RAT:SRC

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Src
Protein Name(s)	Proto-oncogene tyrosine-protein kinase Src Proto-oncogene c-Src pp60c-src p60-Src
External Links
UniProt	Q9WUD9
EMBL	AF130457 AF157016 AABR06027223 CH474005 CH474005 CH474005 CH474005 CH474005 DQ120509 DQ120510
RefSeq	NP_114183.1 XP_008760609.1 XP_008760610.1 XP_008760611.1
UniGene	Rn.112600
BioGrid	249840
DIP	DIP-42731N
IntAct	Q9WUD9
MINT	MINT-1488989
STRING	10116.ENSRNOP00000012739
ChEMBL	CHEMBL3014
iPTMnet	Q9WUD9
PhosphoSite	Q9WUD9
PaxDb	Q9WUD9
PRIDE	Q9WUD9
Ensembl	ENSRNOT00000012739 ENSRNOT00000080516
GeneID	83805
KEGG	rno:83805
UCSC	RGD:620795
CTD	6714
RGD	620795
eggNOG	KOG0197 COG0515
GeneTree	ENSGT00760000118938
HOGENOM	HOG000233858
HOVERGEN	HBG008761
InParanoid	Q9WUD9
KO	K05704
OMA	CQCWRKD
OrthoDB	EOG7GTT2V
TreeFam	TF351634
BRENDA	2.7.10.2
Reactome	R-RNO-1227986 R-RNO-1295596 R-RNO-1433557 R-RNO-1433559 R-RNO-177929 R-RNO-180292 R-RNO-186763 R-RNO-191647 R-RNO-354192 R-RNO-354194 R-RNO-372708 R-RNO-389356 R-RNO-389513 R-RNO-3928662 R-RNO-3928663 R-RNO-3928664 R-RNO-3928665 R-RNO-418592 R-RNO-418885 R-RNO-430116 R-RNO-437239 R-RNO-4420097 R-RNO-456926 R-RNO-5218921 R-RNO-5607764 R-RNO-5663220 R-RNO-5673000
NextBio	35583878
PRO	PR:Q9WUD9
Proteomes	UP000002494
Genevisible	Q9WUD9
GO	GO:0005884 GO:0005901 GO:0005829 GO:0070062 GO:0031234 GO:0005770 GO:0005764 GO:0005743 GO:0043005 GO:0005634 GO:0048471 GO:0005886 GO:0014069 GO:0032587 GO:0005524 GO:0050839 GO:0019899 GO:0030331 GO:0070851 GO:0020037 GO:0005158 GO:0044325 GO:0016301 GO:0004715 GO:0008022 GO:0032403 GO:0019901 GO:0005080 GO:0004713 GO:0005102 GO:0032148 GO:0034332 GO:0086098 GO:0045453 GO:0060444 GO:0007049 GO:0016477 GO:0008283 GO:0071398 GO:0071498 GO:0071456 GO:0032869 GO:0071222 GO:0036120 GO:0071393 GO:0034614 GO:0007173 GO:0030900 GO:0045087 GO:0007229 GO:0035556 GO:2000811 GO:0043154 GO:2001237 GO:0051895 GO:2001243 GO:0051902 GO:0032463 GO:0045892 GO:0048011 GO:0048477 GO:0036035 GO:0018105 GO:0038083 GO:0043065 GO:0090263 GO:0045785 GO:0045737 GO:0050715 GO:2000573 GO:0010634 GO:0070374 GO:0010628 GO:0010907 GO:0046628 GO:1902533 GO:2000394 GO:0043406 GO:0043552 GO:0010641 GO:0071803 GO:0031954 GO:0051897 GO:0051222 GO:0014911 GO:0045893 GO:0050847 GO:0046777 GO:0031648 GO:2001286 GO:0060491 GO:0042127 GO:0022407 GO:2000641 GO:0033146 GO:0071801 GO:0043393 GO:0010447 GO:0042493 GO:0051602 GO:0070542 GO:0042542 GO:0070555 GO:0009612 GO:0051385 GO:0031667 GO:0009615 GO:0016337 GO:0043149 GO:0034446 GO:0045056 GO:0007179 GO:0060065
Gene3D	3.30.505.10
InterPro	IPR011009 IPR000719 IPR017441 IPR001245 IPR000980 IPR001452 IPR008266 IPR020635
Pfam	PF07714 PF00017 PF00018
PRINTS	PR00401 PR00452 PR00109
SMART	SM00252 SM00326 SM00219
SUPFAM	SSF50044 SSF55550 SSF56112
PROSITE	PS00107 PS50011 PS00109 PS50001 PS50002

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0038083	peptidyl-tyrosine autophosphorylation	PMID:18583343^[1]	ECO:0000315			P		Figure 5 shows src autophosphorylation of src involving its own tyrosine amino acid residues.	complete CACAO 11815
involved_in	GO:0071393	cellular response to progesterone stimulus	PMID:21440892^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051895	negative regulation of focal adhesion assembly	PMID:21440892^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050847	progesterone receptor signaling pathway	PMID:21440892^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000573	positive regulation of DNA biosynthetic process	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16530387^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045737	positive regulation of cyclin-dependent protein serine/threonine kinase activity	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045453	bone resorption	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P05480	P		Seeded From UniProt	complete
involved_in	GO:0043552	positive regulation of phosphatidylinositol 3-kinase activity	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043406	positive regulation of MAP kinase activity	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032148	activation of protein kinase B activity	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031954	positive regulation of protein autophosphorylation	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12931	F		Seeded From UniProt	complete
involved_in	GO:0018105	peptidyl-serine phosphorylation	PMID:16530387^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010641	positive regulation of platelet-derived growth factor receptor signaling pathway	PMID:16530387^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:16530387^[3]	ECO:0000303	author statement without traceable support used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P12003	C		Seeded From UniProt	complete
part_of	GO:0099091	postsynaptic specialization, intracellular component	PMID:14529711^[4]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0099091	postsynaptic specialization, intracellular component	PMID:14529711^[4]	ECO:0000279	western blot evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:9005855^[5]	ECO:0006054	pharmacological assay evidence used in manual assertion		C	part_of:(UBERON:0002240)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:14529711^[4]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:9005855^[5]	ECO:0006013	patch-clamp recording evidence used in manual assertion		C	part_of:(UBERON:0002240)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:14529711^[4]	ECO:0000279	western blot evidence used in manual assertion		C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:0098962	regulation of postsynaptic neurotransmitter receptor activity	PMID:9005855^[5]	ECO:0006054	pharmacological assay evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002240)	Seeded From UniProt	complete
involved_in	GO:0098962	regulation of postsynaptic neurotransmitter receptor activity	PMID:9005855^[5]	ECO:0006013	patch-clamp recording evidence used in manual assertion		P	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002240)	Seeded From UniProt	complete
involved_in	GO:2000386	positive regulation of ovarian follicle development	PMID:22905678^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902533	positive regulation of intracellular signal transduction	PMID:19713443^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0098609	cell-cell adhesion	PMID:15591141^[8]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071456	cellular response to hypoxia	PMID:20380727^[9]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071398	cellular response to fatty acid	PMID:20149623^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071222	cellular response to lipopolysaccharide	PMID:20149623^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070542	response to fatty acid	PMID:19736311^[11]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051602	response to electrical stimulus	PMID:20356829^[12]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051385	response to mineralocorticoid	PMID:16157790^[13]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051222	positive regulation of protein transport	PMID:15007081^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0050839	cell adhesion molecule binding	PMID:19948503^[15]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:67396	F		Seeded From UniProt	complete
involved_in	GO:0050715	positive regulation of cytokine secretion	PMID:19736311^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048011	neurotrophin TRK receptor signaling pathway	PMID:15546918^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046628	positive regulation of insulin receptor signaling pathway	PMID:14985360^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045785	positive regulation of cell adhesion	PMID:15735685^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045056	transcytosis	PMID:15007081^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:20197063^[19]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2737 RGD:68424	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:12618293^[20]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2641 RGD:2737 RGD:68424	F		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:15304482^[21]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:69222	F		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	PMID:11834728^[22]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:68395	F		Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:15322113^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	PMID:19737347^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0042542	response to hydrogen peroxide	PMID:12226102^[25]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	PMID:20149623^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034332	adherens junction organization	PMID:15389520^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032869	cellular response to insulin stimulus	PMID:19952103^[27]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031667	response to nutrient levels	PMID:20357031^[28]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:22203672^[29]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:1561386	F		Seeded From UniProt	complete
enables	GO:0030331	estrogen receptor binding	PMID:14751567^[30]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2581	F		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:12700184^[31]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:1306273	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:15069201^[32]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620556	F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:22905678^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0014911	positive regulation of smooth muscle cell migration	PMID:19736311^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:20356829^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010907	positive regulation of glucose metabolic process	PMID:19230846^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:20333648^[34]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:19763735^[35]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010447	response to acidic pH	PMID:12081562^[36]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:20333648^[34]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0009612	response to mechanical stimulus	PMID:15731459^[37]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008283	cell population proliferation	PMID:15856020^[38]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:19737347^[24]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:11373	F		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:15856020^[38]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005901	caveola	PMID:20167931^[39]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:6253989^[40]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005158	insulin receptor binding	PMID:19952103^[27]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2917	F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:11478920^[41]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2737	F		Seeded From UniProt	complete
enables	GO:0005080	protein kinase C binding	PMID:19952103^[27]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:61925	F		Seeded From UniProt	complete
enables	GO:0005080	protein kinase C binding	PMID:15337529^[42]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:67383	F		Seeded From UniProt	complete
enables	GO:0005080	protein kinase C binding	PMID:14751567^[30]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3395	F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:12488346^[43]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001545	primary ovarian follicle growth	PMID:22905678^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000701142 UniProtKB:P12931	P		Seeded From UniProt	complete
involved_in	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000701142 UniProtKB:P12931	P		Seeded From UniProt	complete
enables	GO:0070851	growth factor receptor binding	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000701142 UniProtKB:P12931	F		Seeded From UniProt	complete
involved_in	GO:0050847	progesterone receptor signaling pathway	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000701142 RGD:620795	P		Seeded From UniProt	complete
involved_in	GO:0045453	bone resorption	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98397 PANTHER:PTN000701142	P		Seeded From UniProt	complete
involved_in	GO:0038083	peptidyl-tyrosine autophosphorylation	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002521528 UniProtKB:Q9H3Y6 WB:WBGene00005077	P		Seeded From UniProt	complete
involved_in	GO:0036035	osteoclast development	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98397 PANTHER:PTN000701142	P		Seeded From UniProt	complete
part_of	GO:0031234	extrinsic component of cytoplasmic side of plasma membrane	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002521528 UniProtKB:P08631	C		Seeded From UniProt	complete
involved_in	GO:0030154	cell differentiation	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002521528 RGD:621423	P		Seeded From UniProt	complete
involved_in	GO:0007173	epidermal growth factor receptor signaling pathway	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000701142 RGD:620795	P		Seeded From UniProt	complete
involved_in	GO:0007169	transmembrane receptor protein tyrosine kinase signaling pathway	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002521528 UniProtKB:P07948	P		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0262733 PANTHER:PTN002521528 RGD:2641 RGD:620795 RGD:621017 UniProtKB:P12931	F		Seeded From UniProt	complete
enables	GO:0004715	non-membrane spanning protein tyrosine kinase activity	PMID:21873635^[44]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:95527 PANTHER:PTN002521528 UniProtKB:P09769 UniProtKB:P51451 UniProtKB:Q13882 WB:WBGene00005077	F		Seeded From UniProt	complete
involved_in	GO:2000588	positive regulation of platelet-derived growth factor receptor-beta signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:1900182	positive regulation of protein localization to nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0086098	angiotensin-activated signaling pathway involved in heart process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0071803	positive regulation of podosome assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0071560	cellular response to transforming growth factor beta stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0071498	cellular response to fluid shear stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0071375	cellular response to peptide hormone stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
enables	GO:0071253	connexin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
involved_in	GO:0070374	positive regulation of ERK1 and ERK2 cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0060491	regulation of cell projection assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0060444	branching involved in mammary gland duct morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0060065	uterus development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0050731	positive regulation of peptidyl-tyrosine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0048477	oogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
enables	GO:0046875	ephrin receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
involved_in	GO:0045453	bone resorption	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0043393	regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0042476	odontogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0036120	cellular response to platelet-derived growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0036035	osteoclast development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0034614	cellular response to reactive oxygen species	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0034446	substrate adhesion-dependent cell spreading	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0033146	regulation of intracellular estrogen receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0030900	forebrain development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0016477	cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
involved_in	GO:0010954	positive regulation of protein processing	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	P		Seeded From UniProt	complete
part_of	GO:0005901	caveola	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
part_of	GO:0005884	actin filament	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	F		Seeded From UniProt	complete
part_of	GO:0002102	podosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P05480 ensembl:ENSMUSP00000090237	C		Seeded From UniProt	complete
involved_in	GO:2001286	regulation of caveolin-mediated endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:2000811	negative regulation of anoikis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:2000641	regulation of early endosome to late endosome transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:2000394	positive regulation of lamellipodium morphogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0097110	scaffold protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0071902	positive regulation of protein serine/threonine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0070851	growth factor receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0070555	response to interleukin-1	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0051974	negative regulation of telomerase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0051902	negative regulation of mitochondrial depolarization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0051219	phosphoprotein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0051057	positive regulation of small GTPase mediated signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0046875	ephrin receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0044325	ion channel binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0043149	stress fiber assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0042169	SH2 domain binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0035556	intracellular signal transduction	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0032463	negative regulation of protein homooligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0032211	negative regulation of telomere maintenance via telomerase	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0022407	regulation of cell-cell adhesion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0019900	kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0010634	positive regulation of epithelial cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0010632	regulation of epithelial cell migration	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
involved_in	GO:0007229	integrin-mediated signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
involved_in	GO:0007179	transforming growth factor beta receptor signaling pathway	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	P		Seeded From UniProt	complete
part_of	GO:0005901	caveola	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005770	late endosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	C		Seeded From UniProt	complete
enables	GO:0005178	integrin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0005102	signaling receptor binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P12931 ensembl:ENSP00000362680	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR008266	F		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020635	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR001245 InterPro:IPR008266 InterPro:IPR020635	P		Seeded From UniProt	complete
enables	GO:0004715	non-membrane spanning protein tyrosine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.10.2	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	PMID:12007793^[45]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-RNO-9612145 Reactome:R-RNO-9037056 Reactome:R-RNO-8937915 Reactome:R-RNO-8937895	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-RNO-548972	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	Reactome:R-RNO-9612145 Reactome:R-RNO-9037056	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	P		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0007155	cell adhesion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0130	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0829	F		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0999 UniProtKB-SubCell:SL-0168	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0496	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C		Seeded From UniProt	complete
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Notes

References

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

↑ Arachiche, A et al. (2008) Localization of PTP-1B, SHP-2, and Src exclusively in rat brain mitochondria and functional consequences. J. Biol. Chem. 283 24406-11 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Hsu, SP et al. (2011) Extra-nuclear activation of progesterone receptor in regulating arterial smooth muscle cell migration. Atherosclerosis 217 83-9 PubMed GONUTS page
↑ ^3.00 ^3.01 ^3.02 ^3.03 ^3.04 ^3.05 ^3.06 ^3.07 ^3.08 ^3.09 ^3.10 ^3.11 ^3.12 Choudhury, GG et al. (2006) c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells. Cell. Signal. 18 1854-64 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Kalia, LV & Salter, MW (2003) Interactions between Src family protein tyrosine kinases and PSD-95. Neuropharmacology 45 720-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Yu, XM et al. (1997) NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science 275 674-8 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Du, XY et al. (2012) The proto-oncogene c-src is involved in primordial follicle activation through the PI3K, PKC and MAPK signaling pathways. Reprod. Biol. Endocrinol. 10 58 PubMed GONUTS page
↑ Nishida, T et al. (2009) FGF-1-induced reactions for biogenesis of apoE-HDL are mediated by src in rat astrocytes. J. Biochem. 146 881-6 PubMed GONUTS page
↑ Wong, CH et al. (2005) Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes. Endocrinology 146 1192-204 PubMed GONUTS page
↑ Wang, Y et al. (2010) Decay accelerating factor (CD55) protects neuronal cells from chemical hypoxia-induced injury. J Neuroinflammation 7 24 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Maa, MC et al. (2010) Butyrate reduced lipopolysaccharide-mediated macrophage migration by suppression of Src enhancement and focal adhesion kinase activity. J. Nutr. Biochem. 21 1186-92 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Potula, HS et al. (2009) Src-dependent STAT-3-mediated expression of monocyte chemoattractant protein-1 is required for 15(S)-hydroxyeicosatetraenoic acid-induced vascular smooth muscle cell migration. J. Biol. Chem. 284 31142-55 PubMed GONUTS page
↑ ^12.0 ^12.1 Chen, LY et al. (2010) Learning induces neurotrophin signaling at hippocampal synapses. Proc. Natl. Acad. Sci. U.S.A. 107 7030-5 PubMed GONUTS page
↑ Callera, GE et al. (2005) c-Src-dependent nongenomic signaling responses to aldosterone are increased in vascular myocytes from spontaneously hypertensive rats. Hypertension 46 1032-8 PubMed GONUTS page
↑ ^14.0 ^14.1 Shajahan, AN et al. (2004) Role of Src-induced dynamin-2 phosphorylation in caveolae-mediated endocytosis in endothelial cells. J. Biol. Chem. 279 20392-400 PubMed GONUTS page
↑ Müller, MM et al. (2009) Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src. J. Cell Biol. 187 569-81 PubMed GONUTS page
↑ Obara, Y et al. (2004) PKA phosphorylation of Src mediates Rap1 activation in NGF and cAMP signaling in PC12 cells. J. Cell. Sci. 117 6085-94 PubMed GONUTS page
↑ Schliess, F et al. (2004) Involvement of integrins and Src in insulin signaling toward autophagic proteolysis in rat liver. J. Biol. Chem. 279 21294-301 PubMed GONUTS page
↑ Pera, IL et al. (2005) The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue. Oncogene 24 3187-95 PubMed GONUTS page
↑ Wang, WW et al. (2010) Transduced PDZ1 domain of PSD-95 decreases Src phosphorylation and increases nNOS (Ser847) phosphorylation contributing to neuroprotection after cerebral ischemia. Brain Res. 1328 162-70 PubMed GONUTS page
↑ Chen, M et al. (2003) Tyrosine kinase and tyrosine phosphatase participate in regulation of interactions of NMDA receptor subunit 2A with Src and Fyn mediated by PSD-95 after transient brain ischemia. Neurosci. Lett. 339 29-32 PubMed GONUTS page
↑ Li, Y et al. (2004) Dual phosphorylations underlie modulation of unitary KCNQ K(+) channels by Src tyrosine kinase. J. Biol. Chem. 279 45399-407 PubMed GONUTS page
↑ Cayabyab, FS & Schlichter, LC (2002) Regulation of an ERG K+ current by Src tyrosine kinase. J. Biol. Chem. 277 13673-81 PubMed GONUTS page
↑ Melendez, J et al. (2004) Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin. J. Biol. Chem. 279 53516-23 PubMed GONUTS page
↑ ^24.0 ^24.1 Mallozzi, C et al. (2009) Peroxynitrite induces tyrosine residue modifications in synaptophysin C-terminal domain, affecting its interaction with src. J. Neurochem. 111 859-69 PubMed GONUTS page
↑ Saito, S et al. (2002) Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and c-Src. J. Biol. Chem. 277 44695-700 PubMed GONUTS page
↑ Lee, NP & Cheng, CY (2005) Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis. J. Cell. Physiol. 202 344-60 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 Jacob, AI et al. (2010) The regulatory domain of protein kinase C delta positively regulates insulin receptor signaling. J. Mol. Endocrinol. 44 155-69 PubMed GONUTS page
↑ Wang, ZJ et al. (2010) Decrease in dietary K intake stimulates the generation of superoxide anions in the kidney and inhibits K secretory channels in the CCD. Am. J. Physiol. Renal Physiol. 298 F1515-22 PubMed GONUTS page
↑ Rafiq, K et al. (2012) c-Cbl ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G. J. Biol. Chem. 287 5327-39 PubMed GONUTS page
↑ ^30.0 ^30.1 Longo, M et al. (2004) Interaction of estrogen receptor alpha with protein kinase C alpha and c-Src in osteoblasts during differentiation. Bone 34 100-11 PubMed GONUTS page
↑ Chen, YM et al. (2003) Fer kinase/FerT and adherens junction dynamics in the testis: an in vitro and in vivo study. Biol. Reprod. 69 656-72 PubMed GONUTS page
↑ Gingrich, JR et al. (2004) Unique domain anchoring of Src to synaptic NMDA receptors via the mitochondrial protein NADH dehydrogenase subunit 2. Proc. Natl. Acad. Sci. U.S.A. 101 6237-42 PubMed GONUTS page
↑ Gupte, RS et al. (2009) Synergistic activation of glucose-6-phosphate dehydrogenase and NAD(P)H oxidase by Src kinase elevates superoxide in type 2 diabetic, Zucker fa/fa, rat liver. Free Radic. Biol. Med. 47 219-28 PubMed GONUTS page
↑ ^34.0 ^34.1 Tung, WH et al. (2010) EV71 induces COX-2 expression via c-Src/PDGFR/PI3K/Akt/p42/p44 MAPK/AP-1 and NF-kappaB in rat brain astrocytes. J. Cell. Physiol. 224 376-86 PubMed GONUTS page
↑ Hsieh, HL et al. (2010) Lipoteichoic acid induces matrix metalloproteinase-9 expression via transactivation of PDGF receptors and NF-kappaB activation in rat brain astrocytes. Neurotox Res 17 344-59 PubMed GONUTS page
↑ Tsuganezawa, H et al. (2002) Role of c-SRC and ERK in acid-induced activation of NHE3. Kidney Int. 62 41-50 PubMed GONUTS page
↑ Sedding, DG et al. (2005) Caveolin-1 facilitates mechanosensitive protein kinase B (Akt) signaling in vitro and in vivo. Circ. Res. 96 635-42 PubMed GONUTS page
↑ ^38.0 ^38.1 Murillo, MM et al. (2005) Involvement of EGF receptor and c-Src in the survival signals induced by TGF-beta1 in hepatocytes. Oncogene 24 4580-7 PubMed GONUTS page
↑ Lu, T et al. (2010) Regulation of coronary arterial BK channels by caveolae-mediated angiotensin II signaling in diabetes mellitus. Circ. Res. 106 1164-73 PubMed GONUTS page
↑ Courtneidge, SA et al. (1980) The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60proto-src) are associated with the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 77 3783-7 PubMed GONUTS page
↑ Liu, Y et al. (2001) NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion. Brain Res. 909 51-8 PubMed GONUTS page
↑ Rosenzweig, T et al. (2004) Src tyrosine kinase regulates insulin-induced activation of protein kinase C (PKC) delta in skeletal muscle. Cell. Signal. 16 1299-308 PubMed GONUTS page
↑ Brown, D et al. (2003) pp60c-Src Kinase mediates growth effects of the full-length precursor progastrin1-80 peptide on rat intestinal epithelial cells, in vitro. Endocrinology 144 201-11 PubMed GONUTS page
↑ ^44.00 ^44.01 ^44.02 ^44.03 ^44.04 ^44.05 ^44.06 ^44.07 ^44.08 ^44.09 ^44.10 ^44.11 ^44.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Salvi, M et al. (2002) Characterization and location of Src-dependent tyrosine phosphorylation in rat brain mitochondria. Biochim. Biophys. Acta 1589 181-95 PubMed GONUTS page

[PMID:18583343-1] Arachiche, A et al. (2008) Localization of PTP-1B, SHP-2, and Src exclusively in rat brain mitochondria and functional consequences. J. Biol. Chem. 283 24406-11 PubMed GONUTS page

[PMID:21440892-2] 2.0 ^2.1 ^2.2 Hsu, SP et al. (2011) Extra-nuclear activation of progesterone receptor in regulating arterial smooth muscle cell migration. Atherosclerosis 217 83-9 PubMed GONUTS page

[PMID:16530387-3] 3.00 ^3.01 ^3.02 ^3.03 ^3.04 ^3.05 ^3.06 ^3.07 ^3.08 ^3.09 ^3.10 ^3.11 ^3.12 Choudhury, GG et al. (2006) c-Src couples PI 3 kinase/Akt and MAPK signaling to PDGF-induced DNA synthesis in mesangial cells. Cell. Signal. 18 1854-64 PubMed GONUTS page

[PMID:14529711-4] 4.0 ^4.1 ^4.2 ^4.3 Kalia, LV & Salter, MW (2003) Interactions between Src family protein tyrosine kinases and PSD-95. Neuropharmacology 45 720-8 PubMed GONUTS page

[PMID:9005855-5] 5.0 ^5.1 ^5.2 ^5.3 Yu, XM et al. (1997) NMDA channel regulation by channel-associated protein tyrosine kinase Src. Science 275 674-8 PubMed GONUTS page

[PMID:22905678-6] 6.0 ^6.1 ^6.2 Du, XY et al. (2012) The proto-oncogene c-src is involved in primordial follicle activation through the PI3K, PKC and MAPK signaling pathways. Reprod. Biol. Endocrinol. 10 58 PubMed GONUTS page

[PMID:19713443-7] Nishida, T et al. (2009) FGF-1-induced reactions for biogenesis of apoE-HDL are mediated by src in rat astrocytes. J. Biochem. 146 881-6 PubMed GONUTS page

[PMID:15591141-8] Wong, CH et al. (2005) Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes. Endocrinology 146 1192-204 PubMed GONUTS page

[PMID:20380727-9] Wang, Y et al. (2010) Decay accelerating factor (CD55) protects neuronal cells from chemical hypoxia-induced injury. J Neuroinflammation 7 24 PubMed GONUTS page

[PMID:20149623-10] 10.0 ^10.1 ^10.2 Maa, MC et al. (2010) Butyrate reduced lipopolysaccharide-mediated macrophage migration by suppression of Src enhancement and focal adhesion kinase activity. J. Nutr. Biochem. 21 1186-92 PubMed GONUTS page

[PMID:19736311-11] 11.0 ^11.1 ^11.2 Potula, HS et al. (2009) Src-dependent STAT-3-mediated expression of monocyte chemoattractant protein-1 is required for 15(S)-hydroxyeicosatetraenoic acid-induced vascular smooth muscle cell migration. J. Biol. Chem. 284 31142-55 PubMed GONUTS page

[PMID:20356829-12] 12.0 ^12.1 Chen, LY et al. (2010) Learning induces neurotrophin signaling at hippocampal synapses. Proc. Natl. Acad. Sci. U.S.A. 107 7030-5 PubMed GONUTS page

[PMID:16157790-13] Callera, GE et al. (2005) c-Src-dependent nongenomic signaling responses to aldosterone are increased in vascular myocytes from spontaneously hypertensive rats. Hypertension 46 1032-8 PubMed GONUTS page

[PMID:15007081-14] 14.0 ^14.1 Shajahan, AN et al. (2004) Role of Src-induced dynamin-2 phosphorylation in caveolae-mediated endocytosis in endothelial cells. J. Biol. Chem. 279 20392-400 PubMed GONUTS page

[PMID:19948503-15] Müller, MM et al. (2009) Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L and recruitment of SHP-2 and c-Src. J. Cell Biol. 187 569-81 PubMed GONUTS page

[PMID:15546918-16] Obara, Y et al. (2004) PKA phosphorylation of Src mediates Rap1 activation in NGF and cAMP signaling in PC12 cells. J. Cell. Sci. 117 6085-94 PubMed GONUTS page

[PMID:14985360-17] Schliess, F et al. (2004) Involvement of integrins and Src in insulin signaling toward autophagic proteolysis in rat liver. J. Biol. Chem. 279 21294-301 PubMed GONUTS page

[PMID:15735685-18] Pera, IL et al. (2005) The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue. Oncogene 24 3187-95 PubMed GONUTS page

[PMID:20197063-19] Wang, WW et al. (2010) Transduced PDZ1 domain of PSD-95 decreases Src phosphorylation and increases nNOS (Ser847) phosphorylation contributing to neuroprotection after cerebral ischemia. Brain Res. 1328 162-70 PubMed GONUTS page

[PMID:12618293-20] Chen, M et al. (2003) Tyrosine kinase and tyrosine phosphatase participate in regulation of interactions of NMDA receptor subunit 2A with Src and Fyn mediated by PSD-95 after transient brain ischemia. Neurosci. Lett. 339 29-32 PubMed GONUTS page

[PMID:15304482-21] Li, Y et al. (2004) Dual phosphorylations underlie modulation of unitary KCNQ K(+) channels by Src tyrosine kinase. J. Biol. Chem. 279 45399-407 PubMed GONUTS page

[PMID:11834728-22] Cayabyab, FS & Schlichter, LC (2002) Regulation of an ERG K+ current by Src tyrosine kinase. J. Biol. Chem. 277 13673-81 PubMed GONUTS page

[PMID:15322113-23] Melendez, J et al. (2004) Cardiomyocyte apoptosis triggered by RAFTK/pyk2 via Src kinase is antagonized by paxillin. J. Biol. Chem. 279 53516-23 PubMed GONUTS page

[PMID:19737347-24] 24.0 ^24.1 Mallozzi, C et al. (2009) Peroxynitrite induces tyrosine residue modifications in synaptophysin C-terminal domain, affecting its interaction with src. J. Neurochem. 111 859-69 PubMed GONUTS page

[PMID:12226102-25] Saito, S et al. (2002) Ligand-independent trans-activation of the platelet-derived growth factor receptor by reactive oxygen species requires protein kinase C-delta and c-Src. J. Biol. Chem. 277 44695-700 PubMed GONUTS page

[PMID:15389520-26] Lee, NP & Cheng, CY (2005) Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis. J. Cell. Physiol. 202 344-60 PubMed GONUTS page

[PMID:19952103-27] 27.0 ^27.1 ^27.2 Jacob, AI et al. (2010) The regulatory domain of protein kinase C delta positively regulates insulin receptor signaling. J. Mol. Endocrinol. 44 155-69 PubMed GONUTS page

[PMID:20357031-28] Wang, ZJ et al. (2010) Decrease in dietary K intake stimulates the generation of superoxide anions in the kidney and inhibits K secretory channels in the CCD. Am. J. Physiol. Renal Physiol. 298 F1515-22 PubMed GONUTS page

[PMID:22203672-29] Rafiq, K et al. (2012) c-Cbl ubiquitin ligase regulates focal adhesion protein turnover and myofibril degeneration induced by neutrophil protease cathepsin G. J. Biol. Chem. 287 5327-39 PubMed GONUTS page

[PMID:14751567-30] 30.0 ^30.1 Longo, M et al. (2004) Interaction of estrogen receptor alpha with protein kinase C alpha and c-Src in osteoblasts during differentiation. Bone 34 100-11 PubMed GONUTS page

[PMID:12700184-31] Chen, YM et al. (2003) Fer kinase/FerT and adherens junction dynamics in the testis: an in vitro and in vivo study. Biol. Reprod. 69 656-72 PubMed GONUTS page

[PMID:15069201-32] Gingrich, JR et al. (2004) Unique domain anchoring of Src to synaptic NMDA receptors via the mitochondrial protein NADH dehydrogenase subunit 2. Proc. Natl. Acad. Sci. U.S.A. 101 6237-42 PubMed GONUTS page

[PMID:19230846-33] Gupte, RS et al. (2009) Synergistic activation of glucose-6-phosphate dehydrogenase and NAD(P)H oxidase by Src kinase elevates superoxide in type 2 diabetic, Zucker fa/fa, rat liver. Free Radic. Biol. Med. 47 219-28 PubMed GONUTS page

[PMID:20333648-34] 34.0 ^34.1 Tung, WH et al. (2010) EV71 induces COX-2 expression via c-Src/PDGFR/PI3K/Akt/p42/p44 MAPK/AP-1 and NF-kappaB in rat brain astrocytes. J. Cell. Physiol. 224 376-86 PubMed GONUTS page

[PMID:19763735-35] Hsieh, HL et al. (2010) Lipoteichoic acid induces matrix metalloproteinase-9 expression via transactivation of PDGF receptors and NF-kappaB activation in rat brain astrocytes. Neurotox Res 17 344-59 PubMed GONUTS page

[PMID:12081562-36] Tsuganezawa, H et al. (2002) Role of c-SRC and ERK in acid-induced activation of NHE3. Kidney Int. 62 41-50 PubMed GONUTS page

[PMID:15731459-37] Sedding, DG et al. (2005) Caveolin-1 facilitates mechanosensitive protein kinase B (Akt) signaling in vitro and in vivo. Circ. Res. 96 635-42 PubMed GONUTS page

[PMID:15856020-38] 38.0 ^38.1 Murillo, MM et al. (2005) Involvement of EGF receptor and c-Src in the survival signals induced by TGF-beta1 in hepatocytes. Oncogene 24 4580-7 PubMed GONUTS page

[PMID:20167931-39] Lu, T et al. (2010) Regulation of coronary arterial BK channels by caveolae-mediated angiotensin II signaling in diabetes mellitus. Circ. Res. 106 1164-73 PubMed GONUTS page

[PMID:6253989-40] Courtneidge, SA et al. (1980) The protein encoded by the transforming gene of avian sarcoma virus (pp60src) and a homologous protein in normal cells (pp60proto-src) are associated with the plasma membrane. Proc. Natl. Acad. Sci. U.S.A. 77 3783-7 PubMed GONUTS page

[PMID:11478920-41] Liu, Y et al. (2001) NMDA receptor activation results in tyrosine phosphorylation of NMDA receptor subunit 2A(NR2A) and interaction of Pyk2 and Src with NR2A after transient cerebral ischemia and reperfusion. Brain Res. 909 51-8 PubMed GONUTS page

[PMID:15337529-42] Rosenzweig, T et al. (2004) Src tyrosine kinase regulates insulin-induced activation of protein kinase C (PKC) delta in skeletal muscle. Cell. Signal. 16 1299-308 PubMed GONUTS page

[PMID:12488346-43] Brown, D et al. (2003) pp60c-Src Kinase mediates growth effects of the full-length precursor progastrin1-80 peptide on rat intestinal epithelial cells, in vitro. Endocrinology 144 201-11 PubMed GONUTS page

[PMID:21873635-44] 44.00 ^44.01 ^44.02 ^44.03 ^44.04 ^44.05 ^44.06 ^44.07 ^44.08 ^44.09 ^44.10 ^44.11 ^44.12 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:12007793-45] Salvi, M et al. (2002) Characterization and location of Src-dependent tyrosine phosphorylation in rat brain mitochondria. Biochim. Biophys. Acta 1589 181-95 PubMed GONUTS page

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