PTPN12

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains a C-terminal PEST motif, which serves as a protein-protein interaction domain, and may regulate protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of the oncogene c-ABL and thus may play a role in oncogenesis. This PTP was also shown to interact with, and dephosphorylate, various products related to cytoskeletal structure and cell adhesion, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin. This suggests it has a regulatory role in controlling cell shape and mobility. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq]

protein tyrosine phosphatase, non-receptor type 12

Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades (PubMed:18559503).
Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2 (PubMed:17329398, PubMed:27134172).
Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (PubMed:27134172).

Cellular response to epidermal growth factor stimulusManual Assertion Based On ExperimentIMP:UniProtKB
Negative regulation of ERBB signaling pathwayTAS:Reactome
Negative regulation of platelet-derived growth factor receptor-beta signaling pathwayTAS:Reactome
Peptidyl-tyrosine dephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Protein dephosphorylationManual Assertion Based On ExperimentIDA:UniProtKB
Regulation of epidermal growth factor receptor signaling pathwayManual Assertion Based On ExperimentIMP:UniProtKB
Tissue regenerationIEA:Ensembl

Cytoplasm
Cell junction, focal adhesion
Cell projection, podosome
Partial translocation to focal adhesion sites may be mediated by interaction with SORBS2.

Phosphorylated by STK24/MST3 and this results in inhibition of its activity.