Tyrosine-protein kinase transforming protein Src

Details

Name
Tyrosine-protein kinase transforming protein Src
Synonyms
  • 2.7.10.2
  • p60-Src
  • pp60v-src
  • v-Src
Gene Name
V-SRC
Organism
RSV-SRA
Amino acid sequence
>lcl|BSEQ0013014|Tyrosine-protein kinase transforming protein Src
MGSSKSKPKDPSQRRCSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKL
FGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWL
AHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETT
KGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHR
LTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPG
TMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRL
PQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQ
GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMGNGEVLDRVERGYR
MPCPPECPESLHDLMCQCWRRDPEERPTFEYLQAQLLPACVLEVAE
Number of residues
526
Molecular Weight
58877.475
Theoretical pI
7.87
GO Classification
Functions
ATP binding / non-membrane spanning protein tyrosine kinase activity
General Function
Non-membrane spanning protein tyrosine kinase activity
Specific Function
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0008211|1581 bp
ATGGGGAGTAGCAAGAGCAAGCCTAAGGACCCCAGCCAGCGCCGGCGCAGCCTGGAGCCA
CCCGACAGCACCCACCACGGGGGATTCCCAGCCTCGCAGACCCCCAACAAGACAGCAGCC
CCCGACACGCACCGCACCCCCAGCCGCTCCTTCGGGACCGTGGCCACCGAGCCCAAGCTC
TTCGGGGGCTTCAACACTTCTGACACCGTTACGTCGCCGCAGCGTGCCGGGGCACTGGCT
GGCGGCGTCACCACTTTCGTGGCTCTCTACGACTACGAGTCCTGGATTGAAACGGACTTG
TCCTTCAAGAAAGGAGAACGGCTGCAGATTGTCAACAACACGGAAGGTAACTGGTGGCTG
GCTCATTCCCTCACTACAGGACAGACGGGCTACATCCCCAGTAACTATGTCGCGCCCTCA
GACTCCATCCAGGCTGAAGAGTGGTACTTTGGGAAGATCACTCGTCGGGAGTCCGAGCGG
CTGCTGCTCAACCCCGAAAACCCCCGGGGAACCTTCTTGGTCCGGGAGAGCGAGACGACA
AAAGGTGCCTATTGCCTCTCCGTTTCTGACTTTGACAACGCCAAGGGGCTCAATGTGAAG
CACTACAAGATCCGCAAGCTGGACAGCGGCGGCTTCTACATCACCTCACGCACACAGTTC
AGCAGCCTGCAGCAGCTGGTGGCCTACTACTCCAAACATGCTGATGGCTTGTGCCACCGC
CTGACCAACGTCTGCCCCACGTCCAAGCCCCAGACCCAGGGACTCGCCAAGGACGCGTGG
GAAATCCCCCGGGAGTCGCTGCGGCTGGAGGTGAAGCTGGGGCAGGGCTGCTTTGGAGAG
GTCTGGATGGGGACCTGGAACGGCACCACCAGAGTGGCCATAAAGACTCTGAAGCCCGGC
ACCATGTCCCCGGAGGCCTTCCTGCAGGAAGCCCAAGTGATGAAGAAGCTCCGGCATGAG
AAGCTGGTTCAACTGTACGCAGTGGTGTCGGAAGAGCCCATCTACATCGTCATTGAGTAC
ATGAGCAAGGGGAGCCTCCTGGATTTCCTGAAGGGAGAGATGGGCAAGTACCTGCGGCTG
CCACAGCTCGTTGATATGGCTGCTCAGATTGCATCCGGCATGGCCTATGTGGAGAGGATG
AACTACGTGCACCGAGACCTGCGGGCGGCCAACATCCTGGTGGGGGAGAACCTGGTGTGC
AAGGTGGCTGACTTTGGGCTGGCACGCCTCATCGAGGACAACGAGTACACAGCACGGCAA
GGTGCCAAGTTCCCCATCAAGTGGACAGCCCCCGAGGCAGCCCTCTATGGCCGGTTCACC
ATCAAGTCGGATGTCTGGTCCTTCGGCATCCTGCTGACTGAGCTGACCACCAAGGGCCGG
GTGCCATACCCAGGGATGGGCAACGGGGAGGTGCTGGACCGGGTGGAGAGGGGCTACCGC
ATGCCCTGCCCGCCCGAGTGCCCCGAGTCGCTGCATGACCTTATGTGCCAGTGCTGGCGG
AGGGACCCTGAGGAGCGGCCCACTTTCGAGTACCTGCAGGCCCAGCTGCTCCCTGCTTGT
GTGTTGGAGGTCGCTGAGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00524
UniProtKB Entry NameSRC_RSVSA
GenBank Protein ID459676
GenBank Gene IDL29199
General References
  1. Czernilofsky AP, Levinson AD, Varmus HE, Bishop JM, Tischer E, Goodman HM: Nucleotide sequence of an avian sarcoma virus oncogene (src) and proposed amino acid sequence for gene product. Nature. 1980 Sep 18;287(5779):198-203. [Article]
  2. Czernilofsky AP, Levinson AD, Varmus HE, Bishop JM, Tischer E, Goodman H: Corrections to the nucleotide sequence of the src gene of Rous sarcoma virus. Nature. 1983 Feb 24;301(5902):736-8. [Article]
  3. Takeya T, Hanafusa H: Structure and sequence of the cellular gene homologous to the RSV src gene and the mechanism for generating the transforming virus. Cell. 1983 Mar;32(3):881-90. [Article]
  4. Neil JC, Ghysdael J, Vogt PK, Smart JE: Homologous tyrosine phosphorylation sites in transformation-specific gene products of distinct avian sarcoma viruses. Nature. 1981 Jun 25;291(5817):675-7. [Article]
  5. Waksman G, Kominos D, Robertson SC, Pant N, Baltimore D, Birge RB, Cowburn D, Hanafusa H, Mayer BJ, Overduin M, Resh MD, Rios CB, Silverman L, Kuriyan J: Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature. 1992 Aug 20;358(6388):646-53. [Article]
  6. Waksman G, Shoelson SE, Pant N, Cowburn D, Kuriyan J: Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms. Cell. 1993 Mar 12;72(5):779-90. [Article]
  7. Plummer MS, Holland DR, Shahripour A, Lunney EA, Fergus JH, Marks JS, McConnell P, Mueller WT, Sawyer TK: Design, synthesis, and cocrystal structure of a nonpeptide Src SH2 domain ligand. J Med Chem. 1997 Nov 7;40(23):3719-25. [Article]
  8. Lubman OY, Waksman G: Dissection of the energetic coupling across the Src SH2 domain-tyrosyl phosphopeptide interface. J Mol Biol. 2002 Feb 15;316(2):291-304. [Article]
  9. Davidson JP, Lubman O, Rose T, Waksman G, Martin SF: Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding. J Am Chem Soc. 2002 Jan 16;124(2):205-15. [Article]
  10. Lubman OY, Waksman G: Structural and thermodynamic basis for the interaction of the Src SH2 domain with the activated form of the PDGF beta-receptor. J Mol Biol. 2003 May 2;328(3):655-68. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB084342-METHYLCARBAMOYL-3-(4-PHOSPHONOOXY-PHENYL)-CYCLOPROPANECARBOXYLIC ACIDexperimentalunknownDetails