PTPRG

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

2H4V, 2HY3, 2NLK, 2PBN, 3JXH, 3QCB, 3QCC, 3QCD, 3QCE, 3QCF, 3QCG, 3QCH, 3QCI, 3QCJ, 3QCK, 3QCL, 3QCM, 3QCN

Identifiers
AliasesPTPRG, HPTPG, PTPG, R-PTP-GAMMA, RPTPG, protein tyrosine phosphatase, receptor type G, protein tyrosine phosphatase receptor type G
External IDsOMIM: 176886; MGI: 97814; HomoloGene: 2129; GeneCards: PTPRG; OMA:PTPRG - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for PTPRG
Genomic location for PTPRG
Band3p14.2Start61,561,569 bp[1]
End62,297,609 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • lower lobe of lung

  • caput epididymis

  • synovial joint

  • buccal mucosa cell

  • oocyte

  • pericardium

  • corpus epididymis

  • urethra

  • stromal cell of endometrium
    n/a
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • protein tyrosine phosphatase activity
  • phosphatase activity
  • transmembrane receptor protein tyrosine phosphatase activity
  • protein binding
  • phosphoprotein phosphatase activity
  • hydrolase activity
  • identical protein binding
Cellular component
  • integral component of membrane
  • integral component of plasma membrane
  • extracellular exosome
  • membrane
  • extracellular space
Biological process
  • regulation of homophilic cell adhesion
  • protein dephosphorylation
  • negative regulation of epithelial cell migration
  • transmembrane receptor protein tyrosine kinase signaling pathway
  • dephosphorylation
  • brain development
  • negative regulation of neuron projection development
  • peptidyl-tyrosine dephosphorylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5793

19270

Ensembl

ENSG00000144724

n/a

UniProt

P23470

Q05909

RefSeq (mRNA)

NM_002841
NM_001375471

NM_008981
NM_001347593

RefSeq (protein)

NP_002832
NP_001362400

NP_001334522
NP_033007

Location (UCSC)Chr 3: 61.56 – 62.3 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Receptor-type tyrosine-protein phosphatase gamma is an enzyme that in humans is encoded by the PTPRG gene.[4][5]

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 PTP possesses an extracellular region, a single transmembrane region, and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. The extracellular region of this PTP contains a carbonic anhydrase-like (CAH) domain, which is also found in the extracellular region of PTPRBETA/ZETA. This gene is located in a chromosomal region that is frequently deleted in renal cell carcinoma and lung carcinoma, thus is thought to be a candidate tumor suppressor gene.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000144724 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ LaForgia S, Morse B, Levy J, Barnea G, Cannizzaro LA, Li F, Nowell PC, Boghosian-Sell L, Glick J, Weston A, et al. (Jul 1991). "Receptor protein-tyrosine phosphatase gamma is a candidate tumor suppressor gene at human chromosome region 3p21". Proc Natl Acad Sci U S A. 88 (11): 5036–40. Bibcode:1991PNAS...88.5036L. doi:10.1073/pnas.88.11.5036. PMC 51802. PMID 1711217.
  5. ^ a b "Entrez Gene: PTPRG protein tyrosine phosphatase, receptor type, G".

Further reading

  • Kaplan R, Morse B, Huebner K, et al. (1990). "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain". Proc. Natl. Acad. Sci. U.S.A. 87 (18): 7000–4. Bibcode:1990PNAS...87.7000K. doi:10.1073/pnas.87.18.7000. PMC 54670. PMID 2169617.
  • Krueger NX, Streuli M, Saito H (1990). "Structural diversity and evolution of human receptor-like protein tyrosine phosphatases". EMBO J. 9 (10): 3241–52. doi:10.1002/j.1460-2075.1990.tb07523.x. PMC 552056. PMID 2170109.
  • Latif F, Tory K, Modi W, et al. (1993). "A MspI polymorphism and linkage mapping of the human protein-tyrosine phosphatase G (PTPRG) gene". Hum. Mol. Genet. 2 (1): 91. doi:10.1093/hmg/2.1.91. PMID 7683956.
  • Barnea G, Silvennoinen O, Shaanan B, et al. (1993). "Identification of a carbonic anhydrase-like domain in the extracellular region of RPTP gamma defines a new subfamily of receptor tyrosine phosphatases". Mol. Cell. Biol. 13 (3): 1497–506. doi:10.1128/mcb.13.3.1497. PMC 359461. PMID 8382771.
  • Kastury K, Ohta M, Lasota J, et al. (1997). "Structure of the human receptor tyrosine phosphatase gamma gene (PTPRG) and relation to the familial RCC t(3;8) chromosome translocation". Genomics. 32 (2): 225–35. doi:10.1006/geno.1996.0109. PMID 8833149.
  • van Niekerk CC, Poels LG (1999). "Reduced expression of protein tyrosine phosphatase gamma in lung and ovarian tumors". Cancer Lett. 137 (1): 61–73. doi:10.1016/S0304-3835(98)00344-9. PMID 10376795.
  • Kawachi H, Tamura H, Watakabe I, et al. (1999). "Protein tyrosine phosphatase zeta/RPTPbeta interacts with PSD-95/SAP90 family". Brain Res. Mol. Brain Res. 72 (1): 47–54. doi:10.1016/S0169-328X(99)00204-1. PMID 10521598.
  • Liu S, Kulp SK, Sugimoto Y, et al. (2002). "Involvement of breast epithelial-stromal interactions in the regulation of protein tyrosine phosphatase-gamma (PTPgamma) mRNA expression by estrogenically active agents". Breast Cancer Res. Treat. 71 (1): 21–35. doi:10.1023/A:1013343718942. PMID 11859871. S2CID 6175175.
  • 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Liu S, Sugimoto Y, Kulp SK, et al. (2003). "Estrogenic down-regulation of protein tyrosine phosphatase gamma (PTP gamma) in human breast is associated with estrogen receptor alpha". Anticancer Res. 22 (6C): 3917–23. PMID 12553013.
  • Liu S, Sugimoto Y, Sorio C, et al. (2004). "Function analysis of estrogenically regulated protein tyrosine phosphatase gamma (PTPgamma) in human breast cancer cell line MCF-7". Oncogene. 23 (6): 1256–62. doi:10.1038/sj.onc.1207235. PMID 14676845.
  • van Doorn R, Zoutman WH, Dijkman R, et al. (2005). "Epigenetic profiling of cutaneous T-cell lymphoma: promoter hypermethylation of multiple tumor suppressor genes including BCL7a, PTPRG, and p73". J. Clin. Oncol. 23 (17): 3886–96. doi:10.1200/JCO.2005.11.353. PMID 15897551.
  • Liu T, Qian WJ, Gritsenko MA, et al. (2006). "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry". J. Proteome Res. 4 (6): 2070–80. doi:10.1021/pr0502065. PMC 1850943. PMID 16335952.
  • v
  • t
  • e
  • 2h4v: Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma
    2h4v: Crystal Structure of the Human Tyrosine Receptor Phosphatase Gamma
  • 2hy3: Crystal structure of the human tyrosine receptor phosphate gamma in complex with vanadate
    2hy3: Crystal structure of the human tyrosine receptor phosphate gamma in complex with vanadate
  • 2nlk: Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG)
    2nlk: Crystal structure of D1 and D2 catalytic domains of human Protein Tyrosine Phosphatase Gamma (D1+D2 PTPRG)
  • 2pbn: Crystal structure of the human tyrosine receptor phosphate gamma
    2pbn: Crystal structure of the human tyrosine receptor phosphate gamma
  • v
  • t
  • e
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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