PTPN14

Tyrosine-protein phosphatase non-receptor type 14 is an enzyme that in humans is encoded by the PTPN14 gene.

PTPN14
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2BZL
Identifiers
Aliases	PTPN14, PEZ, PTP36, protein tyrosine phosphatase, non-receptor type 14, CATLPH, protein tyrosine phosphatase non-receptor type 14, PTPD2
External IDs	OMIM: 603155 MGI: 102467 HomoloGene: 3941 GeneCards: PTPN14
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.3-q41 Start 214,348,700 bp End 214,552,449 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 H6|1 95.03 cM Start 189,460,465 bp End 189,608,892 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parietal pleura tibia visceral pleura nipple germinal epithelium vulva lactiferous duct renal medulla synovial joint seminal vesicula Top expressed in condyle lip epidermis semi-lunar valve fossa hair follicle molar renal corpuscle external carotid artery internal carotid artery More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphoprotein phosphatase activity hydrolase activity phosphatase activity receptor tyrosine kinase binding transcription coregulator activity protein binding protein tyrosine phosphatase activity Cellular component nucleus cytoplasm cytoskeleton nucleoplasm Biological process negative regulation of cell population proliferation regulation of transcription, DNA-templated protein dephosphorylation regulation of protein export from nucleus transcription, DNA-templated dephosphorylation lymphangiogenesis peptidyl-tyrosine dephosphorylation cellular response to cytokine stimulus regulation of nucleic acid-templated transcription Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5784 19250 Ensembl ENSG00000152104 ENSMUSG00000026604 UniProt Q15678 Q62130 RefSeq (mRNA) NM_005401 NM_001033287 NM_008976 RefSeq (protein) NP_005392 NP_033002 Location (UCSC) Chr 1: 214.35 – 214.55 Mb Chr 1: 189.46 – 189.61 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

The protein encoded by this gene is a member of the PTP family and PTPN14 subfamily of tyrosine protein phosphatases. PTPs are known to be signalling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal noncatalytic domain similar to that of band 4.1 superfamily cytoskeleton-associated proteins, which suggested the membrane or cytoskeleton localization of this protein. The specific function of this PTP has not yet been determined.

Interactions

PTPN14 has been shown to interact with Beta-catenin.

Further reading

• Gyapay G, Morissette J, Vignal A, Dib C, Fizames C, Millasseau P, Marc S, Bernardi G, Lathrop M, Weissenbach J (Jun 1994). "The 1993-94 Généthon human genetic linkage map". Nature Genetics. 7 (2 Spec No): 246–339. doi:10.1038/ng0694supp-246. PMID 7545953. S2CID 24662426.
• Ogata M, Takada T, Mori Y, Oh-hora M, Uchida Y, Kosugi A, Miyake K, Hamaoka T (Apr 1999). "Effects of overexpression of PTP36, a putative protein tyrosine phosphatase, on cell adhesion, cell growth, and cytoskeletons in HeLa cells". The Journal of Biological Chemistry. 274 (18): 12905–9. doi:10.1074/jbc.274.18.12905. PMID 10212280.
• Ogata M, Takada T, Mori Y, Uchida Y, Miki T, Okuyama A, Kosugi A, Sawada M, Oh-hora M, Hamaoka T (Jul 1999). "Regulation of phosphorylation level and distribution of PTP36, a putative protein tyrosine phosphatase, by cell-substrate adhesion". The Journal of Biological Chemistry. 274 (29): 20717–24. doi:10.1074/jbc.274.29.20717. PMID 10400706.
• Aoyama K, Matsuda T, Aoki N (Dec 1999). "Characterization of newly identified four isoforms for a putative cytosolic protein tyrosine phosphatase PTP36". Biochemical and Biophysical Research Communications. 266 (2): 523–31. doi:10.1006/bbrc.1999.1845. PMID 10600535.
• Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (Sep 2000). "Translocation of protein tyrosine phosphatase Pez/PTPD2/PTP36 to the nucleus is associated with induction of cell proliferation". Journal of Cell Science. 113 ( Pt 17) (17): 3117–23. doi:10.1242/jcs.113.17.3117. hdl:2440/9579. PMID 10934049.
• Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y (Jun 2003). "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin". Molecular Biology of the Cell. 14 (6): 2520–9. doi:10.1091/mbc.E02-09-0577. PMC 194899. PMID 12808048.
• Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T (Aug 2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology. 14 (16): 1436–50. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• Barr AJ, Debreczeni JE, Eswaran J, Knapp S (Jun 2006). "Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-A resolution". Proteins. 63 (4): 1132–6. doi:10.1002/prot.20958. PMID 16534812. S2CID 7186900.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Tyrosine-protein phosphatase non-receptor type 14 (PTPN14)