PTPRD

Revision as of 13:38, 6 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Protein tyrosine phosphatase, receptor type, D
File:PBB Protein PTPRD image.jpg
PDB rendering based on 1lar.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PTPRD ; HPTP; HPTP-DELTA; HPTPD; MGC119750; MGC119751; MGC119752; MGC119753; PTPD; R-PTP-DELTA
External IDs Template:OMIM5 HomoloGene88669
RNA expression pattern
File:PBB GE PTPRD 205712 at tn.png
File:PBB GE PTPRD 213362 at tn.png
File:PBB GE PTPRD 214043 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, D, also known as PTPRD, 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 region, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, thus represents a receptor-type PTP. The extracellular region of this protein is composed of three Ig-like and eight fibronectin type III-like domains. Studies of the similar genes in chick and fly suggest the role of this PTP is in promoting neurite growth, and regulating neurons axon guidance. Multiple tissue specific alternatively spliced transcript variants of this gene have been reported.[1]

References

  1. 1.0 1.1 "Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D".

Further reading

  • 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.
  • Schaapveld RQ, van den Maagdenberg AM, Schepens JT; et al. (1995). "The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization". Genomics. 27 (1): 124–30. PMID 7665159.
  • Pulido R, Krueger NX, Serra-Pagès C; et al. (1995). "Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms". J. Biol. Chem. 270 (12): 6722–8. PMID 7896816.
  • Mizuno K, Hasegawa K, Katagiri T; et al. (1993). "MPTP delta, a putative murine homolog of HPTP delta, is expressed in specialized regions of the brain and in the B-cell lineage". Mol. Cell. Biol. 13 (9): 5513–23. PMID 8355697.
  • Pulido R, Serra-Pagès C, Tang M, Streuli M (1996). "The LAR/PTP delta/PTP sigma subfamily of transmembrane protein-tyrosine-phosphatases: multiple human LAR, PTP delta, and PTP sigma isoforms are expressed in a tissue-specific manner and associate with the LAR-interacting protein LIP.1". Proc. Natl. Acad. Sci. U.S.A. 92 (25): 11686–90. PMID 8524829.
  • Wagner J, Gordon LA, Heng HH; et al. (1997). "Physical mapping of receptor type protein tyrosine phosphatase sigma (PTPRS) to human chromosome 19p13.3". Genomics. 38 (1): 76–8. doi:10.1006/geno.1996.0594. PMID 8954782.
  • Wallace MJ, Fladd C, Batt J, Rotin D (1998). "The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma". Mol. Cell. Biol. 18 (5): 2608–16. PMID 9566880.
  • Serra-Pagès C, Medley QG, Tang M; et al. (1998). "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611–20. PMID 9624153.
  • Blanchetot C, den Hertog J (2000). "Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs". J. Biol. Chem. 275 (17): 12446–52. PMID 10777529.
  • Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J (2003). "Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases". J. Biol. Chem. 277 (49): 47263–9. doi:10.1074/jbc.M205810200. PMID 12376545.
  • 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.
  • Woodings JA, Sharp SJ, Machesky LM (2003). "MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta". Biochem. J. 371 (Pt 2): 463–71. doi:10.1042/BJ20021962. PMID 12570871.
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8. doi:10.1186/gb-2004-5-2-r8. PMID 14759258.
  • Sato M, Takahashi K, Nagayama K; et al. (2005). "Identification of chromosome arm 9p as the most frequent target of homozygous deletions in lung cancer". Genes Chromosomes Cancer. 44 (4): 405–14. doi:10.1002/gcc.20253. PMID 16114034.
  • Purdie KJ, Lambert SR, Teh MT; et al. (2007). "Allelic imbalances and microdeletions affecting the PTPRD gene in cutaneous squamous cell carcinomas detected using single nucleotide polymorphism microarray analysis". Genes Chromosomes Cancer. 46 (7): 661–9. doi:10.1002/gcc.20447. PMID 17420988.

Template:WikiDoc Sources