PTPRB

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Protein tyrosine phosphatase, receptor type, B
File:PBB Protein PTPRB image.jpg
PDB rendering based on 2ahs.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PTPRB ; DKFZp686E2262; DKFZp686H15164; FLJ44133; HPTP-BETA; HPTPB; MGC142023; MGC59935; PTPB; R-PTP-BETA
External IDs Template:OMIM5 Template:MGI HomoloGene2125
RNA expression pattern
File:PBB GE PTPRB 205846 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Protein tyrosine phosphatase, receptor type, B, also known as PTPRB, is a human gene.[1]

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 contains an extracellular domain, a single transmembrane segment and one intracytoplasmic catalytic domain, thus belongs to receptor type PTP. The extracellular region of this PTP is composed of multiple fibronectin type_III repeats, which was shown to interact with neuronal receptor and cell adhesion molecules, such as contactin and tenascin C. This protein was also found to interact with sodium channels, and thus may regulate sodium channels by altering tyrosine phosphorylation status. The functions of the interaction partners of this protein implicate the roles of this PTP in cell adhesion, neurite growth, and neuronal differentiation.[1]

References

  1. 1.0 1.1 "Entrez Gene: PTPRB protein tyrosine phosphatase, receptor type, B".

Further reading

  • Peles E, Schlessinger J, Grumet M (1998). "Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: implications for intercellular signaling". Trends Biochem. Sci. 23 (4): 121–4. PMID 9584610.
  • Dewang PM, Hsu NM, Peng SZ, Li WR (2005). "Protein tyrosine phosphatases and their inhibitors". Curr. Med. Chem. 12 (1): 1–22. PMID 15638728.
  • Ramachandran C, Aebersold R, Tonks NK, Pot DA (1992). "Sequential dephosphorylation of a multiply phosphorylated insulin receptor peptide by protein tyrosine phosphatases". Biochemistry. 31 (17): 4232–8. PMID 1373652.
  • Harder KW, Anderson LL, Duncan AM, Jirik FR (1993). "The gene for receptor-like protein tyrosine phosphatase (PTPRB) is assigned to chromosome 12q15-->q21". Cytogenet. Cell Genet. 61 (4): 269–70. PMID 1486802.
  • De Vries L, Li RY, Ragab A; et al. (1991). "Expression of a truncated protein-tyrosine phosphatase mRNA in human lung". FEBS Lett. 282 (2): 285–8. PMID 1645282.
  • 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. 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. PMID 2170109.
  • Gaits F, Li RY, Ragab A; et al. (1995). "Increase in receptor-like protein tyrosine phosphatase activity and expression level on density-dependent growth arrest of endothelial cells". Biochem. J. 311 ( Pt 1): 97–103. PMID 7575486.
  • Peles E, Nativ M, Campbell PL; et al. (1995). "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin". Cell. 82 (2): 251–60. PMID 7628014.
  • Sakurai T, Lustig M, Nativ M; et al. (1997). "Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta". J. Cell Biol. 136 (4): 907–18. PMID 9049255.
  • Peles E, Nativ M, Lustig M; et al. (1997). "Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions". EMBO J. 16 (5): 978–88. doi:10.1093/emboj/16.5.978. PMID 9118959.
  • Feito MJ, Bragardo M, Buonfiglio D; et al. (1997). "gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules". Int. Immunol. 9 (8): 1141–7. PMID 9263011.
  • Fachinger G, Deutsch U, Risau W (1999). "Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2". Oncogene. 18 (43): 5948–53. doi:10.1038/sj.onc.1202992. PMID 10557082.
  • Meng K, Rodriguez-Peña A, Dimitrov T; et al. (2000). "Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2603–8. doi:10.1073/pnas.020487997. PMID 10706604.
  • Ratcliffe CF, Qu Y, McCormick KA; et al. (2000). "A sodium channel signaling complex: modulation by associated receptor protein tyrosine phosphatase beta". Nat. Neurosci. 3 (5): 437–44. doi:10.1038/74805. PMID 10769382.
  • Adamsky K, Schilling J, Garwood J; et al. (2001). "Glial tumor cell adhesion is mediated by binding of the FNIII domain of receptor protein tyrosine phosphatase beta (RPTPbeta) to tenascin C.". Oncogene. 20 (5): 609–18. doi:10.1038/sj.onc.1204119. PMID 11313993.
  • Cheburkin IuV, Kniazeva TG, Peter S; et al. (2002). "[Molecular portrait of human kidney carcinomas: the gene expression profiling of protein-tyrosine kinases and tyrosine phosphatases which controlled regulatory signals in the cells]". Mol. Biol. (Mosk.). 36 (3): 480–90. PMID 12068634.
  • Nawroth R, Poell G, Ranft A; et al. (2002). "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts". EMBO J. 21 (18): 4885–95. PMID 12234928.
  • 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. PMID 12477932.

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