Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-114277	Ser17	DASQRRRsLEPAENV	Homo sapiens
pmid	sentence
11804588	Pka activated src both in vitro and in vivo by phosphorylating src on serine 17

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247988	Ser17	DASQRRRsLEPAENV	Homo sapiens
pmid	sentence
11804588	PKA activated Src both in vitro and in vivo by phosphorylating Src on serine 17 within its amino terminus

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277543	Ser43	QTPSKPAsADGHRGP	Homo sapiens	HEK-293T Cell
pmid	sentence
33388549	Concurrently, ROCK1 was able to phosphorylate GSK-3β at Ser9, which phosphorylated Src at Ser51 and Ser492 residues, leading to Src inactivation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277544	Ser493	CPPECPEsLHDLMCQ	Homo sapiens	HEK-293T Cell
pmid	sentence
33388549	Concurrently, ROCK1 was able to phosphorylate GSK-3β at Ser9, which phosphorylated Src at Ser51 and Ser492 residues, leading to Src inactivation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277225	Ser70	LFGGFNSsDTVTSPQ	Homo sapiens	HEK-293 Cell
pmid	sentence
27169346	PI3Kγ mediated phosphorylation of Src enhances Src activity protein kinase activity of PI3K phosphorylates serine residue 70 on Src to enhance its activity and induce EGFR transactivation following βAR stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-71950	Ser75	NSSDTVTsPQRAGPL	Homo sapiens	Neuron
pmid	sentence
10544291	These results present compelling evidence that cdk5/p35 kinase is responsible for the novel phosphorylation of c-src at ser75 in neuronal cells, raising the intriguing possibility that c-src acts as an effector of cdk5/p35 kinase during neuronal development.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-202800	Thr216	AGERRKGtDVNVFNT	Homo sapiens
pmid	sentence
24103589	Location of sites in human lipocortin i that are phosphorylated by protein tyrosine kinases and protein kinases a and cthe primary site of phosphorylation by protein kinase c was also near the amino terminus at ser-27. The major site of phosphorylation by adenosine cyclic 3',5'-phosphate dependent protein kinase was on the carboxy-terminal half of the molecule at thr-216

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276398	Tyr10	AAVACVDyFAADVLM	Homo sapiens	Ishikawa Cell
pmid	sentence
22203677	We further confirmed that the Tyr-10 residue of KLF16 is phosphorylated in uterine cells (Fig. 7c). Additional experiments using both pharmacological and dominant negative inhibitors of Src further supported a role for this tyrosine kinase in modulating the activity of KLF16 (Fig. 7, d and f).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247424	Tyr100	QMLQSDPySVPARDY	Chlorocebus aethiops
pmid	sentence
15229287	The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreadingWhen phosphorylated, the vinculin tail exhibited significantly less binding to the vinculin head domain than the unphosphorylated tail.

Identifier	Residue	Sequence	Organism
SIGNOR-247428	Tyr1133	WVRKTPWyQ	Chlorocebus aethiops
pmid	sentence
15229287	The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreadingWhen phosphorylated, the vinculin tail exhibited significantly less binding to the vinculin head domain than the unphosphorylated tail.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274107	Tyr1006	PATPLLDyALEVEKI	Homo sapiens	HEK-293 Cell
pmid	sentence
32420483	We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274108	Tyr227	KVDATADyICKVKWG	Homo sapiens	HEK-293 Cell
pmid	sentence
32420483	We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274109	Tyr252	EAYPEEAyIADLDAK	Homo sapiens	HEK-293 Cell
pmid	sentence
32420483	We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274106	Tyr682	SRTTDGVyEGVAIGG	Homo sapiens	HEK-293 Cell
pmid	sentence
32420483	We demonstrate the binding of PIP2 to the CoA-binding domain of ACLY and identify the six tyrosine residues of ACLY that are phosphorylated by Lyn. Three of them (Y682, Y252, Y227) can be also phosphorylated by Src and they are located in catalytic, citrate binding and ATP binding domains, respectively. PI3K and Lyn inhibitors reduce the ACLY enzyme activity, ACLY-mediated Acetyl-CoA synthesis, phospholipid synthesis, histone acetylation and cell growth. Thus, PIP2/PIP3 binding and Src tyrosine kinases-mediated stimulation of ACLY links oncogenic pathways to Acetyl-CoA-dependent pro-growth and survival metabolic pathways in cancer cells.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-44239	Tyr1016	DVVDADEyLIPQQGF	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site

Identifier	Residue	Sequence	Organism
SIGNOR-44243	Tyr1110	GSVQNPVyHNQPLNP	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site.

Identifier	Residue	Sequence	Organism
SIGNOR-44251	Tyr1172	ISLDNPDyQQDFFPK	Homo sapiens
pmid	sentence
8845374	Revealed that peptides derived from egfr residues y992, y1086, y1101, and y1148 bound directly to the sh2 domain of c-src (figure 8c). These experiments demonstrate that a specific subset of egfr receptor c-src phosphorylation sites are also ligands for the sh2 domain of c-src.Cellular src functions as a co-transducer of transmembrane signals emanating from a variety of growth factor receptors, including egfr

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-235921	Tyr869	LGAEEKEyHAEGGKV	Homo sapiens	Fibroblast
pmid	sentence
11983694	In summary, this study describes a novel mechanism for metal-induced egfr transactivation, which is likely to be mediated by src through the phosphorylation site of tyr-845 on egfr. emanating from a variety of growth factor receptors, including egfry845 (e-e-k-e-y845-h-a-e)

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263104	Tyr104	RSPSTGLyDNLEKYH	Homo sapiens	HEK-293 Cell
pmid	sentence
24996174	In this study, we investigated the potential regulation of SIRT2 function by c-Src. We found that the protein levels of SIRT2 were decreased by c-Src, and subsequently rescued by the addition of a Src specific inhibitor, SU6656, or by siRNA-mediated knockdown of c-Src. The c-Src interacts with and phosphorylates SIRT2 at Tyr104.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165035	Tyr1063	FGLARDIyKDPDYVR	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Identifier	Residue	Sequence	Organism
SIGNOR-165039	Tyr1333	ARGGQVFyNSEYGEL	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Identifier	Residue	Sequence	Organism
SIGNOR-165043	Tyr1337	QVFYNSEyGELSEPS	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Identifier	Residue	Sequence	Organism
SIGNOR-165047	Tyr830	PLEEQCEyLSYDASQ	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Identifier	Residue	Sequence	Organism
SIGNOR-165051	Tyr833	EQCEYLSyDASQWEF	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Identifier	Residue	Sequence	Organism
SIGNOR-165055	Tyr853	HLGRVLGyGAFGKVV	Homo sapiens
pmid	sentence
20431062	Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk.

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276393	Tyr108	GKLHYPRyECISAYD	Homo sapiens	HEK-293 Cell
pmid	sentence
22198508	These results indicate that Y108 (for Src-family kinases) and Y136 (for EGFR kinase) are involved in the tyrosine phosphorylation of hKv4.3 channels.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-168545	Tyr110	RGHAAIDyTQLGLRF	Homo sapiens
pmid	sentence
20943948	Here, we show that the interaction of noxa1 and tks proteins is dependent on src activity. Interestingly, the abolishment of src-mediated phosphorylation of tyr110 on noxa1 and of tyr508 on tks4 blocks their binding and decreases nox1-dependent ros generation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247163	Tyr1105	CSEVERTyLKTKSSS	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247167	Tyr1267	PATGEQVyQQDWAQN	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247171	Tyr1387	GRCPSDPyKHSLPSQ	in vitro
pmid	sentence
10195142	To gain further insight into the roles of Src and Fyn in the phosphorylation and regulation of the NMDA receptor, we have characterized the tyrosine phosphorylation of NR2A and NR2B by exogenous Src and FynIn the case of NR2A, three potential tyrosine phosphorylation sites have been proposed: Tyr1105, Tyr1267 and Tyr1387 (Zheng et al. 1998; Bi et al. 2000), all of which are similarly located in the C-terminal, cytoplasmic domain.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-61670	Tyr1105	RNEEENIySVPHDST	Homo sapiens
pmid	sentence
9819392	Phosphorylation of y1105, but not the minor site, was modulated in vivo to a greater extent by overexpression of c-src than by the egf receptor and was efficiently catalyzed by c-src in vitro. Mutation of y1105 from tyr to phe resulted in complete loss of p-tyr-dependent complex formation, indicating that p-y1105 was the sole p-tyr residue mediating binding to p120

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276170	Tyr1109	KGYSDEIyVVPDDSQ	in vitro
pmid	sentence
9819392	Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation. Phosphorylation of Y1105, but not the minor site, was modulated in vivo to a greater extent by overexpression of c-Src than by the EGF receptor and was efficiently catalyzed by c-Src in vitro, indicating that Y1105 is a selective and preferential target of c-Src both in vitro and in vivo.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276897	Tyr1113	PSPVWMNySYSSLCL	Homo sapiens	HEK-293T Cell
pmid	sentence
25805816	Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276895	Tyr1115	PVWMNYSySSLCLSS	Homo sapiens	HEK-293T Cell
pmid	sentence
25805816	Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276896	Tyr1164	KKEIEDLySRLGKQP	Homo sapiens	HEK-293T Cell
pmid	sentence
25805816	Using Western blot and mass spectrometry, we now identify three sites in WNK4 that are phosphorylated by c-Src: Tyr(1092), Tyr(1094), and Tyr(1143), and show that both c-Src and protein tyrosine phosphatase type 1D (PTP-1D) coimmunoprecipitate with WNK4.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277550	Tyr112	NSYVAGQyDDAASYQ	in vitro
pmid	sentence
33686238	Here, we show that tyrosine kinase c-Src interacts with and phosphorylates G6PD at Tyr 112. This phosphorylation enhances catalytic activity of G6PD by dramatically decreasing its Km value and increasing its Kcat value for substrate glucose-6-phosphate.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-246480	Tyr112	PGQIVETyTEEDPEG	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246484	Tyr228	YPGGSDNyGSLSRVT	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246488	Tyr257	APSRQDVyGPQPQVR	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246492	Tyr280	HRFHPEPyGLEDDQR	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246496	Tyr291	DDQRSMGyDDLDYGM	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246500	Tyr296	MGYDDLDyGMMSDYG	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246504	Tyr302	DYGMMSDyGTARRTG	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Identifier	Residue	Sequence	Organism
SIGNOR-246508	Tyr96	QDHSHLLySTIPRMQ	in vitro
pmid	sentence
11382764	Identification of Src phosphorylation sites in the catenin p120ctn.Using selected tyrosine to phenylalanine p120 mutants as dominant negative reagents, it may now be possible to selectively block events postulated to be dependent on p120 tyrosine phosphorylation.combinations of Tyr _ Phe mutations at residues 96, 112, 228, 257, 280, 291, 296, and 302

Publications:

8

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-44247	Tyr1125	APSRDPHyQDPHSTA	Homo sapiens
pmid	sentence
8845374	The c-terminal autophosphorylation domain of egfr was extensively phosphorylated by c-src./These studies revealed that y1086 was phosphorylated to a significantly higher extent by c-src than by egfr. Additionally, y1101 was identified as a unique c-src phosphorylation site

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-247134	Tyr114	FHRNDSIyEELQKHD	in vitro
pmid	sentence
15835917	The human tumor suppressor Fhit is a homodimeric histidine triad (HIT) protein of 147 amino acids which has Ap3A hydrolase activity. We have recently discovered that Fhit is phosphorylated in vivo and is phosphorylated in vitro by Src kinaseMALDI-TOF and HPLC-ESI tandem mass spectrometry of intact Fhit and proteolytic peptides of Fhit demonstrated that Fhit is phosphorylated on Y114 on either one or both subunitsThe decreases in the values of Km and kcat for the phosphorylated forms in comparison to those of unphosphorylated Fhit favor the formation and lifetime of the Fhit_Ap3A complex, which may enhance the tumor suppressor activity of Fhit.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263198	Tyr1149	CTQPRPNyASNFSVI	in vitro
pmid	sentence
28135906	GAK is phosphorylated by c-Src and translocated from the centrosome to chromatin at the end of telophase. Cyclin G-associated kinase (GAK) harbors a consensus phosphorylation motif (Y412) for c-Src; however, its physiological significance remains elusive. Here, we show that GAK is phosphorylated by c-Src not only at Y412 but also at Y1149.

Identifier	Residue	Sequence	Organism
SIGNOR-263197	Tyr412	KGDLDISyITSRIAV	in vitro
pmid	sentence
28135906	GAK is phosphorylated by c-Src and translocated from the centrosome to chromatin at the end of telophase. Cyclin G-associated kinase (GAK) harbors a consensus phosphorylation motif (Y412) for c-Src; however, its physiological significance remains elusive. Here, we show that GAK is phosphorylated by c-Src not only at Y412 but also at Y1149.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-246381	Tyr115	QPQPDSVyLVPTPSK	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-197927	Tyr128	SKAQQGLyQVPGPSP	Homo sapiens
pmid	sentence
22710723	Furthermore, we demonstrate that src phosphorylates p130cas y128. We engineered crc cells homozygous for a p130cas y128f knock-in mutant and found that these cells exhibit significantly reduced migration and colony formation

Identifier	Residue	Sequence	Organism
SIGNOR-246385	Tyr165	PSPATDLyQVPPGPG	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246389	Tyr179	GGPAQDIyQVPPSAG	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246393	Tyr192	AGMGHDIyQVPPSMD	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246397	Tyr234	AQPEQDEyDIPRHLL	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-100363	Tyr249	APGPQDIyDVPPVRG	Homo sapiens
pmid	sentence
12972425	We tested synthetic peptides modeled on cas phosphorylation sites, and found that the sequence containing tyrosine 253 was phosphorylated by src most efficiently. Using cells derived from cas-deficient mice, we confirmed that cas greatly enhanced the ability of src to transform cells.

Identifier	Residue	Sequence	Organism
SIGNOR-246401	Tyr267	SQYGQEVyDTPPMAV	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246405	Tyr287	RDPLLEVyDVPPSVE	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246409	Tyr362	SPPAEDVyDVPPPAP	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246413	Tyr387	RPGPGTLyDVPRERV	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-246417	Tyr653	QDSPDGQyENSEGGW	Mus musculus
pmid	sentence
12972425	Cas is a member of the focal adhesion complex. Phosphorylation of Cas by Src is an important event leading to cell transformation. Using mass spectrometry, we have mapped 11 sites in Cas that are phosphorylated by Src. These sites are all located between residues 132 and 414 of CasBased on these data, 11 tyrosine residues (132, 169, 183, 196, 238, 253, 271, 291, 301, 391, and 414) were phosphorylated by Src\|the biological activity of Cas depends on its phosphorylation by Src (16–18). After phosphorylation, Cas associates with a number of proteins, including Crk, Src, phosphatidylinositol 3-kinase, Nck, and phospholipase Cgamma, via SH2 binding motifs

Identifier	Residue	Sequence	Organism
SIGNOR-111056	Tyr664	EGGWMEDyDYVHLQG	Homo sapiens
pmid	sentence
11604500	The loss of activity in the cas-f668/f670 mutant is consistent with the notion that src, once initially bound by its sh3 domain, phosphorylates the tyr668/670 site to further stabilize its interaction by sh2 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-111060	Tyr666	GWMEDYDyVHLQGKE	Homo sapiens
pmid	sentence
11604500	The loss of activity in the cas-f668/f670 mutant is consistent with the notion that src, once initially bound by its sh3 domain, phosphorylates the tyr668/670 site to further stabilize its interaction by sh2 binding.

Publications:

14

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-45122	Tyr1161	FGMTRDIyETDYYRK	Homo sapiens
pmid	sentence
8940173	Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor

Identifier	Residue	Sequence	Organism
SIGNOR-246264	Tyr1165	RDIYETDyYRKGGKG	in vitro
pmid	sentence
7493944	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Identifier	Residue	Sequence	Organism
SIGNOR-45126	Tyr1165	RDIYETDyYRKGGKG	Homo sapiens
pmid	sentence
8940173	Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor

Identifier	Residue	Sequence	Organism
SIGNOR-45130	Tyr1166	DIYETDYyRKGGKGL	Homo sapiens
pmid	sentence
8940173	Src phosphorylates the insulin-like growth factor type i receptor on the autophosphorylation sites. Requirement for transformation by srcsrc kinase can substitute for the receptor kinase in phosphorylating and activating the igf-i receptor

Publications:

4

Organism:

Homo Sapiens, In Vitro

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-246272	Tyr1161	FGMTRDIyETDYYRK	in vitro
pmid	sentence
7493944	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Identifier	Residue	Sequence	Organism
SIGNOR-246268	Tyr1166	DIYETDYyRKGGKGL	in vitro
pmid	sentence
7493944	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Identifier	Residue	Sequence	Organism
SIGNOR-246276	Tyr1346	SFDERQPyAHMNGGR	in vitro
pmid	sentence
7493944	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247193	Tyr973	RLGNGVLyASVNPEY	in vitro
pmid	sentence
8940173	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Identifier	Residue	Sequence	Organism
SIGNOR-247197	Tyr980	YASVNPEyFSAADVY	in vitro
pmid	sentence
8940173	The insulin-like growth factor type I (IGF-I) receptor can become tyrosine phosphorylated and enzymatically activated either in response to ligand or because of the activity of the Src tyrosine kinaseWe mapped the sites of IGF-I receptor autophosphorylation to peptides representing three different receptor domains: tyrosines 943 and 950 in the juxtamembrane region; tyrosines 1131, 1135, and 1136 within the kinase domain; and tyrosine 1316 in the carboxyl-terminal domain.

Publications:

5

Organism:

In Vitro

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187843	Tyr1173	QDTSKFWyKADISRE	Homo sapiens	Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell
pmid	sentence
19732724	Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187847	Tyr1206	SHSFRGAyGLAMKVA	Homo sapiens	Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell
pmid	sentence
19732724	Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187851	Tyr1256	KGCSNEPyFGSLTAL	Homo sapiens	Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell
pmid	sentence
19732724	Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding. tensin-3 is a src substrate

Identifier	Residue	Organism	Cell Line
SIGNOR-187854		Homo sapiens	Breast Cancer Cell, Lung Cancer Cell, Melanoma Cell
pmid	sentence
19732724	Although sh2 domains have not been reported previously to be phosphorylated, the tensin-3 sh2 domain is a physiologic substrate for src. Tyrosines in the sh2 domain contribute to the biological activity of tensin-3, and phosphorylation of these tyrosines can regulate ligand binding.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-86718	Tyr1176	AVQQQEVyGMMPRDE	Homo sapiens
pmid	sentence
11971983	Using mutagenesis on recombinant peptides, we identified the residue y1176 located in the calpain cleavage site of alpha ii-spectrin, near the sh3 domain, as an in vitro substrate for src kinase and lmw-ptp a. phosphorylation of this residue decreases spectrin sensitivity to calpain in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275585	Tyr118	EDLADKPyTFEDYDV	Homo sapiens	HEK-293 Cell
pmid	sentence
25948553	We found that frataxin can be phosphorylated by Src. Phosphorylation occurs primarily on Y118 and promotes frataxin ubiquitination, a signal for degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-85938	Tyr1229	SSTDRSPyEKVSAGN	Homo sapiens
pmid	sentence
11152665	The c-src tyrosine kinase regulates signaling of the human df3/muc1 carcinoma-associated antigen with gsk3 beta and betBeta-catenin c-src phosphorylates the muc1 cytoplasmic domain at a yekv motif c-src-mediated phosphorylation of muc1 increases binding of muc1 and betBeta-catenin

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142724	Tyr125	PIPLQETyDVCEQPP	Homo sapiens
pmid	sentence
16317717	The wave/scar proteins regulate actin polymerisation at the leading edge of motile cells via activation of the arp2/3 complex in response to extracellular cues.Src-dependent phosphorylation of scar1 promotes its association with the arp2/3 complex

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276668	Tyr126	AKSVTCTySPALNKM	Homo sapiens	HEK-293T Cell
pmid	sentence
25071020	We recently found that ISGylation of the p53 tumor suppressor is an important novel mechanism to control its stability. Here we identified that Isg15-dependent regulation of p53 can be enhanced by different oncogenes. We further show that the Src-mediated phosphorylation of p53 on Tyr126 and Tyr220 has a positive effect on p53 ISGylation by enhancing Herc5 binding.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276669	Tyr220	RHSVVVPyEPPEVGS	Homo sapiens	HEK-293T Cell
pmid	sentence
25071020	We recently found that ISGylation of the p53 tumor suppressor is an important novel mechanism to control its stability. Here we identified that Isg15-dependent regulation of p53 can be enhanced by different oncogenes. We further show that the Src-mediated phosphorylation of p53 on Tyr126 and Tyr220 has a positive effect on p53 ISGylation by enhancing Herc5 binding.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-187201	Tyr128	YWGIDEIyLESCCQA	Homo sapiens	Neuron
pmid	sentence
19622611	In the present study we show that an n-terminal tyrosine of kv2.1 (y124), which is a known target of src kinase, is critical for the apoptotic current surge..Kv2.1-mediated k+ currents are also enhanced during non-injurious conditions through direct phosphorylation of intracellular n-terminal residue tyrosine 124 (y124) by src kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266307	Tyr13	AVLADVSyLMAMEKS	Homo sapiens	HEK-293 Cell
pmid	sentence
16725308	Here, we demonstrate that c-Src kinase activity increases the interaction between GRK2 and Galphaq. Tyrosine phosphorylation of GRK2 appears to be critically involved in the modulation of this interaction since the stimulatory effect of c-Src is not observed with a GRK2 mutant with impaired tyrosine phosphorylation (GRK2 Y13,86,92F), whereas a mutant that mimics GRK2 tyrosine phosphorylation in these residues displays an increased interaction with Galphaq.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266306	Tyr86	ARPLVEFyEEIKKYE	Homo sapiens	HEK-293 Cell
pmid	sentence
16725308	Here, we demonstrate that c-Src kinase activity increases the interaction between GRK2 and Galphaq. Tyrosine phosphorylation of GRK2 appears to be critically involved in the modulation of this interaction since the stimulatory effect of c-Src is not observed with a GRK2 mutant with impaired tyrosine phosphorylation (GRK2 Y13,86,92F), whereas a mutant that mimics GRK2 tyrosine phosphorylation in these residues displays an increased interaction with Galphaq.

Identifier	Residue	Sequence
SIGNOR-266293	Tyr92	FYEEIKKyEKLETEE
pmid	sentence
16725308	Here, we demonstrate that c-Src kinase activity increases the interaction between GRK2 and Galphaq. Tyrosine phosphorylation of GRK2 appears to be critically involved in the modulation of this interaction since the stimulatory effect of c-Src is not observed with a GRK2 mutant with impaired tyrosine phosphorylation (GRK2 Y13,86,92F), whereas a mutant that mimics GRK2 tyrosine phosphorylation in these residues displays an increased interaction with Galphaq.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266305	Tyr92	FYEEIKKyEKLETEE	Homo sapiens	HEK-293 Cell
pmid	sentence
16725308	Here, we demonstrate that c-Src kinase activity increases the interaction between GRK2 and Galphaq. Tyrosine phosphorylation of GRK2 appears to be critically involved in the modulation of this interaction since the stimulatory effect of c-Src is not observed with a GRK2 mutant with impaired tyrosine phosphorylation (GRK2 Y13,86,92F), whereas a mutant that mimics GRK2 tyrosine phosphorylation in these residues displays an increased interaction with Galphaq.

Publications:

4

Organism:

Homo Sapiens,

Identifier	Residue	Sequence	Organism
SIGNOR-92460	Tyr130	VLDVLKFyDSNTVKQ	Homo sapiens
pmid	sentence
12215529	Pak2 became tyrosine phosphorylated in its n-terminal regulatory domain, where y130 was identified as the major phosphoacceptor site. Tyrosine phosphorylation-mediated superactivation of pak2 could be induced by overexpression of different src kinases or by inhibiting cellular tyrosine phosphatases with pervanadate and could be blocked by the src kinase inhibitor pp1 or by mutating the y130 residue.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276373	Tyr1311	DSKVDLIyQNTTAMT	Homo sapiens	HEK-293 Cell
pmid	sentence
22898603	We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276375	Tyr1320	NTTAMTIyENLAPVT	Homo sapiens	HEK-293 Cell
pmid	sentence
22898603	We demonstrate here that DEP-1 is phosphorylated in a Src- and Fyn-dependent manner on Y1311 and Y1320, which bind the Src SH2 domain. This allows DEP-1-catalyzed dephosphorylation of Src inhibitory Y529 and favors the VEGF-induced phosphorylation of Src substrates VE-cadherin and Cortactin.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188531	Tyr1325	RLLEGNFyGSLFSVP	Homo sapiens
pmid	sentence
19834457	The nr2a subunit of the nmda receptor is tyrosine-phosphorylated, with tyr 1325 as its one of the major phosphorylation sitewe also show that the tyr 1325 phosphorylation site is required for src-induced potentiation of the nmda receptor channel in the striatum.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276189	Tyr136	GIAVPDVySACKRFE	in vitro
pmid	sentence
34838714	We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of the Src family (Src, Yes1, FGR, and the related Abl1), and of the FAK, EPHA, FGFR, and VEGFR families (Figure 2B), suggesting phosphorylation of Glo1 on Y136 by multiple different kinases. In vitro kinase assays revealed that all the members of the Src family, as well as Epha5 and VEGFR3, can efficiently phosphorylate recombinant Glo1 on Y136 (Figure 2C–D).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247119	Tyr139	KVEEPSIyESVRVHT	Homo sapiens	B-lymphocyte
pmid	sentence
10880360	Src family kinases mediate receptor-stimulated, phosphoinositide 3-kinase-dependent, tyrosine phosphorylation of dual adaptor for phosphotyrosine and 3-phosphoinositides-1 in endothelial and B cell linesyrosine phosphorylation of DAPP-1 appears important for appropriate intracellular targeting and creates a potential binding site for Src homology 2 domain-containing proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118007	Tyr14	VDSEGHLyTVPIREQ	Homo sapiens
pmid	sentence
12921535	Caveolin-1 is phosphorylated on tyr(14) in response to both oxidative and hyperosmotic stress. In the present paper, we show that this phosphorylation requires activation of the src family kinase fyn

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276402	Tyr14	GAIMDEDyYGSAAEW	Chlorocebus aethiops
pmid	sentence
22238675	Here we show that c-Src interacts with TH1 by GST-pull down assay, coimmunoprecipitation and confocal microscopy assay. The interaction leads to phosphorylation of TH1 at Tyr-6 in vivo and in vitro. Phosphorylation of TH1 decreases its association with A-Raf and PAK1.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276386	Tyr142	MELALGQyHRNGCIS	Rattus norvegicus	Blood Platelet
pmid	sentence
21992875	We found that 1) SERT exists in a tyrosine-phosphorylated form, 2) inhibition of tyrosine kinase(s) reduces SERT expression levels by facilitating SERT protein degradation, 3) Src-kinase activity up-regulates SERT protein expression with a concomitant increase in 5-HT uptake and tyrosine phosphorylation, and 4) mutation of Tyr47 or Tyr142 abolishes src-induced increases in transport function and phosphorylation of SERT.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276385	Tyr47	SGQISNGySAVPSPG	Rattus norvegicus	Blood Platelet
pmid	sentence
21992875	We found that 1) SERT exists in a tyrosine-phosphorylated form, 2) inhibition of tyrosine kinase(s) reduces SERT expression levels by facilitating SERT protein degradation, 3) Src-kinase activity up-regulates SERT protein expression with a concomitant increase in 5-HT uptake and tyrosine phosphorylation, and 4) mutation of Tyr47 or Tyr142 abolishes src-induced increases in transport function and phosphorylation of SERT.

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-167529	Tyr142	ALETSRLyEDSGYSS	Homo sapiens
pmid	sentence
20717963	We found that emi1 stability was regulated by phosphorylation and mutation of tyrosine 142 reduced the stability. Our data suggested bcr-abl-induced emi1 phosphorylation might be mediated by src kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133227	Tyr146	KEVHKSGyLSSERLI	Homo sapiens
pmid	sentence
15647376	N this study we have demonstrated that ezrin y145 is a direct target for phosphorylation by the tyrosine kinase src evidence from this study suggests that a positive feedback loop exists whereby src-mediated ezrin y145 phosphorylation sustains src activity._

Identifier	Residue	Sequence	Organism
SIGNOR-132907	Tyr478	PPPPPPVyEPVSYHV	Homo sapiens
pmid	sentence
15623525	Src phosphorylates ezrin at tyrosine 477 and induces a phosphospecific association between ezrin and a kelch-repeat protein family member

Identifier	Residue	Sequence	Organism
SIGNOR-196443	Tyr478	PPPPPPVyEPVSYHV	Homo sapiens
pmid	sentence
22397367	Ezrin, a member of the erm family of proteins, is frequently over-expressed in human breast cancers, and is required for motility and invasion of epithelial cells. In particular, ezrin phosphorylation on y477 by src is specific to ezrin within the erm family, and is required for hgf-induced scattering of epithelial cells.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247180	Tyr1474	GSSNGHVyEKLSSIE	in vitro
pmid	sentence
11483655	We have investigated the tyrosine phosphorylation of NMDA receptor subunits NR2A and NR2B by exogenous Src Phosphorylation-site specific antibodies identified NR2B Tyr1472 as a phosphorylation site for intrinsic PSD tyrosine kinases

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-65714	Tyr1477	LFITEEDyQALRTSI	Homo sapiens
pmid	sentence
10089883	Egf-mediated clathrin phosphorylation is followed by clathrin redistribution to the cell periphery and is the product of downstream activation of src kinase by egf receptor (egfr) signaling

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273804	Tyr149	MGISVVSyTLKDIHD	Homo sapiens	T-98G Cell
pmid	sentence
24983503	Taken together, we conclude that mitochondrial c-Src phosphorylates flotillin-1 at Tyr56 and Tyr149, and that these phosphorylations are required for its interaction with CxII and the prevention of ROS production.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273805	Tyr56	NVKSEKVyTRHGVPI	Homo sapiens	T-98G Cell
pmid	sentence
24983503	Taken together, we conclude that mitochondrial c-Src phosphorylates flotillin-1 at Tyr56 and Tyr149, and that these phosphorylations are required for its interaction with CxII and the prevention of ROS production.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188974	Tyr151	IEFVNQYyGSFKEAK	Homo sapiens
pmid	sentence
19875457	We identify human inos residue tyr(1055) as a target for src-mediated phosphorylation. src kinase-mediated phosphorylation stabilizes inducible nitric-oxide synthase in normal cells and cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277533	Tyr1510	LVKLQQTyAALNSKA	Homo sapiens	MDA-MB-231 Cell
pmid	sentence
33087447	IQGAP1 was phosphorylated exclusively on Tyr-1510 under conditions with enhanced MET or c-Src signaling, including in human lung cancer cell lines. This phosphorylation was significantly reduced by chemical inhibitors of MET or c-Src or by siRNA-mediated knockdown of MET.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184908	Tyr153	YGPRPEEyEFLTPVE	Homo sapiens
pmid	sentence
19321744	Studies confirmed that activated src kinase binds and phosphorylates rhogdi2 in vitro and vivo. Mutagenesis revealed that tyr-153 and, to a lesser degree, tyr-24 were the primary src phosphorylation sites. Phosphorylation decreased the amount of rac1 in rhogdi2 complexes and increased rhogdi2 association with cell membranes.

Identifier	Residue	Sequence	Organism
SIGNOR-184912	Tyr24	ELDSKLNyKPPPQKS	Homo sapiens
pmid	sentence
19321744	Studies confirmed that activated src kinase binds and phosphorylates rhogdi2 in vitro and vivo. Mutagenesis revealed that tyr-153 and, to a lesser degree, tyr-24 were the primary src phosphorylation sites. Phosphorylation decreased the amount of rac1 in rhogdi2 complexes and increased rhogdi2 association with cell membranes.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-149282	Tyr156	YGPRAEEyEFLTPVE	Homo sapiens
pmid	sentence
16943322	We show here that src kinase binds and phosphorylates rhogdi both in vitro and in vivo at tyr156. analysis of rho gtpase-rhogdi complexes using in vitro assays of complexation and in vivo by coimmunoprecipitation analysis indicates that src-mediated phosphorylation of tyr156 causes a dramatic decrease in the ability of rhogdi to form a complex with rhoa, rac1, or cdc42.

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, IL6 Signaling, Integrin Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-263037	Tyr156	GSRNALKyEHKEIEY	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-263038	Tyr163	YEHKEIEyVETVTSR	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-263039	Tyr274	SNVVRKDyDTLSKCS	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-263040	Tyr293	PAPSGRAyTSPLIDM	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-263041	Tyr37	LINLGKNyEKAVNAM	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Identifier	Residue	Sequence	Organism
SIGNOR-263042	Tyr439	VVIPPPDyLECLSMG	in vitro
pmid	sentence
21840312	Here, we report that overexpression of IRTKS increases the speed of wound closure of HT1080 cells in a Src-dependent manner. Active Src phosphorylates IRTKS in vivo and in vitro. Deletion mapping and mutation analysis revealed that six tyrosine residues (Y37, Y156, Y163, Y274, Y293 and Y439) were Src-stimulated phosphorylation sites on IRTKS. Disruption of Src-stimulated IRTKS phosphorylation abolished the effect of IRTKS on wound closure. Collectively, these data suggest Src-stimulated IRTKS phosphorylation is essential for its function in cell motility.

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247138	Tyr160	QVPQQPTyVQALFDF	Homo sapiens	HEK-293 Cell
pmid	sentence
20554525	In our work we show that, in contrast to BCR-ABL and prolactin, NPM-ALK phosphorylates Grb2 mainly in Tyr160)Previous reports suggested an inhibitory role of Grb2 Tyr7, Tyr37, Tyr52, and Tyr209 phosphorylation in receptor tyrosine kinase signaling (16) (43). Instead, in our system Grb2 Tyr160 mutation was not show to have a role in ALCL proliferation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-179601	Tyr165	VGSEEDLyDDLHSSS	Homo sapiens	A-431 Cell
pmid	sentence
18653540	This observation strongly argues for the positive role of tyr94 phosphorylation in egf-induced asef activation following the activation of rac1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-98271	Tyr168	TLMEKDSyPRFLKSP	Homo sapiens
pmid	sentence
12588871	Src-mediated rgs16 tyrosine phosphorylation promotes rgs16 stability. / this result suggests src phosphorylates native rgs16 at residue tyr177 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-98275	Tyr177	RFLKSPAyRDLAAQA	Homo sapiens
pmid	sentence
12588871	Src-mediated rgs16 tyrosine phosphorylation promotes rgs16 stability. hosphorylation on tyr(168) was mediated by the epidermal growth factor receptor (egfr).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271706	Tyr171	IPTSAPVyQQPQQQP	Homo sapiens	Blood Platelet
pmid	sentence
19718473	Integrin-dependent translocation of LASP-1 to the cytoskeleton of activated platelets correlates with LASP-1 phosphorylation at tyrosine 171 by Src-kinase

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-159240	Tyr173	EDEGGEVyEDLMKAE	Homo sapiens	Lymphoma Cell
pmid	sentence
17998938	Activation of rac1 and the exchange factor vav3 are involved in npm-alk signaling in anaplastic large cell lymphomas.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273810	Tyr174	LFKEENPyARFENN	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
23678037	Src induction leads to phosphorylation at PBF residue Y174. Abrogation of this residue results in PM retention and a markedly reduced ability to bind NIS.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-141103	Tyr177	GVRWAKLySLVIWGC	Homo sapiens
pmid	sentence
16226010	Here we demonstrate that egf is capable of inducing src-mediated phosphorylation of the tyrosine residues 177 and 347 of bkr. Their replacement by phenylalanine led to bkr mutants which are unable to activate the camp pathway.

Identifier	Residue	Sequence	Organism
SIGNOR-141107	Tyr347	RKKSWEVyQGVCQKG	Homo sapiens
pmid	sentence
16226010	Here we demonstrate that egf is capable of inducing src-mediated phosphorylation of the tyrosine residues 177 and 347 of bkr. Their replacement by phenylalanine led to bkr mutants which are unable to activate the camp pathway.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277573	Tyr179	TSCGSPNyAAPEVIS	Homo sapiens	HEK-293T Cell
pmid	sentence
34673141	We show here that Src signaling leads to direct phosphorylation of the AMPK-α subunit on a novel site, tyrosine 179, resulting in suppression of AMPK-T172 phosphorylation and autophagy upon integrin-mediated cell adhesion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247072	Tyr185	KQCEQAVyQTILEED	Mus musculus	Neuron
pmid	sentence
11279201	Dab1 is rapidly phosphorylated when neurons isolated from embryonic brains are stimulated with Reelin, and several tyrosines have been implicated in this response. Mice with phenylalanine substitutions of all five tyrosines (Tyr(185), Tyr(198), Tyr(200), Tyr(220), and Tyr(232)) exhibit a reeler phenotype, implying that tyrosine phosphorylation is critical for Dab1 function. Here we report that, although Src can phosphorylate all five tyrosines in vitro, Tyr(198) and Tyr(220) represent the major sites of Reelin-induced Dab1 phosphorylation in embryonic neurons.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247076	Tyr198	EDVEDPVyQYIVFEA	Mus musculus	Neuron
pmid	sentence
11279201	Dab1 is rapidly phosphorylated when neurons isolated from embryonic brains are stimulated with Reelin, and several tyrosines have been implicated in this response. Mice with phenylalanine substitutions of all five tyrosines (Tyr(185), Tyr(198), Tyr(200), Tyr(220), and Tyr(232)) exhibit a reeler phenotype, implying that tyrosine phosphorylation is critical for Dab1 function. Here we report that, although Src can phosphorylate all five tyrosines in vitro, Tyr(198) and Tyr(220) represent the major sites of Reelin-induced Dab1 phosphorylation in embryonic neurons.

Identifier	Residue	Sequence	Organism
SIGNOR-247080	Tyr220	PETEENIyQVPTSQK	Mus musculus
pmid	sentence
11279201	Dab1 is rapidly phosphorylated when neurons isolated from embryonic brains are stimulated with Reelin, and several tyrosines have been implicated in this response. Mice with phenylalanine substitutions of all five tyrosines (Tyr(185), Tyr(198), Tyr(200), Tyr(220), and Tyr(232)) exhibit a reeler phenotype, implying that tyrosine phosphorylation is critical for Dab1 function. Here we report that, although Src can phosphorylate all five tyrosines in vitro, Tyr(198) and Tyr(220) represent the major sites of Reelin-induced Dab1 phosphorylation in embryonic neurons.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247084	Tyr232	SQKKEGVyDVPKSQP	Mus musculus	Neuron
pmid	sentence
11279201	Dab1 is rapidly phosphorylated when neurons isolated from embryonic brains are stimulated with Reelin, and several tyrosines have been implicated in this response. Mice with phenylalanine substitutions of all five tyrosines (Tyr(185), Tyr(198), Tyr(200), Tyr(220), and Tyr(232)) exhibit a reeler phenotype, implying that tyrosine phosphorylation is critical for Dab1 function. Here we report that, although Src can phosphorylate all five tyrosines in vitro, Tyr(198) and Tyr(220) represent the major sites of Reelin-induced Dab1 phosphorylation in embryonic neurons.

Publications:

4

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-114641	Tyr187	FSEEIRFyQLGEEAM	Homo sapiens
pmid	sentence
11812778	The shaker family k+ channel protein, kv1.3, is tyrosine phosphorylated by v-src kinase at tyr137 and tyr449 to modulate current magnitude and kinetic properties.

Identifier	Residue	Sequence	Organism
SIGNOR-114645	Tyr499	EGEEQSQyMHVGSCQ	Homo sapiens
pmid	sentence
11812778	The shaker family k+ channel protein, kv1.3, is tyrosine phosphorylated by v-src kinase at tyr137 and tyr449 to modulate current magnitude and kinetic properties.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99314	Tyr188	SFVGTLQyLAPELLE	Homo sapiens
pmid	sentence
12645577	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Identifier	Residue	Sequence	Organism
SIGNOR-99318	Tyr199	ELLEQQKyTVTVDYW	Homo sapiens
pmid	sentence
12645577	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-100784	Tyr188	SFVGTLQyLAPELLE	Homo sapiens
pmid	sentence
12707358	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-90225	Tyr19	LFMDDDSySHHSGLE	Homo sapiens
pmid	sentence
12091389	We show that caveolin-2 undergoes src-induced phosphorylation on tyrosine 19. we conclude that the tyrosine phosphorylation of caveolin-2 (tyr(p)(19)) may function as a signal that is recognized by the cellular machinery to induce the dissociation of caveolin-2 from caveolin-1 oligomers

Identifier	Residue	Sequence	Organism
SIGNOR-129961	Tyr27	SHHSGLEyADPEKFA	Homo sapiens
pmid	sentence
15504032	Here, we show that cav-2 is phosphorylated at both tyrosines 19 and 27. We reconstituted this phosphorylation event by recombinantly coexpressing c-src and cav-2.Further functional analysis revealed that tyrosine phosphorylation of cav-2 has no effect on its targeting to lipid rafts, but clearly disrupts the hetero-oligomerization of cav-2 with cav-1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273567	Tyr192	MMDGAMGyVQPPPPP	Homo sapiens	MCF-7 Cell
pmid	sentence
21642474	Using dominant-negative, constitutively active mutants, RNAi, and pharmacological studies, we demonstrated that phosphorylation of WBP2 at Tyr192 and Tyr231 could be regulated by c-Src and c-Yes kinases.We further showed that abrogating WBP2 phosphorylation impaired >60% of ERα reporter activity, putatively by blocking nuclear entry of WBP2 and its interaction with ERα.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273568	Tyr231	AEAAASAyYNPGNPH	Homo sapiens	MCF-7 Cell
pmid	sentence
21642474	Using dominant-negative, constitutively active mutants, RNAi, and pharmacological studies, we demonstrated that phosphorylation of WBP2 at Tyr192 and Tyr231 could be regulated by c-Src and c-Yes kinases.We further showed that abrogating WBP2 phosphorylation impaired >60% of ERα reporter activity, putatively by blocking nuclear entry of WBP2 and its interaction with ERα.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266100	Tyr193	SKTMTPTyDAHDGSP	Homo sapiens	HEK-293 Cell
pmid	sentence
26037143	Here we report that Src binds to and phosphorylates Kindlin-2 at Y193. Reciprocally, Kindlin-2-Y193 phosphorylation activates and maintains Src kinase activity. Kindlin-2-Y193 phosphorylation is also involved in its binding capacity with Migfilin and the recruitment of Migfilin to the focal adhesions. Functionally, we demonstrate that Kindlin-2-Y193 phosphorylation regulates Kindlin-2-mediated cell spreading and migration.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276419	Tyr193	VQINDNYyEDLTAKD	Homo sapiens	T-98G Cell
pmid	sentence
22823520	Phosphorylation-site analysis selects c-Src targets, including NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr(193) of respiratory complex I and SDHA (succinate dehydrogenase A) at Tyr(215) of complex II. The phosphorylation of these sites by c-Src is supported by an in vivo assay using cells expressing their phosphorylation-defective mutants.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273807	Tyr195	PGGLDDRySLVSEQL	Homo sapiens	HaCaT Cell
pmid	sentence
25501895	We have discovered that reactive oxygen species (ROS) trigger the c-Src kinase-mediated tyrosine (Tyr)-195 phosphorylation of PKP3. This modification is associated with a change in the subcellular distribution of the protein. Specifically, PKP3 bearing phospho-Tyr-195 is released from the desmosomes, suggesting that phospho-Tyr-195 is relevant for the control of desmosome disassembly and function, at least in cells exposed to ROS.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266351	Tyr197	RSLGPKLyGIFPQGR	Homo sapiens	MCF-7 Cell
pmid	sentence
21822308	We find that CHKA forms a complex with EGFR in a c-Src-dependent manner. Endogenous CHKA and EGFR co-immunoprecipitated from a variety of breast cancer cell lines and immortalized mammary epithelial cells. CHKA interacted with the EGFR kinase domain upon c-Src co-overexpression and was phosphorylated in a c-Src-dependent manner on Y197 and Y333.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266350	Tyr333	LMLIDFEySSYNYRG	Homo sapiens	MCF-7 Cell
pmid	sentence
21822308	We find that CHKA forms a complex with EGFR in a c-Src-dependent manner. Endogenous CHKA and EGFR co-immunoprecipitated from a variety of breast cancer cell lines and immortalized mammary epithelial cells. CHKA interacted with the EGFR kinase domain upon c-Src co-overexpression and was phosphorylated in a c-Src-dependent manner on Y197 and Y333.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277478	Tyr198	IDEAEVIySELMSDF	Homo sapiens	HEK-293T Cell
pmid	sentence
31420453	Src activates GEF-H1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273806	Tyr199	KYPIVEQyLKTKKNS	Homo sapiens	Coronary Artery Smooth Muscle Cell
pmid	sentence
30814251	We report herein that the YLK motif is contained within an SRC homology 2 domain and is directly phosphorylated by SRC proto-oncogene, nonreceptor tyrosine kinase (SRC) at Tyr198. Using a PANX1 Tyr198-specific antibody, SFK inhibitors, SRC knockdown, temperature-dependent SRC cells, and kinase assays, we found that PANX1-mediated ATP release and vasoconstriction involves constitutive phosphorylation of PANX1 Tyr198 by SRC.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-202796	Tyr21	IENEEQEyVQTVKSS	Homo sapiens
pmid	sentence
24103589	The authors identified several phosphorylated residues by a combination of peptide mapping and sequence analysis and showed that recombinant pp60c-src phosphorylates annexin a1 near its amino terminus, at tyrosine 21 (tyr21). Also polyoma virus middle t/pp60c-src complex, recombinant pp50v-abl, and the egf receptor/kinase phosphorylated the same tyrosine residue. It was also shown that serine 27 residue of anxa1 is the primary site phosphorylated by protein kinase c (pkc). In the same study, the threonine 41 residue has been identified as a pkc substrate as well. The adenosine cyclic 3_,5_-phosphate dependent protein kinase a (pka) phosphorylates anxa1 in its carboxyl-terminal core at the threonine 216 residue (thr216) [2].Finally in 2013 caron et al. showed the relevance of y21 phosphorylation for the anxa1 stability. In fact the authors demonstrated that the tyrosine 21 phosphorylation is crucial for anxa1 sumoylation induced by egf

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-155713	Tyr21	VSSDAEEyQPPIWKS	Homo sapiens
pmid	sentence
17560670	Here we report that beta2-chimaerin is tyrosine-phosphorylated by src-family kinases (sfks) upon cell stimulation with epidermal growth factor (egf). Mutational analysis identified tyr-21 in the n-terminal regulatory region as a major phosphorylation site. these results suggest tyr-21 phosphorylation as a novel, sfk-dependent mechanism that negatively regulates beta2-chimaerin rac-gap activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276420	Tyr215	SLRYDTSyFVEYFAL	Homo sapiens	T-98G Cell
pmid	sentence
22823520	Phosphorylation-site analysis selects c-Src targets, including NDUFV2 (NADH dehydrogenase [ubiquinone] flavoprotein 2) at Tyr(193) of respiratory complex I and SDHA (succinate dehydrogenase A) at Tyr(215) of complex II. The phosphorylation of these sites by c-Src is supported by an in vivo assay using cells expressing their phosphorylation-defective mutants.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236246	Tyr216	KLDSGGFyITSRTQF	Homo sapiens	Breast Cancer Cell
pmid	sentence
12753909	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

Identifier	Residue	Sequence	Organism
SIGNOR-29369	Tyr419	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
7578094	These data are consistent with autophosphorylation on y-419 as predicted. Intermolecular autophosphorylation is consistent with the ability of srctk to dimerize, which is analogous to activation of receptor tyrosine kinases such as the egf receptor kinase in response to growth factors.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Axon guidance, EGFR Signaling, IL6 Signaling, Integrin Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-273919	Tyr218	GDGSDHPyYNSIPSK	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273921	Tyr219	DGSDHPYyNSIPSKM	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273920	Tyr283	RQGSSDIySTPEGKL	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-273925	Tyr301	PTGEAPTyVNTQQIP	in vitro
pmid	sentence
11791173	We also obtained tryptic phosphopeptide maps of N-Shc protein phosphorylated in vitro by other tyrosine kinases, TrkB, v-Src and EGFR. The overall patterns of the phosphopeptide maps generated by these tyrosine kinases were similar, although there were some differences among these maps (Figure 4a–d).We performed phosphopeptide mapping analysis using GST-fused N-Shc protein, and found that N-Shc phosphorylated by TrkA in vitro was resolved into at least seven phosphopeptides (Y1 through Y7, Figure 4a). Phosphopeptide mapping revealed that N-Shc has novel tyrosine-phosphorylation sites at Y259/Y260 and Y286; in vivo-phosphorylation of these tyrosines was demonstrated by site-specific anti-pTyr antibodies. Phosphorylated Y286 bound to several proteins, of which one was Crk. The pY221/pY222 site, corresponding to one of the Grb2-binding sites of Shc, also preferentially bound to Crk. The phosphorylation-dependent interaction between N-Shc and Crk was demonstrated in vitro and in vivo.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-247333	Tyr22	GVLPSHYyESFLEKK	Homo sapiens
pmid	sentence
12540842	To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase Tyr-22 and Tyr-322 are the major tyrosine phosphorylation sites by v-Src.

Identifier	Residue	Sequence	Organism
SIGNOR-247337	Tyr322	GDGPAVDyENQDVAS	Homo sapiens
pmid	sentence
12540842	To examine this possibility, STAP-2 was co-transfected with constitutively active tyrosine kinases in HEK-293 cells. STAP-2 was strongly phosphorylated by various tyrosine kinases, including v-Src (Fig.2 A-a), a JAK2 tyrosine kinase Tyr-22 and Tyr-322 are the major tyrosine phosphorylation sites by v-Src.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276081	Tyr2217	ELQDSRVyVSSL	Homo sapiens	HEK-293 Cell
pmid	sentence
17942635	Cotransfection of human embryonic kidney (HEK)-293 cells with hCa(v)1.2b and c-Src resulted in tyrosine phosphorylation of the calcium channel, which was prevented by nitration of tyrosine residues by peroxynitrite. Whole cell calcium currents were reduced by 58 + 5% by the Src kinase inhibitor PP2 and 64 + 6% by peroxynitrite.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-88899	Tyr225	IKGRAQPyDPNFYDE	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Identifier	Residue	Sequence	Organism
SIGNOR-88903	Tyr230	QPYDPNFyDETYDYG	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Identifier	Residue	Sequence	Organism
SIGNOR-88907	Tyr234	PNFYDETyDYGGFTM	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Identifier	Residue	Sequence	Organism
SIGNOR-88911	Tyr236	FYDETYDyGGFTMMF	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Identifier	Residue	Sequence	Organism
SIGNOR-88915	Tyr380	YAGGRGSyGDLGGPI	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Identifier	Residue	Sequence	Organism
SIGNOR-88919	Tyr72	IKALRTDyNASVSVP	Homo sapiens
pmid	sentence
12052863	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. c-src-mediated phosphorylation reversibly inhibits the binding of hnrnp k to the differentiation control element (dice) of the lox mrna 3' untranslated region in vitro and specifically derepresses the translation of dice-bearing mrnas in vivo.We confirmed that tyr 230, 234, 236, and 380 are phosphorylated and identified two additional targets of c-src, tyr 72 and tyr 225 (data not shown).

Publications:

6

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-246307	Tyr226	KRNKPTVyGVSPNYD	Homo sapiens
pmid	sentence
11847100	c-Src-induced c-Abl activation involves phosphorylation of Y245 and Y412, two residues required for c-Abl mitogenic function.

Identifier	Residue	Sequence	Organism
SIGNOR-246311	Tyr393	RLMTGDTyTAHAGAK	Homo sapiens
pmid	sentence
11847100	c-Src-induced c-Abl activation involves phosphorylation of Y245 and Y412, two residues required for c-Abl mitogenic function.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-94796	Tyr228	LNEGKHLyTLDGGDI	Homo sapiens
pmid	sentence
12400005	We found that rack1 is a src substrate. Moreover, src activity is necessary for both the tyrosine phosphorylation of rack1 and the binding of rack1 to src's sh2 domain that occur following pkc activation. To identify the tyrosine(s) on rack1 that is phosphorylated by src, we generated and tested a series of rack1 mutants. We found that src phosphorylates rack1 on tyr 228 and/or tyr 246

Identifier	Residue	Sequence	Organism
SIGNOR-94800	Tyr246	LCFSPNRyWLCAATG	Homo sapiens
pmid	sentence
12400005	We found that rack1 is a src substrate. Moreover, src activity is necessary for both the tyrosine phosphorylation of rack1 and the binding of rack1 to src's sh2 domain that occur following pkc activation. To identify the tyrosine(s) on rack1 that is phosphorylated by src, we generated and tested a series of rack1 mutants. We found that src phosphorylates rack1 on tyr 228 and/or tyr 246

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-195883	Tyr23	SAALDPAyTTLEFEN	Homo sapiens
pmid	sentence
22308320	Here we show that c-src phosphorylates human hnf4_ on three tyrosines phosphomimetic mutants in the lbd decrease p1-hnf4_ protein stability, nuclear localization and transactivation function.

Identifier	Residue	Sequence	Organism
SIGNOR-195896	Tyr286	LQIDDNEyAYLKAII	Homo sapiens
pmid	sentence
22308320	Here we show that c-src phosphorylates human hnf4_ on three tyrosines phosphomimetic mutants in the lbd decrease p1-hnf4_ protein stability, nuclear localization and transactivation function.

Identifier	Residue	Sequence	Organism
SIGNOR-195900	Tyr288	IDDNEYAyLKAIIFF	Homo sapiens
pmid	sentence
22308320	Here we show that c-src phosphorylates human hnf4_ on three tyrosines phosphomimetic mutants in the lbd decrease p1-hnf4_ protein stability, nuclear localization and transactivation function.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247124	Tyr231	LLPLRRGyIGVVNRS	Homo sapiens	HEK-293 Cell
pmid	sentence
9880482	Src-mediated tyrosine phosphorylation of dynamin is required for beta2-adrenergic receptor internalization and mitogen-activated protein kinase signalingHere we demonstrate that activation of beta2-adrenergic receptors (beta2-ARs) leads to c-Src-mediated tyrosine phosphorylation of dynamin, which is required for receptor internalization. Two tyrosine residues, Tyr231 and Tyr597, are identified as the major phosphorylation sites

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247129	Tyr597	NTEQRNVyKDYRQLE	Chlorocebus aethiops	COS Cell
pmid	sentence
12011079	Endocytosis of ligand-activated receptors requires dynamin-mediated GTP hydrolysis, which is regulated by dynamin self-assembly. Here, we demonstrate that phosphorylation of dynamin I by c-Src induces its self-assembly and increases its GTPase activity. Electron microscopic analyses reveal that tyrosine-phosphorylated dynamin I spontaneously self-assembles into large stacks of rings. Tyrosine 597 was identified as being phosphorylated both in vitro and in cultured cells following epidermal growth factor receptor stimulation.

Publications:

2

Organism:

Homo Sapiens, Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-127872	Tyr24	HSTPPSAyGSVKAYT	Homo sapiens
pmid	sentence
15302870	Translocation requires the presence of the annexin 2 binding partner p11 (s100a10) and the phosphorylation of annexin 2 at tyr23 through a src-like tyrosine kinase-dependent mechanism both in vitro and in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275982	Tyr240	RREDKFMyFEFPQPL	Homo sapiens	U-251MG Cell
pmid	sentence
11948419	MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275981	Tyr315	RADNDKEyLVLTLTK	Homo sapiens	U-251MG Cell
pmid	sentence
11948419	MMAC/PTEN is tyrosine phosphorylated. U251 glioblastoma cells were cotransfected with MMAC/PTEN and either Src Lck expression plasmids.Reduced tyrosine phosphorylation of MMAC/PTEN was observed when tyrosine 240 or 315 mutants were mutated to nonphosphorylated residues (Figure 1e).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-113406	Tyr241	SHQGPVIyAQLDHSG	Homo sapiens
pmid	sentence
11751924	Indeed, our studies indicated that cross-linking of pzr by cona lead to activation of c-src, which may be responsible for phosphorylation of pzr and possibly other proteins. Phosphorylation of pzr in turn recruits shp-2, which by itself is an essential signal transducertyrosine residues 241 and 263 embedded in the itims are responsible for the tyrosine phosphorylation of pzr

Identifier	Residue	Sequence	Organism
SIGNOR-113410	Tyr263	NKSESVVyADIRKN	Homo sapiens
pmid	sentence
11751924	Indeed, our studies indicated that cross-linking of pzr by cona lead to activation of c-src, which may be responsible for phosphorylation of pzr and possibly other proteins. Phosphorylation of pzr in turn recruits shp-2, which by itself is an essential signal transducertyrosine residues 241 and 263 embedded in the itims are responsible for the tyrosine phosphorylation of pzr

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-236314	Tyr242	FFQQQMIyDSPPSRA	Homo sapiens
pmid	sentence
19881549	Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276626	Tyr246	PDHKNGHyIIPQMAD	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
24699139	Tyrosines 246 and 293 are required to hold GIT1 in a closed conformation.Hyperphosphorylation of GIT1-N by Src and pervanadate does not affect its binding in vitro to full length GIT1 proteins. Mutations Y246E and Y293E of GIT1 enhance binding to paxillin.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276627	Tyr284	EELAMDVyDEVDRRE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
24699139	Tyrosines 246 and 293 are required to hold GIT1 in a closed conformation.Hyperphosphorylation of GIT1-N by Src and pervanadate does not affect its binding in vitro to full length GIT1 proteins. Mutations Y246E and Y293E of GIT1 enhance binding to paxillin.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275584	Tyr246	RRLCEHKyGNAPRVR	Homo sapiens	Colorectal Cancer Cell
pmid	sentence
32238881	Src phosphorylated BCKDK at the tyrosine 246 (Y246) site in vitro and ex vivo. Knockdown and knockout of Src downregulated the phosphorylation of BCKDK. Importantly, phosphorylation of BCKDK by Src enhanced the activity and stability of BCKDK, thereby promoting the migration, invasion, and EMT of CRC cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275583	Tyr246	RRLCEHKyGNAPRVR	Homo sapiens	Colorectal Cancer Cell
pmid	sentence
32238881	Src phosphorylated BCKDK at the tyrosine 246 (Y246) site in vitro and ex vivo. Knockdown and knockout of Src downregulated the phosphorylation of BCKDK. Importantly, phosphorylation of BCKDK by Src enhanced the activity and stability of BCKDK, thereby promoting the migration, invasion, and EMT of CRC cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-148913	Tyr247	VKGKSDPyHATSGAL	Homo sapiens
pmid	sentence
16916748	The oncogenic tyrosine kinase, v-src, phosphorylates connexin43 (cx43) on y247 and y265 and inhibits cx43 gap junctional communication (gjc), the process of intercellular exchange of ions and metabolites.

Identifier	Residue	Sequence	Organism
SIGNOR-148917	Tyr265	KDCGSQKyAYFNGCS	Homo sapiens
pmid	sentence
16916748	The oncogenic tyrosine kinase, v-src, phosphorylates connexin43 (cx43) on y247 and y265 and inhibits cx43 gap junctional communication (gjc), the process of intercellular exchange of ions and metabolites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247185	Tyr248	EESEDPDyYQYNIQA	Chlorocebus aethiops	COS Cell
pmid	sentence
11934902	c-Src-dependent transcriptional activation of TFII-ITFII-I is a multifunctional transcription factor that is also involved in signal transduction. Here we show that TFII-I undergoes a c-Src-dependent tyrosine phosphorylation on tyrosine residues 248 and 611 and translocates to the nucleus in response to growth factor signaling

Identifier	Residue	Sequence	Organism
SIGNOR-247189	Tyr652	KPELVISyLPPGMAS	Chlorocebus aethiops
pmid	sentence
11934902	C-Src-dependent transcriptional activation of TFII-ITFII-I is a multifunctional transcription factor that is also involved in signal transduction. Here we show that TFII-I undergoes a c-Src-dependent tyrosine phosphorylation on tyrosine residues 248 and 611 and translocates to the nucleus in response to growth factor signaling

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence
SIGNOR-272998	Tyr251	LQFPGAVyGTDGCPV
pmid	sentence
29844931	As a result, we established that Src was able to directly phosphorylate caspase-9 at tyrosine 251, leading to elevated caspase-9 activity.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259814	Tyr254	SKSWWKKyCCFV	Homo sapiens	NCI-H1299 Cell
pmid	sentence
20547754	Regulation of the Rho family small GTPase Wrch-1/RhoU by C-terminal tyrosine phosphorylation requires Src. Phosphorylation at Y254 negatively regulates Wrch-1-mediated biological functions.Serum-stimulated tyrosine phosphorylation and relocalization of Wrch-1 decreases its activation of downstream effectors in a Y254-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247433	Tyr256	LKAALKLyHVSDSEG	Homo sapiens
pmid	sentence
15342783	These data suggest that phosphorylation of villin by c-src is involved in the actin cytoskeleton remodeling necessary for cell migration.To further investigate the role of tyrosine phosphorylated villin in cell migration, we used phosphorylation site mutants (tyrosine to phenylalanine or tyrosine to glutamic acid) in HeLa cells. We determined that tyrosine phosphorylation at residues 60, 81, and 256 of human villin played an essential role in cell migration as well as in the reorganization of the actin cytoskeleton

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247437	Tyr60	KTASSLSyDIHYWIG	Homo sapiens	HeLa Cell
pmid	sentence
15342783	These data suggest that phosphorylation of villin by c-src is involved in the actin cytoskeleton remodeling necessary for cell migration.To further investigate the role of tyrosine phosphorylated villin in cell migration, we used phosphorylation site mutants (tyrosine to phenylalanine or tyrosine to glutamic acid) in HeLa cells. We determined that tyrosine phosphorylation at residues 60, 81, and 256 of human villin played an essential role in cell migration as well as in the reorganization of the actin cytoskeleton

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247441	Tyr81	EQGAAAIyTTQMDDF	Homo sapiens	HeLa Cell
pmid	sentence
15342783	These data suggest that phosphorylation of villin by c-src is involved in the actin cytoskeleton remodeling necessary for cell migration.To further investigate the role of tyrosine phosphorylated villin in cell migration, we used phosphorylation site mutants (tyrosine to phenylalanine or tyrosine to glutamic acid) in HeLa cells. We determined that tyrosine phosphorylation at residues 60, 81, and 256 of human villin played an essential role in cell migration as well as in the reorganization of the actin cytoskeleton

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236310	Tyr259	ASVDSSLyNLPRSYS	Homo sapiens	HEK-293 Cell
pmid	sentence
19881549	Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236306	Tyr317	PPTPGNTyQIPRTFP	Homo sapiens	HEK-293 Cell
pmid	sentence
19881549	Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis

Identifier	Residue	Sequence	Organism
SIGNOR-236318	Tyr373	ASDTDSSyCIPTAGM	Homo sapiens
pmid	sentence
19881549	Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236302	Tyr627	KGDKQVEyLDLDLDS	Homo sapiens	HEK-293 Cell
pmid	sentence
19881549	Using both mutagenesis and mass spectrometry approaches, y242, y259, y317, y373 and y627 of gab1 were identified to be phosphorylated by c-src a gab1 mutant with substitutions of the src phosphorylation sites failed to promote hgf-induced dna synthesis

Publications:

4

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence
SIGNOR-275919	Tyr26	LDDSLQDyPFEDWQL
pmid	sentence
26319181	We identified Tyr 26 as a PDGF-induced and, additionally, Tyr 519 and Tyr 665 as SRC-induced tyrosine phosphorylation sites. Phosphomimetic mutants indicate that phosphorylation of Tyr 519 recruits CNK1 to the nucleus and additional phosphorylation of Tyr 26 enables CNK1 to promote SRE-dependent gene expression.

Identifier	Residue	Sequence
SIGNOR-275918	Tyr519	PPREEDCySETEAED
pmid	sentence
26319181	We identified Tyr 26 as a PDGF-induced and, additionally, Tyr 519 and Tyr 665 as SRC-induced tyrosine phosphorylation sites. Phosphomimetic mutants indicate that phosphorylation of Tyr 519 recruits CNK1 to the nucleus and additional phosphorylation of Tyr 26 enables CNK1 to promote SRE-dependent gene expression.

Identifier	Residue	Sequence
SIGNOR-275920	Tyr665	KEQNRELySEGLGAW
pmid	sentence
26319181	We identified Tyr 26 as a PDGF-induced and, additionally, Tyr 519 and Tyr 665 as SRC-induced tyrosine phosphorylation sites. Phosphomimetic mutants indicate that phosphorylation of Tyr 519 recruits CNK1 to the nucleus and additional phosphorylation of Tyr 26 enables CNK1 to promote SRE-dependent gene expression.

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-111920	Tyr265	RVIGRGSyAKVLLVR	Homo sapiens
pmid	sentence
11713277	Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-111924	Tyr280	LKKTDRIyAMKVVKK	Homo sapiens
pmid	sentence
11713277	Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-111928	Tyr334	RLFFVIEyVNGGDLM	Homo sapiens
pmid	sentence
11713277	Nerve growth factor stimulates multisite tyrosine phosphorylation and activation of the atypical protein kinase c's via a src kinase pathway. tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277217	Tyr272	DFDDEAYyAALGTRP	Homo sapiens	SW-480 Cell
pmid	sentence
27016416	Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277218	Tyr74	NPICNDHyRSVYQKR	Homo sapiens	SW-480 Cell
pmid	sentence
27016416	Phosphorylation of TOPK at Y74, Y272 by Src increases the stability of TOPK and promotes tumorigenesis of colon

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277405	Tyr278	NSKFDTIyQILLKKK	Homo sapiens	HEK-293T Cell
pmid	sentence
30100205	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. Analysis using a c-Src inhibitor and TRIM25 mutant, in which tyrosine 278 is substituted by phenylalanine (Y278F), suggested that the phosphorylation positively regulates K63-linked polyubiquitination of RIG-I and subsequent antiviral signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-182963	Tyr284	KIFPYEEyASWKTEK	Homo sapiens
pmid	sentence
19114990	Tbetarii can also be phosphorylated by src, a non-rtk, on y284, which can serve as a docking site for the recruitment of grb2 and shc, thereby bridging tbetarii to mapk activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277204	Tyr289	MELQTYRyHGHSMSD	Homo sapiens	HEK-293 Cell
pmid	sentence
26848621	Src inactivated PDH through direct phosphorylation of tyrosine-289 of PDH E1α subunit (PDHA1).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-236037	Tyr301	LGYRDSGyYWEVPPS	Chlorocebus aethiops	COS Cell
pmid	sentence
9020159	A-raf behaves like raf-1, being weakly activated by oncogenic ras more strongly activated by oncogenic src, and these signals synergize to give maximal activation. Activation of Raf-1 and A-Raf by Src requires tyrosine phosphorylation at residues 340 and 341 in Raf-1 and 301 and 302 in A-Raf.

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-157781	Tyr301	DDITQEEyGEFYKSL	Homo sapiens
pmid	sentence
17855507	C-src directly phosphorylates hsp90 on tyrosine 300 residue and that this event is essential for vegf-stimulated enos association to hsp90 and thus no release from endothelial cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-236459	Tyr302	GYRDSGYyWEVPPSE	Chlorocebus aethiops
pmid	sentence
9020159	A-raf behaves like raf-1, being weakly activated by oncogenic ras more strongly activated by oncogenic src, and these signals synergize to give maximal activation

Publications:

1

Organism:

Chlorocebus Aethiops

Pathways:

EGFR Signaling, Integrin Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-202192	Tyr307	VTRRTPDyFL	Homo sapiens	Neuron
pmid	sentence
23796501	We found that ?-Syn gene overexpression in sk-n-sh cells and primary neurons led to pp2a/c phosphorylation at y307, a known target of src kinase, and consequent phosphatase inhibition.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139150	Tyr315	QPSCKALyDFEPEND	Homo sapiens
pmid	sentence
16054026	Further, we identified an interaction between fak's second pro-rich motif and endophilin a2's sh3 domain. This interaction served as an autophosphorylation-dependent scaffold to allow src phosphorylation of endophilin a2 at tyr315. Tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp. Together, these results suggest a regulatory mechanism of cell invasion whereby fak promotes cell-surface presentation of mt1-mmp by inhibiting endophilin a2-dependent endocytosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-252620	Tyr315	TFCGTPEyLAPEVLE	Chlorocebus aethiops
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252621	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	HEK-293 Cell
pmid	sentence
12600984	We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252623	Tyr326	EVLEDNDyGRAVDWW	Chlorocebus aethiops	COS Cell
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Publications:

3

Organism:

Chlorocebus Aethiops, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246368	Tyr315	TFCGTPEyLAPEVLE	Chlorocebus aethiops	COS Cell
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246373	Tyr315	TFCGTPEyLAPEVLE	Homo sapiens	HEK-293 Cell
pmid	sentence
12600984	We also showed that phosphorylation of Tyr-315 in Akt induced by Src or EGF is dependent on the integrity of this proline-rich motif. Furthermore, the Akt mutant lacking this proline motif fails to block the transcription activity of Forkhead in 293 cells and poorly stimulates the proliferation of Madin-Darby canine kidney cells. Taken together, our data suggest that the interaction between the SH3 domain of Src family kinases and the proline-rich motif in the C-terminal regulatory region of Akt is required for tyrosine phosphorylation of Akt and its subsequent activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246377	Tyr326	EVLEDNDyGRAVDWW	Chlorocebus aethiops	COS Cell
pmid	sentence
11445557	Regulation of Akt/PKB Activation by Tyrosine PhosphorylationAs shown in Fig. 2 d, while mutation of Tyr340 has little effect on either tyrosine phosphorylation or kinase activity of Akt induced by Src527F, substitution of Tyr315 or Tyr326 with a phenylalanine, respectively, dramatically reduces both the tyrosine phosphorylation and kinase activity of Akt. The combination of these two mutations abolishes Src-induced tyrosine phosphorylation of Akt as well as its kinase activity.

Publications:

3

Organism:

Chlorocebus Aethiops, Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-139154	Tyr315	QPSCKALyDFEPEND	Homo sapiens
pmid	sentence
16054026	These results identified y315 of endophilin a2 as a major phosphorylation site by fak/src complex. tyr315 phosphorylation inhibited endophilin/dynamin interactions, and blockade of tyr315 phosphorylation promoted endocytosis of mt1-mmp.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263201	Tyr319	KKDNDFIyHDRVPDL	Homo sapiens
pmid	sentence
15557335	Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities. Phosphorylation of Alix by Src caused it to translocate from the membrane and cytoskeleton to the cytoplasm and reduced its interaction with binding partners SETA/CIN85, epidermal growth factor receptor, and Pyk2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-252093	Tyr32	QNHFVDEyDPTIEDS	Homo sapiens	HEK-293 Cell
pmid	sentence
25157176	Src binds to and phosphorylates GTP-, but not GDP-, loaded Ras on a conserved Y32 residue within the switch I region in vitro and that in vivo, Ras-Y32 phosphorylation markedly reduces the binding to effector Raf and concomitantly increases binding to GTPase-activating proteins and the rate of GTP hydrolysis

Publications:

1

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, Integrin Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277523	Tyr324	DNLESQTyEVFEKDP	Homo sapiens	HEK-293T Cell
pmid	sentence
32759981	Here, we demonstrate that PRMT5 is phosphorylated at residue Y324 by Src kinase, a negative regulator of its activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277484	Tyr325	AISEELPySEYFEYF	in vitro
pmid	sentence
30317579	C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form).

Identifier	Residue	Sequence	Organism
SIGNOR-277485	Tyr328	EELPYSEyFEYFAPD	in vitro
pmid	sentence
30317579	C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form).

Identifier	Residue	Sequence	Organism
SIGNOR-277486	Tyr331	PYSEYFEyFAPDFTL	in vitro
pmid	sentence
30317579	C-Src also phosphorylated three tyrosine sites of HDAC3 at tyrosine 325, 328, and 331. Importantly, wild-type c-Src increases HDAC3 activity, but not mutant c-SrcK298M (kinase inactive form).

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-123819	Tyr33	TTKDGWVyYANHTEE	Homo sapiens
pmid	sentence
15070730	The tyrosine kinase, src, phosphorylates wwox at tyrosine 33 in the first ww domain and enhances its binding to p73.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-177086	Tyr333	NIMRTYTyEKLLWTT	Homo sapiens
pmid	sentence
22056988	Egfr activation induces translocation of pkm2 into the nucleus, where k433 of pkm2 binds to c-src-phosphorylated y333 of _-cateninthese findings reveal that egf induces _-catenin transactivation via a mechanism distinct from that induced by wnt/wingless and highlight the essential non-metabolic functions of pkm2 in egfr-promoted _-catenin transactivation, cell proliferation and tumorigenesis

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-157365	Tyr335	ILPPSSIyPSVLASG	Homo sapiens
pmid	sentence
17700527	Diacylglycerol kinase-alpha phosphorylation by src on y335 is required for activation, membrane recruitment and hgf-induced cell motility.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97803	Tyr337	SKTKEGKyRVDFHNF	Homo sapiens
pmid	sentence
12556363	Inhibition of c-src with herbimycin a significantly decreased the tyrosine phosphorylation level of romk1... tyrosine dephosphorylation enhances the exocytosis of romk1

Identifier	Residue	Sequence	Organism
SIGNOR-92513	Tyr337	SKTKEGKyRVDFHNF	Homo sapiens
pmid	sentence
12217858	Addition of active c-src and [32p]atp to the purified romk1 protein resulted in the phosphorylation of the romk1 protein. However, c-src did not phosphorylate r1y337a in which tyrosine residue 337 was mutated to alanine. Furthermore, phosphopeptide mapping identified two phosphopeptides from the trypsin-digested romk1 protein.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271702	Tyr34	KDQFPEVyVPTVFEN	Homo sapiens	HeLa Cell
pmid	sentence
23027962	When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.\|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271701	Tyr66	DTAGQEDyDRLRPLS	Homo sapiens	HeLa Cell
pmid	sentence
23027962	When these RhoA mutants were coexpressed with Bcr-Abl, phosphorylation levels of Y34F and Y66F RhoA mutants dramatically decreased to 32% and 17%, respectively. As expected, when Y34 and Y66 were both mutated to phenylalanine, phosphorylation was completely abolished. Together, these observations indicate that Y34 and Y66 are the two predominant phosphorylation sites, and that the Src kinase and Bcr-Abl are the two candidate kinases that may phosphorylate these sites.\|In contrast to active RhoA, RhoAQ63L(Y34,66E) had a dramatic decrease in RBD binding. This binding fraction was even lower than that of WT RhoA, suggesting phosphorylation at these sites could have a negative effect on RhoA activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97635	Tyr340	RGQRDSSyYWEIEAS	Homo sapiens
pmid	sentence
12551923	We also show that phosphorylation of raf-1 on serine 338 by pak1 and tyrosines 340 and 341 by src relieves autoinhibition and that this occurs through a specific decrease in the binding of the raf-1 regulatory domain to its catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-82150	Tyr340	RGQRDSSyYWEIEAS	Homo sapiens
pmid	sentence
10998357	We also show that phosphorylation of raf-1 on serine 338 by pak1 and tyrosines 340 and 341 by src relieves autoinhibition and that this occurs through a specific decrease in the binding of the raf-1 regulatory domain to its catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-32081	Tyr340	RGQRDSSyYWEIEAS	Homo sapiens
pmid	sentence
7692235	We also show that phosphorylation of raf-1 on serine 338 by pak1 and tyrosines 340 and 341 by src relieves autoinhibition and that this occurs through a specific decrease in the binding of the raf-1 regulatory domain to its catalytic domain.

Identifier	Residue	Sequence	Organism
SIGNOR-97639	Tyr341	GQRDSSYyWEIEASE	Homo sapiens
pmid	sentence
12551923	We also show that phosphorylation of raf-1 on serine 338 by pak1 and tyrosines 340 and 341 by src relieves autoinhibition and that this occurs through a specific decrease in the binding of the raf-1 regulatory domain to its catalytic domain.

Publications:

4

Organism:

Homo Sapiens

Pathways:

EGFR Signaling, IL6 Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-274024	Tyr341	PFLNSGTyHSRDEST	Mus musculus
pmid	sentence
27013234	We found that YAP1, the pivotal effector of the Hippo signaling pathway, is a direct SRC phosphorylation target, and YAP1 phosphorylation at three sites in its transcription activation domain is necessary for SRC-YAP1-mediated transformation.

Identifier	Residue	Sequence	Organism
SIGNOR-274025	Tyr357	SGLSMSSySVPRTPD	Mus musculus
pmid	sentence
27013234	We found that YAP1, the pivotal effector of the Hippo signaling pathway, is a direct SRC phosphorylation target, and YAP1 phosphorylation at three sites in its transcription activation domain is necessary for SRC-YAP1-mediated transformation.

Identifier	Residue	Sequence	Organism
SIGNOR-274026	Tyr394	QQNRFPDyLEAIPGT	Mus musculus
pmid	sentence
27013234	We found that YAP1, the pivotal effector of the Hippo signaling pathway, is a direct SRC phosphorylation target, and YAP1 phosphorylation at three sites in its transcription activation domain is necessary for SRC-YAP1-mediated transformation.

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-165862	Tyr341	SEEQLQLyWAMDSTF	Homo sapiens
pmid	sentence
20525694	Phosphorylation of a critical tyrosine (tyr-341) in the linker region of cbl-c by src or a phosphomimetic mutation of this tyrosine (y341e) is sufficient to increase the e3 activity of cbl-c.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-25566	Tyr344	SDRKGGSyTQAASSD	Homo sapiens
pmid	sentence
6304688	Hla-a2 and hla-b7 antigens are phosphorylated in vitro by rous sarcoma virus kinase (pp60v-src) at a tyrosine residue encoded in a highly conserved exon of the intracellular domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-44866	Tyr349	EEPPDHQyYNDFPGK	Homo sapiens
pmid	sentence
8939605	Here, we report the identification of two major and novel Shc tyrosine phosphorylation sites, Y239 and Y240. Y239/240 are co-ordinately phosphorylated by the src protein-tyrosine kinase in vitro, and in response to epidermal growth factor stimulation or in v-src-transformed cells in vivo. phosphorylation of y317 has been implicated in grb2 binding and activation of the ras pathway.

Identifier	Residue	Sequence	Organism
SIGNOR-44870	Tyr350	EPPDHQYyNDFPGKE	Homo sapiens
pmid	sentence
8939605	Here, we report the identification of two major and novel Shc tyrosine phosphorylation sites, Y239 and Y240. Y239/240 are co-ordinately phosphorylated by the src protein-tyrosine kinase in vitro, and in response to epidermal growth factor stimulation or in v-src-transformed cells in vivo. phosphorylation of y317 has been implicated in grb2 binding and activation of the ras pathway.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-186284	Tyr361	KVMENFIyESMRYQP	Homo sapiens	Breast Cancer Cell
pmid	sentence
19556341	Phosphorylation of the 361-tyrosine residue is crucial in the up-regulation of aromatase activity. c-src protein directly phosphorylates aromatase on tyrosine 361.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-166718	Tyr373	SEDDEDCyGNYDNLL	Homo sapiens
pmid	sentence
20643654	Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376

Identifier	Residue	Sequence	Organism
SIGNOR-166722	Tyr376	DEDCYGNyDNLLSQF	Homo sapiens
pmid	sentence
20643654	Src-dependent pdk1 tyr373/376 tyrosine phosphorylation. / optimal activation of pdk1 requires phosphorylation of tyr373/376

Publications:

2

Organism:

Homo Sapiens

Pathways:

Axon guidance, Integrin Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276370	Tyr374	PLPPAPAyLSSPLAL	Homo sapiens	HEK-293 Cell
pmid	sentence
23131831	Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146127	Tyr380	TDSEEQPyLEMDLSS	Homo sapiens
pmid	sentence
16619028	Src kinase phosphorylates caspase-8 on tyr380: a novel mechanism of apoptosis suppressionwe identified caspase-8 as a new substrate for src kinase. Phosphorylation occurs on tyr380, situated in the linker region between the large and the small subunits of human procaspase-8, and results in downregulation of caspase-8 proapoptotic function

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-141307	Tyr386	ASNGNLLyIGFRGLD	Homo sapiens
pmid	sentence
16251431	?7 Neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and src-family kinases

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-141311	Tyr442	KILEEVRyIANRFRC	Homo sapiens	Neuron
pmid	sentence
16251431	Alpha7 neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and src-family kinasesmutant alpha7 nachrs lacking cytoplasmic loop tyrosine residues because of alanine replacement of tyr-386 and tyr-442 were more active than wild-type receptorsexpression of active src reduced _7 nachr activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-169273	Tyr391	LEGQEDHyNNLSASK	Homo sapiens
pmid	sentence
21049038	Human k19 tyrosine 391 is phosphorylated, potentially by src kinase, and is the first well-defined tyrosine phosphorylation site of any keratin protein.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-150476	Tyr397	SVSETDDyAEIIDEE	Homo sapiens
pmid	sentence
15735019	Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates

Identifier	Residue	Sequence	Organism
SIGNOR-150480	Tyr407	IIDEEDTyTMPSTRD	Homo sapiens
pmid	sentence
15735019	Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates

Identifier	Residue	Sequence	Organism
SIGNOR-150484	Tyr576	RYMEDSTyYKASKGK	Homo sapiens
pmid	sentence
15735019	Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates

Identifier	Residue	Sequence	Organism
SIGNOR-134212	Tyr577	YMEDSTYyKASKGKL	Homo sapiens
pmid	sentence
15735019	Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-152967	Tyr742	HMVQTNHyQVSGYPG	Homo sapiens	CACO-2 Cell
pmid	sentence
17289681	We propose that fak/c-src bipartite enzyme is a sensor of cytoplasmic shrinkage, and that the phosphorylation on fak tyr-861 by src and subsequent reorganization of f-actin can initiate an anti-apoptotic signaling pathway that protects cells from hyperosmotic stress.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-152971	Tyr861	PIGNQHIyQPVGKPD	Homo sapiens	CACO-2 Cell
pmid	sentence
17289681	We propose that fak/c-src bipartite enzyme is a sensor of cytoplasmic shrinkage, and that the phosphorylation on fak tyr-861 by src and subsequent reorganization of f-actin can initiate an anti-apoptotic signaling pathway that protects cells from hyperosmotic stress.

Identifier	Residue	Sequence	Organism
SIGNOR-150492	Tyr861	PIGNQHIyQPVGKPD	Homo sapiens
pmid	sentence
15735019	Surprisingly, we found that expression of SrcMF or Src251 resulted in increased tyrosine phosphorylation of FAK on Tyr(407), Tyr(576), Tyr(577), and Tyr(861), which are considered to be Src kinase substrates

Identifier	Residue	Organism
SIGNOR-157767		Homo sapiens
pmid	sentence
17828307	Fak y397 phosphorylation promotes src sh2 domain binding to fak, presumably leading to conformational src activation with a fak-src complex.

Publications:

8

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277292	Tyr398	HLGADGVyLDDLTDM	Homo sapiens	HEK-293T Cell
pmid	sentence
33203880	Obesity-associated microenvironmental factors and other Src-activating growth factors, including the epidermal growth factor, activate Src and promote Src-mediated lipin-1 phosphorylation on Tyr398, Tyr413 and Tyr795 residues. The tyrosine phosphorylation of lipin-1 markedly increases its PAP activity, accelerating the synthesis of glycerophospholipids and triglyceride.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277293	Tyr413	DPEVAALyFPKNGDP	Homo sapiens	HEK-293T Cell
pmid	sentence
33203880	Obesity-associated microenvironmental factors and other Src-activating growth factors, including the epidermal growth factor, activate Src and promote Src-mediated lipin-1 phosphorylation on Tyr398, Tyr413 and Tyr795 residues. The tyrosine phosphorylation of lipin-1 markedly increases its PAP activity, accelerating the synthesis of glycerophospholipids and triglyceride.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277291	Tyr795	FPNTEPFyAAFGNRP	Homo sapiens	HEK-293T Cell
pmid	sentence
33203880	Obesity-associated microenvironmental factors and other Src-activating growth factors, including the epidermal growth factor, activate Src and promote Src-mediated lipin-1 phosphorylation on Tyr398, Tyr413 and Tyr795 residues. The tyrosine phosphorylation of lipin-1 markedly increases its PAP activity, accelerating the synthesis of glycerophospholipids and triglyceride.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133870	Tyr402	CSIESDIyAEIPDET	Homo sapiens
pmid	sentence
15695828	These data indicate that pyk2 activation via phosphorylation at tyr-402 requires ?V?3 Ligation and src activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250780	Tyr409	TDGLGLSyLSSHIAN	in vitro
pmid	sentence
10210201	Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624.

Identifier	Residue	Sequence	Organism
SIGNOR-250784	Tyr465	VPVPTNLyGDFFTGD	in vitro
pmid	sentence
10210201	Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624.

Identifier	Residue	Sequence	Organism
SIGNOR-250782	Tyr603	LKTPSAAyLWVGTGA	in vitro
pmid	sentence
10210201	Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624.

Identifier	Residue	Sequence	Organism
SIGNOR-250783	Tyr651	ALGGKAAyRTSPRLK	in vitro
pmid	sentence
10210201	Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also revealed Tyr438 as the most prominent site. Additional minor sites were found using the anti-phosphotyrosine bead immunoprecipitation method followed by MALDI-MS and PSD analysis. These sites, representing approximately 5% of the total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and Tyr624.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-245299	Tyr419	RLIEDNEyTARQGAK	Homo sapiens	HEK-293 Cell
pmid	sentence
11007774	Incubation of the inactivated c-Src with PTP1B results in a dose-dependent reactivation of c-Src tyrosine kinase activity. Incubation of c-Src with 2 or 10 g of PTP1B results in partial or full restoration of c-Src kinase activity, respectively. The activation is accompanied by dephosphorylation of c-Src, both of Tyr-419 and of Tyr-530

Identifier	Residue	Sequence	Organism
SIGNOR-248422	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
17974954	Overexpression of PTP1B increased Src specific activity in colon cancer cells by reducing phosphorylation at Y530 of Src.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276978	Tyr419	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
22898603	In addition, our work further reveals that above a threshold expression level, DEP-1 can also dephosphorylate Src Y418 and attenuate downstream signaling and biologic responses, consistent with the quiescent behavior of confluent endothelial cells that express the highest levels of endogenous DEP-1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277004	Tyr419	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
25301722	SRC activation triggered by loss of PTPRO leads to c-CBL degradation.\|These data corroborate that PTPRO directly dephosphorylates SRC at Y416.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248659	Tyr419	RLIEDNEyTARQGAK	Mus musculus
pmid	sentence
18482983	we identify SHP-2 and PTP-PEST as negative regulators of c-Src kinase \| Inactivation of catalytically active c-Src kinase by the phosphatases SHP-2 or PTP-PEST by dephosphorylation of the tyrosine residue Tyr-416 within the c-Src kinase domain prevents the phosphorylation of villin

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-277009	Tyr419	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
22482061	Antisense- or shRNA mediated downregulation of PTEN induced SRC Tyr416 phosphorylation, SRC activation, and ultimately elevated TZMB resistance, whereas induction of PTEN phosphatase activity directly dephosphorylated SRC Tyr416 residue and so abolished SRC activity .\|These observations indicate that the loss of PTEN phosphatase activity induces SRC activation and so implicates SRC in shaping de novo TZMB resistance in PTEN deficient cells .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247979	Tyr419	RLIEDNEyTARQGAK	Homo sapiens	Lung Adenocarcinoma Cell
pmid	sentence
15489898	The increased Src activity is mainly due to the phosphorylation of Tyr-419, rather than the dephosphorylation of Tyr-530 of Src protein. PDGFR, not FAK or EGFR, appears to be the upstream protein tyrosine kinase responsible for the detachment-induced Src activation in the lung tumor cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-254725	Tyr419	RLIEDNEyTARQGAK	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Identifier	Residue	Sequence	Organism
SIGNOR-254726	Tyr530	FTSTEPQyQPGENL	in vitro
pmid	sentence
25624455	PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248670	Tyr419	RLIEDNEyTARQGAK	Mus musculus
pmid	sentence
18482983	we identify SHP-2 and PTP-PEST as negative regulators of c-Src kinase \| Inactivation of catalytically active c-Src kinase by the phosphatases SHP-2 or PTP-PEST by dephosphorylation of the tyrosine residue Tyr-416 within the c-Src kinase domain prevents the phosphorylation of villin

Publications:

1

Organism:

Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-247984	Tyr419	RLIEDNEyTARQGAK	Homo sapiens
pmid	sentence
15489898	The increased Src activity is mainly due to the phosphorylation of Tyr-419, rather than the dephosphorylation of Tyr-530 of Src protein. PDGFR, not FAK or EGFR, appears to be the upstream protein tyrosine kinase responsible for the detachment-induced Src activation in the lung tumor cells.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Axon guidance, EGFR Signaling, IL6 Signaling, Integrin Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism
SIGNOR-60879	Tyr42	DSMKDEEyEQMVKEL	Homo sapiens
pmid	sentence
9792645	C-src phosphorylates IkappaB On tyrosine 42\|NF-kappaB is sequestered in the cytosol by IkappaBalpha and, in most cells, released upon serine phosphorylation of this inhibitory protein which then undergoes rapid, ubiquitin-dependent degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247346	Tyr420	RYVLDDEyVSSFGAK	Homo sapiens
pmid	sentence
11353545	We further demonstrate that Rlk can be phosphorylated and activated by Src kinases, leading to a decrease in its half-life. A specific tyrosine in the activation loop of Rlk, Y420, is required for phosphorylation and activation, as well as for decreased stability, but is not required for lipid RAFT association.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-246513	Tyr421	RLPSSPVyEDAASFK	in vitro
pmid	sentence
15169891	Erk phosphorylation and a mimicking S405,418D double mutation enhanced cortactin binding and activation of N-WASP. In contrast, Src phosphorylation inhibited the ability of cortactin previously phosphorylated by Erk, and that of S405,418D double mutant cortactin, to bind and activate N-WASP. Furthermore, Y-->D mutation of three tyrosine residues targeted by Src (Y421, Y466, and Y482) inhibited the ability of S405,418D cortactin to activate N-WASP.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276859	Tyr43	ILGASDPyVRVTLYD	Homo sapiens
pmid	sentence
25292214	Activation of c-Src by epidermal growth factor (EGF) also promoted tyrosine phosphorylation and enhanced the activity of NEDD4.

Identifier	Residue	Sequence	Organism
SIGNOR-276860	Tyr585	DGEKGLDyGGVAREW	Homo sapiens
pmid	sentence
25292214	Activation of c-Src by epidermal growth factor (EGF) also promoted tyrosine phosphorylation and enhanced the activity of NEDD4.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247320	Tyr432	KEGWMVHyTSKDTLR	Homo sapiens	HeLa Cell
pmid	sentence
12637538	Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation.

Identifier	Residue	Sequence	Organism
SIGNOR-247324	Tyr463	NDTGSRYyKEIPLSE	Homo sapiens
pmid	sentence
12637538	Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation.

Identifier	Residue	Sequence	Organism
SIGNOR-247328	Tyr502	TTANVVYyVGENVVN	Homo sapiens
pmid	sentence
12637538	Here we report that PKD is tyrosine-phosphorylated within the PH domain, leading to activation. This phosphorylation is mediated by a pathway that consists of the Src and Abl tyrosine kinases and occurs in response to stimulation with pervanadate and oxidative stress. Mutational analysis revealed three tyrosine phosphorylation sites (Tyr(432), Tyr(463), and Tyr(502)), which are regulated by the Src-Abl pathway, and phosphorylation of only one of these (Tyr(463)) leads to PKD activation.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-115705	Tyr435	RDFELSNyDCYGKPI	Homo sapiens	Neuron
pmid	sentence
11882681	These findings indicate that glyr function is upregulated by ptks and this modulation is dependent on the tyrosine-413 residue of the beta subunit.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-184613	Tyr438	RVINDPSyKENVMKL	Homo sapiens
pmid	sentence
19289110	Overexpression of regular or active src, but not dominant-negative src, in 2b7-transfected cos-1 cells increased 2b7 activity and phospho-y438-2b7 by 50%

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-30126	Tyr44	SGASTGIyEALELRD	Homo sapiens
pmid	sentence
7629021	The present finding suggested that the tyrosine residue at position 44 in chicken alpha-enolase is the phosphorylation site by the tyrosine kinase. Our data suggest that eno1 was upregulated by caga protein through activating the src and mek/erk signal pathways

Identifier	Residue	Sequence	Organism
SIGNOR-205092	Tyr44	SGASTGIyEALELRD	Homo sapiens
pmid	sentence
24841372	The present finding suggested that the tyrosine residue at position 44 in chicken alpha-enolase is the phosphorylation site by the tyrosine kinase. Our data suggest that eno1 was upregulated by caga protein through activating the src and mek/erk signal pathways

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-98712	Tyr446	GTEPEPVySMEAADY	Homo sapiens
pmid	sentence
12601080	Cortactin was first identified as a substrate of v-src (46) that mediates in vitro phosphorylation of residues tyr-421, tyr-466, and tyr-482 at the c terminus of the murine ortholog (47). Phosphorylation of these residues attenuates the f-actin cross-linking activity

Identifier	Residue	Sequence	Organism
SIGNOR-98716	Tyr470	AYATEAVyESAEAPG	Homo sapiens
pmid	sentence
12601080	Cortactin was first identified as a substrate of v-src (46) that mediates in vitro phosphorylation of residues tyr-421, tyr-466, and tyr-482 at the c terminus of the murine ortholog (47). Phosphorylation of these residues attenuates the f-actin cross-linking activity

Identifier	Residue	Sequence	Organism
SIGNOR-98720	Tyr486	YPAEDSTyDEYENDL	Homo sapiens
pmid	sentence
12601080	Cortactin was first identified as a substrate of v-src (46) that mediates in vitro phosphorylation of residues tyr-421, tyr-466, and tyr-482 at the c terminus of the murine ortholog (47). Phosphorylation of these residues attenuates the f-actin cross-linking activity

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-178159	Tyr4473	VEIGNPTyKMYEGGE	Homo sapiens
pmid	sentence
18381291	The observation that the wild type protein was phosphorylated to a higher level than the y4473f mutant again indicates that phosphorylation of the tyr4473 residue by v-src is occurring in these cellsmutation of tyr4473 to alanine, which abolishes snx17 binding, resulted in impaired receptor recycling and reduced amounts of the mature form of lrp1 on the cell surface

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-146292	Tyr45	GLEPVGHyEEVELTE	Homo sapiens
pmid	sentence
16640565	Src kinase phosphorylates s6k in the n-terminus. tyrosine y39/45 in s6k1/2 is a substrate for src kinase in vitro. tyrosine y39/45 in s6k1/2 is a substrate for src kinase in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273819	Tyr45	SENNKLTySHGNYLF	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
23471971	We found that TI-VAMP is phosphorylated in vitro by c-Src kinase on tyrosine 45 of the Longin domain.Mimicking tyrosine 45 phosphorylation activates both t-SNARE binding and exocytosis of TI-VAMP.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-101535	Tyr4507	TNFTNPVyATLYMGG	Homo sapiens	HEK-293 Cell
pmid	sentence
12789267	We recently observed that the ldl receptor-related protein 1 (lrp-1) is tyrosine phosphorylated in v-src-transformed cells.Of the four tyrosine residues present in the cytoplasmic domain of lrp-1, only tyr 63 is phosphorylated by v-src in vivo or in vitro. Using fibroblasts deficient in src, yes and fyn, we were able to show that there are multiple kinases present in the cell that can phosphorylate lrp-1. Tyrosine-phosphorylated lrp-1 associates with shc, a ptb and sh2 domain containing signaling protein that is involved in the activation of ras

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246351	Tyr451	TDPEALHyDYIDVEM	Chlorocebus aethiops	COS Cell
pmid	sentence
9655255	In this report, site-directed mutagenesis and a transient expression system that permits co-expression of activated pp60c-src (Src527F) and AFAP-110 in Cos-1 cells were used to identify the SH2-binding motif in AFAP-110. Four tyrosine residues, two in the amino terminus (Y93 and Y94) and two in the carboxy terminus (Y451 and Y453), were mutated to phenylalanine, significantly reducing overall steady-state levels of tyrosine phosphorylation and preventing Src527F from forming a stable complex with AFAP-110.

Identifier	Residue	Sequence	Organism
SIGNOR-246355	Tyr453	PEALHYDyIDVEMSA	Chlorocebus aethiops
pmid	sentence
9655255	In this report, site-directed mutagenesis and a transient expression system that permits co-expression of activated pp60c-src (Src527F) and AFAP-110 in Cos-1 cells were used to identify the SH2-binding motif in AFAP-110. Four tyrosine residues, two in the amino terminus (Y93 and Y94) and two in the carboxy terminus (Y451 and Y453), were mutated to phenylalanine, significantly reducing overall steady-state levels of tyrosine phosphorylation and preventing Src527F from forming a stable complex with AFAP-110.

Identifier	Residue	Sequence	Organism
SIGNOR-246359	Tyr93	TSSLPEGyYEEAVPL	Chlorocebus aethiops
pmid	sentence
9655255	In this report, site-directed mutagenesis and a transient expression system that permits co-expression of activated pp60c-src (Src527F) and AFAP-110 in Cos-1 cells were used to identify the SH2-binding motif in AFAP-110. Four tyrosine residues, two in the amino terminus (Y93 and Y94) and two in the carboxy terminus (Y451 and Y453), were mutated to phenylalanine, significantly reducing overall steady-state levels of tyrosine phosphorylation and preventing Src527F from forming a stable complex with AFAP-110.

Identifier	Residue	Sequence	Organism
SIGNOR-246363	Tyr94	SSLPEGYyEEAVPLS	Chlorocebus aethiops
pmid	sentence
9655255	In this report, site-directed mutagenesis and a transient expression system that permits co-expression of activated pp60c-src (Src527F) and AFAP-110 in Cos-1 cells were used to identify the SH2-binding motif in AFAP-110. Four tyrosine residues, two in the amino terminus (Y93 and Y94) and two in the carboxy terminus (Y451 and Y453), were mutated to phenylalanine, significantly reducing overall steady-state levels of tyrosine phosphorylation and preventing Src527F from forming a stable complex with AFAP-110.

Publications:

4

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-95238	Tyr464	QEGSIEVyEDAGSHY	Homo sapiens
pmid	sentence
12408982	Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity.

Identifier	Residue	Sequence	Organism
SIGNOR-85005	Tyr464	QEGSIEVyEDAGSHY	Homo sapiens
pmid	sentence
11113114	Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity.

Identifier	Residue	Sequence	Organism
SIGNOR-95242	Tyr471	YEDAGSHyLCLLKAR	Homo sapiens
pmid	sentence
12408982	Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity.

Identifier	Residue	Sequence	Organism
SIGNOR-85009	Tyr471	YEDAGSHyLCLLKAR	Homo sapiens
pmid	sentence
11113114	Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-67014	Tyr465	VPVDPATyGQFYGGD	Homo sapiens
pmid	sentence
10210201	Identification of tyr438 as the major in vitro c-src phosphorylation site in human gelsolin recently

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263199	Tyr476	LDSSRRQyQEKYKQV	Homo sapiens	HEK-293 Cell
pmid	sentence
26280531	We identified a highly conserved tyrosine residue in the C-linker of HCN channels (Tyr476 in HCN2) that confers modulation by Src. Replacement of this tyrosine by phenylalanine in HCN2 or HCN4 abolished sensitivity to Src inhibitors. Mass spectrometry confirmed that Tyr476 is phosphorylated by Src. Our results have functional implications for HCN channel gating. Furthermore, they indicate that tyrosine phosphorylation contributes in vivo to the fine tuning of HCN channel activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160056	Tyr488	DVYDDGKyVYVVTEL	Homo sapiens	HEK-293 Cell
pmid	sentence
18156174	The results showed that tyr-488 is a major site of src but mutations at tyr-529 or tyr-707 did not significantly decrease src-dependent tyrosine phosphorylation of rsk2 (fig. 4c). However, we have previously characterized the tyr-488 site that is also phosphorylated by fgfr3 (14), and substitution of tyr-488 did not affect rsk2 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273537	Tyr489	SEPVKDPyVMFPQNA	Homo sapiens	HEK-293 Cell
pmid	sentence
24378532	Through deletion and base substitution mutagenesis we have identified Tyr489 of PLEKHG2 as the site phosphorylated by cSrc.Furthermore, PLEKHG2 is tyrosine phosphorylated at Tyr489 by ephrinB2 receptor signaling via cSrc. Investigation of the physiological function of tyrosine phosphorylation at Tyr489 in PLEKHG2 remains a subject for future studies.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273808	Tyr489	SEPVKDPyVMFPQNA	Homo sapiens	HEK-293 Cell
pmid	sentence
24378532	Through deletion and base substitution mutagenesis we have identified Tyr489 of PLEKHG2 as the site phosphorylated by cSrc.The interaction between PLEKHG2 and the full-length of PIK3R3, but not ABL1, occurs in a tyrosine-phosphorylation-dependent manner.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276074	Tyr490	HCAAWHGyYSVAKAL	Homo sapiens	HEK-293T Cell
pmid	sentence
17803936	Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276073	Tyr491	CAAWHGYySVAKALC	Homo sapiens	HEK-293T Cell
pmid	sentence
17803936	Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246471	Tyr493	NKMNEVTySTLNFEA	Homo sapiens	HEK-293 Cell
pmid	sentence
9867848	Recent reports have also suggested that Bgp1 behaves as a signal transduction molecule. Several physiological events promote the Tyr phosphorylation of Bgp1 on one or two Tyr residues within its cytoplasmic domain (Tyr-488 and Tyr-515). BGP becomes Tyr-phosphorylated by Src-like Tyr kinases in activated neutrophils (24) and in human colon carcinoma cellsWe have recently shown that Tyr phosphorylation of the mouse Bgp1 cytoplasmic domain in CT51 mouse colonic carcinoma cells led to its binding to the protein-Tyr phosphatase SHP-1 and that this event required the presence of both Tyr-488 and Tyr-515

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246475	Tyr520	LTATEIIySEVKKQ	Homo sapiens	HEK-293 Cell
pmid	sentence
9867848	Recent reports have also suggested that Bgp1 behaves as a signal transduction molecule. Several physiological events promote the Tyr phosphorylation of Bgp1 on one or two Tyr residues within its cytoplasmic domain (Tyr-488 and Tyr-515). BGP becomes Tyr-phosphorylated by Src-like Tyr kinases in activated neutrophils (24) and in human colon carcinoma cellsWe have recently shown that Tyr phosphorylation of the mouse Bgp1 cytoplasmic domain in CT51 mouse colonic carcinoma cells led to its binding to the protein-Tyr phosphatase SHP-1 and that this event required the presence of both Tyr-488 and Tyr-515

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-128273	Tyr504	APIPSVPyAPFAAIL	Homo sapiens
pmid	sentence
15320955	C3g is activated upon phosphorylation at tyrosine 504 c3g is phosphorylated in vivo on y504 upon coexpression with src or hck, two members of the src family tyrosine kinases.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263200	Tyr505	EGEEEEEyLDKINPI	in vitro
pmid	sentence
10962558	An inhibitor specific for Src family kinase or expression of Csk reduced tyrosine phosphorylation of nectin-2delta. In addition, Src kinase tyrosine phosphorylates the recombinant cytoplasmic region of nectin-2delta in vitro. The major tyrosine phosphorylation site of nectin-2delta was Tyr505 in the cytoplasmic region

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-264705	Tyr508	DMSASAGyEEISDPD	Homo sapiens
pmid	sentence
20943948	C-Src-mediated phosphorylation of NoxA1 and Tks4 induces the reactive oxygen species (ROS)-dependent formation of functional invadopodia in human colon cancer cells\|Here, we show that the interaction of noxa1 and tks proteins is dependent on src activity. Interestingly, the abolishment of src-mediated phosphorylation of tyr110 on noxa1 and of tyr508 on tks4 blocks their binding and decreases nox1-dependent ros generation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-205120	Tyr523	REDSVLSyETVTQME	Homo sapiens
pmid	sentence
24981431	These results indicate that psd-95 phosphorylation by src facilitates the integration of pyk2 to psd-95 signal complex, the activation of pyk2/src, as well as the subsequent tyrosine phosphorylation of nr2a, which ultimately results in the upregulation of nmda receptor function and synaptic transmission.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160052	Tyr529	TITKTVEyLHAQGVV	Homo sapiens	HEK-293 Cell
pmid	sentence
18156174	Together, our findings suggest that src-dependent phosphorylation at tyr-529 facilitates inactive erk binding to rsk2, which might be a general requirement for rsk2 activation by egf through the mek/erk pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-179417	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
18614016	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).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248438	Tyr530	FTSTEPQyQPGENL	Mus musculus	NIH-3T3 Cell
pmid	sentence
10698938	Protein tyrosine phosphatase alpha (PTPalpha) is believed to dephosphorylate physiologically the Src proto-oncogene at phosphotyrosine (pTyr)527, a critical negative-regulatory residue. It thereby activates Src, and PTPalpha overexpression neoplastically transforms NIH 3T3 cells.

Identifier	Residue	Sequence	Organism
SIGNOR-248437	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
17974954	Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B

Publications:

2

Organism:

Mus Musculus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-124774	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
15143158	Ptpd1 activates src tyrosine kinase and increases the magnitude and duration of epidermal growth factor (egf) signaling.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-43315	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
8755732	Rapid digestion of pp60c-src tyrosine kinase (src TK) in combination with electrospray ionization mass spectrometry enabled the determination of the time course for autophosphorylation of three tyrosine sites (Y338, Y419, and Y530) and a correlation with src TK activity. Here, conditions were identified which promoted essentially complete autophosphorylation of y530. Phosphorylation of y530 was directly correlated to a decrease in tyrosine kinase activity

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-248671	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
17974954	Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-248705	Tyr530	FTSTEPQyQPGENL	Rattus norvegicus
pmid	sentence
15735685	The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue

Identifier	Residue	Sequence	Organism
SIGNOR-276977	Tyr530	FTSTEPQyQPGENL	Rattus norvegicus
pmid	sentence
26556953	Expression of Dep1 in transformed rat thyroid PCMPSV cells increased Src activity via Y527 dephosphorylation (corresponding to Y530 in human Src) without affecting the level of phosphorylated Y416 (Y419 in human Src).\|Reciprocally, Dep1 can be phosphorylated by Src and Fyn on Y1311 and Y1320, leading to the dephosphorylation of Y530 Src by Dep1 .

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-277086	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
19350555	PTP-PEST increases dephosphorylation of Src at Y527 and activates it.\|The data presented here supports our hypothesis that PTP-PEST activates Src via dephosphorylating it at Y527 (Tyr530 in human c-Src equivalent to Tyr527 in chicken Src).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248454	Tyr530	FTSTEPQyQPGENL	Mus musculus
pmid	sentence
19088431	LMWPTP dephosphorylated pY(527)-Src and pY(416)-Src in vitro, with greater specificity for pY(527)Src. Activation of LMWPTP produced strong activation of Src mediated by fast dephosphorylation of pY(527)-Src, followed by slower deactivation of this kinase via dephosphorylation of pY(416)Src.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-238074	Tyr530	FTSTEPQyQPGENL	Chlorocebus aethiops
pmid	sentence
15522235	PTPepsilonM activated c-Src kinase probably by directly dephosphorylating phospho-Tyr527, a negative regulatory site of c-Src.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-103607	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
12857726	The tyrosine kinase pp60c-src has also been identified as a good substrate of ptp1b leading to an activation of this kinase (27).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251145	Tyr530	FTSTEPQyQPGENL	in vitro
pmid	sentence
9208935	An eicosapeptide encompassing the C-terminal tail of c-Src (Tyr527) which is conserved in most Src-related protein kinases, is phosphorylated by C-terminal Src kinase (CSK) and by the two Src-related protein kinases c-Fgr and Lyn, with similar kinetic constants.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248473	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
9261115	To determine whether the COOH-terminal or other phosphotyrosine residues within Src are subject to dephosphorylation by SHP-1, the effects of this phosphatase on Src tyrosine phosphorylation were initially examined using CNBr cleavage analysis. As illustrated in Fig.1 A, CNBr treatment of 32P-labeled human Src has been shown previously to yield phosphorylated cleavage fragments of about 31, 9.7, and 4.7 kDa, which, respectively, contain the Src NH2-terminal region encompassing the major sites for serine phosphorylation on Src, Ser-12 and Ser-17 (31-kDa fragment), the inhibitory tyrosine phosphorylation site, Tyr-530 (4.7-kDa fragment), and a key site for autophosphorylation on activated Src, Tyr-419 [} These observations, together with the finding of reduced Src activity in HEY cells expressing a dominant negative form of SHP-1, provide compelling evidence that SHP-1 functions include the positive regulation of Src activation.

Identifier	Residue	Sequence	Organism
SIGNOR-248472	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
17974954	Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248725	Tyr530	FTSTEPQyQPGENL	Homo sapiens
pmid	sentence
15143158	Dephosphorylation of Y527 was more pronounced in cells expressing PTPD1 at each time point tested. PTPD1C1108S drastically inhibited Y527 dephosphorylation\|Activation of src requires dephosphorylation of src residue Y527. This promotes displacement of the SH2 domain from this residue and subsequent autophosphorylation of residue Y416 within the activation loop

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-32014	Tyr530	FTSTEPQyQPGENL	Homo sapiens	Neuron
pmid	sentence
7691597	Endogenous pp60c-src kinase activity is enhanced in the rptp alpha-transfected cells, which may be due to direct dephosphorylation of the regulatory tyr residue at position 527 in pp60c-src by rptp alpha.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158707	Tyr531	RRQYQEKyKQVEQYM	Homo sapiens
pmid	sentence
17977941	These results demonstrate that src tyrosine kinase enhances hcn4 currents by shifting their activation to more positive potentials and increasing the whole cell channel conductance as well as speeding the channel kinetics. The tyrosine residue that mediates most of src s actions on hcn4 channels is tyr531.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-120488	Tyr536	QKGQESEyGNITYPP	Homo sapiens
pmid	sentence
14699166	Recombinant shp-1 had elevated activity subsequent to phosphorylation by src in vitro, and shp-1 variants with mutated phosphorylation sites in the c terminus, shp-1 y538f, and shp-1 y538f,y566f were less active toward src-generated phosphoproteins in intact cells.

Identifier	Residue	Sequence	Organism
SIGNOR-120492	Tyr564	SKHKEDVyENLHTKN	Homo sapiens
pmid	sentence
14699166	Recombinant shp-1 had elevated activity subsequent to phosphorylation by src in vitro, and shp-1 variants with mutated phosphorylation sites in the c terminus, shp-1 y538f, and shp-1 y538f,y566f were less active toward src-generated phosphoproteins in intact cells.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-55857	Tyr537	CKNVVPLyDLLLEML	Homo sapiens	Breast Cancer Cell, HeLa Cell
pmid	sentence
9500442	Although the molecular mechanisms underlying ligand-independent activation of era are not completely understood, phosphorylation of a serine residue in af1 has been implicated in the response to epidermal growth factor. Era is also a target for tyrosine phosphorylation, anda single tyrosine residue located immediately adjacent to af2 has been identified as a substrate for src-family tyrosine kinases.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154564	Tyr54	YLKERRVyVTLTCAF	Homo sapiens
pmid	sentence
17456551	Using fluorescently tagged proteins combined with resonance energy transfer and image cross-correlation spectroscopy approaches, we show in live cells that beta2-adaptin phosphorylation is an important regulatory process for the dissociation of beta-arrestin-AP-2 complexes in CCPs. Finally, we show that beta2-adaptin phosphorylation is involved in the early steps of receptor internalization. Our findings not only unveil beta2-adaptin as a new Src target during AT1R internalization, but also support the role of receptor-mediated signaling in the control of clathrin-dependent endocytosis of receptors.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-131189	Tyr55	AIRNTNEyTEGPTVV	Homo sapiens
pmid	sentence
15564375	Activation of signalling by fibroblast growth factor receptor leads to phosphorylation of the signalling attenuator human sprouty 2 (hspry2) on residue y55. we show that hspry2 is a direct substrate for src family kinases, including src itself.Phosphorylation of hspry2 is required for hspry2 to inhibit activation of the extracellular signal-regulated kinase pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-251100	Tyr551	RYVLDDEyTSSVGSK	Homo sapiens
pmid	sentence
8629002	This interaction of BTK with SRC kinases transphosphorylated BTK on tyrosine at residue 551, which led to BTK activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-75330	Tyr566	RYVLDDQyVSSVGTK	Homo sapiens
pmid	sentence
10688651	Coexpression of v-src and etk led to a transphosphorylation on tyrosine 566 of etk and subsequent autophosphorylation. These events correlated with a substantial increase in the kinase activity of etk.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154006	Tyr573	GTPRRLLyCQRSLLD	Homo sapiens
pmid	sentence
17389600	We show that mt1-mmp is phosphorylated on the unique tyrosine residue located within this cytoplasmic sequence (tyr(573)) and that this phosphorylation requires the kinase src. accordingly, overexpression of a nonphosphorylable mt1-mmp mutant (y573f) blocked sphingosine-1-phosphate-induced migration of human umbilical vein endothelial cells and ht-1080 (human fibrosarcoma) cells and failed to stimulate migration of cells lacking the enzyme (bovine aortic endothelial cells).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188308	Tyr59	SSSAASSySFSDLNS	Homo sapiens	HeLa Cell
pmid	sentence
19789182	Src phosphorylated emerin specifically at y59, y74 and y95; interestingly y-to-f substitutions at identified src sites reduced recombinant emerin binding to endogenous baf

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188312	Tyr74	TRGDADMyDLPKKED	Homo sapiens	HeLa Cell
pmid	sentence
19789182	Src phosphorylated emerin specifically at y59, y74 and y95; interestingly y-to-f substitutions at identified src sites reduced recombinant emerin binding to endogenous baf

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188316	Tyr95	KGYNDDYyEESYFTT	Homo sapiens	HeLa Cell
pmid	sentence
19789182	Src phosphorylated emerin specifically at y59, y74 and y95; interestingly y-to-f substitutions at identified src sites reduced recombinant emerin binding to endogenous baf

Publications:

3

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276850	Tyr590	RFSPYEWyNPHPCNP	Homo sapiens	HEK-293 Cell
pmid	sentence
25201974	GluK2 binds to Src, and the tyrosine residue at position 590 (Y590) on GluK2 is a major site of phosphorylation by Src kinases. GluK2 phosphorylation at Y590 is responsible for increases in whole-cell currents and calcium influx in response to transient kainate stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-246104	Tyr594	TYVDPHTyEDPNQAV	Homo sapiens
pmid	sentence
24457997	SRC phosphorylates EPHA2 on Tyr594\|. It is therefore likely that this phosphorylation site is included in the binding motif of an additional signalling molecule required for cell transformation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277539	Tyr597	NTEQRNVyKDLRQIE	Mus musculus	NIH-3T3 Cell
pmid	sentence
33113375	We used cSrc-transformed NIH 3T3 fibroblasts to examine the effect of mutant Dyn2Y597. Similar to its effect in myotubes, Dyn2Y597F presented reduced enrichment at podosomes, whereas Dyn2Y597E clearly targeted podosome rosettes (Figures S9B and S9C). Moreover, Dyn2Y597F significantly reduced the podosome area, ECM degradation ability, and lifespan of the podosome in cSrc-transformed NIH 3T3 fibroblasts, whereas Dyn2Y597E displayed contradictory effects (Figures S9D–S9G).

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276655	Tyr612	LLTAALWyIYSHTRS	Homo sapiens	HMEC-1 Cell
pmid	sentence
25070888	We identified epidermal growth factor (EGF) and vascular endothelial growth factor (VEGF) as Src-activators that induce endoglin turnover following (612)YIY(614) phosphorylation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276654	Tyr614	TAALWYIySHTRSPS	Homo sapiens	HMEC-1 Cell
pmid	sentence
25070888	We identified epidermal growth factor (EGF) and vascular endothelial growth factor (VEGF) as Src-activators that induce endoglin turnover following (612)YIY(614) phosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277598	Tyr625	RSGTMNSyEMRKALE	in vitro
pmid	sentence
35697802	CAPN2 itself was a bone fide substrate of SRC that was primarily phosphorylated at Y625 by SRC and exhibited increased proteolysis activity upon phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263195	Tyr63	LKELFEPyGAVYQIN	in vitro
pmid	sentence
17855367	Site-directed mutagenesis of putative tyrosine phosphorylation sites in CUGBP2 identified tyrosine 39 as a c-Src target, and a CUGBP2 with a mutated tyrosine 39 displayed an attenuated ability to bind COX-2 mRNA.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-118206	Tyr64	DTAGQEDyDRLRPLS	Homo sapiens
pmid	sentence
14506284	Epidermal growth factor-dependent regulation of cdc42 is mediated by the src tyrosine kinaseegf signaling through src appears to have dual regulatory effects on cdc42: 1). it leads to the activation of cdc42 as mediated by the vav2 guanine nucleotide exchange factor, and 2). it results in the phosphorylation of cdc42, which stimulates the binding of rhogdi, perhaps to direct the movement of cdc42 to a specific cellular site to trigger a signaling response, because cdc42-rhogdi interactions are essential for cdc42-induced cellular transformation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-247310	Tyr644	RNEGTATyAAAVLFR	Homo sapiens
pmid	sentence
14517306	Tyrosine phosphorylation of plakoglobin causes contrary effects on its association with desmosomes and adherens junction components and modulates beta-catenin-mediated transcriptionFor instance, Src, which mainly phosphorylates Tyr86 in beta-catenin, modifies Tyr643 in plakoglobin, decreasing the interaction with E-cadherin and alpha-catenin and increasing the interaction with the alpha-catenin-equivalent protein in desmosomes, desmoplakin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-134459	Tyr649	TDERSWVySPLHYSA	Homo sapiens
pmid	sentence
15738269	Phosphorylation by src of the tyrosine adjacent to s650 (y649 in human pipki gamma) was shown to enhance pipki gamma targeting to focal adhesions. We find that y649 phosphorylation does not stimulate directly pipki gamma binding to talin, but may do so indirectly by inhibiting s650 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-274008	Tyr650	PMELEPMySNVNPGD	in vitro
pmid	sentence
12051764	Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2.

Identifier	Residue	Sequence	Organism
SIGNOR-274010	Tyr662	PGDSNPIySQIWSIQ	in vitro
pmid	sentence
12051764	Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2.

Identifier	Residue	Sequence	Organism
SIGNOR-274007	Tyr692	HEELTVLySELKKTH	in vitro
pmid	sentence
12051764	Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2.

Identifier	Residue	Sequence	Organism
SIGNOR-274009	Tyr722	EEDDEENyENVPRVL	in vitro
pmid	sentence
12051764	Tyrosine phosphorylation of SPAP2a by c-Src and in vitro. Tyrosine-phosphorylated SPAP2 is specifically associated with SH2 domain-containing tyrosine kinases Syk and Zap70 and SH2 domain-containing tyrosine phosphatases SHP-1 and SHP-2. Site-specific mutagenesis studies revealed that tyrosyl residues 650 and 662 embedded in the ITIMs are responsible for the binding of Syk and Zap70 while tyrosyl residues 692 and 722 embedded in the ITIMs are involved in interactions with SHP-1 and SHP-2.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-106454	Tyr654	RNEGVATyAAAVLFR	Homo sapiens
pmid	sentence
11279024	Beta-catenin is a good substrate of pp60c- src tyrosine kinase in vitro;this kinase modifies specifically tyr-86 and tyr-654,although consistently detected, this negative effect of tyr-86 phosphorylation on tbp binding was clearly less important than the positive effect observed after tyr-654 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246462	Tyr658	GEMDTTSyDVSVLNS	Cricetulus griseus	CHO Cell
pmid	sentence
16027153	cadherins also act to prevent epithelial cell motilityCadherin-cytoskeletal interactions occur through a number of adaptor proteins that interact with the C-terminal portion of the cadherin cytoplasmic tail, including the _-, _-, and _-catenin (6, 10). Additionally, VE-cadherin stability at the plasma membrane may be regulated by the binding of p120-catenin to the juxtamembrane region of the cytoplasmic tailWe show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Tyr-658 and Tyr-731, via tyrosine kinase activation or phosphatase inactivation was sufficient to prevent the binding of p120- and beta-catenin, respectively, to the cytoplasmic tail of VE-cadherinVE-cadherin becomes phosphorylated on Tyr-658 and/or Tyr-731 in response to Src kinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246466	Tyr731	PYDTLHIyGYEGSES	Cricetulus griseus	CHO Cell
pmid	sentence
16027153	cadherins also act to prevent epithelial cell motilityCadherin-cytoskeletal interactions occur through a number of adaptor proteins that interact with the C-terminal portion of the cadherin cytoplasmic tail, including the _-, _-, and _-catenin (6, 10). Additionally, VE-cadherin stability at the plasma membrane may be regulated by the binding of p120-catenin to the juxtamembrane region of the cytoplasmic tailWe show here that tyrosine phosphorylation of the adherens junction protein VE-cadherin at two critical tyrosines, Tyr-658 and Tyr-731, via tyrosine kinase activation or phosphatase inactivation was sufficient to prevent the binding of p120- and beta-catenin, respectively, to the cytoplasmic tail of VE-cadherinVE-cadherin becomes phosphorylated on Tyr-658 and/or Tyr-731 in response to Src kinase activity.

Publications:

2

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-111189	Tyr66	DPTIEDSyTKICSVD	Homo sapiens	HEK-293 Cell
pmid	sentence
11682467	The small gtpase, r-ras, affects cell adhesion by maintaining integrin activity. Activated src oncogene phosphorylates r-ras and suppresses integrin activity. the src phosphorylation site in r-ras was tyrosine 66

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-78706	Tyr67	NASLESLySACSMQS	Homo sapiens
pmid	sentence
10871840	Grb10 tyrosine phosphorylation was stimulated by expression of constitutively active src or fyn in cells and by incubation with purified src or fyn in vitro. The insulin stimulated or src/fyn-mediated tyrosine phosphorylation in vivo was significantly reduced when grb10 tyrosine 67 was changed to glycine. This mutant form of grb10 bound with higher affinity to the ir in cells than that of the wild-type protein, suggesting that tyrosine phosphorylation of grb10 may normally negatively regulate its binding to the ir.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-99002	Tyr679	DRPKDEVySKYYTPV	Homo sapiens
pmid	sentence
12621061	Stat5 is activated by a broad spectrum of cytokines, as well as non-receptor tyrosine kinases, such as src. these conformational differences may in part be due to differential effects of prl and src on stat5b tyrosine phosphorylation, since src induced several additional sites of tyrosine phosphorylation of stat5b at residues other than tyr-699, including tyr-724 and tyr-679.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188352	Tyr68	GQTVDDPyATFVKML	Homo sapiens
pmid	sentence
19802004	Tyrosine phosphorylation of cofilin at y68 by v-src leads to its degradation through ubiquitin-proteasome pathway

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-148818	Tyr685	LDARPSLyAQVQKPP	Homo sapiens
pmid	sentence
16909109	In vitro src assay, the ve-cadherin cytoplasmic domain is directly phosphorylated by purified src as well as the tyrosine residue 685 (tyr)685-containing peptide finally, we found that in a vegf-induced wound-healing assay, cadherin adhesive activity was impaired by src kinase inhibitors.RPSLY(685)aqvq.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary

Identifier	Residue	Sequence	Organism
SIGNOR-103769	Tyr69	PVPNQPVyNQPVYNQ	Homo sapiens
pmid	sentence
12871937	Plscr1 is phosphorylated by c-src, within the tandem repeat sequence 68vynqpvynqp77.\|The EGF-mediated Interaction between PLSCR1 and Shc Requires Phosphorylation of Tyr69 and Tyr74 in PLSCR1

Identifier	Residue	Sequence	Organism
SIGNOR-103773	Tyr74	PVYNQPVyNQPVGAA	Homo sapiens
pmid	sentence
12871937	Plscr1 is phosphorylated by c-src, within the tandem repeat sequence 68vynqpvynqp77.\|The EGF-mediated Interaction between PLSCR1 and Shc Requires Phosphorylation of Tyr69 and Tyr74 in PLSCR1

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-111078	Tyr694	LAKAVDGyVKPQIKQ	Homo sapiens
pmid	sentence
11641791	Src can thus directly tyrosine-phosphorylate the activation site of stat5 (tyr 694 in stat5a), and src may contribute to epo-induced signal transduction via stat5.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-235696	Tyr701	DGPKGTGyIKTELIS	Homo sapiens
pmid	sentence
14978237	The tyr701 phosphorylation of signal transducer and activator of transcription 1 (stat1) induced by interferon-gamma (ifn-gamma) and 12-o-tetradecanoylphorbol 13-acetate (tpa) was inhibited by the protein kinase c (pkc) inhibitor staurosporine, the tyrosine kinase inhibitor herbimycin, or the src kinase inhibitor pp2. An association between c-src and stat1 was increased by ifn-gamma and tpa, indicating the direct phosphorylation of stat1 by pkc-dependent c-src activation.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Lung

Pathways:

EGFR Signaling, IL6 Signaling, Rhabdomyosarcoma

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247341	Tyr705	DPGSAAPyLKTKFIC	Homo sapiens	HEK-293 Cell
pmid	sentence
14551213	In the present study, we have delineated the mechanism by which Galpha16 stimulates STAT3 in human embryonic kidney 293 cells. A constitutively active Galpha16 mutant, Galpha16QL, stimulated STAT3-dependent luciferase activity as well as the phosphorylation of STAT3 at both Tyr705 and Ser727.The involvement of tyrosine kinases such as c-Src and Janus kinase 2 and 3 (JAK2 and JAK3) in Galpha16QL-induced activation of STAT3 was illustrated by the combined use of selective inhibitors and dominant negative mutants.

Identifier	Residue	Organism	Cell Line
SIGNOR-235445		Mus musculus	NIH-3T3 Cell
pmid	sentence
9566874	Previous studies have demonstrated that one STAT family member, Stat3, possesses constitutively elevated tyrosine phosphorylation and DNA-binding activity in fibroblasts stably transformed by the Src oncoprotein.We conclude that Stat3 activation by the Src oncoprotein leads to specific gene regulation and that Stat3 is one of the critical signaling pathways involved in Src oncogenesis.

Publications:

2

Organism:

Homo Sapiens, Mus Musculus

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-102097	Tyr707	QDPPPELyFVKVDVT	Homo sapiens
pmid	sentence
12808100	Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via src kinase family-dependent phosphorylation of tyrosine 707

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277335	Tyr732	YDRLVDEySLNAGKQ	Homo sapiens	HEK-293T Cell
pmid	sentence
28054552	Mechanistically, c-Src phosphorylation of HK1 at Tyr732 robustly decreases its Km and increases its Vmax by disrupting its dimer formation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-246457	Tyr734	KDNDSHVyAVIEDTM	Homo sapiens
pmid	sentence
14739293	Phosphorylation of gp140 and p80 are mediated by Src family kinases at multiple Tyr residues including Tyr(734).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140728	Tyr736	FGMSRNLySGDYYRI	Homo sapiens
pmid	sentence
16186108	Here, using baculoviral co-expression of the ddr2 cytosolic domain and src, we show that src targets three tyrosine residues (tyr-736, tyr-740, and tyr-741) in the activation loop of ddr2 for phosphorylation. This phosphorylation by src stimulates ddr2 cis-autophosphorylation of additional tyrosine residues.

Identifier	Residue	Sequence	Organism
SIGNOR-140763	Tyr740	RNLYSGDyYRIQGRA	Homo sapiens
pmid	sentence
16186108	Here, using baculoviral co-expression of the ddr2 cytosolic domain and src, we show that src targets three tyrosine residues (tyr-736, tyr-740, and tyr-741) in the activation loop of ddr2 for phosphorylation. This phosphorylation by src stimulates ddr2 cis-autophosphorylation of additional tyrosine residues.

Identifier	Residue	Sequence	Organism
SIGNOR-140767	Tyr741	NLYSGDYyRIQGRAV	Homo sapiens
pmid	sentence
16186108	Here, using baculoviral co-expression of the ddr2 cytosolic domain and src, we show that src targets three tyrosine residues (tyr-736, tyr-740, and tyr-741) in the activation loop of ddr2 for phosphorylation. This phosphorylation by src stimulates ddr2 cis-autophosphorylation of additional tyrosine residues.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181743	Tyr737	THRQGHIyMEMNFTN	Homo sapiens
pmid	sentence
18938240	The phosphorylation of beta2-adaptin on tyrosine residue 737 (y737) negatively regulates its interaction with betaarrestin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-152831	Tyr74	HKPLEGKyEWQEVEK	Homo sapiens
pmid	sentence
17254967	Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-152835	Tyr88	KGSLPEFyYRPPRPP	Homo sapiens	Breast Cancer Cell
pmid	sentence
17254967	Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-152839	Tyr89	GSLPEFYyRPPRPPK	Homo sapiens	Breast Cancer Cell
pmid	sentence
17254967	Src regulates p27 stability through phosphorylation of p27 at tyrosine 74 and tyrosine 88. Our data indicate that phosphorylation by src impairs the cdk2 inhibitory action of p27

Publications:

3

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-274005	Tyr758	GDTRVFLyELLPESP	in vitro
pmid	sentence
18581049	We establish that Src activity is indispensable for the interaction of Crn7 with Golgi membranes. Crn7 binds Src in vivo and can be phosphorylated by recombinant Src in vitro. We demonstrate that tyrosine-758 is the major Src phosphorylation site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-247202	Tyr773	DTANNPLyKEATSTF	Homo sapiens	HOS Cell
pmid	sentence
11723131	The phosphorylation level of beta(3) integrin was modulated using a temperature-sensitive v-Src kinase. Increased beta(3) phosphorylation abolished alpha(v)beta(3)- but not alpha(5)beta(1)-mediated adhesion to fibronectin. Thus, phosphorylation of the cytoplasmic domain of beta(3) is a negative regulator of alpha(v)beta(3)-fibronectin binding strength.

Identifier	Residue	Sequence	Organism
SIGNOR-247207	Tyr785	STFTNITyRGT	Homo sapiens
pmid	sentence
11723131	The phosphorylation level of beta(3) integrin was modulated using a temperature-sensitive v-Src kinase. Increased beta(3) phosphorylation abolished alpha(v)beta(3)- but not alpha(5)beta(1)-mediated adhesion to fibronectin. Thus, phosphorylation of the cytoplasmic domain of beta(3) is a negative regulator of alpha(v)beta(3)-fibronectin binding strength.

Publications:

2

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-247316	Tyr783	EGRNPGFyVEANPMP	in vitro
pmid	sentence
7682059	The phosphorylation of purified phospholipase C-gamma 1 (PLC-gamma 1) and PLC-gamma 2 by src-family-protein tyrosine kinases (PTKs) P56lck, p53/56lyn, p59hck, p59fyn, and p60src was studied in vitro. All five PTKs phosphorylated PLC-gamma 1 and PLC-gamma 2, suggesting that both PLC-gamma isozymes can be phosphorylated in cells by any of the src-family PTKs in response to the activation of cell surface receptors.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-274048	Tyr797	TLMSVPRyLPRPANP
pmid	sentence
31286874	Activated c-Src phosphorylated E-cadherin at the tyrosine 797 site to initiate RNF43-mediated E-cadherin ubiquitination at lysine 816 and subsequent degradation

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-111306	Tyr798	YIDAFSDyANFK	Homo sapiens
pmid	sentence
7518772	Transient overexpression of c-src together with rptp alpha in human embryonic kidney 293 cells increased phosphorylation of tyr789, suggesting that c-src may phosphorylate rptp alpha in vivo.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-266367	Tyr8	MAQFDTEyQRLEASY	Homo sapiens
pmid	sentence
27934868	Src phosphorylates mATG9 at Tyr8 to maintain its endocytic and constitutive trafficking in unstressed conditions. In response to starvation, phosphorylation of mATG9 at Tyr8 by Src and at Ser14 by ULK1 functionally cooperate to promote interactions between mATG9 and the AP1/2 complex, leading to redistribution of mATG9 from the plasma membrane and juxta-nuclear region to the peripheral pool for autophagy initiation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276857	Tyr80	LLDACGFyWGPLSVH	in vitro
pmid	sentence
31101761	SOCS1 is phosphorylated on Y80 by SRC family kinase members SRC and YES1.

Publications:

1

Organism:

In Vitro

Pathways:

IL6 Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-277520	Tyr81	WEVGSITyDTLSAQA	Homo sapiens
pmid	sentence
32653904	Two kinases, i.e. abelson-tyrosine protein kinase (ABL)1 and Src were identified as eNOS Tyr81 kinases as their inhibition and down-regulation significantly reduced the basal and Yoda1-induced tyrosine phosphorylation and activity of eNOS.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184772	Tyr828	RMDSEDVyDDVETIP	Homo sapiens
pmid	sentence
19296573	Cd133 (prominin-1) is phosphorylated on cytoplasmic tyrosine-828 and tyrosine-852 by src

Identifier	Residue	Sequence	Organism
SIGNOR-184776	Tyr852	GYHKDHVyGIHNPVM	Homo sapiens
pmid	sentence
19296573	Cd133 (prominin-1) is phosphorylated on cytoplasmic tyrosine-828 and tyrosine-852 by src

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143234	Tyr852	NDPTAPPyDSLLVFD	Homo sapiens
pmid	sentence
16371504	Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-143238	Tyr860	DSLLVFDyEGSGSTA	Homo sapiens	Melanoma Cell
pmid	sentence
16371504	Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-143242	Tyr884	SSGGEQDyDYLNDWG	Homo sapiens	Melanoma Cell
pmid	sentence
16371504	Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-143246	Tyr886	GGEQDYDyLNDWGPR	Homo sapiens	Melanoma Cell
pmid	sentence
16371504	Src-mediated phosphorylation of the n-cadherin cytoplasmic domain results in a significant reduction in beta-catenin bindingbeta-catenin dissociates from n-cadherin and redistributes to the nucleus of transmigrating melanoma cells to activate gene transcription.Because there were only four tyrosine residues (y852, y860, y884, and y886) in this peptide, all of them were phosphorylated.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276342	Tyr859	KKVSSTHyYLLPERP	in vitro
pmid	sentence
36178070	We identified two Src phosphorylation sites within the MHR (Y859, Y860). Addition of Src-phosphorylated MHR to the Ack1 KD enhanced enzymatic activity.

Identifier	Residue	Sequence	Organism
SIGNOR-276341	Tyr860	KVSSTHYyLLPERPS	in vitro
pmid	sentence
36178070	We identified two Src phosphorylation sites within the MHR (Y859, Y860). Addition of Src-phosphorylated MHR to the Ack1 KD enhanced enzymatic activity.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-106458	Tyr86	VADIDGQyAMTRAQR	Homo sapiens	SW-480 Cell
pmid	sentence
11279024	beta-catenin is a good substrate of pp60c- srctyrosine kinase in vitro;this kinase modifies specifically tyr-86 and tyr-654although consistently detected, this negative effect of tyr-86 phosphorylation on tbp binding was clearly less important than the positive effect observed after tyr-654 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263977	Tyr88	PQSSSPVyGSSAKTS	Homo sapiens	HT-29 Cell
pmid	sentence
27447856	Here, we demonstrate that Src kinase directly phosphorylates Y88 paxillin\|In this study, we also show how pY88 paxillin transduces a signal to activate Akt

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-101655	Tyr892	PYRSPPPyVPP	Homo sapiens
pmid	sentence
12795607	Tyrosine 892 is now thought to be the principal site for recognition by the c-src tyrosine kinase;. We show that upon tyrosine phosphorylation, beta-dystroglycan undergoes a profound change in its sub-cellular localization (e.g., from the plasma membrane to an internal membrane compartment). One possibility is that the net negative charge at position 892 causes the redistribution of beta-dystroglycan to this intracellular vesicular location

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-109533	Tyr9	ARTTSQLyDAVPIQS	Homo sapiens
pmid	sentence
11481331	Using site-directed mutants, we show that, although phosphorylation on tyr-373/376 is important for pdk1 activity, phosphorylation on tyr-9 has no effect on the activity of the kinase. Both of these residues can be phosphorylated by v-src tyrosine kinase in vitro, and co-expression of v-src leads to tyrosine phosphorylation and activation of pdk1.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism
SIGNOR-103999	Tyr900	EHAPAEMyDIMKTCW	Homo sapiens
pmid	sentence
12878163	C-src phosphorylates tyr900 in the second part of the kinase domain of c-kit.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-157716	Tyr95	KFPECGFyGMYDKIL	Homo sapiens
pmid	sentence
17804414	Critical for the regulation of pkd1 activity in response to oxidative stress are src- and abl-mediated tyrosine phosphorylations that eventually lead to protein kinase cdelta (pkcdelta)-mediated activation of pkd1. our data suggest that pkd1 phosphorylation at tyr95 generates a binding motif for pkcdelta, and that oxidative stress-mediated pkcdelta/pkd interaction results in pkd1 activation loop phosphorylation and activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-92931	Tyr986	NSFNNPAyYVLEGVP	Homo sapiens
pmid	sentence
12235291	Ship2 could be phosphorylated in vitro by recombinant src kinase and tyrosines 986-987 in the npxy motif of ship2 appear to be the major sites of phosphorylation for src both in vitro and in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-92935	Tyr987	SFNNPAYyVLEGVPH	Homo sapiens
pmid	sentence
12235291	Ship2 could be phosphorylated in vitro by recombinant src kinase and tyrosines 986-987 in the npxy motif of ship2 appear to be the major sites of phosphorylation for src both in vitro and in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276612	Tyr99	REMLEGFyEEISKGR	Mus musculus
pmid	sentence
24331927	Our results show that only Src can efficiently phosphorylate FHOD1 at Y99 to enable the downstream activation by ROCK.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-258089		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-254741		Homo sapiens
pmid	sentence
25624455	PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264706
pmid	sentence
20943948	Recently, we have shown that tyrosine kinase c-Src substrate Tks4 and Tks5 proteins are novel members of the organizer superfamily

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-270262		Homo sapiens	Neuron
pmid	sentence
11882681	These findings indicate that glyr function is upregulated by ptks and this modulation is dependent on the tyrosine-413 residue of the beta subunit.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney

Identifier	Residue	Organism
SIGNOR-260314		Mus musculus
pmid	sentence
26059978	Importantly, coimmunoprecipitation of SR-BI and Src demonstrated that the two proteins are directly associated in WT macrophages (Fig. 7B), suggesting that SR-BI plays a direct role in activation of Src in macrophages.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251109
pmid	sentence
23967200	C-Src-induced STAT3 activation regulates MMP3 levels

Publications:

1

Identifier	Residue	Organism
SIGNOR-258264		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-268372		Homo sapiens
pmid	sentence
15494734	Here we show that different regions of the intracellular domain of DCC directly interacted with the tyrosine kinases Src and focal adhesion kinase (FAK). Netrin activated both FAK and Src and stimulated tyrosine phosphorylation of DCC. Inhibition of Src family kinases reduced DCC tyrosine phosphorylation and blocked both axon attraction and outgrowth of neurons in response to netrin. Mutation of the tyrosine phosphorylation residue in DCC abolished its function of mediating netrin-induced axon attraction. On the basis of our observations, we suggest a model in which DCC functions as a kinase-coupled receptor, and FAK and Src act immediately downstream of DCC in netrin signaling.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-206280		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251108
pmid	sentence
15345719	In this study, we investigated the possible role of the Gβγ heterodimer in signaling Gi-induced Src activation

Publications:

1

Identifier	Residue	Organism
SIGNOR-191304		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270248		Homo sapiens
pmid	sentence
24841372	The present finding suggested that the tyrosine residue at position 44 in chicken alpha-enolase is the phosphorylation site by the tyrosine kinase. Our data suggest that eno1 was upregulated by caga protein through activating the src and mek/erk signal pathways

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-113767		Homo sapiens
pmid	sentence
11782488	Herbimycin a and pp2, specific inhibitors of src family kinases, both inhibited h2o2-mediated c-src and bmk1 activation.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Organism	Cell Line
SIGNOR-254740		Homo sapiens	Monocyte
pmid	sentence
25624455	PTKs of the JAK and SRC families have a regulatory role in LFA-1 affinity triggering, with JAKs showing a positive role (3), whereas SRCs possibly have a negative role.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-102354		Homo sapiens	Breast Cancer Cell
pmid	sentence
12810717	Tiam1 cooperated with src to induce activation of rac1 in vivo and the formation of membrane ruffles.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-247966		Homo sapiens	U2-OS Cell
pmid	sentence
18069897	We show that PR55gamma binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-261267		Homo sapiens	HeLa Cell
pmid	sentence
11003644	Splicing of the c-src N1 exon in neuronal cells depends in part on an intronic cluster of RNA regulatory elements called the downstream control sequence (DCS). \|nPTB binds more stably to the DCS RNA than PTB does but is a weaker repressor of splicing in vitro. nPTB also greatly enhances the binding of two other proteins, hnRNP H and KSRP, to the DCS RNA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-277132		Homo sapiens
pmid	sentence
27314562	Collectively, these results suggest that PTPRB inhibits Src activation and down -- regulation of PTPRB activates Src signalling pathway required for cell invasion in A549 cells.\|Knockdown of PTPRB increased Src phosphorylation and cell invasion, which was reversed by Src inhibitor PP2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-196751		Homo sapiens	Lung Cancer Cell
pmid	sentence
22439932	Ror1 binds to and phosphorylates c-src / ror1 kinase-dependent c-src activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-263196		Homo sapiens	HEK-293 Cell
pmid	sentence
8647432	Phosphorylation of multiple tyrosine-containing motifs found on Sin correlated with c-Crk and cellular phosphoprotein binding to Sin as well as increased c-Src activity. These data suggest that (1) SH2 and SH3 ligand sites on Sin cooperatively activate the signaling potential of c-Src, (2) Sin acts as both an activator and a substrate for c-Src, and (3) phosphorylated Sin may serve as a signaling effector molecule for Src by binding to multiple cellular proteins.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190699		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-193624		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-256526		in vitro
pmid	sentence
11007482	Here we demonstrate that Galphas and Galphai, but neither Galphaq, Galpha12 nor Gbetay, directly stimulate the kinase activity of downregulated c-Src

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-206691		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-194925		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-113776		Homo sapiens
pmid	sentence
11782488	Herbimycin a and pp2, specific inhibitors of src family kinases, both inhibited h2o2-mediated c-src and bmk1 activation.

Identifier	Residue	Organism
SIGNOR-93549		Homo sapiens
pmid	sentence
12351660	Treatment of l6 cells with pp2 or su6656, specific inhibitors of src family kinases, and transient transfection of dominant-inhibitory src inhibited the formation of myotubes and expression of myogenin.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain, Myotube

Identifier	Residue	Organism
SIGNOR-217442		Homo sapiens
pmid	sentence
12707358	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Identifier	Residue	Organism
SIGNOR-217439		Homo sapiens
pmid	sentence
12645577	These results indicate that c-src can associate with ikkbeta and phosphorylate its tyrosine residues after tnf-alfa or tpa stimulation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-271870		Homo sapiens	HEK-293 Cell
pmid	sentence
21937427	These data support an idea that Amotl2 Tyr-103 can be phosphorylated by FGF receptor tyrosine kinase activity. We then determined whether Amotl2 Tyr-103 is required for its interaction with c-Src. \|Amotl2 promotes MAPK/ERK activation via c-Src, which is dependent on phosphorylation of tyrosine residue at position 103 but independent of the C-terminal PDZ-binding domain.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258103		in vitro
pmid	sentence
22037378	Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. \| The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-235888		Homo sapiens
pmid	sentence
17251915	Ep2 can also promote the transactivation of epidermal growth factor receptor (egfr) expressed in colon cancer cells through src, which activates the proteolytic release of the egfr ligands amphiregulin (ar) and transforming growth factor-alfa (tgfalfa)125, thereby stimulating the egfr- network.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251107
pmid	sentence
15345719	In this study, we investigated the possible role of the Gβγ heterodimer in signaling Gi-induced Src activation

Publications:

1

Identifier	Residue	Organism
SIGNOR-47152		Homo sapiens
pmid	sentence
9096340	Expression of v-src, a transforming nonreceptor tyrosine kinase, results in ras activation, and ras function in nih 3t3 cells suppresses transformation by v-src, indicating that in these cells ras-dependent signaling pathways are required for v-src to exert its biological effects.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-158954		Homo sapiens
pmid	sentence
17991704	N attractive hypothesis consistent with our present data is that the gef responsible for rac activation in mce cells may be activated by src family kinase tyrosine phosphorylationour results present a novel mechanism by which the pi3k and src signaling cascades cooperate to activate rac and promote intestinal epithelial cell migration downstream of egfr.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-256527		in vitro
pmid	sentence
11007482	Here we demonstrate that Galphas and Galphai, but neither Galphaq, Galpha12 nor Gbetay, directly stimulate the kinase activity of downregulated c-Src

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-267796		Homo sapiens	Neuron
pmid	sentence
11882681	These findings indicate that glyr function is upregulated by ptks and this modulation is dependent on the tyrosine-413 residue of the beta subunit.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney

Identifier	Residue	Organism
SIGNOR-86008		Homo sapiens
pmid	sentence
11389730	The phosphorylation of p120-gap by p60c-src inhibited its ability to stimulate the ha-ras-gtpase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-265179		Homo sapiens	HEK-293 Cell
pmid	sentence
19535918	UNC80 is a protein that is associated with the NALCN Na(+) leak cation channel, and is required for the activation of this channel by the neuropeptide substance P through GPCRs in a G-protein-independent fashion. Here, we show that UNC80 binds Src kinases and recruits Src into the channel complex.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-236537		Homo sapiens
pmid	sentence
17251915	Ep2 can also promote the transactivation of epidermal growth factor receptor (egfr) expressed in colon cancer cells through src, which activates the proteolytic release of the egfr ligands amphiregulin (ar) and transforming growth factor-alfa (tgfalfa)125, thereby stimulating the egfr- network.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-177116		Homo sapiens
pmid	sentence
22080863	We found that tcptp dephosphorylates and inactivates src family kinases to regulate t cell responses._

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-236534		Homo sapiens
pmid	sentence
17251915	Ep2 can also promote the transactivation of epidermal growth factor receptor (egfr) expressed in colon cancer cells through src, which activates the proteolytic release of the egfr ligands amphiregulin (ar) and transforming growth factor-alfa (tgfalfa)125, thereby stimulating the egfr- network.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Identifier	Residue	Organism
SIGNOR-101002		Homo sapiens
pmid	sentence
12730241	Insulin receptor-phosphorylated irs5/dok4 associates with rasgap, crk, src, and fyn, but not phosphatidylinositol 3-kinase p85, grb2, shp-2, nck, or phospholipase cgamma src homology 2 domains, and activates mapk in cells.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle, Kidney

Identifier	Residue	Organism
SIGNOR-178610		Homo sapiens
pmid	sentence
18455992	Instead, shh rapidly and locally stimulated phosphorylation of the src family kinase (sfk) members src and fyn in a smo-dependent fashion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-266101		Homo sapiens	HEK-293 Cell
pmid	sentence
26037143	Here we report that Src binds to and phosphorylates Kindlin-2 at Y193. Reciprocally, Kindlin-2-Y193 phosphorylation activates and maintains Src kinase activity. Kindlin-2-Y193 phosphorylation is also involved in its binding capacity with Migfilin and the recruitment of Migfilin to the focal adhesions. Functionally, we demonstrate that Kindlin-2-Y193 phosphorylation regulates Kindlin-2-mediated cell spreading and migration.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-261274		in vitro
pmid	sentence
9858532	We show here that this component of the DCS complex is hnRNP H and that, like hnRNP F and KSRP, hnRNP H is needed for src N1 splicing in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-259056		Homo sapiens
pmid	sentence
30889378	SRC can directly phosphorylate and inhibit LATS

Publications:

1

Organism:

Homo Sapiens

Pathways: