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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Receptor-type tyrosine-protein phosphatase delta''' is an [[enzyme]] that in humans is encoded by the ''PTPRD'' [[gene]].<ref name="pmid7896816">{{cite journal | vauthors = Pulido R, Krueger NX, Serra-Pagès C, Saito H, Streuli M | 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 | date = Apr 1995 | pmid = 7896816 | pmc =  | doi = 10.1074/jbc.270.12.6722 }}</ref><ref name="pmid8355697">{{cite journal | vauthors = Mizuno K, Hasegawa K, Katagiri T, Ogimoto M, Ichikawa T, Yakura H | 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 | date = Sep 1993 | pmid = 8355697 | pmc = 360267 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5789| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PTPRD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lar.
| PDB = {{PDB2|1lar}}, {{PDB2|1x5z}}, {{PDB2|2dlh}}, {{PDB2|2fh7}}, {{PDB2|2nv5}}
| Name = Protein tyrosine phosphatase, receptor type, D
| HGNCid = 9668
| Symbol = PTPRD
| AltSymbols =; HPTP; HPTP-DELTA; HPTPD; MGC119750; MGC119751; MGC119752; MGC119753; PTPD; R-PTP-DELTA
| OMIM = 601598
| ECnumber = 
| Homologene = 88669
| MGIid = 
| GeneAtlas_image1 = PBB_GE_PTPRD_205712_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTPRD_213362_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTPRD_214043_at_tn.png
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0006796 |text = phosphate metabolic process}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5789
    | Hs_Ensembl = ENSG00000153707
    | Hs_RefseqProtein = NP_001035802
    | Hs_RefseqmRNA = NM_001040712
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 8304246
    | Hs_GenLoc_end = 9008735
    | Hs_Uniprot = P23468
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Protein tyrosine phosphatase, receptor type, D''', also known as '''PTPRD''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref name="entrez"/>
{{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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
== Clinical significance ==
{{reflist|2}}
 
==Further reading==
Mutations in the ''PTPRD'' gene are associated with [[autism]],<ref name="urlResult Content View">{{cite web | url = http://www.abstracts2view.com/pas/view.php?nu=PAS10L1_120&terms | title = Autism Is Associated with Inherited Deletions in PTPRD and NCAM2  |vauthors=Lei N, etal | authorlink = | year = 2010  | format = | work = PAS 2010; Abstract 2320.1 | publisher = Pediatric Academic Societies | pages = | archiveurl = | archivedate = | quote = | accessdate = }}</ref> [[obsessive–compulsive disorder]],<ref>{{Cite web|title = OCD: New Genetic Marker Reported|url = http://guardianlv.com/2014/06/ocd-new-genetic-marker-reported/|accessdate = 2015-08-16}}</ref> and [[breast cancer]].<ref name=nature11412>{{cite journal | vauthors= ((Cancer Genome Atlas Network)), Koboldt DC, Fulton RS, McLellan MD, Schmidt H, Kalicki-Veizer J, etal | title = Comprehensive molecular portraits of human breast tumours | journal = Nature | volume = 490 | issue = 7418 | pages = 61–70 | date = October 2012 | pmid = 23000897 | pmc = 3465532 | doi = 10.1038/nature11412 }}</ref>
 
== Interactions ==
 
PTPRD has been shown to [[Protein-protein interaction|interact]] with [[PTPRS]]<ref name=pmid9566880>{{cite journal | vauthors = 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 | date = May 1998 | pmid = 9566880 | pmc = 110640 }}</ref> and [[liprin-alpha-1]].<ref name=pmid8524829>{{cite journal | vauthors = 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 = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 92 | issue = 25 | pages = 11686–90 | date = Dec 1995 | pmid = 8524829 | pmc = 40467 | doi = 10.1073/pnas.92.25.11686 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 | pmc = 552056 | doi =  }}
| citations =
* {{cite journal | vauthors = Schaapveld RQ, van den Maagdenberg AM, Schepens JT, Weghuis DO, Geurts van Kessel A, Wieringa B, Hendriks WJ | 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 = 10.1006/geno.1995.1014 }}
*{{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 | vauthors = 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 | pmc = 40467 | doi = 10.1073/pnas.92.25.11686 }}
*{{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 | vauthors = Wagner J, Gordon LA, Heng HH, Tremblay ML, Olsen AS | 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=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 | vauthors = 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 | pmc = 110640 | 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 | vauthors = Serra-Pagès C, Medley QG, Tang M, Hart A, Streuli M | 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 = 10.1074/jbc.273.25.15611 }}
*{{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 | vauthors = 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 = 10.1074/jbc.275.17.12446 }}
*{{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 | vauthors = 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=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 | vauthors = 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 | pmc = 1223315 | doi = 10.1042/BJ20021962 }}
*{{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 | vauthors = 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 | pmc = 395752 | doi = 10.1186/gb-2004-5-2-r8 }}
*{{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 | vauthors = Sato M, Takahashi K, Nagayama K, Arai Y, Ito N, Okada M, Minna JD, Yokota J, Kohno T | 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=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 | vauthors = Purdie KJ, Lambert SR, Teh MT, Chaplin T, Molloy G, Raghavan M, Kelsell DP, Leigh IM, Harwood CA, Proby CM, Young BD | 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 | pmc = 2426828 | doi = 10.1002/gcc.20447 }}
*{{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.20447 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5789}}
{{WikiDoc Sources}}
{{Protein tyrosine phosphatases}}
 
 
{{gene-9-stub}}

Latest revision as of 18:58, 7 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Receptor-type tyrosine-protein phosphatase delta is an enzyme that in humans is encoded by the PTPRD gene.[1][2][3]

Function

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.[3]

Clinical significance

Mutations in the PTPRD gene are associated with autism,[4] obsessive–compulsive disorder,[5] and breast cancer.[6]

Interactions

PTPRD has been shown to interact with PTPRS[7] and liprin-alpha-1.[8]

References

  1. Pulido R, Krueger NX, Serra-Pagès C, Saito H, Streuli M (Apr 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. doi:10.1074/jbc.270.12.6722. PMID 7896816.
  2. Mizuno K, Hasegawa K, Katagiri T, Ogimoto M, Ichikawa T, Yakura H (Sep 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. PMC 360267. PMID 8355697.
  3. 3.0 3.1 "Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D".
  4. Lei N, et al. (2010). "Autism Is Associated with Inherited Deletions in PTPRD and NCAM2". PAS 2010; Abstract 2320.1. Pediatric Academic Societies.
  5. "OCD: New Genetic Marker Reported". Retrieved 2015-08-16.
  6. Cancer Genome Atlas Network, Koboldt DC, Fulton RS, McLellan MD, Schmidt H, Kalicki-Veizer J, et al. (October 2012). "Comprehensive molecular portraits of human breast tumours". Nature. 490 (7418): 61–70. doi:10.1038/nature11412. PMC 3465532. PMID 23000897.
  7. Wallace MJ, Fladd C, Batt J, Rotin D (May 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. PMC 110640. PMID 9566880.
  8. Pulido R, Serra-Pagès C, Tang M, Streuli M (Dec 1995). "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. doi:10.1073/pnas.92.25.11686. PMC 40467. PMID 8524829.

Further reading