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Protein

Transient receptor potential cation channel subfamily V member 2

Gene

TRPV2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB-KW
  • cation channel activity Source: MGI
  • ion channel activity Source: ProtInc
  • ion transmembrane transporter activity Source: ProtInc

GO - Biological processi

  • calcium ion transmembrane transport Source: Reactome
  • ion transmembrane transport Source: Reactome
  • positive regulation of axon extension Source: Ensembl
  • positive regulation of calcium ion import Source: Ensembl
  • response to heat Source: Ensembl
  • response to temperature stimulus Source: MGI
  • sensory perception Source: ProtInc
  • transmembrane transport Source: Reactome
  • transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Protein family/group databases

TCDBi1.A.4.2.8. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 2
Short name:
TrpV2
Alternative name(s):
Osm-9-like TRP channel 2
Short name:
OTRPC2
Vanilloid receptor-like protein 1
Short name:
VRL-1
Gene namesi
Name:TRPV2
Synonyms:VRL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:18082. TRPV2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 390390CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei391 – 41121HelicalSequence AnalysisAdd
BLAST
Topological domaini412 – 43423ExtracellularSequence AnalysisAdd
BLAST
Transmembranei435 – 45521HelicalSequence AnalysisAdd
BLAST
Topological domaini456 – 47116CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST
Topological domaini493 – 4931ExtracellularSequence Analysis
Transmembranei494 – 51421HelicalSequence AnalysisAdd
BLAST
Topological domaini515 – 53723CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei538 – 55821HelicalSequence AnalysisAdd
BLAST
Intramembranei572 – 60938Pore-formingSequence AnalysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence AnalysisAdd
BLAST
Topological domaini643 – 764122CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • axonal growth cone Source: Ensembl
  • cell body Source: Ensembl
  • cell surface Source: Ensembl
  • endomembrane system Source: Ensembl
  • growth cone membrane Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • melanosome Source: UniProtKB-SubCell
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38292.

Polymorphism and mutation databases

BioMutaiTRPV2.
DMDMi62901477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 764764Transient receptor potential cation channel subfamily V member 2PRO_0000215342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi570 – 5701N-linked (GlcNAc...)Sequence Analysis
Modified residuei763 – 7631PhosphoserineBy similarity

Post-translational modificationi

N-glycosylated.By similarity
Phosphorylated by PKA.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9Y5S1.
PaxDbiQ9Y5S1.
PRIDEiQ9Y5S1.

PTM databases

PhosphoSiteiQ9Y5S1.

Expressioni

Gene expression databases

BgeeiQ9Y5S1.
CleanExiHS_TRPV2.
ExpressionAtlasiQ9Y5S1. baseline and differential.
GenevisibleiQ9Y5S1. HS.

Organism-specific databases

HPAiHPA044993.

Interactioni

Subunit structurei

Homotetramer (Probable). 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 (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi119520. 1 interaction.
STRINGi9606.ENSP00000342222.

Structurei

Secondary structure

1
764
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi76 – 849Combined sources
Helixi88 – 914Combined sources
Helixi94 – 1018Combined sources
Helixi108 – 1103Combined sources
Turni113 – 1153Combined sources
Helixi119 – 1257Combined sources
Helixi135 – 14511Combined sources
Helixi151 – 1533Combined sources
Turni159 – 1635Combined sources
Helixi166 – 1727Combined sources
Helixi176 – 1849Combined sources
Helixi196 – 1983Combined sources
Helixi212 – 2187Combined sources
Helixi222 – 2309Combined sources
Helixi248 – 2558Combined sources
Helixi260 – 28021Combined sources
Helixi286 – 2883Combined sources
Helixi297 – 3037Combined sources
Helixi307 – 3159Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F37X-ray1.70A/B69-319[»]
ProteinModelPortaliQ9Y5S1.
SMRiQ9Y5S1. Positions 70-681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y5S1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 11443ANK 1PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati115 – 16147ANK 2PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati162 – 20746ANK 3PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati208 – 24336ANK 4PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati244 – 29249ANK 5PROSITE-ProRule annotation1 PublicationAdd
BLAST
Repeati293 – 31927ANK 6PROSITE-ProRule annotation1 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 388388Required for interaction with SLC50A1By similarityAdd
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG281194.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9Y5S1.
KOiK04971.
OMAiWDLLIPR.
OrthoDBiEOG7V49XW.
PhylomeDBiQ9Y5S1.
TreeFamiTF314711.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERiPTHR10582:SF5. PTHR10582:SF5. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5S1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSPSSSPVF RLETLDGGQE DGSEADRGKL DFGSGLPPME SQFQGEDRKF
60 70 80 90 100
APQIRVNLNY RKGTGASQPD PNRFDRDRLF NAVSRGVPED LAGLPEYLSK
110 120 130 140 150
TSKYLTDSEY TEGSTGKTCL MKAVLNLKDG VNACILPLLQ IDRDSGNPQP
160 170 180 190 200
LVNAQCTDDY YRGHSALHIA IEKRSLQCVK LLVENGANVH ARACGRFFQK
210 220 230 240 250
GQGTCFYFGE LPLSLAACTK QWDVVSYLLE NPHQPASLQA TDSQGNTVLH
260 270 280 290 300
ALVMISDNSA ENIALVTSMY DGLLQAGARL CPTVQLEDIR NLQDLTPLKL
310 320 330 340 350
AAKEGKIEIF RHILQREFSG LSHLSRKFTE WCYGPVRVSL YDLASVDSCE
360 370 380 390 400
ENSVLEIIAF HCKSPHRHRM VVLEPLNKLL QAKWDLLIPK FFLNFLCNLI
410 420 430 440 450
YMFIFTAVAY HQPTLKKQAA PHLKAEVGNS MLLTGHILIL LGGIYLLVGQ
460 470 480 490 500
LWYFWRRHVF IWISFIDSYF EILFLFQALL TVVSQVLCFL AIEWYLPLLV
510 520 530 540 550
SALVLGWLNL LYYTRGFQHT GIYSVMIQKV ILRDLLRFLL IYLVFLFGFA
560 570 580 590 600
VALVSLSQEA WRPEAPTGPN ATESVQPMEG QEDEGNGAQY RGILEASLEL
610 620 630 640 650
FKFTIGMGEL AFQEQLHFRG MVLLLLLAYV LLTYILLLNM LIALMSETVN
660 670 680 690 700
SVATDSWSIW KLQKAISVLE MENGYWWCRK KQRAGVMLTV GTKPDGSPDE
710 720 730 740 750
RWCFRVEEVN WASWEQTLPT LCEDPSGAGV PRTLENPVLA SPPKEDEDGA
760
SEENYVPVQL LQSN
Length:764
Mass (Da):85,981
Last modified:November 1, 1999 - v1
Checksum:iA73E3696E70F91E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521P → S in AAD41724 (Ref. 2) Curated
Sequence conflicti82 – 821A → V in AAD41724 (Ref. 2) Curated
Sequence conflicti200 – 2001K → N in AAD41724 (Ref. 2) Curated
Sequence conflicti459 – 4591V → L in AAD41724 (Ref. 2) Curated
Sequence conflicti465 – 4662FI → YT in AAD41724 (Ref. 2) Curated
Sequence conflicti477 – 4782QA → HS in AAD41724 (Ref. 2) Curated
Sequence conflicti485 – 4851Q → L in AAD41724 (Ref. 2) Curated
Sequence conflicti491 – 4911A → V in AAD41724 (Ref. 2) Curated
Sequence conflicti535 – 5362LL → MV in AAD41724 (Ref. 2) Curated
Sequence conflicti540 – 5401L → V in AAD41724 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171G → A.
Corresponds to variant rs3813768 [ dbSNP | Ensembl ].
VAR_024678
Natural varianti764 – 7641N → S.
Corresponds to variant rs8071215 [ dbSNP | Ensembl ].
VAR_059838

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129112 mRNA. Translation: AAD26363.1.
AF103906 mRNA. Translation: AAD41724.1.
AJ487963 mRNA. Translation: CAD32310.1.
AK289705 mRNA. Translation: BAF82394.1.
AC093484 Genomic DNA. No translation available.
CH471222 Genomic DNA. Translation: EAX04508.1.
BC018926 mRNA. Translation: AAH18926.1.
BC051305 mRNA. Translation: AAH51305.1.
CCDSiCCDS32576.1.
RefSeqiNP_057197.2. NM_016113.4.
UniGeneiHs.279746.

Genome annotation databases

EnsembliENST00000338560; ENSP00000342222; ENSG00000187688.
GeneIDi51393.
KEGGihsa:51393.
UCSCiuc002gpy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF129112 mRNA. Translation: AAD26363.1.
AF103906 mRNA. Translation: AAD41724.1.
AJ487963 mRNA. Translation: CAD32310.1.
AK289705 mRNA. Translation: BAF82394.1.
AC093484 Genomic DNA. No translation available.
CH471222 Genomic DNA. Translation: EAX04508.1.
BC018926 mRNA. Translation: AAH18926.1.
BC051305 mRNA. Translation: AAH51305.1.
CCDSiCCDS32576.1.
RefSeqiNP_057197.2. NM_016113.4.
UniGeneiHs.279746.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F37X-ray1.70A/B69-319[»]
ProteinModelPortaliQ9Y5S1.
SMRiQ9Y5S1. Positions 70-681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119520. 1 interaction.
STRINGi9606.ENSP00000342222.

Chemistry

ChEMBLiCHEMBL5051.
GuidetoPHARMACOLOGYi508.

Protein family/group databases

TCDBi1.A.4.2.8. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSiteiQ9Y5S1.

Polymorphism and mutation databases

BioMutaiTRPV2.
DMDMi62901477.

Proteomic databases

MaxQBiQ9Y5S1.
PaxDbiQ9Y5S1.
PRIDEiQ9Y5S1.

Protocols and materials databases

DNASUi51393.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338560; ENSP00000342222; ENSG00000187688.
GeneIDi51393.
KEGGihsa:51393.
UCSCiuc002gpy.3. human.

Organism-specific databases

CTDi51393.
GeneCardsiGC17P016318.
HGNCiHGNC:18082. TRPV2.
HPAiHPA044993.
MIMi606676. gene.
neXtProtiNX_Q9Y5S1.
PharmGKBiPA38292.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG281194.
GeneTreeiENSGT00550000074425.
HOGENOMiHOG000234630.
HOVERGENiHBG054085.
InParanoidiQ9Y5S1.
KOiK04971.
OMAiWDLLIPR.
OrthoDBiEOG7V49XW.
PhylomeDBiQ9Y5S1.
TreeFamiTF314711.

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Miscellaneous databases

EvolutionaryTraceiQ9Y5S1.
GeneWikiiTRPV2.
GenomeRNAii51393.
NextBioi54925.
PROiQ9Y5S1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5S1.
CleanExiHS_TRPV2.
ExpressionAtlasiQ9Y5S1. baseline and differential.
GenevisibleiQ9Y5S1. HS.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view]
PANTHERiPTHR10582:SF5. PTHR10582:SF5. 1 hit.
PfamiPF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01768. TRPVRECEPTOR.
SMARTiSM00248. ANK. 4 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A capsaicin-receptor homologue with a high threshold for noxious heat."
    Caterina M.J., Rosen T.A., Tominaga M., Brake A.J., Julius D.
    Nature 398:436-441(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Lymphoblast.
  2. "Cloning and functional expression of VRL, a vanilloid receptor-like gene."
    Garcia R.L., Delmas P., Cesare P., England S., Liapi A., Wood J.N.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lymphoblast.
  3. Kelsell R.E.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "Crystal structure of the human TRPV2 channel ankyrin repeat domain."
    McCleverty C.J., Koesema E., Patapoutian A., Lesley S.A., Kreusch A.
    Protein Sci. 15:2201-2206(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 69-319, ANK REPEATS.

Entry informationi

Entry nameiTRPV2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5S1
Secondary accession number(s): A6NML2, A8K0Z0, Q9Y670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.