HUMAN:SRC

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Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SRC (synonyms: SRC1)
Protein Name(s)	Proto-oncogene tyrosine-protein kinase Src Proto-oncogene c-Src pp60c-src p60-Src
External Links
UniProt	P12931
EMBL	AL133293 AL133293 CH471077 CH471077 CH471077 CH471077 BC011566 BC051270 K03218 M16237 M16243 M16244 M16245 K03212 K03213 K03214 K03215 K03216 K03217 X02647 X03995 X03996 X03997 X03998 X03999 X04000
IPI	IPI00328867 IPI00641230
PIR	A26891
RefSeq	NP_005408.1 NP_938033.1
UniGene	Hs.195659
PDB	1A07 1A08 1A09 1A1A 1A1B 1A1C 1A1E 1FMK 1HCS 1HCT 1KSW 1O41 1O42 1O43 1O44 1O45 1O46 1O47 1O48 1O49 1O4A 1O4B 1O4C 1O4D 1O4E 1O4F 1O4G 1O4H 1O4I 1O4J 1O4K 1O4L 1O4M 1O4N 1O4O 1O4P 1O4Q 1O4R 1SHD 1Y57 1YI6 1YOJ 1YOL 1YOM 2BDF 2BDJ 2H8H 2SRC
PDBsum	1A07 1A08 1A09 1A1A 1A1B 1A1C 1A1E 1FMK 1HCS 1HCT 1KSW 1O41 1O42 1O43 1O44 1O45 1O46 1O47 1O48 1O49 1O4A 1O4B 1O4C 1O4D 1O4E 1O4F 1O4G 1O4H 1O4I 1O4J 1O4K 1O4L 1O4M 1O4N 1O4O 1O4P 1O4Q 1O4R 1SHD 1Y57 1YI6 1YOJ 1YOL 1YOM 2BDF 2BDJ 2H8H 2SRC
ProteinModelPortal	P12931
SMR	P12931
DIP	DIP-1059N
IntAct	P12931
MINT	MINT-93621
STRING	P12931
PhosphoSite	P12931
DMDM	125711
OGP	P12931
PRIDE	P12931
Ensembl	ENST00000358208 ENST00000373567 ENST00000373578 ENST00000445403
GeneID	6714
KEGG	hsa:6714
UCSC	uc002xgx.1
CTD	6714
GeneCards	GC20P035973
H-InvDB	HIX0015793
HGNC	HGNC:11283
HPA	CAB004023
MIM	190090
neXtProt	NX_P12931
PharmGKB	PA36111
eggNOG	prNOG06370
HOVERGEN	HBG008761
OMA	TDLSFKK
BRENDA	2.7.10.2
Pathway_Interaction_DB	alphasynuclein_pathway amb2_neutrophils_pathway arf6cyclingpathway nfkappabatypicalpathway pi3kcipathway pi3kciaktpathway endothelinpathway epha_fwdpathway epha2_fwdpathway ephbfwdpathway ephrinbrevpathway fgf_pathway glypican_1pathway avb3_integrin_pathway lysophospholipid_pathway a4b1_paxindep_pathway pdgfrbpathway er_nongenomic_pathway ar_tf_pathway p38alphabetapathway s1p_s1p3_pathway met_pathway prlsignalingeventspathway ptp1bpathway vegfr1_2_pathway ret_pathway syndecan_2_pathway syndecan_3_pathway txa2pathway pi3kplctrkpathway
Reactome	REACT_111045 REACT_111102 REACT_111155 REACT_11123 REACT_604 REACT_6900
DrugBank	DB01254
NextBio	26186
PMAP-CutDB	P12931
ArrayExpress	P12931
Bgee	P12931
CleanEx	HS_SRC
Genevestigator	P12931
GermOnline	ENSG00000197122
GO	GO:0005901 GO:0005856 GO:0005829 GO:0005743 GO:0005634 GO:0005524 GO:0046875 GO:0020037 GO:0005178 GO:0044325 GO:0004715 GO:0042169 GO:0005070 GO:0007411 GO:0045453 GO:0007155 GO:0007049 GO:0034329 GO:0016044 GO:0007173 GO:0008543 GO:0044419 GO:0007243 GO:0050900 GO:0048011 GO:0030168 GO:0033625 GO:0007265 GO:0045124 GO:0043114 GO:0070555 GO:0007172 GO:0031295
InterPro	IPR011009 IPR000719 IPR017441 IPR001245 IPR000980 IPR001452 IPR008266 IPR020635
Gene3D	G3DSA:3.30.505.10
KO	K05704
Pfam	PF07714 PF00017 PF00018
PRINTS	PR00401 PR00452 PR00109
SMART	SM00252 SM00326 SM00219
SUPFAM	SSF56112 SSF50044
PROSITE	PS00107 PS50011 PS00109 PS50001 PS50002

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F	Seeded From UniProt
	GO:0004672	protein kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	F	Seeded From UniProt
	GO:0004672	protein kinase activity	PMID:18616680^[1]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0004672	protein kinase activity	Reactome:REACT_23900	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	PMID:9020193^[2]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004713	protein tyrosine kinase activity	Reactome:REACT_23775	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.2	F	Seeded From UniProt
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	PMID:19267251^[3]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0005070	SH3/SH2 adaptor activity	PMID:9020193^[2]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0005102	receptor binding	PMID:19332538^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q12913	F	Seeded From UniProt
	GO:0005178	integrin binding	PMID:19267251^[3]	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15546919^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q8R5G7	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15749833^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6K9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16291744^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P12814	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:16291744^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q05397	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17412687^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q8N4X5	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17474147^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P42684	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17474147^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q13905	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17474147^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q9ULH1	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:17525734^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q9C0H9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18328427^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P25445	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:18377662^[12]	IPI: Inferred from Physical Interaction	UniProtKB:P35968	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19262695^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P31749	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19372587^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P04626	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19419966^[15]	IPI: Inferred from Physical Interaction	UniProtKB:O95786	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19419966^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q13114	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19419966^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q7Z434	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19419966^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UHD2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19732724^[16]	IPI: Inferred from Physical Interaction	UniProtKB:Q68CZ2	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20100835^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q13761	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20935677^[18]	IPI: Inferred from Physical Interaction	UniProtKB:P03372-4	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:21278788^[19]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:7537265^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q07666	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:8681387^[21]	IPI: Inferred from Physical Interaction	UniProtKB:P03406	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:9763511^[22]	IPI: Inferred from Physical Interaction	UniProtKB:P10636	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F	Seeded From UniProt
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C	Seeded From UniProt
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C	Seeded From UniProt
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C	Seeded From UniProt
	GO:0005743	mitochondrial inner membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0999	C	Seeded From UniProt
	GO:0005743	mitochondrial inner membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0168	C	Seeded From UniProt
	GO:0005743	mitochondrial inner membrane	PMID:12615910^[23]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111036	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111042	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111049	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111069	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111070	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111072	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111112	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111136	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111152	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111179	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111182	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111186	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111199	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111205	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111237	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111242	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111244	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_111251	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_12408	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15323	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15348	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15349	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15368	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15371	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15375	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15397	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15403	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15405	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15464	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15490	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15500	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15535	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_15545	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_19203	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_19264	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_19380	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_20585	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22183	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22199	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22200	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22213	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22278	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22281	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22309	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22408	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_22439	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23775	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23781	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23801	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23808	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23821	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23899	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23900	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23931	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23958	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_23960	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_24010	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005829	cytosol	Reactome:REACT_9975	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005856	cytoskeleton	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0206	C	Seeded From UniProt
	GO:0005856	cytoskeleton	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0090	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C	Seeded From UniProt
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_10125	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_111096	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_115797	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_12601	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_16991	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_17048	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9401	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9975	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005886	plasma membrane	Reactome:REACT_9997	TAS: Traceable Author Statement		C	Seeded From UniProt
	GO:0005901	caveola	PMID:17848177^[24]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0006468	protein phosphorylation	PMID:18616680^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006468	protein phosphorylation	Reactome:REACT_23900	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007049	cell cycle	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0131	P	Seeded From UniProt
	GO:0007155	cell adhesion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0130	P	Seeded From UniProt
	GO:0007165	signal transduction	PMID:10734107^[25]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007165	signal transduction	PMID:9020193^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007172	signal complex assembly	PMID:9924018^[26]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007173	epidermal growth factor receptor signaling pathway	Reactome:REACT_9417	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007243	intracellular protein kinase cascade	PMID:15248232^[27]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0007243	intracellular protein kinase cascade	PMID:9020193^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007265	Ras protein signal transduction	Reactome:REACT_12033	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007411	axon guidance	Reactome:REACT_18266	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0007596	blood coagulation	Reactome:REACT_604	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0008543	fibroblast growth factor receptor signaling pathway	Reactome:REACT_9470	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C	Seeded From UniProt
	GO:0016044	cellular membrane organization	Reactome:REACT_11123	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F	Seeded From UniProt
	GO:0016301	kinase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	F	Seeded From UniProt
	GO:0016301	kinase activity	Reactome:REACT_9997	TAS: Traceable Author Statement		F	Seeded From UniProt
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P	Seeded From UniProt
	GO:0016310	phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0016310	phosphorylation	Reactome:REACT_9997	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0016477	cell migration	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F	Seeded From UniProt
	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F	Seeded From UniProt
	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0019904	protein domain specific binding	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	F	Seeded From UniProt
	GO:0020037	heme binding	PMID:21036157^[28]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0030168	platelet activation	Reactome:REACT_798	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0030900	forebrain development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0031295	T cell costimulation	Reactome:REACT_19183	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0031295	T cell costimulation	Reactome:REACT_19344	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0033146	regulation of intracellular estrogen receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0033625	positive regulation of integrin activation	PMID:19267251^[3]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0042169	SH2 domain binding	PMID:8070403^[29]	IPI: Inferred from Physical Interaction	UniProtKB:P56945	F	Seeded From UniProt
	GO:0043114	regulation of vascular permeability	PMID:19267251^[3]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0044325	ion channel binding	PMID:12538589^[30]	IPI: Inferred from Physical Interaction	UniProtKB:Q9HBA0	F	Seeded From UniProt
	GO:0044419	interspecies interaction between organisms	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0945	P	Seeded From UniProt
	GO:0045124	regulation of bone resorption	PMID:19267251^[3]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0045453	bone resorption	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0045453	bone resorption	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P05480	P	Seeded From UniProt
	GO:0046875	ephrin receptor binding	PMID:12925710^[31]	IPI: Inferred from Physical Interaction	UniProtKB:P54762	F	Seeded From UniProt
	GO:0048011	nerve growth factor receptor signaling pathway	Reactome:REACT_11061	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0048477	oogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0050900	leukocyte migration	Reactome:REACT_12051	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0060065	uterus development	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0060444	branching involved in mammary gland duct morphogenesis	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0070374	positive regulation of ERK1 and ERK2 cascade	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:0070555	response to interleukin-1	PMID:19281832^[32]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0090263	positive regulation of canonical Wnt receptor signaling pathway	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000105159	P	Seeded From UniProt
	GO:2001237	negative regulation of extrinsic apoptotic signaling pathway	PMID:19767770^[33]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:2001243	negative regulation of intrinsic apoptotic signaling pathway	PMID:19767770^[33]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	PMID:22303479^[34]	IDA: Inferred from Direct Assay		F	c-Src involved in STAT3 phosphorylation induced by Piwil2: Figure 4.	complete
edit table

Notes

References

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

↑ ^1.0 ^1.1 Kurata A et al. (2008) TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling. Cancer Sci 99: 1827-34 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Luttrell LM et al. (1997) Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J Biol Chem 272: 4637-44 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Somanath PR et al. (2009) Cooperation between integrin alphavbeta3 and VEGFR2 in angiogenesis. Angiogenesis 12: 177-85 PubMed GONUTS page
↑ Sallee JL & Burridge K (2009) Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem 284: 14997-5006 PubMed GONUTS page
↑ I ST et al. (2004) ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner. J Cell Sci 117: 6071-84 PubMed GONUTS page
↑ Funakoshi-Tago M et al. (2005) Functional role of c-Src in IL-1-induced NF-kappa B activation: c-Src is a component of the IKK complex. J Biochem 137: 189-97 PubMed GONUTS page
↑ ^7.0 ^7.1 Zhang Z et al. (2006) Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration. J Biol Chem 281: 1746-54 PubMed GONUTS page
↑ Xu J et al. (2007) XB130, a novel adaptor protein for signal transduction. J Biol Chem 282: 16401-12 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Wu C et al. (2007) Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening. Proteomics 7: 1775-85 PubMed GONUTS page
↑ Di Stefano P et al. (2007) p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. EMBO J 26: 2843-55 PubMed GONUTS page
↑ Kleber S et al. (2008) Yes and PI3K bind CD95 to signal invasion of glioblastoma. Cancer Cell 13: 235-48 PubMed GONUTS page
↑ Bhattacharya R et al. (2008) Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration*. J Mol Signal 3: 8 PubMed GONUTS page
↑ Lodeiro M et al. (2009) c-Src regulates Akt signaling in response to ghrelin via beta-arrestin signaling-independent and -dependent mechanisms. PLoS One 4: e4686 PubMed GONUTS page
↑ Hawthorne VS et al. (2009) ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. Mol Cancer Res 7: 592-600 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Johnsen IB et al. (2009) The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling. J Biol Chem 284: 19122-31 PubMed GONUTS page
↑ Qian X et al. (2009) The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell 16: 246-58 PubMed GONUTS page
↑ Goh YM et al. (2010) Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm. J Biol Chem 285: 10122-9 PubMed GONUTS page
↑ Zhang XT et al. (2011) A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30: 770-80 PubMed GONUTS page
↑ Jung J et al. (2011) Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src. Oncogene 30: 2264-74 PubMed GONUTS page
↑ Taylor SJ et al. (1995) Functional interaction between c-Src and its mitotic target, Sam 68. J Biol Chem 270: 10120-4 PubMed GONUTS page
↑ Lee CH et al. (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85: 931-42 PubMed GONUTS page
↑ Lee G et al. (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111 ( Pt 21): 3167-77 PubMed GONUTS page
↑ Miyazaki T et al. (2003) Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J Cell Biol 160: 709-18 PubMed GONUTS page
↑ Banfi C et al. (2007) Tissue factor induction by protease-activated receptor 1 requires intact caveolin-enriched membrane microdomains in human endothelial cells. J Thromb Haemost 5: 2437-44 PubMed GONUTS page
↑ Maudsley S et al. (2000) The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J Biol Chem 275: 9572-80 PubMed GONUTS page
↑ Luttrell LM et al. (1999) Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283: 655-61 PubMed GONUTS page
↑ Mosheimer BA et al. (2004) Expression and function of RANK in human monocyte chemotaxis. Arthritis Rheum 50: 2309-16 PubMed GONUTS page
↑ Yao X et al. (2010) Heme controls the regulation of protein tyrosine kinases Jak2 and Src. Biochem Biophys Res Commun 403: 30-5 PubMed GONUTS page
↑ Sakai R et al. (1994) A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 13: 3748-56 PubMed GONUTS page
↑ Xu H et al. (2003) Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress. J Biol Chem 278: 11520-7 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
↑ Luo SF et al. (2009) Activation of ROS/NF-kappaB and Ca2+/CaM kinase II are necessary for VCAM-1 induction in IL-1beta-treated human tracheal smooth muscle cells. Toxicol Appl Pharmacol 237: 8-21 PubMed GONUTS page
↑ ^33.0 ^33.1 Mamidipudi V & Cartwright CA (2009) A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathways. Oncogene 28: 4421-33 PubMed GONUTS page
↑ Lu Y et al. (2012) Piwil2 suppresses p53 by inducing phosphorylation of signal transducer and activator of transcription 3 in tumor cells. PLoS One 7: e30999 PubMed GONUTS page

[PMID:18616680-0] 1.0 ^1.1 Kurata A et al. (2008) TUSC4/NPRL2, a novel PDK1-interacting protein, inhibits PDK1 tyrosine phosphorylation and its downstream signaling. Cancer Sci 99: 1827-34 PubMed GONUTS page

[PMID:9020193-1] 2.0 ^2.1 ^2.2 ^2.3 Luttrell LM et al. (1997) Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J Biol Chem 272: 4637-44 PubMed GONUTS page

[PMID:19267251-2] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 Somanath PR et al. (2009) Cooperation between integrin alphavbeta3 and VEGFR2 in angiogenesis. Angiogenesis 12: 177-85 PubMed GONUTS page

[PMID:19332538-3] Sallee JL & Burridge K (2009) Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J Biol Chem 284: 14997-5006 PubMed GONUTS page

[PMID:15546919-4] I ST et al. (2004) ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner. J Cell Sci 117: 6071-84 PubMed GONUTS page

[PMID:15749833-5] Funakoshi-Tago M et al. (2005) Functional role of c-Src in IL-1-induced NF-kappa B activation: c-Src is a component of the IKK complex. J Biochem 137: 189-97 PubMed GONUTS page

[PMID:16291744-6] 7.0 ^7.1 Zhang Z et al. (2006) Phosphorylated alpha-actinin and protein-tyrosine phosphatase 1B coregulate the disassembly of the focal adhesion kinase x Src complex and promote cell migration. J Biol Chem 281: 1746-54 PubMed GONUTS page

[PMID:17412687-7] Xu J et al. (2007) XB130, a novel adaptor protein for signal transduction. J Biol Chem 282: 16401-12 PubMed GONUTS page

[PMID:17474147-8] 9.0 ^9.1 ^9.2 Wu C et al. (2007) Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening. Proteomics 7: 1775-85 PubMed GONUTS page

[PMID:17525734-9] Di Stefano P et al. (2007) p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. EMBO J 26: 2843-55 PubMed GONUTS page

[PMID:18328427-10] Kleber S et al. (2008) Yes and PI3K bind CD95 to signal invasion of glioblastoma. Cancer Cell 13: 235-48 PubMed GONUTS page

[PMID:18377662-11] Bhattacharya R et al. (2008) Src homology 2 (SH2) domain containing protein tyrosine phosphatase-1 (SHP-1) dephosphorylates VEGF Receptor-2 and attenuates endothelial DNA synthesis, but not migration*. J Mol Signal 3: 8 PubMed GONUTS page

[PMID:19262695-12] Lodeiro M et al. (2009) c-Src regulates Akt signaling in response to ghrelin via beta-arrestin signaling-independent and -dependent mechanisms. PLoS One 4: e4686 PubMed GONUTS page

[PMID:19372587-13] Hawthorne VS et al. (2009) ErbB2-mediated Src and signal transducer and activator of transcription 3 activation leads to transcriptional up-regulation of p21Cip1 and chemoresistance in breast cancer cells. Mol Cancer Res 7: 592-600 PubMed GONUTS page

[PMID:19419966-14] 15.0 ^15.1 ^15.2 ^15.3 Johnsen IB et al. (2009) The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling. J Biol Chem 284: 19122-31 PubMed GONUTS page

[PMID:19732724-15] Qian X et al. (2009) The Tensin-3 protein, including its SH2 domain, is phosphorylated by Src and contributes to tumorigenesis and metastasis. Cancer Cell 16: 246-58 PubMed GONUTS page

[PMID:20100835-16] Goh YM et al. (2010) Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm. J Biol Chem 285: 10122-9 PubMed GONUTS page

[PMID:20935677-17] Zhang XT et al. (2011) A positive feedback loop of ER-α36/EGFR promotes malignant growth of ER-negative breast cancer cells. Oncogene 30: 770-80 PubMed GONUTS page

[PMID:21278788-18] Jung J et al. (2011) Translationally controlled tumor protein induces human breast epithelial cell transformation through the activation of Src. Oncogene 30: 2264-74 PubMed GONUTS page

[PMID:7537265-19] Taylor SJ et al. (1995) Functional interaction between c-Src and its mitotic target, Sam 68. J Biol Chem 270: 10120-4 PubMed GONUTS page

[PMID:8681387-20] Lee CH et al. (1996) Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain. Cell 85: 931-42 PubMed GONUTS page

[PMID:9763511-21] Lee G et al. (1998) Tau interacts with src-family non-receptor tyrosine kinases. J Cell Sci 111 ( Pt 21): 3167-77 PubMed GONUTS page

[PMID:12615910-22] Miyazaki T et al. (2003) Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J Cell Biol 160: 709-18 PubMed GONUTS page

[PMID:17848177-23] Banfi C et al. (2007) Tissue factor induction by protease-activated receptor 1 requires intact caveolin-enriched membrane microdomains in human endothelial cells. J Thromb Haemost 5: 2437-44 PubMed GONUTS page

[PMID:10734107-24] Maudsley S et al. (2000) The beta(2)-adrenergic receptor mediates extracellular signal-regulated kinase activation via assembly of a multi-receptor complex with the epidermal growth factor receptor. J Biol Chem 275: 9572-80 PubMed GONUTS page

[PMID:9924018-25] Luttrell LM et al. (1999) Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science 283: 655-61 PubMed GONUTS page

[PMID:15248232-26] Mosheimer BA et al. (2004) Expression and function of RANK in human monocyte chemotaxis. Arthritis Rheum 50: 2309-16 PubMed GONUTS page

[PMID:21036157-27] Yao X et al. (2010) Heme controls the regulation of protein tyrosine kinases Jak2 and Src. Biochem Biophys Res Commun 403: 30-5 PubMed GONUTS page

[PMID:8070403-28] Sakai R et al. (1994) A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 13: 3748-56 PubMed GONUTS page

[PMID:12538589-29] Xu H et al. (2003) Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress. J Biol Chem 278: 11520-7 PubMed GONUTS page

[PMID:12925710-30] 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:19281832-31] Luo SF et al. (2009) Activation of ROS/NF-kappaB and Ca2+/CaM kinase II are necessary for VCAM-1 induction in IL-1beta-treated human tracheal smooth muscle cells. Toxicol Appl Pharmacol 237: 8-21 PubMed GONUTS page

[PMID:19767770-32] 33.0 ^33.1 Mamidipudi V & Cartwright CA (2009) A novel pro-apoptotic function of RACK1: suppression of Src activity in the intrinsic and Akt pathways. Oncogene 28: 4421-33 PubMed GONUTS page

[PMID:22303479-33] Lu Y et al. (2012) Piwil2 suppresses p53 by inducing phosphorylation of signal transducer and activator of transcription 3 in tumor cells. PLoS One 7: e30999 PubMed GONUTS page

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HUMAN:SRC

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