Tyrosine-protein kinase transforming protein Src
Details
- Name
- Tyrosine-protein kinase transforming protein Src
- Kind
- protein
- Synonyms
- 2.7.10.2
- p60-Src
- pp60v-src
- v-Src
- Gene Name
- V-SRC
- UniProtKB Entry
- P00524Swiss-Prot
- Organism
- RSV-SRA
- NCBI Taxonomy ID
- 269446
- 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
- FunctionsATP binding / non-membrane spanning protein tyrosine kinase activity
- General 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. Causes mitotic slippage in addition to cytokinesis failure in the host cell (PubMed:30135207). Phosphorylates and attenuates the activity of host CDK1, possibly causing the mitotic slippage (PubMed:30135207).
- Specific Function
- ATP binding
- Pfam Domain Function
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P00524 UniProtKB Entry Name SRC_RSVSA GenBank Protein ID 459676 GenBank Gene ID L29199 PDB ID(s) 1BKL, 1BKM, 1IS0, 1KC2, 1NZL, 1NZV, 1SHA, 1SHB, 1SKJ, 1SPR, 1SPS - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-METHYLCARBAMOYL-3-(4-PHOSPHONOOXY-PHENYL)-CYCLOPROPANECARBOXYLIC ACID experimental unknown target Details