PTPN12

From Wikipedia, the free encyclopedia

Protein tyrosine phosphatase, non-receptor type 12

Identifiers

PTPN12; PTP-PEST; PTPG1

External IDs

OMIM: 600079 MGI: 104673 HomoloGene: 37691

Gene ontology
Molecular Function:	• non-membrane spanning protein tyrosine phosphatase activity • hydrolase activity • SH3 domain binding
Cellular Component:	• soluble fraction • cytoplasm • cytosol
Biological Process:	• protein amino acid dephosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002835 (mRNA)
NP_002826 (protein)

NM_011203 (mRNA)
NP_035333 (protein)

Location

Chr 7: 77 - 77.11 Mb

Chr 5: 20.5 - 20.57 Mb

Pubmed search

[1]

[2]

Protein tyrosine phosphatase, non-receptor type 12, also known as PTPN12, is a human gene.^[1]

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be 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 be related to protein intracellular half-life. This PTP was found to bind and dephosphorylate the product of oncogene c-ABL, thus may play a role in oncogenesis. This PTP was shown to interact with, and dephosphorylate, various of cytoskeleton and cell adhesion molecules, such as p130 (Cas), CAKbeta/PTK2B, PSTPIP1, and paxillin, which suggested its regulatory roles in controlling cell shape and mobility.^[1]

[edit] References

^ ^a ^b Entrez Gene: PTPN12 protein tyrosine phosphatase, non-receptor type 12.

[edit] Further reading

Takekawa M, Itoh F, Hinoda Y, et al. (1993). "Cloning and characterization of a human cDNA encoding a novel putative cytoplasmic protein-tyrosine-phosphatase.". Biochem. Biophys. Res. Commun. 189 (2): 1223–30. PMID 1472029.
Yi T, Cleveland JL, Ihle JN (1991). "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification.". Blood 78 (9): 2222–8. PMID 1932742.
Takekawa M, Itoh F, Hinoda Y, et al. (1994). "Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells.". FEBS Lett. 339 (3): 222–8. PMID 7509295.
Garton AJ, Tonks NK (1994). "PTP-PEST: a protein tyrosine phosphatase regulated by serine phosphorylation.". EMBO J. 13 (16): 3763–71. PMID 7520867.
Habib T, Herrera R, Decker SJ (1994). "Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase.". J. Biol. Chem. 269 (41): 25243–6. PMID 7929214.
Yang Q, Co D, Sommercorn J, Tonks NK (1993). "Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase.". J. Biol. Chem. 268 (23): 17650. PMID 8349645.
Yang Q, Co D, Sommercorn J, Tonks NK (1993). "Cloning and expression of PTP-PEST. A novel, human, nontransmembrane protein tyrosine phosphatase.". J. Biol. Chem. 268 (9): 6622–8. PMID 8454633.
Charest A, Wagner J, Jacob S, et al. (1996). "Phosphotyrosine-independent binding of SHC to the NPLH sequence of murine protein-tyrosine phosphatase-PEST. Evidence for extended phosphotyrosine binding/phosphotyrosine interaction domain recognition specificity.". J. Biol. Chem. 271 (14): 8424–9. PMID 8626541.
Garton AJ, Flint AJ, Tonks NK (1996). "Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.". Mol. Cell. Biol. 16 (11): 6408–18. PMID 8887669.
Charest A, Wagner J, Kwan M, Tremblay ML (1997). "Coupling of the murine protein tyrosine phosphatase PEST to the epidermal growth factor (EGF) receptor through a Src homology 3 (SH3) domain-mediated association with Grb2.". Oncogene 14 (14): 1643–51. doi:10.1038/sj.onc.1201008. PMID 9135065.
Garton AJ, Burnham MR, Bouton AH, Tonks NK (1997). "Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition.". Oncogene 15 (8): 877–85. doi:10.1038/sj.onc.1201279. PMID 9285683.
Dowbenko D, Spencer S, Quan C, Lasky LA (1998). "Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein.". J. Biol. Chem. 273 (2): 989–96. PMID 9422760.
Shen Y, Schneider G, Cloutier JF, et al. (1998). "Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin.". J. Biol. Chem. 273 (11): 6474–81. PMID 9497381.
Côté JF, Charest A, Wagner J, Tremblay ML (1998). "Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model.". Biochemistry 37 (38): 13128–37. doi:10.1021/bi981259l. PMID 9748319.
Wu Y, Dowbenko D, Lasky LA (1998). "PSTPIP 2, a second tyrosine phosphorylated, cytoskeletal-associated protein that binds a PEST-type protein-tyrosine phosphatase.". J. Biol. Chem. 273 (46): 30487–96. PMID 9804817.
"Toward a complete human genome sequence." (1999). Genome Res. 8 (11): 1097–108. PMID 9847074.
Li J, Nishizawa K, An W, et al. (1999). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.". EMBO J. 17 (24): 7320–36. doi:10.1093/emboj/17.24.7320. PMID 9857189.
Garton AJ, Tonks NK (1999). "Regulation of fibroblast motility by the protein tyrosine phosphatase PTP-PEST.". J. Biol. Chem. 274 (6): 3811–8. PMID 9920935.
Angers-Loustau A, Côté JF, Charest A, et al. (1999). "Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts.". J. Cell Biol. 144 (5): 1019–31. PMID 10085298.
Nishiya N, Iwabuchi Y, Shibanuma M, et al. (1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain.". J. Biol. Chem. 274 (14): 9847–53. PMID 10092676.