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Q9H1D0

- TRPV6_HUMAN

UniProt

Q9H1D0 - TRPV6_HUMAN

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Protein

Transient receptor potential cation channel subfamily V member 6

Gene

TRPV6

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

Functioni

Calcium selective cation channel probably involved in Ca2+ uptake in various tissues, including Ca2+ reabsorption in intestine. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both, a rapid Ca2+-dependent and a slower Ca2+-calmodulin-dependent mechanism, the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg2+ in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating By similarity.By similarity

GO - Molecular functioni

  1. calcium channel activity Source: UniProtKB
  2. calmodulin binding Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane transport Source: Reactome
  2. calcium ion transport Source: UniProtKB
  3. ion transmembrane transport Source: Reactome
  4. regulation of calcium ion-dependent exocytosis Source: UniProtKB
  5. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.

Protein family/group databases

TCDBi1.A.4.2.11. the transient receptor potential ca(2+) channel (trp-cc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily V member 6
Short name:
TrpV6
Alternative name(s):
CaT-like
Short name:
CaT-L
Calcium transport protein 1
Short name:
CaT1
Epithelial calcium channel 2
Short name:
ECaC2
Gene namesi
Name:TRPV6
Synonyms:ECAC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:14006. TRPV6.

Subcellular locationi

Cell membrane By similarity; Multi-pass membrane protein By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: UniProtKB
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi542 – 5421D → A: Abolishes channel activity. 1 Publication
Mutagenesisi702 – 7021T → A: Abolishes phosphorylation by PKC/PRKCA, achieves faster channel inactivation and no effect on binding to calmodulin. 1 Publication

Organism-specific databases

PharmGKBiPA37832.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 725725Transient receptor potential cation channel subfamily V member 6PRO_0000215354Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611Phosphotyrosine; by SRCBy similarity
Glycosylationi358 – 3581N-linked (GlcNAc...)Sequence Analysis
Modified residuei702 – 7021Phosphothreonine; by PKC/PRKCA1 Publication

Post-translational modificationi

Glycosylated.By similarity
Phosphorylation at Tyr-161 by SRC leads to an increased calcium influx through the channel. Probably dephosphorylated at this site by PTPN1 By similarity. Phosphorylation by PRKCA at the calmodulin binding site delays channel inactivation.By similarity1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9H1D0.
PaxDbiQ9H1D0.
PRIDEiQ9H1D0.

PTM databases

PhosphoSiteiQ9H1D0.

Expressioni

Tissue specificityi

Expressed at high levels in the gastrointestinal tract, including esophagus, stomach, duodenum, jejunum, ileum and colon, and in pancreas, placenta, prostate and salivary gland. Expressed at moderate levels in liver, kidney and testis. Expressed in locally advanced prostate cancer, metastatic and androgen-insensitive prostatic lesions but not detected in healthy prostate tissue and benign prostatic hyperplasia.2 Publications

Gene expression databases

BgeeiQ9H1D0.
CleanExiHS_TRPV6.
ExpressionAtlasiQ9H1D0. baseline.
GenevestigatoriQ9H1D0.

Organism-specific databases

HPAiHPA062864.

Interactioni

Subunit structurei

Homotetramer and probably heterotetramer with TRPV5. Interacts with TRPV5. Interacts with S100A10 and probably with the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is required for the trafficking to the plasma membrane. Interacts with BSPRY By similarity. Interacts with calmodulin.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PTPN1P180316EBI-7198335,EBI-968788

Protein-protein interaction databases

BioGridi120683. 6 interactions.
IntActiQ9H1D0. 2 interactions.
MINTiMINT-1472896.
STRINGi9606.ENSP00000352358.

Structurei

3D structure databases

ProteinModelPortaliQ9H1D0.
SMRiQ9H1D0. Positions 44-612.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 328328CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini350 – 38738ExtracellularSequence AnalysisAdd
BLAST
Topological domaini409 – 41911CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini441 – 4488ExtracellularSequence Analysis
Topological domaini470 – 49223CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini578 – 725148CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei524 – 54421Pore-formingBy similarityAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei329 – 34921HelicalSequence AnalysisAdd
BLAST
Transmembranei388 – 40821HelicalSequence AnalysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence AnalysisAdd
BLAST
Transmembranei449 – 46921HelicalSequence AnalysisAdd
BLAST
Transmembranei493 – 51321HelicalSequence AnalysisAdd
BLAST
Transmembranei557 – 57721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati44 – 7431ANK 1Add
BLAST
Repeati78 – 10730ANK 2Add
BLAST
Repeati116 – 14530ANK 3Add
BLAST
Repeati162 – 19130ANK 4Add
BLAST
Repeati195 – 23743ANK 5Add
BLAST
Repeati239 – 26830ANK 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 10311Interaction with calmodulinBy similarityAdd
BLAST
Regioni598 – 6025Interaction with S100A10By similarity
Regioni691 – 71121Interaction with calmodulinAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi541 – 5455Selectivity filterBy similarity

Sequence similaritiesi

Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG278734.
GeneTreeiENSGT00550000074425.
HOVERGENiHBG061442.
InParanoidiQ9H1D0.
KOiK04975.
OMAiPRVTGLY.
OrthoDBiEOG70087C.
PhylomeDBiQ9H1D0.
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.
IPR008344. TRPV5/TRPV6.
IPR008345. TRPV6_channel.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01766. ECACCHANNEL1.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
TIGRFAMsiTIGR00870. trp. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9H1D0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLSLPKEKG LILCLWSKFC RWFQRRESWA QSRDEQNLLQ QKRIWESPLL
60 70 80 90 100
LAAKDNDVQA LNKLLKYEDC KVHQRGAMGE TALHIAALYD NLEAAMVLME
110 120 130 140 150
AAPELVFEPM TSELYEGQTA LHIAVVNQNM NLVRALLARR ASVSARATGT
160 170 180 190 200
AFRRSPCNLI YFGEHPLSFA ACVNSEEIVR LLIEHGADIR AQDSLGNTVL
210 220 230 240 250
HILILQPNKT FACQMYNLLL SYDRHGDHLQ PLDLVPNHQG LTPFKLAGVE
260 270 280 290 300
GNTVMFQHLM QKRKHTQWTY GPLTSTLYDL TEIDSSGDEQ SLLELIITTK
310 320 330 340 350
KREARQILDQ TPVKELVSLK WKRYGRPYFC MLGAIYLLYI ICFTMCCIYR
360 370 380 390 400
PLKPRTNNRT SPRDNTLLQQ KLLQEAYMTP KDDIRLVGEL VTVIGAIIIL
410 420 430 440 450
LVEVPDIFRM GVTRFFGQTI LGGPFHVLII TYAFMVLVTM VMRLISASGE
460 470 480 490 500
VVPMSFALVL GWCNVMYFAR GFQMLGPFTI MIQKMIFGDL MRFCWLMAVV
510 520 530 540 550
ILGFASAFYI IFQTEDPEEL GHFYDYPMAL FSTFELFLTI IDGPANYNVD
560 570 580 590 600
LPFMYSITYA AFAIIATLLM LNLLIAMMGD THWRVAHERD ELWRAQIVAT
610 620 630 640 650
TVMLERKLPR CLWPRSGICG REYGLGDRWF LRVEDRQDLN RQRIQRYAQA
660 670 680 690 700
FHTRGSEDLD KDSVEKLELG CPFSPHLSLP MPSVSRSTSR SSANWERLRQ
710 720
GTLRRDLRGI INRGLEDGES WEYQI
Length:725
Mass (Da):83,210
Last modified:June 1, 2002 - v2
Checksum:i3DA775E7D4E1CC65
GO
Isoform 2 (identifier: Q9H1D0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     25-192: Missing.

Show »
Length:557
Mass (Da):64,370
Checksum:i40C1A0C54EEC3D5A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371N → D in AAG41951. (PubMed:11097838)Curated
Sequence conflicti74 – 741Q → H in AAG41951. (PubMed:11097838)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571C → R.2 Publications
Corresponds to variant rs4987657 [ dbSNP | Ensembl ].
VAR_022251
Natural varianti359 – 3591R → Q.
Corresponds to variant rs4987665 [ dbSNP | Ensembl ].
VAR_052393
Natural varianti378 – 3781M → V.2 Publications
Corresponds to variant rs4987667 [ dbSNP | Ensembl ].
VAR_022252
Natural varianti681 – 6811M → T.2 Publications
Corresponds to variant rs4987682 [ dbSNP | Ensembl ].
VAR_022253

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei25 – 192168Missing in isoform 2. 1 PublicationVSP_013439Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF304463 mRNA. Translation: AAG41951.1.
AF365927 mRNA. Translation: AAL40230.1.
AF365928 mRNA. Translation: AAM00356.1.
AH010730 Genomic DNA. Translation: AAK50426.1.
AJ243500 mRNA. Translation: CAC20416.2.
AJ243501 mRNA. Translation: CAC20417.2.
AJ487964 mRNA. Translation: CAD32311.1.
AY225461 Genomic DNA. Translation: AAO38052.1.
AK291707 mRNA. Translation: BAF84396.1.
CH236959 Genomic DNA. Translation: EAL23776.1.
CCDSiCCDS5874.1. [Q9H1D0-1]
PIRiJC7531.
RefSeqiNP_061116.3. NM_018646.4.
UniGeneiHs.302740.

Genome annotation databases

EnsembliENST00000359396; ENSP00000352358; ENSG00000165125. [Q9H1D0-1]
GeneIDi55503.
KEGGihsa:55503.
UCSCiuc003wbw.1. human. [Q9H1D0-1]

Polymorphism databases

DMDMi62901469.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

TRPV6 entry

SeattleSNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF304463 mRNA. Translation: AAG41951.1 .
AF365927 mRNA. Translation: AAL40230.1 .
AF365928 mRNA. Translation: AAM00356.1 .
AH010730 Genomic DNA. Translation: AAK50426.1 .
AJ243500 mRNA. Translation: CAC20416.2 .
AJ243501 mRNA. Translation: CAC20417.2 .
AJ487964 mRNA. Translation: CAD32311.1 .
AY225461 Genomic DNA. Translation: AAO38052.1 .
AK291707 mRNA. Translation: BAF84396.1 .
CH236959 Genomic DNA. Translation: EAL23776.1 .
CCDSi CCDS5874.1. [Q9H1D0-1 ]
PIRi JC7531.
RefSeqi NP_061116.3. NM_018646.4.
UniGenei Hs.302740.

3D structure databases

ProteinModelPortali Q9H1D0.
SMRi Q9H1D0. Positions 44-612.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120683. 6 interactions.
IntActi Q9H1D0. 2 interactions.
MINTi MINT-1472896.
STRINGi 9606.ENSP00000352358.

Chemistry

ChEMBLi CHEMBL1628465.
GuidetoPHARMACOLOGYi 512.

Protein family/group databases

TCDBi 1.A.4.2.11. the transient receptor potential ca(2+) channel (trp-cc) family.

PTM databases

PhosphoSitei Q9H1D0.

Polymorphism databases

DMDMi 62901469.

Proteomic databases

MaxQBi Q9H1D0.
PaxDbi Q9H1D0.
PRIDEi Q9H1D0.

Protocols and materials databases

DNASUi 55503.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359396 ; ENSP00000352358 ; ENSG00000165125 . [Q9H1D0-1 ]
GeneIDi 55503.
KEGGi hsa:55503.
UCSCi uc003wbw.1. human. [Q9H1D0-1 ]

Organism-specific databases

CTDi 55503.
GeneCardsi GC07M142568.
H-InvDB HIX0007162.
HGNCi HGNC:14006. TRPV6.
HPAi HPA062864.
MIMi 606680. gene.
neXtProti NX_Q9H1D0.
PharmGKBi PA37832.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG278734.
GeneTreei ENSGT00550000074425.
HOVERGENi HBG061442.
InParanoidi Q9H1D0.
KOi K04975.
OMAi PRVTGLY.
OrthoDBi EOG70087C.
PhylomeDBi Q9H1D0.
TreeFami TF314711.

Enzyme and pathway databases

Reactomei REACT_169333. TRP channels.

Miscellaneous databases

GeneWikii TRPV6.
GenomeRNAii 55503.
NextBioi 59887.
PROi Q9H1D0.
SOURCEi Search...

Gene expression databases

Bgeei Q9H1D0.
CleanExi HS_TRPV6.
ExpressionAtlasi Q9H1D0. baseline.
Genevestigatori Q9H1D0.

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.
IPR008344. TRPV5/TRPV6.
IPR008345. TRPV6_channel.
[Graphical view ]
Pfami PF12796. Ank_2. 2 hits.
PF00520. Ion_trans. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
PR01765. ECACCHANNEL.
PR01766. ECACCHANNEL1.
SMARTi SM00248. ANK. 5 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
TIGRFAMsi TIGR00870. trp. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
  2. "1,25-dihydroxyvitamin D3 increases the expression of the CaT1 epithelial calcium channel in the Caco-2 human intestinal cell line."
    Wood R.J., Tchack L., Taparia S.
    BMC Physiol. 1:11-11(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Structural conservation of the genes encoding CaT1, CaT2, and related cation channels."
    Peng J.-B., Brown E.M., Hediger M.A.
    Genomics 76:99-109(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  4. "Expression of CaT-like, a novel calcium selective channel, correlates with the malignancy of prostate cancer."
    Wissenbach U., Niemeyer B.A., Fixemer T., Schneidewind A., Trost C., Cavalie A., Reus K., Meese E., Bonkhoff H., Flockerzi V.
    J. Biol. Chem. 276:19461-19468(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-157; VAL-378 AND THR-681, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Placenta.
  5. "A CaT1 splice variant lacking ankyrin repeats."
    Peng J.-B., Brown E.M., Hediger M.A.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. Kelsell R.E.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. SeattleSNPs variation discovery resource
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-157; VAL-378 AND THR-681.
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "Competitive regulation of CaT-like-mediated Ca2+ entry by protein kinase C and calmodulin."
    Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., Trost C.
    Proc. Natl. Acad. Sci. U.S.A. 98:3600-3605(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CALMODULIN, PHOSPHORYLATION AT THR-702, MUTAGENESIS OF THR-702.
  11. "Ca2+ dependence of the Ca2+-selective TRPV6 channel."
    Bodding M., Flockerzi V.
    J. Biol. Chem. 279:36546-36552(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-542.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiTRPV6_HUMAN
AccessioniPrimary (citable) accession number: Q9H1D0
Secondary accession number(s): A4D2I8
, Q8TDL3, Q8WXR8, Q96LC5, Q9H1D1, Q9H296
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2002
Last modified: October 29, 2014
This is version 129 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. SIMILARITY comments
    Index of protein domains and families

External Data

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