- PTPRD
Protein tyrosine phosphatase, receptor type, D, also known as PTPRD, is a human
gene .cite web | title = Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5789| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5789| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Krueger NX, Streuli M, Saito H |title=Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3241–52 |year= 1990 |pmid= 2170109 |doi=
*cite journal | author=Schaapveld RQ, van den Maagdenberg AM, Schepens JT, "et al." |title=The mouse gene Ptprf encoding the leukocyte common antigen-related molecule LAR: cloning, characterization, and chromosomal localization. |journal=Genomics |volume=27 |issue= 1 |pages= 124–30 |year= 1995 |pmid= 7665159 |doi=
*cite journal | author=Pulido R, Krueger NX, Serra-Pagès C, "et al." |title=Molecular characterization of the human transmembrane protein-tyrosine phosphatase delta. Evidence for tissue-specific expression of alternative human transmembrane protein-tyrosine phosphatase delta isoforms. |journal=J. Biol. Chem. |volume=270 |issue= 12 |pages= 6722–8 |year= 1995 |pmid= 7896816 |doi=
*cite journal | author=Mizuno K, Hasegawa K, Katagiri T, "et al." |title=MPTP delta, a putative murine homolog of HPTP delta, is expressed in specialized regions of the brain and in the B-cell lineage. |journal=Mol. Cell. Biol. |volume=13 |issue= 9 |pages= 5513–23 |year= 1993 |pmid= 8355697 |doi=
*cite journal | author=Pulido R, Serra-Pagès C, Tang M, Streuli M |title=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. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11686–90 |year= 1996 |pmid= 8524829 |doi=
*cite journal | author=Wagner J, Gordon LA, Heng HH, "et al." |title=Physical mapping of receptor type protein tyrosine phosphatase sigma (PTPRS) to human chromosome 19p13.3. |journal=Genomics |volume=38 |issue= 1 |pages= 76–8 |year= 1997 |pmid= 8954782 |doi= 10.1006/geno.1996.0594
*cite journal | author=Wallace MJ, Fladd C, Batt J, Rotin D |title=The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2608–16 |year= 1998 |pmid= 9566880 |doi=
*cite journal | author=Serra-Pagès C, Medley QG, Tang M, "et al." |title=Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15611–20 |year= 1998 |pmid= 9624153 |doi=
*cite journal | author=Blanchetot C, den Hertog J |title=Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine phosphatase domains of various RPTPs. |journal=J. Biol. Chem. |volume=275 |issue= 17 |pages= 12446–52 |year= 2000 |pmid= 10777529 |doi=
*cite journal | author=Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J |title=Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47263–9 |year= 2003 |pmid= 12376545 |doi= 10.1074/jbc.M205810200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Woodings JA, Sharp SJ, Machesky LM |title=MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta. |journal=Biochem. J. |volume=371 |issue= Pt 2 |pages= 463–71 |year= 2003 |pmid= 12570871 |doi= 10.1042/BJ20021962
*cite journal | author=Hillman RT, Green RE, Brenner SE |title=An unappreciated role for RNA surveillance. |journal=Genome Biol. |volume=5 |issue= 2 |pages= R8 |year= 2005 |pmid= 14759258 |doi= 10.1186/gb-2004-5-2-r8
*cite journal | author=Sato M, Takahashi K, Nagayama K, "et al." |title=Identification of chromosome arm 9p as the most frequent target of homozygous deletions in lung cancer. |journal=Genes Chromosomes Cancer |volume=44 |issue= 4 |pages= 405–14 |year= 2005 |pmid= 16114034 |doi= 10.1002/gcc.20253
*cite journal | author=Purdie KJ, Lambert SR, Teh MT, "et al." |title=Allelic imbalances and microdeletions affecting the PTPRD gene in cutaneous squamous cell carcinomas detected using single nucleotide polymorphism microarray analysis. |journal=Genes Chromosomes Cancer |volume=46 |issue= 7 |pages= 661–9 |year= 2007 |pmid= 17420988 |doi= 10.1002/gcc.20447PBB_Controls
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