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
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, Imai K, Yachi A (March 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. 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, Yi; Ceacareanu Alice Corina; Hassid Aviv (August 2003). "Nitric oxide-induced inhibition of aortic smooth muscle cell motility: role of PTP-PEST and adaptor proteins p130cas and Crk". Am. J. Physiol. Heart Circ. Physiol. 285 (2): H710–21. doi:10.1152/ajpheart.01127.2002. ISSN 0363-6135. PMID 12714323. S2CID 42587789.
  8. ^ Garton, A J; Burnham M R; Bouton A H; Tonks N K (August 1997). "Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877–85. doi:10.1038/sj.onc.1201279. ISSN 0950-9232. PMID 9285683.
  9. ^ Côté, J F; Charest A; Wagner J; Tremblay M L (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): 13128–37. doi:10.1021/bi981259l. ISSN 0006-2960. PMID 9748319.
  10. ^ Garton, A J; Flint A J; Tonks N K (November 1996). "Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST". Mol. Cell. Biol. 16 (11): 6408–18. doi:10.1128/MCB.16.11.6408. ISSN 0270-7306. PMC 231642. PMID 8887669.
  11. ^ Charest, A; Wagner J; Kwan M; Tremblay M L (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): 1643–51. doi:10.1038/sj.onc.1201008. ISSN 0950-9232. PMID 9135065.
  12. ^ Dowbenko, D; Spencer S; Quan C; Lasky L A (January 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. doi:10.1074/jbc.273.2.989. ISSN 0021-9258. PMID 9422760.
  13. ^ Nishiya, N; Iwabuchi Y; Shibanuma M; Côté J F; Tremblay M L; Nose K (April 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. doi:10.1074/jbc.274.14.9847. ISSN 0021-9258. PMID 10092676.
  14. ^ Shen, Y; Lyons P; Cooley M; Davidson D; Veillette A; Salgia R; Griffin J D; Schaller M D (January 2000). "The noncatalytic domain of protein-tyrosine phosphatase-PEST targets paxillin for dephosphorylation in vivo". J. Biol. Chem. 275 (2): 1405–13. doi:10.1074/jbc.275.2.1405. ISSN 0021-9258. PMID 10625692.
  15. ^ Côté, J F; Turner C E; Tremblay M L (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". J. Biol. Chem. 274 (29): 20550–60. doi:10.1074/jbc.274.29.20550. ISSN 0021-9258. PMID 10400685.
  16. ^ Shen, Y; Schneider G; Cloutier J F; Veillette A; Schaller M D (March 1998). "Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin". J. Biol. Chem. 273 (11): 6474–81. doi:10.1074/jbc.273.11.6474. ISSN 0021-9258. PMID 9497381.
  17. ^ Habib, T; Herrera R; Decker S J (October 1994). "Activators of protein kinase C stimulate association of Shc and the PEST tyrosine phosphatase". J. Biol. Chem. 269 (41): 25243–6. doi:10.1016/S0021-9258(18)47237-7. ISSN 0021-9258. PMID 7929214.
  18. ^ Charest, A; Wagner J; Jacob S; McGlade C J; Tremblay M L (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". J. Biol. Chem. 271 (14): 8424–9. doi:10.1074/jbc.271.14.8424. ISSN 0021-9258. PMID 8626541.

Further reading

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