Module talk:ImportProtein/testcases
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{{#invoke:ImportProtein | main | height=100 | width = 500 | include = all | exclude = "Domain","Beta-strand region","Helical region","Hydrogen bonded turn" | usenotes = "other","modified","active" | substitute = "Proton acceptor":"Active site:proton acceptor" | file=LOCUS SRC_HUMAN 536 aa linear PRI 06-MAR-2013
DEFINITION RecName: Full=Proto-oncogene tyrosine-protein kinase Src; AltName: Full=Proto-oncogene c-Src; AltName: Full=pp60c-src; Short=p60-Src. ACCESSION P12931 VERSION P12931.3 GI:125711 DBSOURCE UniProtKB: locus SRC_HUMAN, accession P12931; class: standard. extra accessions:E1P5V4,Q76P87,Q86VB9,Q9H5A8 created: Oct 1, 1989. sequence updated: Jan 23, 2007. annotation updated: Mar 6, 2013. xrefs: AL133293.28, CAC10573.1, CAC34523.1, CH471077.2, EAW76065.1, EAW76064.1, EAW76066.1, EAW76067.1, BC011566.1, AAH11566.1, BC051270.1, AAH51270.2, K03218.1, AAA60584.1, M16237.1, M16243.1, M16244.1, M16245.1, K03212.1, K03213.1, K03214.1, K03215.1, K03216.1, K03217.1, X02647.1, CAA26485.1, X03995.1, X03996.1, X03997.1, X03998.1, X03999.1, X04000.1, TVHUSC, NP_005408.1, NP_938033.1, 1A07_A, 1A07_B, 1A08_A, 1A08_B, 1A09_A, 1A09_B, 1A1A_A, 1A1A_B, 1A1B_A, 1A1B_B, 1A1C_A, 1A1C_B, 1A1E_A, 1A1E_B, 1FMK_A, 1HCS_B, 1HCT_B, 1KSW_A, 1O41_A, 1O42_A, 1O43_A, 1O44_A, 1O45_A, 1O46_A, 1O47_A, 1O48_A, 1O49_A, 1O4A_A, 1O4B_A, 1O4C_A, 1O4D_A, 1O4E_A, 1O4F_A, 1O4G_A, 1O4H_A, 1O4I_A, 1O4J_A, 1O4K_A, 1O4L_A, 1O4M_A, 1O4N_A, 1O4O_A, 1O4P_A, 1O4Q_A, 1O4R_A, 1SHD_A, 1Y57_A, 1YI6_A, 1YI6_B, 1YOJ_A, 1YOJ_B, 1YOL_A, 1YOL_B, 1YOM_A, 1YOM_B, 2BDF_A, 2BDF_B, 2BDJ_A, 2H8H_A, 2SRC_A, 4F59_A, 4F5A_A, 4F5B_A, 4HXJ_A, 4HXJ_B xrefs (non-sequence databases): IPI:IPI00328867, IPI:IPI00641230, UniGene:Hs.195659, PDBsum:1A07, PDBsum:1A08, PDBsum:1A09, PDBsum:1A1A, PDBsum:1A1B, PDBsum:1A1C, PDBsum:1A1E, PDBsum:1FMK, PDBsum:1HCS, PDBsum:1HCT, PDBsum:1KSW, PDBsum:1O41, PDBsum:1O42, PDBsum:1O43, PDBsum:1O44, PDBsum:1O45, PDBsum:1O46, PDBsum:1O47, PDBsum:1O48, PDBsum:1O49, PDBsum:1O4A, PDBsum:1O4B, PDBsum:1O4C, PDBsum:1O4D, PDBsum:1O4E, PDBsum:1O4F, PDBsum:1O4G, PDBsum:1O4H, PDBsum:1O4I, PDBsum:1O4J, PDBsum:1O4K, PDBsum:1O4L, PDBsum:1O4M, PDBsum:1O4N, PDBsum:1O4O, PDBsum:1O4P, PDBsum:1O4Q, PDBsum:1O4R, PDBsum:1SHD, PDBsum:1Y57, PDBsum:1YI6, PDBsum:1YOJ, PDBsum:1YOL, PDBsum:1YOM, PDBsum:2BDF, PDBsum:2BDJ, PDBsum:2H8H, PDBsum:2SRC, PDBsum:4F59, PDBsum:4F5A, PDBsum:4F5B, PDBsum:4HXJ, ProteinModelPortal:P12931, SMR:P12931, DIP:DIP-1059N, IntAct:P12931, MINT:MINT-93621, STRING:P12931, PhosphoSite:P12931, DMDM:125711, OGP:P12931, PaxDb:P12931, PRIDE:P12931, DNASU:6714, Ensembl:ENST00000358208, Ensembl:ENSP00000350941, Ensembl:ENSG00000197122, Ensembl:ENST00000360723, Ensembl:ENSP00000353950, Ensembl:ENST00000373558, Ensembl:ENSP00000362659, Ensembl:ENST00000373567, Ensembl:ENSP00000362668, Ensembl:ENST00000373578, Ensembl:ENSP00000362680, Ensembl:ENST00000445403, Ensembl:ENSP00000408503, GeneID:6714, KEGG:hsa:6714, UCSC:uc002xgx.3, CTD:6714, GeneCards:GC20P035973, HGNC:11283, HPA:CAB004023, MIM:190090, neXtProt:NX_P12931, PharmGKB:PA36111, eggNOG:COG0515, HOGENOM:HOG000233858, HOVERGEN:HBG008761, KO:K05704, OMA:CQCWRKD, BioCyc:MetaCyc:HS02256-MONOMER, BRENDA:2.7.10.2, Pathway_Interaction_DB:alphasynuclein_pathway, Pathway_Interaction_DB:amb2_neutrophils_pathway, Pathway_Interaction_DB:arf6cyclingpathway, Pathway_Interaction_DB:nfkappabatypicalpathway, Pathway_Interaction_DB:pi3kcipathway, Pathway_Interaction_DB:pi3kciaktpathway, Pathway_Interaction_DB:endothelinpathway, Pathway_Interaction_DB:epha_fwdpathway, Pathway_Interaction_DB:epha2_fwdpathway, Pathway_Interaction_DB:ephbfwdpathway, Pathway_Interaction_DB:ephrinbrevpathway, Pathway_Interaction_DB:fgf_pathway, Pathway_Interaction_DB:glypican_1pathway, Pathway_Interaction_DB:avb3_integrin_pathway, Pathway_Interaction_DB:lysophospholipid_pathway, Pathway_Interaction_DB:a4b1_paxindep_pathway, Pathway_Interaction_DB:pdgfrbpathway, Pathway_Interaction_DB:er_nongenomic_pathway, Pathway_Interaction_DB:ar_tf_pathway, Pathway_Interaction_DB:p38alphabetapathway, Pathway_Interaction_DB:s1p_s1p3_pathway, Pathway_Interaction_DB:met_pathway, Pathway_Interaction_DB:prlsignalingeventspathway, Pathway_Interaction_DB:ptp1bpathway, Pathway_Interaction_DB:vegfr1_2_pathway, Pathway_Interaction_DB:ret_pathway, Pathway_Interaction_DB:syndecan_2_pathway, Pathway_Interaction_DB:syndecan_3_pathway, Pathway_Interaction_DB:txa2pathway, Pathway_Interaction_DB:pi3kplctrkpathway, Reactome:REACT_111045, Reactome:REACT_111102, Reactome:REACT_111155, Reactome:REACT_11123, Reactome:REACT_116125, Reactome:REACT_604, Reactome:REACT_6900, BindingDB:P12931, ChEMBL:CHEMBL267, ChiTaRS:SRC, DrugBank:DB01254, EvolutionaryTrace:P12931, GenomeRNAi:6714, NextBio:26186, PMAP-CutDB:P12931, ArrayExpress:P12931, Bgee:P12931, CleanEx:HS_SRC, Genevestigator:P12931, GermOnline:ENSG00000197122, GO:0005901, GO:0005856, GO:0005829, GO:0005770, GO:0005764, GO:0005743, GO:0005634, GO:0005524, GO:0020037, GO:0005178, GO:0004715, GO:0005070, GO:0007411, GO:0045453, GO:0060444, GO:0007155, GO:0007049, GO:0016044, GO:0071393, GO:0007173, GO:0008543, GO:0030900, GO:0007243, GO:0050900, GO:2000811, GO:0043154, GO:2001237, GO:0051895, GO:2001243, GO:0032463, GO:0048011, GO:0048477, GO:0018108, GO:0030168, GO:0090263, GO:0033625, GO:0051897, GO:0050847, GO:0007265, GO:0045124, GO:0033146, GO:0043114, GO:0070555, GO:0007172, GO:0031295, GO:0060065, GO:0019048, Gene3D:3.30.505.10, InterPro:IPR011009, InterPro:IPR000719, InterPro:IPR017441, InterPro:IPR001245, InterPro:IPR000980, InterPro:IPR001452, InterPro:IPR008266, InterPro:IPR020635, Pfam:PF07714, Pfam:PF00017, Pfam:PF00018, PRINTS:PR00401, PRINTS:PR00452, PRINTS:PR00109, SMART:SM00252, SMART:SM00326, SMART:SM00219, SUPFAM:SSF56112, SUPFAM:SSF50044, PROSITE:PS00107, PROSITE:PS50011, PROSITE:PS00109, PROSITE:PS50001, PROSITE:PS50002 KEYWORDS 3D-structure; Alternative splicing; ATP-binding; Cell adhesion; Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Host-virus interaction; Immunity; Kinase; Lipoprotein; Membrane; Mitochondrion; Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; S-nitrosylation; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation. SOURCE Homo sapiens (human) ORGANISM Homo sapiens Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. REFERENCE 1 (residues 1 to 536) AUTHORS Deloukas,P., Matthews,L.H., Ashurst,J., Burton,J., Gilbert,J.G., Jones,M., Stavrides,G., Almeida,J.P., Babbage,A.K., Bagguley,C.L., Bailey,J., Barlow,K.F., Bates,K.N., Beard,L.M., Beare,D.M., Beasley,O.P., Bird,C.P., Blakey,S.E., Bridgeman,A.M., Brown,A.J., Buck,D., Burrill,W., Butler,A.P., Carder,C., Carter,N.P., Chapman,J.C., Clamp,M., Clark,G., Clark,L.N., Clark,S.Y., Clee,C.M., Clegg,S., Cobley,V.E., Collier,R.E., Connor,R., Corby,N.R., Coulson,A., Coville,G.J., Deadman,R., Dhami,P., Dunn,M., Ellington,A.G., Frankland,J.A., Fraser,A., French,L., Garner,P., Grafham,D.V., Griffiths,C., Griffiths,M.N., Gwilliam,R., Hall,R.E., Hammond,S., Harley,J.L., Heath,P.D., Ho,S., Holden,J.L., Howden,P.J., Huckle,E., Hunt,A.R., Hunt,S.E., Jekosch,K., Johnson,C.M., Johnson,D., Kay,M.P., Kimberley,A.M., King,A., Knights,A., Laird,G.K., Lawlor,S., Lehvaslaiho,M.H., Leversha,M., Lloyd,C., Lloyd,D.M., Lovell,J.D., Marsh,V.L., Martin,S.L., McConnachie,L.J., McLay,K., McMurray,A.A., Milne,S., Mistry,D., Moore,M.J., Mullikin,J.C., Nickerson,T., Oliver,K., Parker,A., Patel,R., Pearce,T.A., Peck,A.I., Phillimore,B.J., Prathalingam,S.R., Plumb,R.W., Ramsay,H., Rice,C.M., Ross,M.T., Scott,C.E., Sehra,H.K., Shownkeen,R., Sims,S., Skuce,C.D., Smith,M.L., Soderlund,C., Steward,C.A., Sulston,J.E., Swann,M., Sycamore,N., Taylor,R., Tee,L., Thomas,D.W., Thorpe,A., Tracey,A., Tromans,A.C., Vaudin,M., Wall,M., Wallis,J.M., Whitehead,S.L., Whittaker,P., Willey,D.L., Williams,L., Williams,S.A., Wilming,L., Wray,P.W., Hubbard,T., Durbin,R.M., Bentley,D.R., Beck,S. and Rogers,J. TITLE The DNA sequence and comparative analysis of human chromosome 20 JOURNAL Nature 414 (6866), 865-871 (2001) PUBMED 11780052 REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. REFERENCE 2 (residues 1 to 536) AUTHORS Mural,R.J., Istrail,S., Sutton,G.G., Florea,L., Halpern,A.L., Mobarry,C.M., Lippert,R., Walenz,B., Shatkay,H., Dew,I., Miller,J.R., Flanigan,M.J., Edwards,N.J., Bolanos,R., Fasulo,D., Halldorsson,B.V., Hannenhalli,S., Turner,R., Yooseph,S., Lu,F., Nusskern,D.R., Shue,B.C., Zheng,X.H., Zhong,F., Delcher,A.L., Huson,D.H., Kravitz,S.A., Mouchard,L., Reinert,K., Remington,K.A., Clark,A.G., Waterman,M.S., Eichler,E.E., Adams,M.D., Hunkapiller,M.W., Myers,E.W. and Venter,J.C. TITLE Direct Submission JOURNAL Submitted (??-SEP-2005) REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. REFERENCE 3 (residues 1 to 536) AUTHORS Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H., Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M., Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S., Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F., Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J., Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K., Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T., Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J., Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B., Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E., Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L., Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M., Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A., Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E., Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M., Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N., Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W., Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J., Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L., Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S., Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E., Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S., Makowski,K.A., Bosak,S. and Malek,J. CONSRTM MGC Project Team TITLE The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) JOURNAL Genome Res. 14 (10B), 2121-2127 (2004) PUBMED 15489334 REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).; TISSUE=Lung, and Skin Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to Morin, Ryan]] REFERENCE 4 (residues 1 to 536) AUTHORS Tanaka,A., Gibbs,C.P., Arthur,R.R., Anderson,S.K., Kung,H.J. and Fujita,D.J. TITLE DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes JOURNAL Mol. Cell. Biol. 7 (5), 1978-1983 (1987) PUBMED 3299057 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-185 (ISOFORM 1). REFERENCE 5 (residues 1 to 536) AUTHORS Anderson,S.K., Gibbs,C.P., Tanaka,A., Kung,H.J. and Fujita,D.J. TITLE Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src JOURNAL Mol. Cell. Biol. 5 (5), 1122-1129 (1985) PUBMED 2582238 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 186-536 (ISOFORM 1). REFERENCE 6 (residues 1 to 536) AUTHORS Pyper,J.M. and Bolen,J.B. TITLE Neuron-specific splicing of C-SRC RNA in human brain JOURNAL J. Neurosci. Res. 24 (1), 89-96 (1989) PUBMED 2681803 REMARK NUCLEOTIDE SEQUENCE [MRNA] OF 98-139 (ISOFORM 2). REFERENCE 7 (residues 1 to 536) AUTHORS Parker,R.C., Mardon,G., Lebo,R.V., Varmus,H.E. and Bishop,J.M. TITLE Isolation of duplicated human c-src genes located on chromosomes 1 and 20 JOURNAL Mol. Cell. Biol. 5 (4), 831-838 (1985) PUBMED 2581127 REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 376-536 (ISOFORM 1). REFERENCE 8 (residues 1 to 536) AUTHORS Smart,J.E., Oppermann,H., Czernilofsky,A.P., Purchio,A.F., Erikson,R.L. and Bishop,J.M. TITLE Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src) JOURNAL Proc. Natl. Acad. Sci. U.S.A. 78 (10), 6013-6017 (1981) PUBMED 6273838 REMARK PHOSPHORYLATION AT TYR-419. REFERENCE 9 (residues 1 to 536) AUTHORS Rosen,N., Bolen,J.B., Schwartz,A.M., Cohen,P., DeSeau,V. and Israel,M.A. TITLE Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues JOURNAL J. Biol. Chem. 261 (29), 13754-13759 (1986) PUBMED 3093483 REMARK ROLE IN TUMOR TISSUES. REFERENCE 10 (residues 1 to 536) AUTHORS Cartwright,C.A., Kamps,M.P., Meisler,A.I., Pipas,J.M. and Eckhart,W. TITLE pp60c-src activation in human colon carcinoma JOURNAL J. Clin. Invest. 83 (6), 2025-2033 (1989) PUBMED 2498394 REMARK ROLE IN COLON CARCINOMA. REFERENCE 11 (residues 1 to 536) AUTHORS Pyper,J.M. and Bolen,J.B. TITLE Identification of a novel neuronal C-SRC exon expressed in human brain JOURNAL Mol. Cell. Biol. 10 (5), 2035-2040 (1990) PUBMED 1691439 REMARK ALTERNATIVE SPLICING. REFERENCE 12 (residues 1 to 536) AUTHORS Kaplan,K.B., Bibbins,K.B., Swedlow,J.R., Arnaud,M., Morgan,D.O. and Varmus,H.E. TITLE Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527 JOURNAL EMBO J. 13 (20), 4745-4756 (1994) PUBMED 7525268 REMARK SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-530. REFERENCE 13 (residues 1 to 536) AUTHORS Stover,D.R., Liebetanz,J. and Lydon,N.B. TITLE Cdc2-mediated modulation of pp60c-src activity JOURNAL J. Biol. Chem. 269 (43), 26885-26889 (1994) PUBMED 7929427 REMARK PHOSPHORYLATION, AND ENZYME REGULATION. REFERENCE 14 (residues 1 to 536) AUTHORS David-Pfeuty,T. and Nouvian-Dooghe,Y. TITLE Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells JOURNAL J. Virol. 69 (3), 1699-1713 (1995) PUBMED 7853507 REMARK SUBCELLULAR LOCATION, AND FUNCTION. REFERENCE 15 (residues 1 to 536) AUTHORS Rabinowich,H., Manciulea,M., Metes,D., Sulica,A., Herberman,R.B., Corey,S.J. and Whiteside,T.L. TITLE Physical and functional association of Fc mu receptor on human natural killer cells with the zeta- and Fc epsilon RI gamma-chains and with src family protein tyrosine kinases JOURNAL J. Immunol. 157 (4), 1485-1491 (1996) PUBMED 8759729 REMARK INTERACTION WITH FCAMR, ENZYME REGULATION, AND FUNCTION. REFERENCE 16 (residues 1 to 536) AUTHORS Grano,M., Galimi,F., Zambonin,G., Colucci,S., Cottone,E., Zallone,A.Z. and Comoglio,P.M. TITLE Hepatocyte growth factor is a coupling factor for osteoclasts and osteoblasts in vitro JOURNAL Proc. Natl. Acad. Sci. U.S.A. 93 (15), 7644-7648 (1996) PUBMED 8755529 REMARK FUNCTION IN HGF SIGNALING PATHWAY. REFERENCE 17 (residues 1 to 536) AUTHORS Yang,E.B., Zhang,K., Cheng,L.Y. and Mack,P. TITLE Butein, a specific protein tyrosine kinase inhibitor JOURNAL Biochem. Biophys. Res. Commun. 245 (2), 435-438 (1998) PUBMED 9571170 REMARK ENZYME REGULATION. REFERENCE 18 (residues 1 to 536) AUTHORS Chang,B.Y., Conroy,K.B., Machleder,E.M. and Cartwright,C.A. TITLE RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells JOURNAL Mol. Cell. Biol. 18 (6), 3245-3256 (1998) PUBMED 9584165 REMARK INTERACTION WITH GNB2L1. REFERENCE 19 (residues 1 to 536) AUTHORS Luttrell,L.M., Ferguson,S.S., Daaka,Y., Miller,W.E., Maudsley,S., Della Rocca,G.J., Lin,F., Kawakatsu,H., Owada,K., Luttrell,D.K., Caron,M.G. and Lefkowitz,R.J. TITLE Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes JOURNAL Science 283 (5402), 655-661 (1999) PUBMED 9924018 REMARK INTERACTION WITH ADRB2 AND ARRB1. REFERENCE 20 (residues 1 to 536) AUTHORS Miller,W.E., Maudsley,S., Ahn,S., Khan,K.D., Luttrell,L.M. and Lefkowitz,R.J. TITLE beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis JOURNAL J. Biol. Chem. 275 (15), 11312-11319 (2000) PUBMED 10753943 REMARK INTERACTION WITH ARRB1 AND ARRB2. REFERENCE 21 (residues 1 to 536) AUTHORS Rebhun,J.F., Chen,H. and Quilliam,L.A. TITLE Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral JOURNAL J. Biol. Chem. 275 (18), 13406-13410 (2000) PUBMED 10747847 REMARK INTERACTION WITH RALGPS1. REFERENCE 22 (residues 1 to 536) AUTHORS Giglione,C., Gonfloni,S. and Parmeggiani,A. TITLE Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm JOURNAL Eur. J. Biochem. 268 (11), 3275-3283 (2001) PUBMED 11389730 REMARK FUNCTION IN PHOSPHORYLATION OF RASA1 AND RASGRF1. REFERENCE 23 (residues 1 to 536) AUTHORS Li,Y., Kuwahara,H., Ren,J., Wen,G. and Kufe,D. TITLE The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin JOURNAL J. Biol. Chem. 276 (9), 6061-6064 (2001) PUBMED 11152665 REMARK INTERACTION WITH MUC1. REFERENCE 24 (residues 1 to 536) AUTHORS Chang,B.Y., Chiang,M. and Cartwright,C.A. TITLE The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1 JOURNAL J. Biol. Chem. 276 (23), 20346-20356 (2001) PUBMED 11279199 REMARK INTERACTION WITH GNB2L1. REFERENCE 25 (residues 1 to 536) AUTHORS Korkaya,H., Jameel,S., Gupta,D., Tyagi,S., Kumar,R., Zafrullah,M., Mazumdar,M., Lal,S.K., Xiaofang,L., Sehgal,D., Das,S.R. and Sahal,D. TITLE The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK JOURNAL J. Biol. Chem. 276 (45), 42389-42400 (2001) PUBMED 11518702 REMARK INTERACTION WITH HEV ORF3 PROTEIN. REFERENCE 26 (residues 1 to 536) AUTHORS Lee,H., Park,D.S., Wang,X.B., Scherer,P.E., Schwartz,P.E. and Lisanti,M.P. TITLE Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1 JOURNAL J. Biol. Chem. 277 (37), 34556-34567 (2002) PUBMED 12091389 REMARK INTERACTION WITH CAV2. REFERENCE 27 (residues 1 to 536) AUTHORS Wong,C.W., McNally,C., Nickbarg,E., Komm,B.S. and Cheskis,B.J. TITLE Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade JOURNAL Proc. Natl. Acad. Sci. U.S.A. 99 (23), 14783-14788 (2002) PUBMED 12415108 REMARK INTERACTION WITH PELP1. Retracted:[Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ. Proc. Natl. Acad. Sci. U.S.A. 2009 Aug 18;106(33):14180. PMID: 19666546] REFERENCE 28 (residues 1 to 536) AUTHORS Miyazaki,T., Neff,L., Tanaka,S., Horne,W.C. and Baron,R. TITLE Regulation of cytochrome c oxidase activity by c-Src in osteoclasts JOURNAL J. Cell Biol. 160 (5), 709-718 (2003) PUBMED 12615910 REMARK FUNCTION, AND SUBCELLULAR LOCATION. REFERENCE 29 (residues 1 to 536) AUTHORS Vindis,C., Cerretti,D.P., Daniel,T.O. and Huynh-Do,U. TITLE EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis JOURNAL J. Cell Biol. 162 (4), 661-671 (2003) PUBMED 12925710 REMARK INTERACTION WITH EPHB1. REFERENCE 30 (residues 1 to 536) AUTHORS Kamath,J.R., Liu,R., Enstrom,A.M., Lou,Q. and Lam,K.S. TITLE Development and characterization of potent and specific peptide inhibitors of p60c-src protein tyrosine kinase using pseudosubstrate-based inhibitor design approach JOURNAL J. Pept. Res. 62 (6), 260-268 (2003) PUBMED 14632929 REMARK ENZYME REGULATION. REFERENCE 31 (residues 1 to 536) AUTHORS Taniyama,Y., Weber,D.S., Rocic,P., Hilenski,L., Akers,M.L., Park,J., Hemmings,B.A., Alexander,R.W. and Griendling,K.K. TITLE Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal adhesions JOURNAL Mol. Cell. Biol. 23 (22), 8019-8029 (2003) PUBMED 14585963 REMARK FUNCTION IN PHOSPHORYLATION OF PDPK1, AND INTERACTION WITH PTK2B/PYK2. REFERENCE 32 (residues 1 to 536) AUTHORS Wang,X.B., Lee,H., Capozza,F., Marmon,S., Sotgia,F., Brooks,J.W., Campos-Gonzalez,R. and Lisanti,M.P. TITLE Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27) JOURNAL Biochemistry 43 (43), 13694-13706 (2004) PUBMED 15504032 REMARK INTERACTION WITH CAV2. REFERENCE 33 (residues 1 to 536) AUTHORS Benes,C.H., Wu,N., Elia,A.E., Dharia,T., Cantley,L.C. and Soltoff,S.P. TITLE The C2 domain of PKCdelta is a phosphotyrosine binding domain JOURNAL Cell 121 (2), 271-280 (2005) PUBMED 15851033 REMARK INTERACTION WITH CDCP1. REFERENCE 34 (residues 1 to 536) AUTHORS Yang,K., Kim,J.H., Kim,H.J., Park,I.S., Kim,I.Y. and Yang,B.S. TITLE Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation JOURNAL J. Biol. Chem. 280 (47), 39058-39066 (2005) PUBMED 16186108 REMARK FUNCTION IN PHOSPHORYLATION OF DDR2. REFERENCE 35 (residues 1 to 536) AUTHORS Franco,M., Furstoss,O., Simon,V., Benistant,C., Hong,W.J. and Roche,S. TITLE The adaptor protein Tom1L1 is a negative regulator of Src mitogenic signaling induced by growth factors JOURNAL Mol. Cell. Biol. 26 (5), 1932-1947 (2006) PUBMED 16479011 REMARK INTERACTION WITH TOM1L2. REFERENCE 36 (residues 1 to 536) AUTHORS Maudsley,S., Davidson,L., Pawson,A.J., Freestone,S.H., Lopez de Maturana,R., Thomson,A.A. and Millar,R.P. TITLE Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5 JOURNAL Neuroendocrinology 84 (5), 285-300 (2006) PUBMED 17202804 REMARK INTERACTION WITH TGFB1I1. REFERENCE 37 (residues 1 to 536) AUTHORS Huang,H., Lu,F.I., Jia,S., Meng,S., Cao,Y., Wang,Y., Ma,W., Yin,K., Wen,Z., Peng,J., Thisse,C., Thisse,B. and Meng,A. TITLE Amotl2 is essential for cell movements in zebrafish embryo and regulates c-Src translocation JOURNAL Development 134 (5), 979-988 (2007) PUBMED 17293535 REMARK INTERACTION WITH AMOTL2. REFERENCE 38 (residues 1 to 536) AUTHORS Di Stefano,P., Damiano,L., Cabodi,S., Aramu,S., Tordella,L., Praduroux,A., Piva,R., Cavallo,F., Forni,G., Silengo,L., Tarone,G., Turco,E. and Defilippi,P. TITLE p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity JOURNAL EMBO J. 26 (12), 2843-2855 (2007) PUBMED 17525734 REMARK INTERACTION WITH SRCIN1. REFERENCE 39 (residues 1 to 536) AUTHORS Jeulin,C., Seltzer,V., Bailbe,D., Andreau,K. and Marano,F. TITLE EGF mediates calcium-activated chloride channel activation in the human bronchial epithelial cell line 16HBE14o-: involvement of tyrosine kinase p60c-src JOURNAL Am. J. Physiol. 295, L489-L496 (2008) PUBMED 18586953 REMARK FUNCTION. REFERENCE 40 (residues 1 to 536) AUTHORS Yang,K.J., Shin,S., Piao,L., Shin,E., Li,Y., Park,K.A., Byun,H.S., Won,M., Hong,J., Kweon,G.R., Hur,G.M., Seok,J.H., Chun,T., Brazil,D.P., Hemmings,B.A. and Park,J. TITLE Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding JOURNAL J. Biol. Chem. 283 (3), 1480-1491 (2008) PUBMED 18024423 REMARK INTERACTION WITH PDPK1. REFERENCE 41 (residues 1 to 536) AUTHORS Zahedi,R.P., Lewandrowski,U., Wiesner,J., Wortelkamp,S., Moebius,J., Schutz,C., Walter,U., Gambaryan,S. and Sickmann,A. TITLE Phosphoproteome of resting human platelets JOURNAL J. Proteome Res. 7 (2), 526-534 (2008) PUBMED 18088087 REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS SPECTROMETRY.; TISSUE=Platelet REFERENCE 42 (residues 1 to 536) AUTHORS Le Romancer,M., Treilleux,I., Leconte,N., Robin-Lespinasse,Y., Sentis,S., Bouchekioua-Bouzaghou,K., Goddard,S., Gobert-Gosse,S. and Corbo,L. TITLE Regulation of estrogen rapid signaling through arginine methylation by PRMT1 JOURNAL Mol. Cell 31 (2), 212-221 (2008) PUBMED 18657504 REMARK INTERACTION WITH PTK2/FAK1; PI3KR1/2 AND ESR1. REFERENCE 43 (residues 1 to 536) AUTHORS Daub,H., Olsen,J.V., Bairlein,M., Gnad,F., Oppermann,F.S., Korner,R., Greff,Z., Keri,G., Stemmann,O. and Mann,M. TITLE Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle JOURNAL Mol. Cell 31 (3), 438-448 (2008) PUBMED 18691976 REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].; TISSUE=Cervix carcinoma REFERENCE 44 (residues 1 to 536) AUTHORS Voss,M., Lettau,M. and Janssen,O. TITLE Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening JOURNAL BMC Immunol. 10, 53 (2009) PUBMED 19807924 REMARK INTERACTION WITH FASLG. Publication Status: Online-Only REFERENCE 45 (residues 1 to 536) AUTHORS Johnsen,I.B., Nguyen,T.T., Bergstroem,B., Fitzgerald,K.A. and Anthonsen,M.W. TITLE The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling JOURNAL J. Biol. Chem. 284 (28), 19122-19131 (2009) PUBMED 19419966 REMARK FUNCTION, AND INTERACTION WITH TRAF3; MAVS; DDX58 AND TBK1. REFERENCE 46 (residues 1 to 536) AUTHORS Chabot,C., Spring,K., Gratton,J.P., Elchebly,M. and Royal,I. TITLE New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival JOURNAL Mol. Cell. Biol. 29 (1), 241-253 (2009) PUBMED 18936167 REMARK PHOSPHORYLATION AT TYR-419, AND DEPHOSPHORYLATION BY PTPRJ AT TYR-419. REFERENCE 47 (residues 1 to 536) AUTHORS Oppermann,F.S., Gnad,F., Olsen,J.V., Hornberger,R., Greff,Z., Keri,G., Mann,M. and Daub,H. TITLE Large-scale proteomics analysis of the human kinome JOURNAL Mol. Cell. Proteomics 8 (7), 1751-1764 (2009) PUBMED 19369195 REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND TYR-530, AND MASS SPECTROMETRY. REFERENCE 48 (residues 1 to 536) AUTHORS Mayya,V., Lundgren,D.H., Hwang,S.I., Rezaul,K., Wu,L., Eng,J.K., Rodionov,V. and Han,D.K. TITLE Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions JOURNAL Sci. Signal. 2 (84), RA46 (2009) PUBMED 19690332 REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].; TISSUE=Leukemic T-cell Publication Status: Online-Only REFERENCE 49 (residues 1 to 536) AUTHORS Yao,X., Balamurugan,P., Arvey,A., Leslie,C. and Zhang,L. TITLE Heme controls the regulation of protein tyrosine kinases Jak2 and Src JOURNAL Biochem. Biophys. Res. Commun. 403 (1), 30-35 (2010) PUBMED 21036157 REMARK ENZYME REGULATION. REFERENCE 50 (residues 1 to 536) AUTHORS Goh,Y.M., Cinghu,S., Hong,E.T., Lee,Y.S., Kim,J.H., Jang,J.W., Li,Y.H., Chi,X.Z., Lee,K.S., Wee,H., Ito,Y., Oh,B.C. and Bae,S.C. TITLE Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm JOURNAL J. Biol. Chem. 285 (13), 10122-10129 (2010) PUBMED 20100835 REMARK FUNCTION, AND INTERACTION WITH RUNX3. REFERENCE 51 (residues 1 to 536) AUTHORS Mund,T. and Pelham,H.R. TITLE Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2 JOURNAL Proc. Natl. Acad. Sci. U.S.A. 107 (25), 11429-11434 (2010) PUBMED 20534535 REMARK INTERACTION WITH NDFIP1 AND NDFIP2. REFERENCE 52 (residues 1 to 536) AUTHORS Chan,W., Sit,S.T. and Manser,E. TITLE The Cdc42-associated kinase ACK1 is not autoinhibited but requires Src for activation JOURNAL Biochem. J. 435 (2), 355-364 (2011) PUBMED 21309750 REMARK FUNCTION, AND INTERACTION WITH TNK2. REFERENCE 53 (residues 1 to 536) AUTHORS Pan,Q., Qiao,F., Gao,C., Norman,B., Optican,L. and Zelenka,P.S. TITLE Cdk5 targets active Src for ubiquitin-dependent degradation by phosphorylating Src(S75) JOURNAL Cell. Mol. Life Sci. 68 (20), 3425-3436 (2011) PUBMED 21442427 REMARK PHOSPHORYLATION AT SER-75. REFERENCE 54 (residues 1 to 536) AUTHORS Brown,M.T. and Cooper,J.A. TITLE Regulation, substrates and functions of src JOURNAL Biochim. Biophys. Acta 1287 (2-3), 121-149 (1996) PUBMED 8672527 REMARK REVIEW ON FUNCTION. REFERENCE 55 (residues 1 to 536) AUTHORS Thomas,S.M. and Brugge,J.S. TITLE Cellular functions regulated by Src family kinases JOURNAL Annu. Rev. Cell Dev. Biol. 13, 513-609 (1997) PUBMED 9442882 REMARK REVIEW ON FUNCTION. REFERENCE 56 (residues 1 to 536) AUTHORS Ma,Y.C. and Huang,X.Y. TITLE Novel regulation and function of Src tyrosine kinase JOURNAL Cell. Mol. Life Sci. 59 (3), 456-462 (2002) PUBMED 11964124 REMARK REVIEW ON FUNCTION. REFERENCE 57 (residues 1 to 536) AUTHORS Wang,Y., Cao,H., Chen,J. and McNiven,M.A. TITLE A direct interaction between the large GTPase dynamin-2 and FAK regulates focal adhesion dynamics in response to active Src JOURNAL Mol. Biol. Cell 22 (9), 1529-1538 (2011) PUBMED 21411625 REMARK FUNCTION IN FOCAL ADHESION DYNAMICS, AND INTERACTION WITH PTK2/FAK1 AND DNM2. REFERENCE 58 (residues 1 to 536) AUTHORS Zhang,P., Guo,A., Possemato,A., Wang,C., Beard,L., Carlin,C., Markowitz,S.D., Polakiewicz,R.D. and Wang,Z. TITLE Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14 JOURNAL Oncogene (2012) In press PUBMED 22710723 REMARK FUNCTION IN PHOSPHORYLATION OF BCAR1. Publication Status: Available-Online prior to print REFERENCE 59 (residues 1 to 536) AUTHORS Xu,W., Harrison,S.C. and Eck,M.J. TITLE Three-dimensional structure of the tyrosine kinase c-Src JOURNAL Nature 385 (6617), 595-602 (1997) PUBMED 9024657 REMARK X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 86-536. REFERENCE 60 (residues 1 to 536) AUTHORS Charifson,P.S., Shewchuk,L.M., Rocque,W., Hummel,C.W., Jordan,S.R., Mohr,C., Pacofsky,G.J., Peel,M.R., Rodriguez,M., Sternbach,D.D. and Consler,T.G. TITLE Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study JOURNAL Biochemistry 36 (21), 6283-6293 (1997) PUBMED 9174343 REMARK X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 145-249. REFERENCE 61 (residues 1 to 536) AUTHORS Xu,R.X., Word,J.M., Davis,D.G., Rink,M.J., Willard,D.H. Jr. and Gampe,R.T. Jr. TITLE Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide JOURNAL Biochemistry 34 (7), 2107-2121 (1995) PUBMED 7532003 REMARK STRUCTURE BY NMR OF 204-249. REFERENCE 62 (residues 1 to 536) AUTHORS Greenman,C., Stephens,P., Smith,R., Dalgliesh,G.L., Hunter,C., Bignell,G., Davies,H., Teague,J., Butler,A., Stevens,C., Edkins,S., O'Meara,S., Vastrik,I., Schmidt,E.E., Avis,T., Barthorpe,S., Bhamra,G., Buck,G., Choudhury,B., Clements,J., Cole,J., Dicks,E., Forbes,S., Gray,K., Halliday,K., Harrison,R., Hills,K., Hinton,J., Jenkinson,A., Jones,D., Menzies,A., Mironenko,T., Perry,J., Raine,K., Richardson,D., Shepherd,R., Small,A., Tofts,C., Varian,J., Webb,T., West,S., Widaa,S., Yates,A., Cahill,D.P., Louis,D.N., Goldstraw,P., Nicholson,A.G., Brasseur,F., Looijenga,L., Weber,B.L., Chiew,Y.E., DeFazio,A., Greaves,M.F., Green,A.R., Campbell,P., Birney,E., Easton,D.F., Chenevix-Trench,G., Tan,M.H., Khoo,S.K., Teh,B.T., Yuen,S.T., Leung,S.Y., Wooster,R., Futreal,P.A. and Stratton,M.R. TITLE Patterns of somatic mutation in human cancer genomes JOURNAL Nature 446 (7132), 153-158 (2007) PUBMED 17344846 REMARK VARIANT [LARGE SCALE ANALYSIS] THR-237. COMMENT On or before Nov 25, 2009 this sequence version replaced gi:74749849, gi:625219. [FUNCTION] Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of ADRBK1, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. [CATALYTIC ACTIVITY] ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. [ENZYME REGULATION] Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity. [SUBUNIT] Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1. Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with ERBB2, STAT1 and PNN. Interacts with DDR1, DDR2 and DAB2. Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with HEV ORF3 protein; via the SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with ARRB1 and ARRB2. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine). Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with PDGFRA (tyrosine phosphorylated). Interacts with CSF1R. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with FCAMR. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. [INTERACTION] Self; NbExp=2; IntAct=EBI-621482, EBI-621482; P42684:ABL2; NbExp=2; IntAct=EBI-621482, EBI-1102694; P12814:ACTN1; NbExp=2; IntAct=EBI-621482, EBI-351710; Q8R5G7:Arap3 (xeno); NbExp=3; IntAct=EBI-621482, EBI-621463; Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-621482, EBI-346622; P12830:CDH1; NbExp=2; IntAct=EBI-621482, EBI-727477; P00533:EGFR; NbExp=5; IntAct=EBI-621482, EBI-297353; P04626:ERBB2; NbExp=10; IntAct=EBI-621482, EBI-641062; P03372-4:ESR1; NbExp=2; IntAct=EBI-621482, EBI-4309277; P25445:FAS; NbExp=2; IntAct=EBI-621482, EBI-494743; Q9Y6K9:IKBKG; NbExp=3; IntAct=EBI-621482, EBI-81279; P35968:KDR; NbExp=2; IntAct=EBI-621482, EBI-1005487; Q07666:KHDRBS1; NbExp=3; IntAct=EBI-621482, EBI-1364; Q05397:PTK2; NbExp=4; IntAct=EBI-621482, EBI-702142; Q13905:RAPGEF1; NbExp=2; IntAct=EBI-621482, EBI-976876; Q01973:ROR1; NbExp=9; IntAct=EBI-621482, EBI-6082337; Q9C0H9:SRCIN1; NbExp=3; IntAct=EBI-621482, EBI-1393949; Q68CZ2:TNS3; NbExp=13; IntAct=EBI-621482, EBI-1220488. [SUBCELLULAR LOCATION] Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P12931-1; Sequence=Displayed; Name=2; IsoId=P12931-2; Sequence=VSP_012134. [TISSUE SPECIFICITY] Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues. [DOMAIN] The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment. [PTM] Myristoylated at Gly-2, and this is essential for targeting to membranes. [PTM] Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. [PTM] S-nitrosylation is important for activation of its kinase activity (By similarity). [PTM] Ubiquitinated in response to CDK5-mediated phosphorylation. [DISEASE] Note=SRC kinase activity has been shown to be increased in several tumor tissues and tumor cell lines such as colon carcinoma cells. [SIMILARITY] Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. [SIMILARITY] Contains 1 protein kinase domain. [SIMILARITY] Contains 1 SH2 domain. [SIMILARITY] Contains 1 SH3 domain. FEATURES Location/Qualifiers source 1..536 /organism="Homo sapiens" /db_xref="taxon:9606" gene 1..536 /gene="SRC" /gene_synonym="SRC1" Protein 1..536 /gene="SRC" /gene_synonym="SRC1" /product="Proto-oncogene tyrosine-protein kinase Src" /EC_number="2.7.10.2" /note="Proto-oncogene c-Src; pp60c-src; p60-Src" /UniProtKB_evidence="Evidence at protein level" Region 1..536 /gene="SRC" /gene_synonym="SRC1" /region_name="Mature chain" /experiment="experimental evidence, no additional details recorded" /note="Proto-oncogene tyrosine-protein kinase Src. /FTId=PRO_0000088141." Site 2 /gene="SRC" /gene_synonym="SRC1" /site_type="lipid-binding" /experiment="experimental evidence, no additional details recorded" /note="N-myristoyl glycine." Site 17 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine." Site 35 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine." Site 69 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine." Site 74 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine." Site 75 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphoserine; by CDK5." Region 84..145 /gene="SRC" /gene_synonym="SRC1" /region_name="Domain" /experiment="experimental evidence, no additional details recorded" /note="SH3." Region 87..93 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 88..143 /gene="SRC" /gene_synonym="SRC1" /region_name="SH3_Src" /note="Src homology 3 domain of Src Protein Tyrosine Kinase; cd12008" /db_xref="CDD:212941" Site order(88..95,98..99,101..105,109..114,116,118,120..129, 131..135,139..143) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="swapped dimer interface [polypeptide binding]" /db_xref="CDD:212941" Site order(93,95..99,102,118..121,134,136,138..139) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="peptide ligand binding site [polypeptide binding]" /db_xref="CDD:212941" Region 99..102 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 110..114 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 117 /gene="SRC" /gene_synonym="SRC1" /region_name="Splicing variant" /experiment="experimental evidence, no additional details recorded" /note="T -> TRKVDVR (in isoform 2). /FTId=VSP_012134." Region 118..126 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 127..129 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 132..136 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 137..139 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 140..142 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 146..148 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 147..247 /gene="SRC" /gene_synonym="SRC1" /region_name="SH2_Src_Src" /note="Src homology 2 (SH2) domain found in tyrosine kinase sarcoma (Src); cd10365" /db_xref="CDD:198228" Region 151..248 /gene="SRC" /gene_synonym="SRC1" /region_name="Domain" /experiment="experimental evidence, no additional details recorded" /note="SH2." Region 152..154 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site order(158,178,180..183,188,204,206,239) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="autoinhibitory site [polypeptide binding]" /db_xref="CDD:198228" Site order(158,178,204,206) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="phosphotyrosine binding pocket [polypeptide binding]" /db_xref="CDD:198228" Region 158..165 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 167..170 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 174..179 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 176 /gene="SRC" /gene_synonym="SRC1" /region_name="Variant" /experiment="experimental evidence, no additional details recorded" /note="L -> F (in dbSNP:rs6018260). /FTId=VAR_051699." Region 181..183 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 187..195 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site 187 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /inference="non-experimental evidence, no additional details recorded" /note="Phosphotyrosine (By similarity)." Region 196..198 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 199..209 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site order(205,233) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="hydrophobic binding pocket [polypeptide binding]" /db_xref="CDD:198228" Region 211..213 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 215..218 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 221..225 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 226..233 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 237 /gene="SRC" /gene_synonym="SRC1" /region_name="Variant" /experiment="experimental evidence, no additional details recorded" /note="A -> T (in dbSNP:rs34881773). /FTId=VAR_041830." Region 240..242 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 256..259 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 263..522 /gene="SRC" /gene_synonym="SRC1" /region_name="PTKc_Src_like" /note="Catalytic domain of Src kinase-like Protein Tyrosine Kinases; cd05034" /db_xref="CDD:173626" Region 267..269 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 270..523 /gene="SRC" /gene_synonym="SRC1" /region_name="Domain" /experiment="experimental evidence, no additional details recorded" /note="Protein kinase." Region 270..519 /gene="SRC" /gene_synonym="SRC1" /region_name="Pkinase_Tyr" /note="Protein tyrosine kinase; pfam07714" /db_xref="CDD:203736" Region 270..278 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site order(276,278..280,284,296,298,341..344,348,389,393..394, 396,407,424..428,437,471) /gene="SRC" /gene_synonym="SRC1" /site_type="active" /db_xref="CDD:173626" Site order(276,279,284,296,298,341..344,348,389,391,394,396, 407) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="ATP binding site [chemical binding]" /db_xref="CDD:173626" Site 276..284 /gene="SRC" /gene_synonym="SRC1" /site_type="np-binding" /experiment="experimental evidence, no additional details recorded" /note="ATP." Region 283..289 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site order(290,292,324,327,329,342,368,372,400,520) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="SH3/SH2 domain interface [polypeptide binding]" /db_xref="CDD:173626" Region 290..292 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 293..299 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site 298 /gene="SRC" /gene_synonym="SRC1" /site_type="binding" /experiment="experimental evidence, no additional details recorded" /note="ATP." Region 302..304 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 307..319 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 328..332 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 334..336 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 338..341 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 349..353 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 355..358 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 363..382 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Site order(389,393,424..428,437,471) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:173626" Site 389 /gene="SRC" /gene_synonym="SRC1" /site_type="active" /experiment="experimental evidence, no additional details recorded" /note="Proton acceptor." Region 392..394 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 395..397 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Region 399..401 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 403..405 /gene="SRC" /gene_synonym="SRC1" /region_name="Beta-strand region" /experiment="experimental evidence, no additional details recorded" Site order(406..415,417..422,424..430) /gene="SRC" /gene_synonym="SRC1" /site_type="other" /note="activation loop (A-loop)" /db_xref="CDD:173626" Region 410..413 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 417..420 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Site 419 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphotyrosine; by autocatalysis; alternate." Site 419 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /inference="non-experimental evidence, no additional details recorded" /note="Phosphotyrosine; by FAK2; alternate (By similarity)." Region 423..426 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 429..431 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 434..439 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Site 439 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphotyrosine." Region 444..459 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 460..462 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Region 471..479 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 492..501 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Site 501 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /inference="non-experimental evidence, no additional details recorded" /note="S-nitrosocysteine (By similarity)." Region 506..508 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Site 511 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphothreonine." Region 512..520 /gene="SRC" /gene_synonym="SRC1" /region_name="Helical region" /experiment="experimental evidence, no additional details recorded" Region 521..523 /gene="SRC" /gene_synonym="SRC1" /region_name="Hydrogen bonded turn" /experiment="experimental evidence, no additional details recorded" Site 522 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphotyrosine." Site 530 /gene="SRC" /gene_synonym="SRC1" /site_type="modified" /experiment="experimental evidence, no additional details recorded" /note="Phosphotyrosine; by CSK." ORIGIN 1 mgsnkskpkd asqrrrslep aenvhgaggg afpasqtpsk pasadghrgp saafapaaae 61 pklfggfnss dtvtspqrag plaggvttfv alydyesrte tdlsfkkger lqivnntegd 121 wwlahslstg qtgyipsnyv apsdsiqaee wyfgkitrre serlllnaen prgtflvres 181 ettkgaycls vsdfdnakgl nvkhykirkl dsggfyitsr tqfnslqqlv ayyskhadgl 241 chrlttvcpt skpqtqglak daweipresl rlevklgqgc fgevwmgtwn gttrvaiktl 301 kpgtmspeaf lqeaqvmkkl rheklvqlya vvseepiyiv teymskgsll dflkgetgky 361 lrlpqlvdma aqiasgmayv ermnyvhrdl raanilvgen lvckvadfgl arliedneyt 421 arqgakfpik wtapeaalyg rftiksdvws fgillteltt kgrvpypgmv nrevldqver 481 gyrmpcppec peslhdlmcq cwrkepeerp tfeylqafle dyftstepqy qpgenl //}} |
TBD: Some fancy plot with multi-colored boxes and dots and a figure legend. :) Should be a rectangle with various multicolored domains marked out on it. Probably should be drawn in several rows according to "site" or "region" among other things to permit overlaps. Should show all features except those listed in exclude, show note rather than site_type or region_name for those indicated as usenote, and substitute annotation of the active site as directed. |
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(This doesn't work because it isn't written yet!)
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