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
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 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]

Related Research Articles

<span class="mw-page-title-main">PTPN11</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 11 (PTPN11) also known as protein-tyrosine phosphatase 1D (PTP-1D), Src homology region 2 domain-containing phosphatase-2 (SHP-2), or protein-tyrosine phosphatase 2C (PTP-2C) is an enzyme that in humans is encoded by the PTPN11 gene. PTPN11 is a protein tyrosine phosphatase (PTP) Shp2.

<span class="mw-page-title-main">Adapter molecule crk</span> Protein-coding gene in the species Homo sapiens

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.

<span class="mw-page-title-main">MAPK3</span> Protein-coding gene in the species Homo sapiens

Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1, is an enzyme that in humans is encoded by the MAPK3 gene.

<span class="mw-page-title-main">PTPN6</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 6, also known as Src homology region 2 domain-containing phosphatase-1 (SHP-1), is an enzyme that in humans is encoded by the PTPN6 gene.

<span class="mw-page-title-main">PTPN1</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 1 also known as protein-tyrosine phosphatase 1B (PTP1B) is an enzyme that is the founding member of the protein tyrosine phosphatase (PTP) family. In humans it is encoded by the PTPN1 gene. PTP1B is a negative regulator of the insulin signaling pathway and is considered a promising potential therapeutic target, in particular for treatment of type 2 diabetes. It has also been implicated in the development of breast cancer and has been explored as a potential therapeutic target in that avenue as well.

<span class="mw-page-title-main">TGFB1I1</span> Protein-coding gene in the species Homo sapiens

Transforming growth factor beta-1-induced transcript 1 protein is a protein that in humans is encoded by the TGFB1I1 gene. Often put together with and studied alongside TGFB1I1 is the mouse homologue HIC-5. As the name suggests, TGFB1I1 is an induced form of the larger family of TGFB1. Studies suggest TGFB1I1 plays a role in processes of cell growth, proliferation, migration, differentiation and senescence. TGFB1I1 is most localized at focal adhesion complexes of cells, although it may be found active in the cytosol, nucleus and cell membrane as well.

<span class="mw-page-title-main">PTPRA</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.

<span class="mw-page-title-main">PTPN13</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 13 is an enzyme that in humans is encoded by the PTPN13 gene.

<span class="mw-page-title-main">PTPRF</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase F is an enzyme that, in humans, is encoded by the PTPRF gene.

<span class="mw-page-title-main">PTPN2</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 2 is an enzyme that in humans is encoded by the PTPN2 gene.

<span class="mw-page-title-main">PTPRJ</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase eta is an enzyme that in humans is encoded by the PTPRJ gene.

<span class="mw-page-title-main">PTPN7</span> Protein-coding gene in the species Homo sapiens

Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene.

<span class="mw-page-title-main">PTPRM</span> Protein-coding gene in the species Homo sapiens

Receptor-type tyrosine-protein phosphatase mu is an enzyme that in humans is encoded by the PTPRM gene.

<span class="mw-page-title-main">PTP4A1</span> Protein-coding gene in the species Homo sapiens

Protein tyrosine phosphatase type IVA 1 is an enzyme that in humans is encoded by the PTP4A1 gene.

<span class="mw-page-title-main">PTPRR</span> Protein-coding gene in the species Homo sapiens

Protein tyrosine phosphatase receptor-type R is an enzyme that in humans is encoded by the PTPRR gene.

<span class="mw-page-title-main">PSTPIP1</span> Enzyme found in humans

Proline-serine-threonine phosphatase-interacting protein 1 is an enzyme that in humans is encoded by the PSTPIP1 gene.

<span class="mw-page-title-main">IRS4</span> Protein-coding gene in the species Homo sapiens

Insulin receptor substrate 4 is a protein that in humans is encoded by the IRS4 gene.

<span class="mw-page-title-main">PTPN18</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 18 is an enzyme that in humans is encoded by the PTPN18 gene.

<span class="mw-page-title-main">PTPN3</span> Protein-coding gene in the species Homo sapiens

Tyrosine-protein phosphatase non-receptor type 3 is an enzyme that in humans is encoded by the PTPN3 gene.

<span class="mw-page-title-main">DUSP10</span> Protein-coding gene in the species Homo sapiens

Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene.

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

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