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PTPN12

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Protein-coding gene in the species Homo sapiens

PTPN12
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

5J8R

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
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)
Chromosome 7 (human)Genomic location for PTPN12Genomic location for PTPN12
Band7q11.23Start77,537,295 bp
End77,640,069 bp
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)
Chromosome 5 (mouse)Genomic location for PTPN12Genomic location for PTPN12
Band5|5 A3Start20,986,645 bp
End21,055,911 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • epithelium of colon

  • monocyte

  • right lung

  • tibial nerve

  • Achilles tendon

  • lower lobe of lung

  • upper lobe of lung

  • upper lobe of left lung

  • subcutaneous adipose tissue
Top expressed in
  • tail of embryo

  • Gonadal ridge

  • left lung lobe

  • genital tubercle

  • stroma of bone marrow

  • trigeminal ganglion

  • abdominal wall

  • otic placode

  • hair follicle

  • dermis
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
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
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.

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.

Interactions

PTPN12 has been shown to interact with BCAR1, Grb2, PSTPIP1, TGFB1I1, Paxillin and SHC1.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000127947Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000028771Ensembl, 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. ^ "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

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)
Class I
Classical PTPs
Receptor type PTPs
Non receptor type PTPs
VH1-like or
dual specific
phosphatases

(DSPs)
MAPK phosphatases (MKPs)
Slingshots
PRLs
CDC14s
Atypical DSPs
Phosphatase and tensin
homologs (PTENs)
Myotubularins
Class II
Class III
Class IV
Category:
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