PTPN7

Protein-coding gene in the species Homo sapiens
PTPN7
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1ZC0, 2A3K, 2GP0, 2GPH, 2HVL, 2QDC, 2QDM, 2QDP, 3D42, 3D44, 3O4S, 3O4T, 3O4U

Identifiers
AliasesPTPN7, BPTP-4, HEPTP, LC-PTP, LPTP, PTPNI, protein tyrosine phosphatase, non-receptor type 7, protein tyrosine phosphatase non-receptor type 7
External IDsOMIM: 176889; MGI: 2156893; HomoloGene: 15411; GeneCards: PTPN7; OMA:PTPN7 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for PTPN7
Genomic location for PTPN7
Band1q32.1Start202,147,013 bp[1]
End202,161,588 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for PTPN7
Genomic location for PTPN7
Band1|1 E4Start135,060,438 bp[2]
End135,073,055 bp[2]
RNA expression pattern
Bgee
HumanMouse (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
SpeciesHumanMouse
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 MbChr 1: 135.06 – 135.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene.[5][6]

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.[6]

Interactions

PTPN7 has been shown to interact with MAPK3[7][8][9] and MAPK1.[7][9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000143851 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031506 – 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. ^ Adachi M, Sekiya M, Isobe M, Kumura Y, Ogita Z, Hinoda Y, Imai K, Yachi A (September 1992). "Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP". Biochem Biophys Res Commun. 186 (3): 1607–15. doi:10.1016/S0006-291X(05)81592-X. PMID 1510684.
  6. ^ a b "Entrez Gene: PTPN7 protein tyrosine phosphatase, non-receptor type 7".
  7. ^ a b Pettiford SM, Herbst R (February 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.
  8. ^ Saxena M, Williams S, Taskén K, Mustelin T (September 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.
  9. ^ a b Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T (April 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.

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.
  • v
  • t
  • e
  • 1zc0: Crystal structure of human hematopoietic tyrosine phosphatase (HePTP) catalytic domain
    1zc0: Crystal structure of human hematopoietic tyrosine phosphatase (HePTP) catalytic domain
  • 2a3k: Crystal Structure of the Human Protein Tyrosine Phosphatase, PTPN7 (HePTP, Hematopoietic Protein Tyrosine Phosphatase)
    2a3k: Crystal Structure of the Human Protein Tyrosine Phosphatase, PTPN7 (HePTP, Hematopoietic Protein Tyrosine Phosphatase)
  • 2gp0: HePTP Catalytic Domain (residues 44-339), S225D mutant
    2gp0: HePTP Catalytic Domain (residues 44-339), S225D mutant
  • v
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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


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