This product is an active protein and may elicit a biological response in vivo, handle with caution.
Avian sarcoma virus
CDNA FLJ14219 fis clone NT2RP3003800 highly similar to Rattus norvegicus tyrosine protein kinase pp60 c src mRNA
Neuronal CSRC tyrosine specific protein kinase
Proto oncogene tyrosine protein kinase Src
Proto-oncogene tyrosine-protein kinase Src
Protooncogene SRC Rous sarcoma
SRC proto oncogene non receptor tyrosine kinase
Tyrosine kinase pp60c src
Tyrosine protein kinase SRC 1
Tyrosine protein kinase SRC1
v src avian sarcoma (Schmidt Ruppin A2) viral oncogene homolog
V src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog (avian)
v src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog avian
FunctionNon-receptor protein tyrosine kinase that plays pivotal roles in numerous cellular processes such as proliferation, migration, and transformation. In concert with PTK2B, plays an important role in osteoclastic bone resorption. Both the formation of a SRC-PTK2B complex, and SRC kinase activity are necessary for this function. Once it is recruited to the activated integrins, by PTK2B, it phosphorylates CBL which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.
Post-translational modificationsDephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. S-nitrosylation is important for activation of its kinase activity.