C-Src (Tyr-215) (SRC) Antibody – Rabbit Polyclonal

This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq]

Function: Non-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. Ref.18 Ref.30 Ref.35 Ref.37

Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Enzyme regulation: Heme regulates its activity by enhancing the phosphorylation on Tyr-530. Ref.34

Subunit structure: Interacts with DDEF1/ASAP1; via the SH3 domain. Interacts with CCPG1

By similarity. Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with HEV ORF3 protein; via the SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with ARRB1 and ARRB2. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PI3K (alpha and/or beta), PTK2, ESR1 (dimethylated on arginine) and FAK. Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B

By similarity. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via protein kinase domin) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with GNB2L1/RACK1; the interaction is enhanced by tyrosine phosphorylation of GNB2L1 and inhibits SRC activity. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.27 Ref.29 Ref.30 Ref.35 Ref.36 Ref.37

Subcellular location: Cell membrane. Mitochondrion inner membrane Ref.18.

Post-translational modification: Dephosphorylated 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. Ref.23 Ref.25 Ref.26 Ref.28 Ref.31 Ref.32 Ref.33S-nitrosylation is important for activation of its kinase activity

Sequence similarities: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.Contains 1 protein kinase domain.Contains 1 SH2 domain.Contains 1 SH3 domain.