Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11887-00292
Entry Name
UniProt Accession
Theoretical PI
8.16
Molecular Weight
59075.3
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Tyrosine-protein kinase transforming protein Src
Protein Synonyms/Alias
2.7.10.2; pp60v-src; p60-Src; v-Src;
Gene Name
V-SRC
Gene Synonyms/Alias
Created Date
01-MAR-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGSSKSKPK
[1][2]
N-Myristoylation
Organism
Rous sarcoma virus (strain H-19)
NCBI Taxa ID
11887
Reference
[1] Shoji S, Tashiro A, Furuishi K, Takenaka O, Kida Y, Horiuchi S, Funakoshi T,Kubota Y. Antibodies to an NH2-terminal myristoyl glycine moiety can detectNH2-terminal myristoylated proteins in the retrovirus-infected cells. BiochemBiophys Res Commun. 1989 Jul 31;162(2):724-32.[PMID:2547372]
[2] Kamps MP, Buss JE, Sefton BM. Mutation of NH2-terminal glycine of p60srcprevents both myristoylation and morphological transformation. Proc Natl Acad SciU S A. 1985 Jul;82(14):4625-8.[PMID:2991884]
Functional Description
This phosphoprotein, required for both the initiation and the maintenance of neoplastic transformation, is a protein kinase that catalyzes the phosphorylation of tyrosine residues in vitro.
Sequence Annotation
Domain: 81 142 SH3.
Domain: 148 245 SH2.
Domain: 267 517 Protein kinase.
Nucleotide-binding: 273 281 ATP.
Active site: 386 386 Proton acceptor.
Binding site: 295 295 ATP.
Modified residue: 416 416 Phosphotyrosine; by autocatalysis.
Protein Length
526 AA.
Protein Sequence
(Canonical)
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPDETAA PDAHRNPSRS FGTVATEPKL  60
FWGFNTSDTV TSPQRAGALA GGVTTFVALY DYESWTETDL SFKKGERLQI VNNTEGDWWL  120
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRKSETA  180
KGAYCLSVSD FDNAKGPNVK HYKICKLYSG GFYITSRTQF GSLQQLVAYY SKHADGLCHR  240
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE AKLGQGCFGE VWMGTWNGTT RVAIKTLKPG  300
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVIEY MSKGSLLDFL KGEMGKYLRL  360
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ  420
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERAYR  480
MPCPPECPES LHDLMCQCWR KDPEERPTFK YLQAQLLPAC VLEVAE                 526
FASTA
(Canonical)
>LipidDB-11887-00292|P25020
MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPDETAAPDAHRNPSRSFGTVATEPKL
FWGFNTSDTVTSPQRAGALAGGVTTFVALYDYESWTETDLSFKKGERLQIVNNTEGDWWL
AHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRKSETA
KGAYCLSVSDFDNAKGPNVKHYKICKLYSGGFYITSRTQFGSLQQLVAYYSKHADGLCHR
LTNVCPTSKPQTQGLAKDAWEIPRESLRLEAKLGQGCFGEVWMGTWNGTTRVAIKTLKPG
TMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVIEYMSKGSLLDFLKGEMGKYLRL
PQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQ
GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERAYR
MPCPPECPESLHDLMCQCWRKDPEERPTFKYLQAQLLPACVLEVAE
Gene Ontology
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC
Interpro
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom
InterPro; IPR000980; SH2
InterPro; IPR001452; SH3_domain
InterPro; IPR008266; Tyr_kinase_AS
InterPro; IPR020635; Tyr_kinase_cat_dom
Pfam
Pfam; PF07714; Pkinase_Tyr;
Pfam; PF00017; SH2;
Pfam; PF00018; SH3_1;
SMART
SMART; SM00252; SH2;
SMART; SM00326; SH3;
SMART; SM00219; TyrKc;
PROSITE
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00109; PROTEIN_KINASE_TYR;
PROSITE; PS50001; SH2;
PROSITE; PS50002; SH3;
PRINTS
PRINTS; PR00401; SH2DOMAIN;
PRINTS; PR00452; SH3DOMAIN;
PRINTS; PR00109; TYRKINASE;