Protein Tyrosine Phosphatase, Non-Receptor Type 12
"Protein Tyrosine Phosphatase, Non-Receptor Type 12" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.
| Descriptor ID |
D054594
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| MeSH Number(s) |
D08.811.277.352.650.775.300.850 D12.644.360.585.850 D12.776.476.564.850
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| Concept/Terms |
Protein Tyrosine Phosphatase, Non-Receptor Type 12- Protein Tyrosine Phosphatase, Non-Receptor Type 12
- Protein Tyrosine Phosphatase, Non Receptor Type 12
- PEST-Enriched Phosphatase
- PEST Enriched Phosphatase
- Phosphatase, PEST-Enriched
- PEP Protein Tyrosine Phosphatase
- PEP PTPase
- PTPase, PEP
- PTP-PEST
|
Below are MeSH descriptors whose meaning is more general than "Protein Tyrosine Phosphatase, Non-Receptor Type 12".
Below are MeSH descriptors whose meaning is more specific than "Protein Tyrosine Phosphatase, Non-Receptor Type 12".
This graph shows the total number of publications written about "Protein Tyrosine Phosphatase, Non-Receptor Type 12" by people in this website by year, and whether "Protein Tyrosine Phosphatase, Non-Receptor Type 12" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
|---|
| 2011 | 1 | 1 | 2 |
| 2018 | 1 | 0 | 1 |
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Below are the most recent publications written about "Protein Tyrosine Phosphatase, Non-Receptor Type 12" by people in Profiles.
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Spatially interacting phosphorylation sites and mutations in cancer. Nat Commun. 2021 04 19; 12(1):2313.
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PTPN12/PTP-PEST Regulates Phosphorylation-Dependent Ubiquitination and Stability of Focal Adhesion Substrates in Invasive Glioblastoma Cells. Cancer Res. 2018 07 15; 78(14):3809-3822.
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Combinatorial inhibition of PTPN12-regulated receptors leads to a broadly effective therapeutic strategy in triple-negative breast cancer. Nat Med. 2018 05; 24(4):505-511.
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Protein tyrosine phosphatase-PEST and ?8 integrin regulate spatiotemporal patterns of RhoGDI1 activation in migrating cells. Mol Cell Biol. 2015 Apr; 35(8):1401-13.
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Regulation of tumor cell migration by protein tyrosine phosphatase (PTP)-proline-, glutamate-, serine-,and threonine-rich sequence (PEST). Chin J Cancer. 2013 Feb; 32(2):75-83.
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Invited commentary. Ann Thorac Surg. 2012 May; 93(5):1681.
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Ras-induced and extracellular signal-regulated kinase 1 and 2 phosphorylation-dependent isomerization of protein tyrosine phosphatase (PTP)-PEST by PIN1 promotes FAK dephosphorylation by PTP-PEST. Mol Cell Biol. 2011 Nov; 31(21):4258-69.
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Detection of recurrent rearrangement breakpoints from copy number data. BMC Bioinformatics. 2011 Apr 21; 12:114.
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Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase. Cell. 2011 Mar 04; 144(5):703-18.
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FAK phosphorylation by ERK primes ras-induced tyrosine dephosphorylation of FAK mediated by PIN1 and PTP-PEST. Mol Cell. 2009 Jul 10; 35(1):11-25.