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Q9H1D0

- TRPV6_HUMAN

UniProt

Q9H1D0 - TRPV6_HUMAN

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
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (01 Jun 2002)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    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

    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

    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

    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

    ArrayExpressiQ9H1D0.
    BgeeiQ9H1D0.
    CleanExiHS_TRPV6.
    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 44-613.
    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.
    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

    MGLSLPKEKG LILCLWSKFC RWFQRRESWA QSRDEQNLLQ QKRIWESPLL    50
    LAAKDNDVQA LNKLLKYEDC KVHQRGAMGE TALHIAALYD NLEAAMVLME 100
    AAPELVFEPM TSELYEGQTA LHIAVVNQNM NLVRALLARR ASVSARATGT 150
    AFRRSPCNLI YFGEHPLSFA ACVNSEEIVR LLIEHGADIR AQDSLGNTVL 200
    HILILQPNKT FACQMYNLLL SYDRHGDHLQ PLDLVPNHQG LTPFKLAGVE 250
    GNTVMFQHLM QKRKHTQWTY GPLTSTLYDL TEIDSSGDEQ SLLELIITTK 300
    KREARQILDQ TPVKELVSLK WKRYGRPYFC MLGAIYLLYI ICFTMCCIYR 350
    PLKPRTNNRT SPRDNTLLQQ KLLQEAYMTP KDDIRLVGEL VTVIGAIIIL 400
    LVEVPDIFRM GVTRFFGQTI LGGPFHVLII TYAFMVLVTM VMRLISASGE 450
    VVPMSFALVL GWCNVMYFAR GFQMLGPFTI MIQKMIFGDL MRFCWLMAVV 500
    ILGFASAFYI IFQTEDPEEL GHFYDYPMAL FSTFELFLTI IDGPANYNVD 550
    LPFMYSITYA AFAIIATLLM LNLLIAMMGD THWRVAHERD ELWRAQIVAT 600
    TVMLERKLPR CLWPRSGICG REYGLGDRWF LRVEDRQDLN RQRIQRYAQA 650
    FHTRGSEDLD KDSVEKLELG CPFSPHLSLP MPSVSRSTSR SSANWERLRQ 700
    GTLRRDLRGI INRGLEDGES WEYQI 725
    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 44-613.
    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

    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.
    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

    ArrayExpressi Q9H1D0.
    Bgeei Q9H1D0.
    CleanExi HS_TRPV6.
    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

    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 1, 2014
    This is version 128 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

    Dasty 3