PTPN7

Protein tyrosine phosphatase, non-receptor type 7

PDB rendering based on 1zc0.

Available structures
PDB	1ZC0, 2A3K, 2GP0, 2GPH, 2HVL, 2QDC, 2QDM, 2QDP, 3D42, 3D44

Identifiers

Symbols

PTPN7; BPTP-4; FLJ18703; HEPTP; LC-PTP; LPTP; PTPNI

External IDs

OMIM: 176889 MGI: 2156893 HomoloGene: 15411 GeneCards: PTPN7 Gene

EC number

3.1.3.48

Gene Ontology
Molecular function	• protein tyrosine phosphatase activity • protein binding • hydrolase activity
Cellular component	• cytoplasm • cytosol • internal side of plasma membrane
Biological process	• protein dephosphorylation • peptidyl-tyrosine dephosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
202.12 – 202.13 Mb

Chr 1:
137.03 – 137.04 Mb

PubMed search

[1]

[2]

Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene.^[1]^[2]

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.^[2]

Interactions

PTPN7 has been shown to interact with MAPK3^[3]^[4]^[5] and MAPK1.^[3]^[5]

References

^ Adachi M, Sekiya M, Isobe M, Kumura Y, Ogita Z, Hinoda Y, Imai K, Yachi A (Sep 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.
^ ^a ^b "Entrez Gene: PTPN7 protein tyrosine phosphatase, non-receptor type 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5778.
^ ^a ^b Pettiford, S M; Herbst R (Feb. 2000). "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene (ENGLAND) 19 (7): 858–69. doi:10.1038/sj.onc.1203408. ISSN 0950-9232. PMID 10702794.
^ Saxena, M; Williams S, Taskén K, Mustelin T (Sep. 1999). "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase". Nat. Cell Biol. (ENGLAND) 1 (5): 305–11. doi:10.1038/13024. ISSN 1465-7392. PMID 10559944.
^ ^a ^b Saxena, M; Williams S, Brockdorff J, Gilman J, Mustelin T (Apr. 1999). "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. (UNITED STATES) 274 (17): 11693–700. doi:10.1074/jbc.274.17.11693. ISSN 0021-9258. PMID 10206983.

Adachi M, Sekiya M, Arimura Y et al. (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 et al. (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.
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 et al. (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 et al. (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 et al. (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 et al. (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. 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.
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.
Gjörloff-Wingren A, Saxena M, Han S et al. (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.
Tartaglia M, Mehler EL, Goldberg R et al. (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.
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 et al. (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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=379170.
Kosaki K, Suzuki T, Muroya K et al. (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/jc.87.8.3529. PMID 12161469.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.

PDB gallery

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)

2gp0: HePTP Catalytic Domain (residues 44-339), S225D mutant

Esterase: protein tyrosine phosphatases (EC 3.1.3.48)

Class I

Classical PTPs	Receptor type PTPs (PTPRA, PTPRB, PTPRC, PTPRD, PTPRE, PTPRF, PTPRG, PTPRH, PTPRJ, PTPRK, PTPRM, PTPRN, PTPRN2, PTPRO, PTPRQ, PTPRR, PTPRS, PTPRT, PTPRU, PTPRZ1, PTPRZ2) Non receptor type PTPs (PTPN1, PTPN2, PTPN3, PTPN4, PTPN5, PTPN6, PTPN7, PTPN9, PTPN11, PTPN12, PTPN13, PTPN14, PTPN18, PTPN20, PTPN21, PTPN22, PTPN23

VH1-like or dual specific phosphatases (DSPs)	MAPK phosphatases (MKPs) (DUSP1, DUSP2, DUSP4, DUSP5, DUSP6, DUSP7, DUSP8, DUSP9, DUSP10, DUSP16, MK-STYX) Slingshots (SSH1, SSH2, SSH3) PRLs (PTP4A1, PTP4A2, PTP4A3) CDC14s (CDC14A, CDC14B, CDKN3, PTP9Q22) Atypical DSPs (DUSP3, DUSP11, DUSP12, DUSP13A, DUSP13B, DUSP14, DUSP15, DUSP18, DUSP19, DUSP21, DUSP22, DUSP23, DUSP24, DUSP25, DUSP26, DUSP27, EMP2A, RNGTT, STYX) Phosphatase and tensin homologs (PTENs) (PTEN, TPIP, TPTE, TNS, TENC1) Myotubularins (MTM1, MTMR2, MTMR3, MTMR4, MTMR5, MTMR6, MTMR7, MTMR8, MTMR9, MTMR10, MTMR11, MTMR12, MTMR13, MTMR14, MTMR15)

Class II

ACP1

Class III

Cdc25: CDC25A, CDC25B, CDC25C

Class IV

Eyes absent homolog (EYA1, EYA2, EYA3, EYA4)

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

PTPN7

Interactions

References

Further reading