PTPN12
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPTPN12, PTP-PEST, PTPG1, protein tyrosine phosphatase, non-receptor type 12, protein tyrosine phosphatase non-receptor type 12
External IDsOMIM: 600079; MGI: 104673; HomoloGene: 37691; GeneCards: PTPN12; OMA:PTPN12 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

5782

19248

Ensembl

ENSG00000127947

ENSMUSG00000028771

UniProt

Q05209

P35831

RefSeq (mRNA)

NM_001131008
NM_001131009
NM_002835

NM_011203
NM_001356590
NM_001356591
NM_001356592

RefSeq (protein)

NP_001124480
NP_001124481
NP_002826

NP_035333
NP_001343519
NP_001343520
NP_001343521

Location (UCSC)Chr 7: 77.54 – 77.64 MbChr 5: 20.99 – 21.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Tyrosine-protein phosphatase non-receptor type 12 is an enzyme that in humans is encoded by the PTPN12 gene.[5][6]

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.[6]

Interactions

PTPN12 has been shown to interact with BCAR1,[7][8][9][10] Grb2,[11] PSTPIP1,[12] TGFB1I1,[13] Paxillin[14][15][16] and SHC1.[17][18]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000127947 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028771 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Takekawa M, Itoh F, Hinoda Y, Adachi M, Ariyama T, Inazawa J, et al. (March 1994). "Chromosomal localization of the protein tyrosine phosphatase G1 gene and characterization of the aberrant transcripts in human colon cancer cells". FEBS Letters. 339 (3): 222–228. doi:10.1016/0014-5793(94)80420-6. PMID 7509295. S2CID 4885570.
  6. ^ a b "Entrez Gene: PTPN12 protein tyrosine phosphatase, non-receptor type 12".
  7. ^ Lin Y, Ceacareanu AC, Hassid A (August 2003). "Nitric oxide-induced inhibition of aortic smooth muscle cell motility: role of PTP-PEST and adaptor proteins p130cas and Crk". American Journal of Physiology. Heart and Circulatory Physiology. 285 (2) H710–21. doi:10.1152/ajpheart.01127.2002. PMID 12714323. S2CID 42587789.
  8. ^ Garton AJ, Burnham MR, Bouton AH, Tonks NK (August 1997). "Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877–885. doi:10.1038/sj.onc.1201279. PMID 9285683.
  9. ^ Côté JF, Charest A, Wagner J, Tremblay ML (September 1998). "Combination of gene targeting and substrate trapping to identify substrates of protein tyrosine phosphatases using PTP-PEST as a model". Biochemistry. 37 (38): 13128–13137. doi:10.1021/bi981259l. PMID 9748319.
  10. ^ Garton AJ, Flint AJ, Tonks NK (November 1996). "Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST". Molecular and Cellular Biology. 16 (11): 6408–6418. doi:10.1128/MCB.16.11.6408. PMC 231642. PMID 8887669.
  11. ^ Charest A, Wagner J, Kwan M, Tremblay ML (April 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): 1643–1651. doi:10.1038/sj.onc.1201008. PMID 9135065.
  12. ^ Dowbenko D, Spencer S, Quan C, Lasky LA (January 1998). "Identification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting protein". The Journal of Biological Chemistry. 273 (2): 989–996. doi:10.1074/jbc.273.2.989. PMID 9422760.
  13. ^ Nishiya N, Iwabuchi Y, Shibanuma M, Côté JF, Tremblay ML, Nose K (April 1999). "Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain". The Journal of Biological Chemistry. 274 (14): 9847–9853. doi:10.1074/jbc.274.14.9847. PMID 10092676.
  14. ^ Shen Y, Lyons P, Cooley M, Davidson D, Veillette A, Salgia R, et al. (January 2000). "The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo". The Journal of Biological Chemistry. 275 (2): 1405–1413. doi:10.1074/jbc.275.2.1405. PMID 10625692.
  15. ^ Côté JF, Turner CE, Tremblay ML (July 1999). "Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST". The Journal of Biological Chemistry. 274 (29): 20550–20560. doi:10.1074/jbc.274.29.20550. PMID 10400685.
  16. ^ Shen Y, Schneider G, Cloutier JF, Veillette A, Schaller MD (March 1998). "Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin". The Journal of Biological Chemistry. 273 (11): 6474–6481. doi:10.1074/jbc.273.11.6474. PMID 9497381.
  17. ^ Habib T, Herrera R, Decker SJ (October 1994). "Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase". The Journal of Biological Chemistry. 269 (41): 25243–25246. doi:10.1016/S0021-9258(18)47237-7. PMID 7929214.
  18. ^ Charest A, Wagner J, Jacob S, McGlade CJ, Tremblay ML (April 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". The Journal of Biological Chemistry. 271 (14): 8424–8429. doi:10.1074/jbc.271.14.8424. PMID 8626541.

Further reading