activity relationships.	tyrosine hydroxamate	34-54	C-terminal Src kinase	Homo sapiens	130-133
17149882-5	2006	Four classes of phenylalanine and tyrosine hydroxamate derivatives were synthesized and evaluated as metal-mediated inhibitors of Csk, leading to improved inhibition and a better understanding of the structure-activity relationships.	Metals	101-106	C-terminal Src kinase	Homo sapiens	130-133
17172405-6	2006	A c-Src inhibitor, AZD0530, was used to analyze the biological effects of pharmacologically inhibiting c-Src kinase activity.	saracatinib	19-26	C-terminal Src kinase	Homo sapiens	103-115
17223712-0	2007	Rapid activation of c-Src kinase by dioxin is mediated by the Cdc37-HSP90 complex as part of Ah receptor signaling in MCF10A cells.	Dioxins	36-42	C-terminal Src kinase	Homo sapiens	20-32
17223712-1	2007	We investigated the mechanism by which activation of the Ah receptor by dioxin (TCDD) was accompanied by rapid activation of c-Src kinase activity.	Dioxins	72-78	C-terminal Src kinase	Homo sapiens	125-137
17223712-1	2007	We investigated the mechanism by which activation of the Ah receptor by dioxin (TCDD) was accompanied by rapid activation of c-Src kinase activity.	Polychlorinated Dibenzodioxins	80-84	C-terminal Src kinase	Homo sapiens	125-137
17018524-1	2006	Src family tyrosine kinases are down-regulated through phosphorylation of a single C-terminal tyrosine by the nonreceptor tyrosine kinase Csk.	Tyrosine	11-19	C-terminal Src kinase	Homo sapiens	138-141
16959780-2	2006	To prevent constitutive SFK activation, the catalytic activity of SFKs in normal mammalian cells is suppressed mainly by two inhibitors called C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK), which inactivate SFKs by phosphorylating a consensus tyrosine near the C terminus of SFKs (Y(T)).	Tyrosine	257-265	C-terminal Src kinase	Homo sapiens	143-164
16959780-2	2006	To prevent constitutive SFK activation, the catalytic activity of SFKs in normal mammalian cells is suppressed mainly by two inhibitors called C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK), which inactivate SFKs by phosphorylating a consensus tyrosine near the C terminus of SFKs (Y(T)).	Tyrosine	257-265	C-terminal Src kinase	Homo sapiens	166-169
16289966-5	2006	First, CD21 activation triggered Cbl tyrosine phosphorylation, which required c-Src kinase but not PI 3-kinase or Syk kinase activities.	Tyrosine	37-45	C-terminal Src kinase	Homo sapiens	78-90
16720365-0	2006	Negative regulation of T-cell receptor activation by the cAMP-PKA-Csk signalling pathway in T-cell lipid rafts.	Cyclic AMP	57-61	C-terminal Src kinase	Homo sapiens	66-69
16782058-5	2006	Staurosporine binds to the ATP-binding site of Fyn in a similar manner as in the Lck- and Csk-complexes.	Staurosporine	0-13	C-terminal Src kinase	Homo sapiens	90-93
16856837-1	2006	cAMP inhibits Src-family kinase signalling by PKA (protein kinase A)-mediated phosphorylation and activation of Csk (C-terminal Src kinase).	Cyclic AMP	0-4	C-terminal Src kinase	Homo sapiens	112-115
16856837-1	2006	cAMP inhibits Src-family kinase signalling by PKA (protein kinase A)-mediated phosphorylation and activation of Csk (C-terminal Src kinase).	Cyclic AMP	0-4	C-terminal Src kinase	Homo sapiens	117-138
16856837-3	2006	PKA type I is targeted to the TCR-CD3 complex during T-cell activation via an AKAP (A-kinase-anchoring protein) that serves as a scaffold for the cAMP-PKA/Csk pathway in lipid rafts of the plasma membrane during T-cell activation.	Cyclic AMP	146-150	C-terminal Src kinase	Homo sapiens	155-158
16539378-2	2006	Synthetic peptides containing tyrosine analogues displaying different side chain orientations were analyzed by NMR techniques and tested as potential substrates of the nonreceptor tyrosine kinases Syk, Csk, Lyn, and Fyn.	Peptides	10-18	C-terminal Src kinase	Homo sapiens	202-205
16814101-3	2006	This H2O2-induced kinase activation was significantly attenuated by a Src kinase inhibitor PP2, or by transient transfection of carboxyl-terminal Src kinase (CSK) that maintained Src in the dormant form.	Hydrogen Peroxide	5-9	C-terminal Src kinase	Homo sapiens	158-161
16765913-6	2006	Characterization of the Src mutants confirmed that inactivation of Src by Csk through tail tyrosine phosphorylation required the Src SH3 domain.	Tyrosine	91-99	C-terminal Src kinase	Homo sapiens	74-77
16439366-4	2006	C-terminal Src kinase (Csk) specifically phosphorylates Src family kinases on a C-terminal Tyr residue, which down-regulates their activities.	Tyrosine	91-94	C-terminal Src kinase	Homo sapiens	0-21
16439366-4	2006	C-terminal Src kinase (Csk) specifically phosphorylates Src family kinases on a C-terminal Tyr residue, which down-regulates their activities.	Tyrosine	91-94	C-terminal Src kinase	Homo sapiens	23-26