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PTPRD (protein tyrosine phosphatase, receptor type, D)

Identity

Other namesEC 3.1.3.48
HPTP
HPTP-DELTA
HPTPD
MGC119750
MGC119751
MGC119752
MGC119753
OTTHUMP00000022727
PTPD
R-PTP-DELTA
R-PTP-delta
HGNC (Hugo) PTPRD
LocusID (NCBI) 5789
Location 9p24.1
Location_base_pair Starts at 8314246 and ends at 8733946 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Description The PTPRD gene is composed of 36 coding sequence exons and a 5' UTR spliced together from 11 non-coding exons.
Transcription There are five known transcript variants for PTPRD.
Transcript Variant 1: This variant encodes the longest isoform 1 and is 10078 bp in length (Figure A).
Transcript Variant 2: This variant lacks two separate internal segments within the coding region. It thus encodes a protein that lacks a 9 aa, and a 4 aa internal fragments, as compared to isoform 1 and is 10039 bp in length (Figure C).
Transcript Variant 3: This variant lacks an internal segment within the coding region. It thus encodes a protein that lacks a 9 aa internal fragment, as compared to isoform 1 and is 10051 bp in length (Figure D).
Transcript Variant 4: This variant lacks an internal segment within the coding region. It thus encodes a protein that lacks a 411 aa internal fragment, and has one amino acid change, as compared to isoform 1 and is 8845 bp in length (Figure B).
Transcript Variant 5: This variant omits several exons, and utilizes an alternate exon, in the coding region. The resulting protein (isoform 5) retains the same reading frame and has the same N- and C-terminus as isoform 1. This variant is 8848 bp in length (Figure E).
Pseudogene No pseudogenes have been reported.

Protein

 
  Figure A - E: Illustrates the differences between the known PTPRD isoforms, as described in the text.
Description Amino acids: 1912.
Molecular Weight: 214760 Da.
The PTPRD gene belongs to the receptor class 2A subfamily of the protein-tyrosine phosphatases. It contains an extracellular region composed of 8 fibronectin type-III domains and 3 Ig-like C2-type (immunoglobulin-like) domains, a single transmembrane segment and two tandem intracytoplasmic tyrosine-protein phosphatase domains.
Molecular Class: Receptor Tyrosine Phosphatase.
Molecular Function: Receptor Signalling Protein Tyrosine Phosphatase Activity.
Biological Process: Cell Communication ; Signal Transduction.
Expression Brain, Kidney.
Multiple isoforms are generated by either alternate splicing or by alternate transcriptional start sites in a tissue specific manner. The predominant isoform in brain has an extended 711 base pair 5' UTR (L isoform), while the isoform (S) expressed in kidney lacks the extended 5' UTR. In addition, the brain isoform is characterized by the absence of exons 14 to 18 corresponding to amino acid residues 568 to 978 of the 4th through 7th fibronectin III-like domain and by the insertion of a 12 base pair mini-exon sequence between exons 23 and 24 (Nair et al., 2008).
The full length PTPRD isoform has an extracellular region containing three Ig-like and eight FN-III like domains connected via a transmembrane peptide to an intracellular region with two PTPase domains (A), whereas another isoform lacks four of the eight FN-III like domains (B). Furthermore, other PTPRD isoforms exist that lack 9 AA within the second Ig-like domain and 4 AA at the junction of the 2nd and 3rd Ig-like domains (C) or 9 AAs within the 5th FN-III like domain (D). The fifth isoform lacks four of the eight FN-III like domains and has mutation in the second Ig-like domain (E). RT-PCR analysis demonstrated that PTPRD isoforms lacking these short peptides are expressed in kidney, whereas isoforms containing these peptides are expressed in the brain (Pulido et al., 1995).
Localisation Membrane; Single-pass type I membrane protein.
Function A cleavage occurs, separating the extracellular domain from the transmembrane segment. This process called 'ectodomain shedding' is thought to be involved in receptor desensitization, signal transduction and/or membrane localization. Plays key role in promoting neurite growth and regulating axon guidance.
Homology PTPRD shares a PTP domain, involved in dephosphorylating phosphorylated tyrosine residues, with the other receptor-like protein tyrosine phosphatases. The human and mouse PTPRD sequences are 93% identical and 95% homologous.

Implicated in

Entity Lung Adenocarcinoma
Disease Early evidence for the involvement of PTPRD in lung adenocarcinoma came from the detection of homozygous deletions in both primary tumours and cell lines representing both small cell lung carcinoma and non-small cell lung carcinoma (Cox et al., 2005; Zhao et al., 2005; Sato et al., 2005; Nagayama et al., 2007). In addition, somatically acquired PTPRD mutations were found in 11 out of 188 lung adenocarcinoma samples (Weir et al., 2007). Notably, three of the mutations encode predicated inactivating changes in the tyrosine phosphatase domain. Screening for somatic mutations in 623 candidate genes using 188 primary lung adenocarcinoma tissues also revealed sequence changes in PTPRD (Ding et al., 2008).
  
Entity Neuroblastoma
Disease High resolution a CGH analysis of neuroblastoma (NBL) tumours and cell lines identified homozygous and hemizygous intragenic deletions of the PTPRD gene, implicating the gene as a candidate tumor suppressor gene in this type of cancer (Stallings et al., 2006). In addition, the 5' UTR of PTPRD, consisting of 11 noncoding exons, was found to be aberrantly spliced in > 50% of NBL primary tumors and cell lines (Nair et al., 2008). mRNA levels were determined to be significantly reduced in unfavorable tumour subtypes relative to more favorable tumor subtypes.
  
Entity Squamous Cell Carcinoma
Disease Both homozygous and hemizygous deletions affecting the PTPRD gene have been reported in squamous cell carcinoma (Purdie et al., 2007).
  
Entity Colorectal Carcinoma
Disease PTPRD was found to be somatically mutated in colorectal carcinoma with the sequence changes, R28Q, L276P, V901A (Sjoblom et al., 2006).
  
Entity Glioblastoma Multiforme and Malignant Melanoma
Disease A high frequency of deletions in the PTPRD gene were detected in glioblastoma multiforme (GBM) tumours using Affymetrix 250K single nucleotide polymorphism arrays (Solomon et al., 2008). Missense and nonsense mutations of PTPRD were also identified in a subset of the samples lacking deletions, including an inherited mutation with somatic loss of the wild-type allele. The same group also identified 10 somatically acquired mutations in PTPRD among 7 of 57 melanoma tumors (12%). Ectopic reconstitution of wild-type PTPRD expression in GBM and melanoma cell lines harboring deletions or mutations of the endogenous PTPRD gene led to growth suppression and apoptosis, indicating that this gene functions as a tumour suppressor in multiple forms of cancer (Solomon et al., 2008).
  
Entity Restless Leg Syndrome (RLS)
Disease Genome-wide association study of RLS identified three SNPs within the PTPRD gene in the chromosome 9 linkage region (RLS3) as nominally significant (Winkelmann et al., 2007). PTPRD is identified as the fourth genome-wide significant locus for RLS from the genome wide association study in 2458 affected individuals and 4749 controls from Germany, Austria, Czech Republic and Canada (Schormair et al., 2008).
  
Entity Pediatric Asthma
Disease A whole-genome linkage disequilibrium mapping study for asthma on 190 allergic and nonallergic asthma children in Taiwan revealed that polymorphisms of PTPRD are strongly associated with pediatric bronchial asthma in the Taiwanese population (Shyur et al., 2008).
  

External links

Nomenclature
HGNC (Hugo)PTPRD   9668
Cards
AtlasPTPRDID41927ch9p23
Entrez_Gene (NCBI)PTPRD  5789  protein tyrosine phosphatase, receptor type, D
GeneCards (Weizmann)PTPRD
Ensembl (Hinxton)ENSG00000153707 [Gene_View]  chr9:8314246-8733946 [Contig_View]  PTPRD [Vega]
ICGC DataPortalENSG00000153707
cBioPortalPTPRD
AceView (NCBI)PTPRD
Genatlas (Paris)PTPRD
WikiGenes5789
SOURCE (Princeton)NM_001040712 NM_001171025 NM_002839 NM_130391 NM_130392 NM_130393
Genomic and cartography
GoldenPath (UCSC)PTPRD  -  9p24.1   chr9:8314246-8733946 -  9p24.1-p23   [Description]    (hg19-Feb_2009)
EnsemblPTPRD - 9p24.1-p23 [CytoView]
Mapping of homologs : NCBIPTPRD [Mapview]
OMIM601598   
Gene and transcription
Genbank (Entrez)AB208869 AB211400 AK296392 BC028038 BC037801
RefSeq transcript (Entrez)NM_001040712 NM_001171025 NM_002839 NM_130391 NM_130392 NM_130393
RefSeq genomic (Entrez)AC_000141 NC_000009 NC_018920 NG_033963 NT_008413 NW_001839149 NW_004929342
Consensus coding sequences : CCDS (NCBI)PTPRD
Cluster EST : UnigeneHs.446083 [ NCBI ]
CGAP (NCI)Hs.446083
Alternative Splicing : Fast-db (Paris)GSHG0030664
Alternative Splicing GalleryENSG00000153707
Gene ExpressionPTPRD [ NCBI-GEO ]     PTPRD [ SEEK ]   PTPRD [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP23468 (Uniprot)
NextProtP23468  [Medical]
With graphics : InterProP23468
Splice isoforms : SwissVarP23468 (Swissvar)
Catalytic activity : Enzyme3.1.3.48 [ Enzyme-Expasy ]   3.1.3.483.1.3.48 [ IntEnz-EBI ]   3.1.3.48 [ BRENDA ]   3.1.3.48 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)FN3 (PS50853)    IG_LIKE (PS50835)    TYR_PHOSPHATASE_1 (PS00383)    TYR_PHOSPHATASE_2 (PS50056)    TYR_PHOSPHATASE_PTP (PS50055)   
Domains : Interpro (EBI)Fibronectin_type3 [organisation]   Ig-like_dom [organisation]   Ig-like_fold [organisation]   Ig_I-set [organisation]   Ig_sub2 [organisation]   Prot-tyrosine_phosphatase-like [organisation]   Tyr/Dual-sp_Pase [organisation]   Tyr_Pase_AS [organisation]   Tyr_Pase_rcpt/non-rcpt [organisation]  
Related proteins : CluSTrP23468
Domain families : Pfam (Sanger)fn3 (PF00041)    I-set (PF07679)    Y_phosphatase (PF00102)   
Domain families : Pfam (NCBI)pfam00041    pfam07679    pfam00102   
Domain families : Smart (EMBL)FN3 (SM00060)  IGc2 (SM00408)  PTPc (SM00194)  
DMDM Disease mutations5789
Blocks (Seattle)P23468
PDB (SRS)1X5Z    2DLH    2YD6    2YD7   
PDB (PDBSum)1X5Z    2DLH    2YD6    2YD7   
PDB (IMB)1X5Z    2DLH    2YD6    2YD7   
PDB (RSDB)1X5Z    2DLH    2YD6    2YD7   
Human Protein AtlasENSG00000153707 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasP23468
HPRD03358
IPIIPI00852829   IPI00954886   IPI00219860   IPI00375548   IPI00375547   IPI00955467   IPI00796452   IPI01018655   IPI00946346   IPI00947407   IPI00872363   
Protein Interaction databases
DIP (DOE-UCLA)P23468
IntAct (EBI)P23468
FunCoupENSG00000153707
BioGRIDPTPRD
InParanoidP23468
Interologous Interaction database P23468
IntegromeDBPTPRD
STRING (EMBL)PTPRD
Ontologies - Pathways
Ontology : AmiGOtransmembrane receptor protein tyrosine phosphatase activity  receptor binding  protein binding  integral component of plasma membrane  protein dephosphorylation  phosphate-containing compound metabolic process  heterophilic cell-cell adhesion  transmembrane receptor protein tyrosine phosphatase signaling pathway  neuron differentiation  peptidyl-tyrosine dephosphorylation  peptidyl-tyrosine dephosphorylation  positive regulation of dendrite morphogenesis  cell adhesion molecule binding  presynaptic membrane assembly  
Ontology : EGO-EBItransmembrane receptor protein tyrosine phosphatase activity  receptor binding  protein binding  integral component of plasma membrane  protein dephosphorylation  phosphate-containing compound metabolic process  heterophilic cell-cell adhesion  transmembrane receptor protein tyrosine phosphatase signaling pathway  neuron differentiation  peptidyl-tyrosine dephosphorylation  peptidyl-tyrosine dephosphorylation  positive regulation of dendrite morphogenesis  cell adhesion molecule binding  presynaptic membrane assembly  
Protein Interaction DatabasePTPRD
Wikipedia pathwaysPTPRD
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)PTPRD
snp3D : Map Gene to Disease5789
SNP (GeneSNP Utah)PTPRD
SNP : HGBasePTPRD
Genetic variants : HAPMAPPTPRD
Exome VariantPTPRD
1000_GenomesPTPRD 
ICGC programENSG00000153707 
Somatic Mutations in Cancer : COSMICPTPRD 
CONAN: Copy Number AnalysisPTPRD 
Mutations and Diseases : HGMDPTPRD
Genomic VariantsPTPRD  PTPRD [DGVbeta]
dbVarPTPRD
ClinVarPTPRD
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM601598   
MedgenPTPRD
GENETestsPTPRD
Disease Genetic AssociationPTPRD
Huge Navigator PTPRD [HugePedia]  PTPRD [HugeCancerGEM]
General knowledge
Homologs : HomoloGenePTPRD
Homology/Alignments : Family Browser (UCSC)PTPRD
Phylogenetic Trees/Animal Genes : TreeFamPTPRD
Chemical/Protein Interactions : CTD5789
Chemical/Pharm GKB GenePA34013
Clinical trialPTPRD
Cancer Resource (Charite)ENSG00000153707
Other databases
Probes
Litterature
PubMed62 Pubmed reference(s) in Entrez
CoreMinePTPRD
iHOPPTPRD
OncoSearchPTPRD

Bibliography

Developmental regulation of gene expression for the MPTP delta isoforms in the central nervous system and the immune system.
Mizuno K, Hasegawa K, Ogimoto M, Katagiri T, Yakura H.
FEBS Lett. 1994 Dec 5;355(3):223-8.
PMID 7988677
 
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.
Pulido R, Serra-Pages C, Tang M, Streuli M.
Proc Natl Acad Sci U S A. 1995 Dec 5;92(25):11686-90.
PMID 8524829
 
The selective reduction in PTPdelta expression in hepatomas.
Urushibara N, Karasaki H, Nakamura K, Mizuno Y, Ogawa K, Kikuchi K.
Int J Oncol. 1998 Mar;12(3):603-7.
PMID 9472099
 
Protein phosphatase 1 delta is associated with focal adhesions.
Villa-Moruzzi E, Tognarini M, Cecchini G, Marchisio PC.
Cell Adhes Commun. 1998 Jun;5(4):297-305.
PMID 9762470
 
The second catalytic domain of protein tyrosine phosphatase delta (PTP delta) binds to and inhibits the first catalytic domain of PTP sigma.
Wallace MJ, Fladd C, Batt J, Rotin D.
Mol Cell Biol. 1998 May;18(5):2608-16.
PMID 9566880
 
Neuroendocrine dysplasia in mice lacking protein tyrosine phosphatase sigma.
Elchebly M, Wagner J, Kennedy TE, Lanctot C, Michaliszyn E, Itie A, Drouin J, Tremblay ML.
Nat Genet. 1999 Mar;21(3):330-3.
PMID 10080191
 
Neuronal defects and posterior pituitary hypoplasia in mice lacking the receptor tyrosine phosphatase PTPsigma.
Wallace MJ, Batt J, Fladd CA, Henderson JT, Skarnes W, Rotin D.v
Nat Genet. 1999 Mar;21(3):334-8.
PMID 10080192
 
Receptor tyrosine phosphatase-delta is a homophilic, neurite-promoting cell adhesion molecular for CNS neurons.
Wang J, Bixby JL.
Mol Cell Neurosci. 1999 Oct-Nov;14(4-5):370-84.
PMID 10588391
 
Impaired learning with enhanced hippocampal long-term potentiation in PTPdelta-deficient mice.
Uetani N, Kato K, Ogura H, Mizuno K, Kawano K, Mikoshiba K, Yakura H, Asano M, Iwakura Y.
EMBO J. 2000 Jun 15;19(12):2775-85.
PMID 10856223
 
Intra- and intermolecular interactions between intracellular domains of receptor protein-tyrosine phosphatases.
Blanchetot C, Tertoolen LG, Overvoorde J, den Hertog J.
J Biol Chem. 2002 Dec 6;277(49):47263-9. Epub 2002 Oct 9.
PMID 12376545
 
Protein tyrosine phosphatase sigma-deficient mice show aberrant cytoarchitecture and structural abnormalities in the central nervous system.
Meathrel K, Adamek T, Batt J, Rotin D, Doering LC.
J Neurosci Res. 2002 Oct 1;70(1):24-35.
PMID 12237861
 
MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta.
Woodings JA, Sharp SJ, Machesky LM.
Biochem J. 2003 Apr 15;371(Pt 2):463-71.
PMID 12570871
 
A survey of homozygous deletions in human cancer genomes.
Cox C, Bignell G, Greenman C, Stabenau A, Warren W, Stephens P, Davies H, Watt S, Teague J, Edkins S, Birney E, Easton DF, Wooster R, Futreal PA, Stratton MR.
Proc Natl Acad Sci U S A. 2005 Mar 22;102(12):4542-7. Epub 2005 Mar 10.
PMID 15761058
 
Receptor tyrosine phosphatase-dependent cytoskeletal remodeling by the hedgehog-responsive gene MIM/BEG4.
Gonzalez-Quevedo R, Shoffer M, Horng L, Oro AE.
J Cell Biol. 2005 Jan 31;168(3):453-63.
PMID 15684034
 
Identification of chromosome arm 9p as the most frequent target of homozygous deletions in lung cancer.
Sato M, Takahashi K, Nagayama K, Arai Y, Ito N, Okada M, Minna JD, Yokota J, Kohno T.
Genes Chromosomes Cancer. 2005 Dec;44(4):405-14.
PMID 16114034
 
Homozygous deletions and chromosome amplifications in human lung carcinomas revealed by single nucleotide polymorphism array analysis.
Zhao X, Weir BA, LaFramboise T, Lin M, Beroukhim R, Garraway L, Beheshti J, Lee JC, Naoki K, Richards WG, Sugarbaker D, Chen F, Rubin MA, Janne PA, Girard L, Minna J, Christiani D, Li C, Sellers WR, Meyerson M.
Cancer Res. 2005 Jul 1;65(13):5561-70.
PMID 15994928
 
Genome-wide review of transcriptional complexity in mouse protein kinases and phosphatases.
Forrest AR, Taylor DF, Crowe ML, Chalk AM, Waddell NJ, Kolle G, Faulkner GJ, Kodzius R, Katayama S, Wells C, Kai C, Kawai J, Carninci P, Hayashizaki Y, Grimmond SM.
Genome Biol. 2006;7(1):R5. Epub 2006 Jan 26.
PMID 16507138
 
The consensus coding sequences of human breast and colorectal cancers.
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE.
Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7.
PMID 16959974
 
High-resolution analysis of chromosomal breakpoints and genomic instability identifies PTPRD as a candidate tumor suppressor gene in neuroblastoma.
Stallings RL, Nair P, Maris JM, Catchpoole D, McDermott M, O'Meara A, Breatnach F.
Cancer Res. 2006 Apr 1;66(7):3673-80.
PMID 16585193
 
Mammalian motoneuron axon targeting requires receptor protein tyrosine phosphatases sigma and delta.
Uetani N, Chagnon MJ, Kennedy TE, Iwakura Y, Tremblay ML.
J Neurosci. 2006 May 31;26(22):5872-80.
PMID 16738228
 
Protein tyrosine-phosphatase expression profiling in gastric cancer tissues.
Wu CW, Kao HL, Li AF, Chi CW, Lin WC.
Cancer Lett. 2006 Oct 8;242(1):95-103. Epub 2005 Dec 7.
PMID 16338072
 
Homozygous deletion scanning of the lung cancer genome at a 100-kb resolution.
Nagayama K, Kohno T, Sato M, Arai Y, Minna JD, Yokota J.
Genes Chromosomes Cancer. 2007 Nov;46(11):1000-10.
PMID 17674361
 
Allelic imbalances and microdeletions affecting the PTPRD gene in cutaneous squamous cell carcinomas detected using single nucleotide polymorphism microarray analysis.
Purdie KJ, Lambert SR, Teh MT, Chaplin T, Molloy G, Raghavan M, Kelsell DP, Leigh IM, Harwood CA, Proby CM, Young BD.
Genes Chromosomes Cancer. 2007 Jul;46(7):661-9.
PMID 17420988
 
Genome-wide loss of heterozygosity and copy number analysis in melanoma using high-density single-nucleotide polymorphism arrays.
Stark M, Hayward N.
Cancer Res. 2007 Mar 15;67(6):2632-42.
PMID 17363583
 
Characterizing the cancer genome in lung adenocarcinoma.
Weir BA, Woo MS, Getz G, Perner S, Ding L, Beroukhim R, Lin WM, Province MA, Kraja A, Johnson LA, Shah K, Sato M, Thomas RK, Barletta JA, Borecki IB, Broderick S, Chang AC, Chiang DY, Chirieac LR, Cho J, Fujii Y, Gazdar AF, Giordano T, Greulich H, Hanna M, Johnson BE, Kris MG, Lash A, Lin L, Lindeman N, Mardis ER, McPherson JD, Minna JD, Morgan MB, Nadel M, Orringer MB, Osborne JR, Ozenberger B, Ramos AH, Robinson J, Roth JA, Rusch V, Sasaki H, Shepherd F, Sougnez C, Spitz MR, Tsao MS, Twomey D, Verhaak RG, Weinstock GM, Wheeler DA, Winckler W, Yoshizawa A, Yu S, Zakowski MF, Zhang Q, Beer DG, Wistuba II, Watson MA, Garraway LA, Ladanyi M, Travis WD, Pao W, Rubin MA, Gabriel SB, Gibbs RA, Varmus HE, Wilson RK, Lander ES, Meyerson M.
Nature. 2007 Dec 6;450(7171):893-8. Epub 2007 Nov 4.
PMID 17982442
 
Genome-wide association study of restless legs syndrome identifies common variants in three genomic regions.
Winkelmann J, Schormair B, Lichtner P, Ripke S, Xiong L, Jalilzadeh S, Fulda S, Putz B, Eckstein G, Hauk S, Trenkwalder C, Zimprich A, Stiasny-Kolster K, Oertel W, Bachmann CG, Paulus W, Peglau I, Eisensehr I, Montplaisir J, Turecki G, Rouleau G, Gieger C, Illig T, Wichmann HE, Holsboer F, Muller-Myhsok B, Meitinger T.
Nat Genet. 2007 Aug;39(8):1000-6. Epub 2007 Jul 18.
PMID 17637780
 
Somatic mutations affect key pathways in lung adenocarcinoma.
Ding L, Getz G, Wheeler DA, Mardis ER, McLellan MD, Cibulskis K, Sougnez C, Greulich H, Muzny DM, Morgan MB, Fulton L, Fulton RS, Zhang Q, Wendl MC, Lawrence MS, Larson DE, Chen K, Dooling DJ, Sabo A, Hawes AC, Shen H, Jhangiani SN, Lewis LR, Hall O, Zhu Y, Mathew T, Ren Y, Yao J, Scherer SE, Clerc K, Metcalf GA, Ng B, Milosavljevic A, Gonzalez-Garay ML, Osborne JR, Meyer R, Shi X, Tang Y, Koboldt DC, Lin L, Abbott R, Miner TL, Pohl C, Fewell G, Haipek C, Schmidt H, Dunford-Shore BH, Kraja A, Crosby SD, Sawyer CS, Vickery T, Sander S, Robinson J, Winckler W, Baldwin J, Chirieac LR, Dutt A, Fennell T, Hanna M, Johnson BE, Onofrio RC, Thomas RK, Tonon G, Weir BA, Zhao X, Ziaugra L, Zody MC, Giordano T, Orringer MB, Roth JA, Spitz MR, Wistuba II, Ozenberger B, Good PJ, Chang AC, Beer DG, Watson MA, Ladanyi M, Broderick S, Yoshizawa A, Travis WD, Pao W, Province MA, Weinstock GM, Varmus HE, Gabriel SB, Lander ES, Gibbs RA, Meyerson M, Wilson RK.
Nature. 2008 Oct 23;455(7216):1069-75.
PMID 18948947
 
Genomic changes in progression of low-grade gliomas.
Idbaih A, Carvalho Silva R, Criniere E, Marie Y, Carpentier C, Boisselier B, Taillibert S, Rousseau A, Mokhtari K, Ducray F, Thillet J, Sanson M, Hoang-Xuan K, Delattre JY.
J Neurooncol. 2008 Nov;90(2):133-40. Epub 2008 Jul 11.
PMID 18618226
 
Aberrant splicing of the PTPRD gene mimics microdeletions identified at this locus in neuroblastomas.
Nair P, De Preter K, Vandesompele J, Speleman F, Stallings RL.
Genes Chromosomes Cancer. 2008 Mar;47(3):197-202.
PMID 18050303
 
PTPRD (protein tyrosine phosphatase receptor type delta) is associated with restless legs syndrome.
Schormair B, Kemlink D, Roeske D, Eckstein G, Xiong L, Lichtner P, Ripke S, Trenkwalder C, Zimprich A, Stiasny-Kolster K, Oertel W, Bachmann CG, Paulus W, Hogl B, Frauscher B, Gschliesser V, Poewe W, Peglau I, Vodicka P, Vavrova J, Sonka K, Nevsimalova S, Montplaisir J, Turecki G, Rouleau G, Gieger C, Illig T, Wichmann HE, Holsboer F, Muller-Myhsok B, Meitinger T, Winkelmann J.
Nat Genet. 2008 Aug;40(8):946-8. Epub 2008 Jul 27.
PMID 18660810
 
The polymorphisms of protein-tyrosine phosphatase receptor-type delta gene and its association with pediatric asthma in the Taiwanese population.
Shyur SD, Wang JY, Lin CG, Hsiao YH, Liou YH, Wu YJ, Wu LS.
Eur J Hum Genet. 2008 Oct;16(10):1283-8. Epub 2008 Apr 16.
PMID 18414509
 
Screening of AMP-activated protein kinase alpha2 subunit interacting proteins by bacterial two-hybrid system.
Fu QY, Gao YQ.
Mol Biol Rep. 2009 Feb;36(2):337-44. Epub 2007 Nov 22.
PMID 18034317
 
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Contributor(s)

Written01-2009Laavanya Parthasarathi, Raymond L Stallings
Royal College of Surgeons in Ireland and Children's Research Centre, Our Lady's Children's Hospital, Crumlin, Dublin, Ireland

Citation

This paper should be referenced as such :
Parthasarathi, L ; Stallings, RL
PTPRD (protein tyrosine phosphatase, receptor type, D)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(12):968-971.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/PTPRDID41927ch9p23.html

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