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TRPV2 (transient receptor potential cation channel, subfamily V, member 2)

Written2012-03V'yacheslav Lehen'kyi, Natalia Prevarskaya
Inserm, U-1003, Universite des Sciences et Technologies de Lille (USTL), Villeneuve d'Ascq, France

(Note : for Links provided by Atlas : click)

Identity

Alias_namestransient receptor potential cation channel
Alias_symbol (synonym)VRL
VRL-1
VRL1
Other alias
HGNC (Hugo) TRPV2
LocusID (NCBI) 51393
Atlas_Id 45817
Location 17p11.2  [Link to chromosome band 17p11]
Location_base_pair Starts at 16318856 and ends at 16340317 bp from pter ( according to hg19-Feb_2009)  [Mapping TRPV2.png]
Local_order Colocolizes upstream with UBB (ubiquitin B) and FTLP12 (ferritin, light polypeptide pseudogene 12), and downstream with C17orf76-AS1 (C17orf76 antisense RNA 1) (non-protein coding).
 
  Schematic representation of human TRPV2 gene and neighbouring genes. UBB: ubiquitin B; FTLP12: ferritin, light polypeptide pseudogene 12; C17orf76-AS1: C17orf76 antisense RNA 1 non-protein coding.

DNA/RNA

 
  Genomic structure of human TRPV2 gene. The coding region is shown with red colour. The non-translated regions are shown with black colour.
Description TRPV2 gene consists of 15 exons and 14 introns spanning 1 to 21462 bp of DNA from 17p11.2 and includes a 5'-/3'- non-coding regions. The position of exons is: 1-292, 2021-2327, 4574-4707, 7058-7348, 7928-8226, 10558-10728, 11181-11336, 11908-12006, 12776-12846, 13276-13441, 16243-16309, 16425-16759, 18033-18157, 19349-19428, 21248-21462.
Transcription mRNA product length 2829 bp. No alternative splice variants have been found so far.

Protein

Note A transmembrane protein of vanilloid family, member 2, TRPV2 channel.
 
  The canonical form comprises 764 aa (MW ~86 kDa) and is composed of six transmembrane spanning domains and a pore forming region between transmembrane domains 5 and 6. The N-terminal and C-terminal tails are in cytoplasmatic side. Six N-terminal ankyrin (ANK) repeats are present in N-terminal tail.
Description It is a glycosylated membrane protein (764 aa, MW ~86 kDa) with 6 transmembrane regions and a pore-forming loop. N- and C-terminal tails are in cytoplasmic side. TRPV2 contains 6 ankyrin repeats may play a role in the interaction between subunits and is probably homotetramer. Interacts with a cAMP-dependent protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and ACBD3. Interacts with SLC50A1; the interaction probably occurs intracellularly and depends on TRPV2 N-glycosylation. This protein forms a non-selective cationic channel in the plasma membrane and is activated by temperatures higher than 52 degrees Celsius; and is not activated by vanilloids and acidic pH.
Expression TRPV2 channel is expressed in the advanced stages of prostate cancer. TRPV2 transcript levels are higher in patients with metastatic cancer (stage M1) compared with primary solid tumors (stages T2a and T2b). TRPV2 channel is expressed in PC3 and DU-145 cell lines derived from bone and brain metastasis, respectively (Monet et al., 2009; Monet et al., 2010). TRPV2 protein is expressed in human hepatoblastoma (HepG2) cells (Vriens et al., 2004). TRPV2 was found to be more expressed at both the mRNA and protein levels in cirrhotic livers compared with chronic hepatitis, whereas it also occurred in moderately and well-differentiated tumors compared with that of poorly differentiated tumors (Liu et al., 2010). In hepatocellular carcinoma the increased expression of TRPV2 was identified in 16/55 (29%) cases. The enhanced TRPV2 mRNA and protein expression was also found in high-grade and -stage urothelial carcinoma specimens and urothelial carcinoma cell lines. Both the full-length TRPV2 (hTRPV2) and a short splice-variant (s-TRPV2) were detected in normal human urothelial cells and normal bladder specimens, whereas a progressive decline of s-TRPV2 in pTa, pT1, and pT2 stages was observed, up to a complete loss in pT3 and pT4 urothelial carcinoma specimens (Caprodossi et al., 2008). TRPV2 mRNA was abundantly expressed in T24 cells as well (a poorly differentiated urothelial carcinoma cell line). TRPV2 is also expressed in the rat dorsal root ganglia and in F-11 cells, a hybridoma derived from rat dorsal root ganglia and mouse neuroblastoma (Yamada et al., 2010). TRPV2 is expressed in the human larynx, which may act as laryngeal nociceptors perceiving luminal noxious stimuli. TRPV2 mRNA and protein are expressed in benign astrocyte tissues, and its expression progressively declined in high-grade glioma tissues as histological grade increased (n = 49 cases), and in U87MG cells and in MZC, FCL and FSL primary glioma cells (Nabissi et al., 2010).
Localisation The biotinylation studies as well as calcium imaging experiments in some works suggest its expression on the plasma membrane (Monet et al., 2009; Monet et al., 2010). It translocates from the cytoplasm to the plasma membrane upon ligand stimulation.
Function TRPV2 is a calcium-permeable, non-selective cation channel with an outward rectification. Seems to be regulated, at least in part, by IGF-I, PDGF and neuropeptide head activator. May transduce physical stimuli in mast cells. Activated by temperatures higher than 52 degrees Celsius; is not activated by vanilloids and acidic pH.
Homology TRPV2 channel shares around 50% homology with TRPV1.

Mutations

Note An experimental mutation published in the C-Terminus. In this study the authors identified a calmodulin binding site on the C-termini of TRPV2 (654-683). The R679 and K681 single mutants of TRPV2 caused a 50% decrease in binding affinity and a double mutation of K661/K664 of the same peptide lowered the binding affinity by up to 75% (Holakovska et al., 2011).

Implicated in

Note
  
Entity Liver cancer
Disease TRPV2 protein is expressed in human hepatoblastoma (HepG2) cells and human hepatocellular carcinoma (Vriens et al., 2004).
Prognosis Quantitative RT-PCR and Western blotting analysis revealed that expression of TRPV2 at both the mRNA and protein levels were increased in cirrhotic livers compared with chronic hepatitis, whereas that also occurred in moderately and well-differentiated tumors compared with that of poorly differentiated tumors (Liu et al., 2010). Immunohistochemistry of the 55 human hepatocellular carcinoma samples showed that the expression of TRPV2 increased when going from normal liver or chronic hepatitis to cirrhosis. Increased TRPV2 expression was observed in tissues of liver cirrhosis (31/37, 83,8%). In HCC, increased expression of TRPV2 was identified in 16/55 (29%) cases. Clinicopathologic assessment suggested a significant association between TRPV2 expression and portal vein invasion and histopathologic differentiation (P = 0,036 and 0,001, respectively). The data suggest that TRPV2 plays a role in human hepatocarcinogenesis and might be a prognostic marker of patients with human hepatocellular carcinoma.
Oncogenesis Heat induces calcium entry into HepG2 cells.
  
  
Entity Bladder cancer
Disease TRPV2 channel is expressed in urothelial carcinoma and TRPV2 mRNA is abundantly expressed in T24 cells (a poorly differentiated urothelial carcinoma cell line) (Yamada et al., 2010).
Prognosis Enhanced TRPV2 mRNA and protein expression was found in high-grade and -stage UC specimens and UC cell lines. Both the full-length TRPV2 (hTRPV2) and a short splice-variant (s-TRPV2) were detected in NHUC and normal bladder specimens, whereas a progressive decline of s-TRPV2 in pTa, pT1, and pT2 stages was observed, up to a complete loss in pT3 and pT4 UC specimens (Caprodossi et al., 2008).
Oncogenesis The expression level in UC cells is correlated with high-grade disease. The administration of CBD increased intracellular calcium concentrations in T24 cells. In addition, the viability of T24 cells progressively decreases with increasing concentrations of CBD, whereas RT4 cells are mostly unaffected. Cell death occurs via apoptosis caused by continuous influx of calcium through TRPV2.
  
  
Entity Glia cancer
Disease TRPV2 channel is expressed in glioma cells: U87MG, MZC, FCL and FSL primary human glioma cells (Nabissi et al., 2010).
Prognosis The findings indicate that TRPV2 negatively controls glioma cell survival and proliferation.
Oncogenesis TRPV2 silencing increases U87MG cell proliferation as shown by the increased percentage of cells incorporating 5-bromo-2-deoxyuridine expressing beta(III)-tubulin and rescued glioma cells to Fas-induced apoptosis. In addition, transfection of TRPV2 in MZC glioma cells, by inducing Fas overexpression, resulted in a reduced viability and an increased spontaneous and Fas-induced apoptosis. These findings indicate that TRPV2 negatively controls glioma cell survival and proliferation, as well as resistance to Fas-induced apoptotic cell death in an ERK-dependent manner (Nabissi et al., 2010).
  
  
Entity Prostate cancer
Disease TRPV2 channel is expressed in the advanced stages of prostate cancer. TRPV2 transcript levels are higher in patients with metastatic cancer (stage M1) compared with primary solid tumors (stages T2a and T2b). TRPV2 channel is expressed in PC3 and DU-145 cell lines derived from bone and brain metastasis, respectively (Monet et al., 2009; Monet et al., 2010).
Prognosis TRPV2 channel indicated that it is primarily involved in cancer cell migration and not in cell growth. A role for TRPV2 in prostate cancer progression to the aggressive castration-resistant stage has been suggested, prompting evaluation of TRPV2 as a potential prognostic marker and therapeutic target in the setting of advanced prostate cancer.
Oncogenesis TRPV2 silencing decreases prostate cancer cell migration not affecting cell proliferation (Monet et al., 2009). Introducing TRPV2 into androgen-dependent LNCaP cells enhanced cell migration along with expression of invasion markers matrix metalloproteinase (MMP) 9 and cathepsin B. Small interfering RNA-mediated silencing of TRPV2 reduced the growth and invasive properties of PC3 prostate tumors established in nude mice xenografts, and diminished expression of invasive enzymes MMP2, MMP9, and cathepsin B (Monet et al., 2010).
  
  
Entity Muscular dystrophy
Note Mechanisms: TRPV2 is a principal Ca(2+)-entry route leading to a sustained [Ca(2+)](i) increase and muscle degeneration (Zanou et al., 2009).
Disease When transgenic mice expressing a TRPV2 mutant in muscle are crossed with mdx mice, the [Ca(2+)](i) increase in muscle fibers is reduced by dominant-negative inhibition of endogenous TRPV2 (Iwata et al., 2009).
Prognosis It was suggested a promising therapeutic target for the treatment of muscular dystrophy.
  
  
Entity Duchenne myopathy
Note Mechanisms: a role of TRPV2 channel in the physiopathology of Duchenne muscular dystrophy has been suggested cause muscles from dystrophin-deficient mice typically present an exaggerated susceptibility to eccentric work characterized by an important force drop and an increased membrane permeability consecutive to repeated lengthening contractions (Zanou et al., 2009).
Disease Duchenne myopathy is a lethal disease due to the absence of dystrophin, a cytoskeletal protein (Zanou et al., 2009).
Prognosis Muscles from dystrophin-deficient mice are largely protected from eccentric work-induced damage by overexpressing a dominant negative mutant of TRPV2 ion channel.
  
  
Entity Norrbottnian congenital insensitivity to pain
Note Mechanisms: a dramatic loss of such nerve fibers was seen in skin from individuals with Norrbottnian congenital insensitivity to pain, further suggesting that these ion channels are expressed primarily on nociceptive primary sensory neurons in human skin (Axelsson et al., 2009).
Disease Nerve fibers immunoreactive for TRPV2 are absent or substantially reduced in number in individuals with Norrbottnian congenital insensitivity to pain, an autosomal disease selectively affecting the development of C-fiber and Adelta-fiber primary afferents (Axelsson et al., 2009).
Prognosis Nerve fibers in human skin express TRPV2 that co-localizes with the sensory neuropeptides CGRP and SP, but not with NF200, VIP or TH.
  
  
Entity Hyperalgesia
Note Mechanisms: upregulation of TRPV2 may play important roles in the mechanical hyperalgesia induced by cisplatin (Hori et al., 2010).
Disease TRPV2 is expressed in sensory neurons and affects mechanical and thermal hyperalgesia examined in a rat model of cisplatin-induced peripheral neuropathy (Kasama et al., 2007).
  

To be noted

TRPV2 knockout mice have been generated. Behavioral and electrophysiological responses to heat and mechanical stimuli were examined TRPV2 knock-out mice (Park et al., 2011). TRPV2 knock-out mice showed reduced embryonic weight and perinatal viability. TRPV2 knock-out mice showed normal behavioral responses to noxious heat over a broad range of temperatures and normal responses to punctate mechanical stimuli, both in the basal state and under hyperalgesic conditions such as peripheral inflammation and L5 spinal nerve ligation. Electrophysiological recordings from skin afferents showed that C-fiber responses to heat and C- and Aδ-fiber responses to noxious mechanical stimuli were unimpaired in the absence of TRPV2. The prevalence of thermosensitive Aδ-fibers was too low to permit comparison between genotypes. Thus, TRPV2 is important for perinatal viability but is not essential for heat or mechanical nociception or hypersensitivity in the adult mouse (Park et al., 2011).

Bibliography

Transient receptor potential vanilloid 1, vanilloid 2 and melastatin 8 immunoreactive nerve fibers in human skin from individuals with and without Norrbottnian congenital insensitivity to pain.
Axelsson HE, Minde JK, Sonesson A, Toolanen G, Hogestatt ED, Zygmunt PM.
Neuroscience. 2009 Sep 15;162(4):1322-32. Epub 2009 May 29.
PMID 19482060
 
Transient receptor potential vanilloid type 2 (TRPV2) expression in normal urothelium and in urothelial carcinoma of human bladder: correlation with the pathologic stage.
Caprodossi S, Lucciarini R, Amantini C, Nabissi M, Canesin G, Ballarini P, Di Spilimbergo A, Cardarelli MA, Servi L, Mammana G, Santoni G.
Eur Urol. 2008 Sep;54(3):612-20. Epub 2007 Oct 16.
PMID 17977643
 
Characterization of calmodulin binding domains in TRPV2 and TRPV5 C-tails.
Holakovska B, Grycova L, Bily J, Teisinger J.
Amino Acids. 2011 Feb;40(2):741-8. Epub 2010 Aug 5.
PMID 20686800
 
Upregulations of P2X(3) and ASIC3 involve in hyperalgesia induced by cisplatin administration in rats.
Hori K, Ozaki N, Suzuki S, Sugiura Y.
Pain. 2010 May;149(2):393-405. Epub 2010 Apr 8.
PMID 20378247
 
Dominant-negative inhibition of Ca2+ influx via TRPV2 ameliorates muscular dystrophy in animal models.
Iwata Y, Katanosaka Y, Arai Y, Shigekawa M, Wakabayashi S.
Hum Mol Genet. 2009 Mar 1;18(5):824-34. Epub 2008 Dec 2.
PMID 19050039
 
RNA interference-mediated knock-down of transient receptor potential vanilloid 1 prevents forepaw inflammatory hyperalgesia in rat.
Kasama S, Kawakubo M, Suzuki T, Nishizawa T, Ishida A, Nakayama J.
Eur J Neurosci. 2007 May;25(10):2956-63. Epub 2007 May 17.
PMID 17509082
 
Clinical significance of transient receptor potential vanilloid 2 expression in human hepatocellular carcinoma.
Liu G, Xie C, Sun F, Xu X, Yang Y, Zhang T, Deng Y, Wang D, Huang Z, Yang L, Huang S, Wang Q, Liu G, Zhong D, Miao X.
Cancer Genet Cytogenet. 2010 Feb;197(1):54-9.
PMID 20113837
 
Lysophospholipids stimulate prostate cancer cell migration via TRPV2 channel activation.
Monet M, Gkika D, Lehen'kyi V, Pourtier A, Vanden Abeele F, Bidaux G, Juvin V, Rassendren F, Humez S, Prevarsakaya N.
Biochim Biophys Acta. 2009 Mar;1793(3):528-39. Epub 2009 Jan 15.
PMID 19321128
 
Role of cationic channel TRPV2 in promoting prostate cancer migration and progression to androgen resistance.
Monet M, Lehen'kyi V, Gackiere F, Firlej V, Vandenberghe M, Roudbaraki M, Gkika D, Pourtier A, Bidaux G, Slomianny C, Delcourt P, Rassendren F, Bergerat JP, Ceraline J, Cabon F, Humez S, Prevarskaya N.
Cancer Res. 2010 Feb 1;70(3):1225-35. Epub 2010 Jan 26.
PMID 20103638
 
TRPV2 channel negatively controls glioma cell proliferation and resistance to Fas-induced apoptosis in ERK-dependent manner.
Nabissi M, Morelli MB, Amantini C, Farfariello V, Ricci-Vitiani L, Caprodossi S, Arcella A, Santoni M, Giangaspero F, De Maria R, Santoni G.
Carcinogenesis. 2010 May;31(5):794-803. Epub 2010 Jan 21.
PMID 20093382
 
TRP vanilloid 2 knock-out mice are susceptible to perinatal lethality but display normal thermal and mechanical nociception.
Park U, Vastani N, Guan Y, Raja SN, Koltzenburg M, Caterina MJ.
J Neurosci. 2011 Aug 10;31(32):11425-36.
PMID 21832173
 
TRPV channels and modulation by hepatocyte growth factor/scatter factor in human hepatoblastoma (HepG2) cells.
Vriens J, Janssens A, Prenen J, Nilius B, Wondergem R.
Cell Calcium. 2004 Jul;36(1):19-28.
PMID 15126053
 
TRPV2 activation induces apoptotic cell death in human T24 bladder cancer cells: a potential therapeutic target for bladder cancer.
Yamada T, Ueda T, Shibata Y, Ikegami Y, Saito M, Ishida Y, Ugawa S, Kohri K, Shimada S.
Urology. 2010 Aug;76(2):509.e1-7. Epub 2010 May 23.
PMID 20546877
 
Essential role of TRPV2 ion channel in the sensitivity of dystrophic muscle to eccentric contractions.
Zanou N, Iwata Y, Schakman O, Lebacq J, Wakabayashi S, Gailly P.
FEBS Lett. 2009 Nov 19;583(22):3600-4. Epub 2009 Oct 17.
PMID 19840792
 

Citation

This paper should be referenced as such :
Lehen'kyi, V ; Prevarskaya, N
TRPV2 (transient receptor potential cation channel, subfamily V, member 2)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(8):563-567.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/TRPV2ID45817ch17p11.html


External links

Nomenclature
HGNC (Hugo)TRPV2   18082
Cards
AtlasTRPV2ID45817ch17p11
Entrez_Gene (NCBI)TRPV2  51393  transient receptor potential cation channel subfamily V member 2
AliasesVRL; VRL-1; VRL1
GeneCards (Weizmann)TRPV2
Ensembl hg19 (Hinxton)ENSG00000187688 [Gene_View]  chr17:16318856-16340317 [Contig_View]  TRPV2 [Vega]
Ensembl hg38 (Hinxton)ENSG00000187688 [Gene_View]  chr17:16318856-16340317 [Contig_View]  TRPV2 [Vega]
ICGC DataPortalENSG00000187688
TCGA cBioPortalTRPV2
AceView (NCBI)TRPV2
Genatlas (Paris)TRPV2
WikiGenes51393
SOURCE (Princeton)TRPV2
Genetics Home Reference (NIH)TRPV2
Genomic and cartography
GoldenPath hg19 (UCSC)TRPV2  -     chr17:16318856-16340317 +  17p11.2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)TRPV2  -     17p11.2   [Description]    (hg38-Dec_2013)
EnsemblTRPV2 - 17p11.2 [CytoView hg19]  TRPV2 - 17p11.2 [CytoView hg38]
Mapping of homologs : NCBITRPV2 [Mapview hg19]  TRPV2 [Mapview hg38]
OMIM606676   
Gene and transcription
Genbank (Entrez)AF103906 AF129112 AJ487963 AK001896 AK289705
RefSeq transcript (Entrez)NM_016113
RefSeq genomic (Entrez)NC_000017 NC_018928 NT_010718 NW_004929405
Consensus coding sequences : CCDS (NCBI)TRPV2
Cluster EST : UnigeneHs.279746 [ NCBI ]
CGAP (NCI)Hs.279746
Alternative Splicing GalleryENSG00000187688
Gene ExpressionTRPV2 [ NCBI-GEO ]   TRPV2 [ EBI - ARRAY_EXPRESS ]   TRPV2 [ SEEK ]   TRPV2 [ MEM ]
Gene Expression Viewer (FireBrowse)TRPV2 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)51393
GTEX Portal (Tissue expression)TRPV2
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9Y5S1   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9Y5S1  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9Y5S1
Splice isoforms : SwissVarQ9Y5S1
PhosPhoSitePlusQ9Y5S1
Domaine pattern : Prosite (Expaxy)ANK_REP_REGION (PS50297)    ANK_REPEAT (PS50088)   
Domains : Interpro (EBI)Ankyrin_rpt    Ankyrin_rpt-contain_dom    Ion_trans_dom    TRP_channel    TRPV1-4_channel    TRPV2_channel   
Domain families : Pfam (Sanger)Ank_2 (PF12796)    Ion_trans (PF00520)   
Domain families : Pfam (NCBI)pfam12796    pfam00520   
Domain families : Smart (EMBL)ANK (SM00248)  
Conserved Domain (NCBI)TRPV2
DMDM Disease mutations51393
Blocks (Seattle)TRPV2
PDB (SRS)2F37   
PDB (PDBSum)2F37   
PDB (IMB)2F37   
PDB (RSDB)2F37   
Structural Biology KnowledgeBase2F37   
SCOP (Structural Classification of Proteins)2F37   
CATH (Classification of proteins structures)2F37   
SuperfamilyQ9Y5S1
Human Protein AtlasENSG00000187688
Peptide AtlasQ9Y5S1
HPRD05980
IPIIPI00183666   IPI00796962   
Protein Interaction databases
DIP (DOE-UCLA)Q9Y5S1
IntAct (EBI)Q9Y5S1
FunCoupENSG00000187688
BioGRIDTRPV2
STRING (EMBL)TRPV2
ZODIACTRPV2
Ontologies - Pathways
QuickGOQ9Y5S1
Ontology : AmiGOion channel activity  cation channel activity  calcium channel activity  plasma membrane  plasma membrane  integral component of plasma membrane  transport  sensory perception  negative regulation of cell proliferation  response to temperature stimulus  response to heat  cell surface  ion transmembrane transporter activity  lamellipodium  growth cone membrane  melanosome  axonal growth cone  cell body  positive regulation of axon extension  calcium ion transmembrane transport  positive regulation of calcium ion import  
Ontology : EGO-EBIion channel activity  cation channel activity  calcium channel activity  plasma membrane  plasma membrane  integral component of plasma membrane  transport  sensory perception  negative regulation of cell proliferation  response to temperature stimulus  response to heat  cell surface  ion transmembrane transporter activity  lamellipodium  growth cone membrane  melanosome  axonal growth cone  cell body  positive regulation of axon extension  calcium ion transmembrane transport  positive regulation of calcium ion import  
REACTOMEQ9Y5S1 [protein]
REACTOME Pathways3295583 [pathway]   
NDEx NetworkTRPV2
Atlas of Cancer Signalling NetworkTRPV2
Wikipedia pathwaysTRPV2
Orthology - Evolution
OrthoDB51393
GeneTree (enSembl)ENSG00000187688
Phylogenetic Trees/Animal Genes : TreeFamTRPV2
HOVERGENQ9Y5S1
HOGENOMQ9Y5S1
Homologs : HomoloGeneTRPV2
Homology/Alignments : Family Browser (UCSC)TRPV2
Gene fusions - Rearrangements
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTRPV2 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TRPV2
dbVarTRPV2
ClinVarTRPV2
1000_GenomesTRPV2 
Exome Variant ServerTRPV2
ExAC (Exome Aggregation Consortium)TRPV2 (select the gene name)
Genetic variants : HAPMAP51393
Genomic Variants (DGV)TRPV2 [DGVbeta]
DECIPHER (Syndromes)17:16318856-16340317  ENSG00000187688
CONAN: Copy Number AnalysisTRPV2 
Mutations
ICGC Data PortalTRPV2 
TCGA Data PortalTRPV2 
Broad Tumor PortalTRPV2
OASIS PortalTRPV2 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTRPV2  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDTRPV2
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch TRPV2
DgiDB (Drug Gene Interaction Database)TRPV2
DoCM (Curated mutations)TRPV2 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)TRPV2 (select a term)
intoGenTRPV2
NCG5 (London)TRPV2
Cancer3DTRPV2(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM606676   
Orphanet
MedgenTRPV2
Genetic Testing Registry TRPV2
NextProtQ9Y5S1 [Medical]
TSGene51393
GENETestsTRPV2
Huge Navigator TRPV2 [HugePedia]
snp3D : Map Gene to Disease51393
BioCentury BCIQTRPV2
ClinGenTRPV2
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD51393
Chemical/Pharm GKB GenePA38292
Clinical trialTRPV2
Miscellaneous
canSAR (ICR)TRPV2 (select the gene name)
Probes
Litterature
PubMed47 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineTRPV2
EVEXTRPV2
GoPubMedTRPV2
iHOPTRPV2
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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