ID SRC_RSVSE Reviewed; 526 AA. AC P63185; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 95. DE RecName: Full=Tyrosine-protein kinase transforming protein Src; DE EC=2.7.10.2; DE AltName: Full=pp60v-src; DE Short=p60-Src; DE Short=v-Src; GN Name=V-SRC; OS Rous sarcoma virus subgroup E (strain Schmidt-Ruppin) (RSV-SR-E). OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes; OC Ortervirales; Retroviridae; Orthoretrovirinae; Alpharetrovirus; OC Rous sarcoma virus. OX NCBI_TaxID=270623; OH NCBI_TaxID=9031; Gallus gallus (Chicken). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2537953; DOI=10.1093/nar/17.3.1252; RA Barnier J.V., Dezelee P., Marx M., Calothy G.; RT "Nucleotide sequence of the src gene of the Schmidt-Ruppin strain of Rous RT sarcoma virus type E."; RL Nucleic Acids Res. 17:1252-1252(1989). CC -!- FUNCTION: This phosphoprotein, required for both the initiation and the CC maintenance of neoplastic transformation, is a protein kinase that CC catalyzes the phosphorylation of tyrosine residues in vitro. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- PTM: The phosphorylated form is termed pp60v-src. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X13745; CAA32012.1; -; Genomic_DNA. DR PDB; 2JYQ; NMR; -; A=144-249. DR PDB; 7PVT; X-ray; 1.60 A; A/C=81-141. DR PDBsum; 2JYQ; -. DR PDBsum; 7PVT; -. DR SMR; P63185; -. DR BindingDB; P63185; -. DR DrugBank; DB01773; 4-[3-carboxymethyl-3-(4-phosphonooxy-benzyl)-ureido]-4-[(3-cyclohexyl-propyl)-methyl-carbamoyl]butyric acid. DR EvolutionaryTrace; P63185; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd10365; SH2_Src_Src; 1. DR CDD; cd12008; SH3_Src; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24418:SF53; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC; 1. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Kinase; Lipoprotein; Myristate; KW Nucleotide-binding; Oncogene; Phosphoprotein; SH2 domain; SH3 domain; KW Transferase; Tyrosine-protein kinase. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000250" FT CHAIN 2..526 FT /note="Tyrosine-protein kinase transforming protein Src" FT /id="PRO_0000088154" FT DOMAIN 81..142 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 148..245 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT DOMAIN 267..517 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 27..53 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 386 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10028" FT BINDING 273..281 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 416 FT /note="Phosphotyrosine; by autocatalysis" FT /evidence="ECO:0000250" FT LIPID 2 FT /note="N-myristoyl glycine; by host" FT /evidence="ECO:0000250" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:2JYQ" FT HELIX 155..162 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 171..176 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 184..192 FT /evidence="ECO:0007829|PDB:2JYQ" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 196..206 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 212..217 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:2JYQ" FT HELIX 223..230 FT /evidence="ECO:0007829|PDB:2JYQ" FT STRAND 237..239 FT /evidence="ECO:0007829|PDB:2JYQ" SQ SEQUENCE 526 AA; 58953 MW; 85D356B6B8ECB14D CRC64; MGSSKSKPKG PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL FGDFNTSDTV TSPQRAGALA GGVTTFVALY DYESWIETDL SFKKGERLQI VNNTEGNWWL AHSVTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG TMSPEAFLQE AQVMKKLRHK KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMGNGE VLDRVERGYR MPCPPECPES LHDLMSQCWR RDPEERPTFE YLQAQLLPAC VLEVAE //