MGI:Src

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000166	nucleotide binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0547	F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:2429328 PMID:11274221^[1]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:4414728 PMID:19920076^[2]	IDA: Inferred from Direct Assay		F	From MGI
	GO:0004672	protein kinase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0004713	protein tyrosine kinase activity	MGI:MGI:2680875 PMID:14636584^[3]	IMP: Inferred from Mutant Phenotype		F	From MGI
	GO:0004713	protein tyrosine kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	MGI:MGI:2152096	IEA: Inferred from Electronic Annotation	EC:2.7.10.2	F	From MGI
	GO:0005080	protein kinase C binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0005102	receptor binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0005102	receptor binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0005158	insulin receptor binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3040548 PMID:14739300^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9QVP9	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3694172 PMID:16298995^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P54763	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3696626 PMID:16267818^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P07141	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3698674 PMID:17000758^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q640L3	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4414728 PMID:19920076^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q60838	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4441150 PMID:10220404^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q8T4F7	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4834990 PMID:18289379^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P70315	F	From MGI
	GO:0005524	ATP binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0067	F	From MGI
	GO:0005524	ATP binding	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR000719 InterPro:IPR017441	F	From MGI
	GO:0005634	nucleus	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0539	C	From MGI
	GO:0005737	cytoplasm	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0963	C	From MGI
	GO:0005739	mitochondrion	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0496	C	From MGI
	GO:0005743	mitochondrial inner membrane	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	C	From MGI
	GO:0005856	cytoskeleton	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0206	C	From MGI
	GO:0005886	plasma membrane	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	C	From MGI
	GO:0005901	caveola	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	C	From MGI
	GO:0005901	caveola	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	C	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:2429328 PMID:11274221^[1]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:3589701 PMID:15937334^[10]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0006468	protein phosphorylation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	P	From MGI
	GO:0007049	cell cycle	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0131	P	From MGI
	GO:0007155	cell adhesion	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0130	P	From MGI
	GO:0007243	intracellular protein kinase cascade	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	P	From MGI
	GO:0008022	protein C-terminus binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0008283	cell proliferation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0010628	positive regulation of gene expression	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0010740	positive regulation of intracellular protein kinase cascade	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0010907	positive regulation of glucose metabolic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0014069	postsynaptic density	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	C	From MGI
	GO:0014911	positive regulation of smooth muscle cell migration	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0016020	membrane	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0472	C	From MGI
	GO:0016301	kinase activity	MGI:MGI:2664443 PMID:12808090^[11]	IMP: Inferred from Mutant Phenotype		F	From MGI
	GO:0016477	cell migration	MGI:MGI:3526739 PMID:15292044^[12]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0016740	transferase activity	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0808	F	From MGI
	GO:0016772	transferase activity, transferring phosphorus-containing groups	MGI:MGI:2152098	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F	From MGI
	GO:0018105	peptidyl-serine phosphorylation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0018108	peptidyl-tyrosine phosphorylation	MGI:MGI:3629864 PMID:12526740^[13]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0019717	synaptosome	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	C	From MGI
	GO:0019899	enzyme binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0019901	protein kinase binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0019904	protein domain specific binding	MGI:MGI:1344938 PMID:8438166^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q06649	F	From MGI
	GO:0020037	heme binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0030331	estrogen receptor binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0030900	forebrain development	MGI:MGI:3590439 PMID:16162939^[15]	IGI: Inferred from Genetic Interaction	MGI:MGI:95602	P	From MGI
	GO:0031954	positive regulation of protein autophosphorylation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0032148	activation of protein kinase B activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0032403	protein complex binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0033146	regulation of intracellular estrogen receptor signaling pathway	MGI:MGI:3589531 PMID:16007215^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857247	P	From MGI
	GO:0034332	adherens junction organization	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0042169	SH2 domain binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0043065	positive regulation of apoptotic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0043406	positive regulation of MAP kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0043552	positive regulation of phosphatidylinositol 3-kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0044325	ion channel binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0045056	transcytosis	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0045453	bone resorption	MGI:MGI:3040548 PMID:14739300^[4]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0045737	positive regulation of cyclin-dependent protein kinase activity	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0045785	positive regulation of cell adhesion	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0045892	negative regulation of transcription, DNA-dependent	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0045893	positive regulation of transcription, DNA-dependent	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0046628	positive regulation of insulin receptor signaling pathway	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0046777	protein autophosphorylation	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0046875	ephrin receptor binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	F	From MGI
	GO:0046875	ephrin receptor binding	MGI:MGI:5294305 PMID:12925710^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q8CBF3	F	From MGI
	GO:0048011	nerve growth factor receptor signaling pathway	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0048477	oogenesis	MGI:MGI:3589531 PMID:16007215^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857247	P	From MGI
	GO:0050715	positive regulation of cytokine secretion	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0050839	cell adhesion molecule binding	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	F	From MGI
	GO:0051222	positive regulation of protein transport	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0060065	uterus development	MGI:MGI:3589531 PMID:16007215^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857247	P	From MGI
	GO:0060444	branching involved in mammary gland duct morphogenesis	MGI:MGI:3589531 PMID:16007215^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857247	P	From MGI
	GO:0070374	positive regulation of ERK1 and ERK2 cascade	MGI:MGI:3690285 PMID:17045821^[18]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0070374	positive regulation of ERK1 and ERK2 cascade	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:0070555	response to interleukin-1	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	P	From MGI
	GO:0090263	positive regulation of canonical Wnt receptor signaling pathway	MGI:MGI:4414728 PMID:19920076^[2]	IGI: Inferred from Genetic Interaction	MGI:MGI:98956 UniProtKB:Q08463	P	From MGI
	GO:2000573	positive regulation of DNA biosynthetic process	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	NCBI:NP_114183	P	From MGI
	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	P	From MGI
	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P12931	P	From MGI
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Andreev J et al. (2001) Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade. J Biol Chem 276: 20130-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Yokoyama N & Malbon CC (2009) Dishevelled-2 docks and activates Src in a Wnt-dependent manner. J Cell Sci 122: 4439-51 PubMed GONUTS page
↑ Ishibe S et al. (2003) Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol Cell 12: 1275-85 PubMed GONUTS page
↑ ^4.0 ^4.1 Miyazaki T et al. (2004) Src kinase activity is essential for osteoclast function. J Biol Chem 279: 17660-6 PubMed GONUTS page
↑ Moeller ML et al. (2006) EphB receptors regulate dendritic spine morphogenesis through the recruitment/phosphorylation of focal adhesion kinase and RhoA activation. J Biol Chem 281: 1587-98 PubMed GONUTS page
↑ Cross M et al. (2005) A proteomics strategy for the enrichment of receptor-associated complexes. Proteomics 5: 4754-63 PubMed GONUTS page
↑ Kostenko EV et al. (2006) Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs. Mol Cell Biol 26: 8964-75 PubMed GONUTS page
↑ Ahern-Djamali SM et al. (1999) Identification of profilin and src homology 3 domains as binding partners for Drosophila enabled. Proc Natl Acad Sci U S A 96: 4977-82 PubMed GONUTS page
↑ Ma T et al. (2008) Dramatic inhibition of osteoclast sealing ring formation and bone resorption in vitro by a WASP-peptide containing pTyr294 amino acid. J Mol Signal 3: 4 PubMed GONUTS page
↑ Auger R et al. (2005) A role for mitogen-activated protein kinase(Erk1/2) activation and non-selective pore formation in P2X7 receptor-mediated thymocyte death. J Biol Chem 280: 28142-51 PubMed GONUTS page
↑ Holgado-Madruga M & Wong AJ (2003) Gab1 is an integrator of cell death versus cell survival signals in oxidative stress. Mol Cell Biol 23: 4471-84 PubMed GONUTS page
↑ Ziehr J et al. (2004) Alterations in cell-adhesive and migratory properties of proximal tubule and collecting duct cells from bcl-2 -/- mice. Am J Physiol Renal Physiol 287: F1154-63 PubMed GONUTS page
↑ Bock HH & Herz J (2003) Reelin activates SRC family tyrosine kinases in neurons. Curr Biol 13: 18-26 PubMed GONUTS page
↑ Ren R et al. (1993) Identification of a ten-amino acid proline-rich SH3 binding site. Science 259: 1157-61 PubMed GONUTS page
↑ Kuo G et al. (2005) Absence of Fyn and Src causes a reeler-like phenotype. J Neurosci 25: 8578-86 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Kim H et al. (2005) c-Src-null mice exhibit defects in normal mammary gland development and ERalpha signaling. Oncogene 24: 5629-36 PubMed GONUTS page
↑ Vindis C et al. (2003) EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis. J Cell Biol 162: 661-71 PubMed GONUTS page
↑ Shi X et al. (2006) CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex. Immunity 25: 595-606 PubMed GONUTS page

[PMID:11274221-0] 1.0 ^1.1 Andreev J et al. (2001) Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade. J Biol Chem 276: 20130-5 PubMed GONUTS page

[PMID:19920076-1] 2.0 ^2.1 ^2.2 Yokoyama N & Malbon CC (2009) Dishevelled-2 docks and activates Src in a Wnt-dependent manner. J Cell Sci 122: 4439-51 PubMed GONUTS page

[PMID:14636584-2] Ishibe S et al. (2003) Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol Cell 12: 1275-85 PubMed GONUTS page

[PMID:14739300-3] 4.0 ^4.1 Miyazaki T et al. (2004) Src kinase activity is essential for osteoclast function. J Biol Chem 279: 17660-6 PubMed GONUTS page

[PMID:16298995-4] Moeller ML et al. (2006) EphB receptors regulate dendritic spine morphogenesis through the recruitment/phosphorylation of focal adhesion kinase and RhoA activation. J Biol Chem 281: 1587-98 PubMed GONUTS page

[PMID:16267818-5] Cross M et al. (2005) A proteomics strategy for the enrichment of receptor-associated complexes. Proteomics 5: 4754-63 PubMed GONUTS page

[PMID:17000758-6] Kostenko EV et al. (2006) Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs. Mol Cell Biol 26: 8964-75 PubMed GONUTS page

[PMID:10220404-7] Ahern-Djamali SM et al. (1999) Identification of profilin and src homology 3 domains as binding partners for Drosophila enabled. Proc Natl Acad Sci U S A 96: 4977-82 PubMed GONUTS page

[PMID:18289379-8] Ma T et al. (2008) Dramatic inhibition of osteoclast sealing ring formation and bone resorption in vitro by a WASP-peptide containing pTyr294 amino acid. J Mol Signal 3: 4 PubMed GONUTS page

[PMID:15937334-9] Auger R et al. (2005) A role for mitogen-activated protein kinase(Erk1/2) activation and non-selective pore formation in P2X7 receptor-mediated thymocyte death. J Biol Chem 280: 28142-51 PubMed GONUTS page

[PMID:12808090-10] Holgado-Madruga M & Wong AJ (2003) Gab1 is an integrator of cell death versus cell survival signals in oxidative stress. Mol Cell Biol 23: 4471-84 PubMed GONUTS page

[PMID:15292044-11] Ziehr J et al. (2004) Alterations in cell-adhesive and migratory properties of proximal tubule and collecting duct cells from bcl-2 -/- mice. Am J Physiol Renal Physiol 287: F1154-63 PubMed GONUTS page

[PMID:12526740-12] Bock HH & Herz J (2003) Reelin activates SRC family tyrosine kinases in neurons. Curr Biol 13: 18-26 PubMed GONUTS page

[PMID:8438166-13] Ren R et al. (1993) Identification of a ten-amino acid proline-rich SH3 binding site. Science 259: 1157-61 PubMed GONUTS page

[PMID:16162939-14] Kuo G et al. (2005) Absence of Fyn and Src causes a reeler-like phenotype. J Neurosci 25: 8578-86 PubMed GONUTS page

[PMID:16007215-15] 16.0 ^16.1 ^16.2 ^16.3 Kim H et al. (2005) c-Src-null mice exhibit defects in normal mammary gland development and ERalpha signaling. Oncogene 24: 5629-36 PubMed GONUTS page

[PMID:12925710-16] Vindis C et al. (2003) EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis. J Cell Biol 162: 661-71 PubMed GONUTS page

[PMID:17045821-17] Shi X et al. (2006) CD44 is the signaling component of the macrophage migration inhibitory factor-CD74 receptor complex. Immunity 25: 595-606 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Src ( synonyms: pp60c-src )
Protein Name(s)	Rous sarcoma oncogene,
External Links
MGI	MGI:98397

MGI:Src

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