P15054 · SRC_AVIS2

Function

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.

Catalytic activity

Features

Showing features for binding site, active site.

158750100150200250300350400450500550
TypeIDPosition(s)Description
Binding site273-281ATP (UniProtKB | ChEBI)
Binding site295ATP (UniProtKB | ChEBI)
Active site386Proton acceptor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextrinsic component of cytoplasmic side of plasma membrane
Molecular FunctionATP binding
Molecular Functionnon-membrane spanning protein tyrosine kinase activity
Molecular Functionsignaling receptor binding
Biological Processbone resorption
Biological Processcell adhesion
Biological Processepidermal growth factor receptor signaling pathway
Biological Processinnate immune response
Biological Processnegative regulation of extrinsic apoptotic signaling pathway
Biological Processnegative regulation of intrinsic apoptotic signaling pathway
Biological Processosteoclast development
Biological Processprogesterone receptor signaling pathway
Biological Processprotein phosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosine-protein kinase transforming protein Src
  • EC number
  • Alternative names
    • pp60v-src (p60-Src; v-Src)

Gene names

    • Name
      V-SRC

Organism names

Accessions

  • Primary accession
    P15054

Phenotypes & Variants

Keywords

PTM/Processing

Features

Showing features for initiator methionine, lipidation, chain, modified residue.

TypeIDPosition(s)Description
Initiator methionine1Removed; by host
Lipidation2N-myristoyl glycine; by host
ChainPRO_00000881482-587Tyrosine-protein kinase transforming protein Src
Modified residue416Phosphotyrosine; by autocatalysis

Post-translational modification

The phosphorylated form is termed pp60v-src.

Keywords

Interaction

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-58Disordered
Compositional bias8-22Basic and acidic residues
Compositional bias27-53Polar residues
Domain81-142SH3
Domain148-245SH2
Domain267-520Protein kinase

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    587
  • Mass (Da)
    65,801
  • Last updated
    2007-01-23 v3
  • Checksum
    0A6925315EF251D9
MGSSKSKPKDPSQRRRSLEPPDSTHHGGFPASQTPNKTAAPDTHRTPSRSFGTVATEPKLFGGFNTSDTVTSPQRAGALAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLTTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNPENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFSSLQQLVAYYSKHADGLCHRLTNVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKDPEERPTFEYLQAFLEDYFTSTEPPVPAWREPIGLELLLAPEASLWGTGAWLRAEGPRFGEQPQSRMWHGEVSGAPSLIKTVLGHP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias8-22Basic and acidic residues
Compositional bias27-53Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M21526
EMBL· GenBank· DDBJ
AAA42583.1
EMBL· GenBank· DDBJ
Genomic RNA
X51863
EMBL· GenBank· DDBJ
CAA36156.1
EMBL· GenBank· DDBJ
Genomic RNA

Similar Proteins

Disclaimer

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