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Q9Y5S1

- TRPV2_HUMAN

UniProt

Q9Y5S1 - TRPV2_HUMAN

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Protein

Transient receptor potential cation channel subfamily V member 2

Gene

TRPV2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. calcium channel activity Source: UniProtKB-KW
  2. cation channel activity Source: MGI
  3. ion channel activity Source: ProtInc
  4. ion transmembrane transporter activity Source: ProtInc

GO - Biological processi

  1. calcium ion transmembrane transport Source: Reactome
  2. ion transmembrane transport Source: Reactome
  3. positive regulation of axon extension Source: Ensembl
  4. positive regulation of calcium ion import Source: Ensembl
  5. response to heat Source: Ensembl
  6. response to temperature stimulus Source: MGI
  7. sensory perception Source: ProtInc
  8. transmembrane transport Source: Reactome
  9. 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: Chromosome 17

Organism-specific databases

HGNCiHGNC:18082. TRPV2.

Subcellular locationi

Cell membrane By similarity; Multi-pass membrane protein By similarity. Cytoplasm By similarity. Melanosome 1 Publication
Note: Translocates from the cytoplasm to the plasma membrane upon ligand stimulation (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV.By similarity

GO - Cellular componenti

  1. axonal growth cone Source: Ensembl
  2. cell body Source: Ensembl
  3. cell surface Source: Ensembl
  4. cytoplasm Source: UniProtKB-KW
  5. endomembrane system Source: Ensembl
  6. growth cone membrane Source: Ensembl
  7. integral component of plasma membrane Source: ProtInc
  8. plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38292.

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.
GenevestigatoriQ9Y5S1.

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 – 849
Helixi88 – 914
Helixi94 – 1018
Helixi108 – 1103
Turni113 – 1153
Helixi119 – 1257
Helixi135 – 14511
Helixi151 – 1533
Turni159 – 1635
Helixi166 – 1727
Helixi176 – 1849
Helixi196 – 1983
Helixi212 – 2187
Helixi222 – 2309
Helixi248 – 2558
Helixi260 – 28021
Helixi286 – 2883
Helixi297 – 3037
Helixi307 – 3159

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Y5S1.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 390390CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini412 – 43423ExtracellularSequence AnalysisAdd
BLAST
Topological domaini456 – 47116CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini493 – 4931ExtracellularSequence Analysis
Topological domaini515 – 53723CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini643 – 764122CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei572 – 60938Pore-formingSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei391 – 41121HelicalSequence AnalysisAdd
BLAST
Transmembranei435 – 45521HelicalSequence AnalysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST
Transmembranei494 – 51421HelicalSequence AnalysisAdd
BLAST
Transmembranei538 – 55821HelicalSequence AnalysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati72 – 11443ANK 11 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati115 – 16147ANK 21 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati162 – 20746ANK 31 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati208 – 24336ANK 41 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati244 – 29249ANK 51 PublicationPROSITE-ProRule annotationAdd
BLAST
Repeati293 – 31927ANK 61 PublicationPROSITE-ProRule annotationAdd
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.
OMAiLSQVLCF.
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. 1 PublicationCurated
Sequence conflicti82 – 821A → V in AAD41724. 1 PublicationCurated
Sequence conflicti200 – 2001K → N in AAD41724. 1 PublicationCurated
Sequence conflicti459 – 4591V → L in AAD41724. 1 PublicationCurated
Sequence conflicti465 – 4662FI → YT in AAD41724. 1 PublicationCurated
Sequence conflicti477 – 4782QA → HS in AAD41724. 1 PublicationCurated
Sequence conflicti485 – 4851Q → L in AAD41724. 1 PublicationCurated
Sequence conflicti491 – 4911A → V in AAD41724. 1 PublicationCurated
Sequence conflicti535 – 5362LL → MV in AAD41724. 1 PublicationCurated
Sequence conflicti540 – 5401L → V in AAD41724. 1 PublicationCurated

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi62901477.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS32576.1.
RefSeqi NP_057197.2. NM_016113.4.
UniGenei Hs.279746.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F37 X-ray 1.70 A/B 69-319 [» ]
ProteinModelPortali Q9Y5S1.
SMRi Q9Y5S1. Positions 70-681.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119520. 1 interaction.
STRINGi 9606.ENSP00000342222.

Chemistry

ChEMBLi CHEMBL5051.
GuidetoPHARMACOLOGYi 508.

Protein family/group databases

TCDBi 1.A.4.2.8. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSitei Q9Y5S1.

Polymorphism databases

DMDMi 62901477.

Proteomic databases

MaxQBi Q9Y5S1.
PaxDbi Q9Y5S1.
PRIDEi Q9Y5S1.

Protocols and materials databases

DNASUi 51393.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338560 ; ENSP00000342222 ; ENSG00000187688 .
GeneIDi 51393.
KEGGi hsa:51393.
UCSCi uc002gpy.3. human.

Organism-specific databases

CTDi 51393.
GeneCardsi GC17P016318.
HGNCi HGNC:18082. TRPV2.
HPAi HPA044993.
MIMi 606676. gene.
neXtProti NX_Q9Y5S1.
PharmGKBi PA38292.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG281194.
GeneTreei ENSGT00550000074425.
HOGENOMi HOG000234630.
HOVERGENi HBG054085.
InParanoidi Q9Y5S1.
KOi K04971.
OMAi LSQVLCF.
OrthoDBi EOG7V49XW.
PhylomeDBi Q9Y5S1.
TreeFami TF314711.

Enzyme and pathway databases

Reactomei REACT_169333. TRP channels.

Miscellaneous databases

EvolutionaryTracei Q9Y5S1.
GeneWikii TRPV2.
GenomeRNAii 51393.
NextBioi 54925.
PROi Q9Y5S1.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5S1.
CleanExi HS_TRPV2.
ExpressionAtlasi Q9Y5S1. baseline and differential.
Genevestigatori Q9Y5S1.

Family and domain databases

Gene3Di 1.25.40.20. 2 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR005821. Ion_trans_dom.
IPR004729. TRP_channel.
IPR008347. TRPV1-4_channel.
IPR024865. TRPV2_channel.
[Graphical view ]
PANTHERi PTHR10582:SF5. PTHR10582:SF5. 1 hit.
Pfami PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR01768. TRPVRECEPTOR.
SMARTi SM00248. ANK. 4 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
TIGRFAMsi TIGR00870. trp. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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: October 29, 2014
This is version 129 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