PTPN12

Last updated

PTPN12
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PTPN12 , PTP-PEST, PTPG1, protein tyrosine phosphatase, non-receptor type 12, protein tyrosine phosphatase non-receptor type 12
External IDs OMIM: 600079; MGI: 104673; HomoloGene: 37691; GeneCards: PTPN12; OMA:PTPN12 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 Mb Chr 5: 20.99 – 21.06 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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

Contents

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. 1 2 3 GRCh38: Ensembl release 89: ENSG00000127947 Ensembl, May 2017
  2. 1 2 3 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. 1 2 "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