PTPN7

PTPN7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1ZC0, 2A3K, 2GP0, 2GPH, 2HVL, 2QDC, 2QDM, 2QDP, 3D42, 3D44, 3O4S, 3O4T, 3O4U
Identifiers
Aliases	PTPN7, BPTP-4, HEPTP, LC-PTP, LPTP, PTPNI, protein tyrosine phosphatase, non-receptor type 7, protein tyrosine phosphatase non-receptor type 7
External IDs	OMIM: 176889; MGI: 2156893; HomoloGene: 15411; GeneCards: PTPN7; OMA:PTPN7 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.1 Start 202,147,013 bp End 202,161,588 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 E4 Start 135,060,438 bp End 135,073,055 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in granulocyte lymph node bone marrow cells appendix thymus blood spleen right testis left testis putamen Top expressed in thymus granulocyte bone marrow spleen striatum of neuraxis embryo pharynx neck yolk sac jejunum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein tyrosine phosphatase activity phosphatase activity protein binding phosphoprotein phosphatase activity hydrolase activity Cellular component cytoplasmic side of plasma membrane cytoskeleton cytoplasm cytosol nucleoplasm Biological process dephosphorylation peptidyl-tyrosine dephosphorylation protein dephosphorylation cellular response to cytokine stimulus Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5778 320139 Ensembl ENSG00000143851 ENSMUSG00000031506 UniProt P35236 Q8BUM3 RefSeq (mRNA) NM_001199797 NM_002832 NM_080588 NM_080589 NM_001364877 NM_001364878 NM_177081 NM_001356382 RefSeq (protein) NP_001186726 NP_002823 NP_542155 NP_001351806 NP_001351807 NP_796055 NP_001343311 Location (UCSC) Chr 1: 202.15 – 202.16 Mb Chr 1: 135.06 – 135.07 Mb PubMed search
Wikidata
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Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene.

Function

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 gene is preferentially expressed in a variety of hematopoietic cells, and is an early response gene in lymphokine stimulated cells. The noncatalytic N-terminus of this PTP can interact with MAP kinases and suppress the MAP kinase activities. This PTP was shown to be involved in the regulation of T cell antigen receptor (TCR) signaling, which was thought to function through dephosphorylating the molecules related to MAP kinase pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Interactions

PTPN7 has been shown to interact with MAPK3 and MAPK1.

Further reading

• Adachi M, Sekiya M, Arimura Y, Takekawa M, Itoh F, Hinoda Y, Imai K, Yachi A (1992). "Protein-tyrosine phosphatase expression in pre-B cell NALM-6". Cancer Res. 52 (3): 737–40. PMID 1370651.
• Zanke B, Suzuki H, Kishihara K, Mizzen L, Minden M, Pawson A, Mak TW (1992). "Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)". Eur. J. Immunol. 22 (1): 235–9. doi:10.1002/eji.1830220134. PMID 1530918. S2CID 29146172.
• Swieter M, Berenstein EH, Swaim WD, Siraganian RP (1995). "Aggregation of IgE receptors in rat basophilic leukemia 2H3 cells induces tyrosine phosphorylation of the cytosolic protein-tyrosine phosphatase HePTP". J. Biol. Chem. 270 (37): 21902–6. doi:10.1074/jbc.270.37.21902. PMID 7545170.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Zanke B, Squire J, Griesser H, Henry M, Suzuki H, Patterson B, Minden M, Mak TW (1994). "A hematopoietic protein tyrosine phosphatase (HePTP) gene that is amplified and overexpressed in myeloid malignancies maps to chromosome 1q32.1". Leukemia. 8 (2): 236–44. PMID 8309248.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Saxena M, Williams S, Gilman J, Mustelin T (1998). "Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 273 (25): 15340–4. doi:10.1074/jbc.273.25.15340. PMID 9624114.
• Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T (1999). "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 274 (17): 11693–700. doi:10.1074/jbc.274.17.11693. PMID 10206983.
• Oh-hora M, Ogata M, Mori Y, Adachi M, Imai K, Kosugi A, Hamaoka T (1999). "Direct suppression of TCR-mediated activation of extracellular signal-regulated kinase by leukocyte protein tyrosine phosphatase, a tyrosine-specific phosphatase". J. Immunol. 163 (3): 1282–8. doi:10.4049/jimmunol.163.3.1282. PMID 10415025.
• Saxena M, Williams S, Taskén K, Mustelin T (1999). "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase". Nat. Cell Biol. 1 (5): 305–11. doi:10.1038/13024. PMID 10559944. S2CID 40413956.
• Pettiford SM, Herbst R (2000). "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene. 19 (7): 858–69. doi:10.1038/sj.onc.1203408. PMID 10702794. S2CID 24843974.
• Gjörloff-Wingren A, Saxena M, Han S, Wang X, Alonso A, Renedo M, Oh P, Williams S, Schnitzer J, Mustelin T (2000). "Subcellular localization of intracellular protein tyrosine phosphatases in T cells". Eur. J. Immunol. 30 (8): 2412–21. doi:10.1002/1521-4141(2000)30:8<2412::AID-IMMU2412>3.0.CO;2-J. PMID 10940933. S2CID 8132613.
• Tartaglia M, Mehler EL, Goldberg R, Zampino G, Brunner HG, Kremer H, van der Burgt I, Crosby AH, Ion A, Jeffery S, Kalidas K, Patton MA, Kucherlapati RS, Gelb BD (2001). "Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome". Nat. Genet. 29 (4): 465–8. doi:10.1038/ng772. PMID 11704759. S2CID 14627986.
• Wang ZX, Zhou B, Wang QM, Zhang ZY (2002). "A kinetic approach for the study of protein phosphatase-catalyzed regulation of protein kinase activity". Biochemistry. 41 (24): 7849–57. doi:10.1021/bi025776m. PMID 12056917.
• Digilio MC, Conti E, Sarkozy A, Mingarelli R, Dottorini T, Marino B, Pizzuti A, Dallapiccola B (2002). "Grouping of Multiple-Lentigines/LEOPARD and Noonan Syndromes on the PTPN11 Gene". Am. J. Hum. Genet. 71 (2): 389–94. doi:10.1086/341528. PMC 379170. PMID 12058348.
• Kosaki K, Suzuki T, Muroya K, Hasegawa T, Sato S, Matsuo N, Kosaki R, Nagai T, Hasegawa Y, Ogata T (2002). "PTPN11 (protein-tyrosine phosphatase, nonreceptor-type 11) mutations in seven Japanese patients with Noonan syndrome". J. Clin. Endocrinol. Metab. 87 (8): 3529–33. doi:10.1210/jcem.87.8.8694. PMID 12161469.
• Pettiford SM, Herbst R (2003). "The protein tyrosine phosphatase HePTP regulates nuclear translocation of ERK2 and can modulate megakaryocytic differentiation of K562 cells". Leukemia. 17 (2): 366–78. doi:10.1038/sj.leu.2402767. PMID 12592337. S2CID 33812913.