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Q9UL62

- TRPC5_HUMAN

UniProt

Q9UL62 - TRPC5_HUMAN

Protein

Short transient receptor potential channel 5

Gene

TRPC5

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 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Has also been shown to be calcium-selective By similarity. May also be activated by intracellular calcium store depletion.By similarity1 Publication

    Enzyme regulationi

    Calcium channel activity is enhanced by MYLK, that promotes its subcellular localization at the plasma membrane.1 Publication

    GO - Molecular functioni

    1. calcium channel activity Source: UniProtKB
    2. inositol 1,4,5 trisphosphate binding Source: Ensembl
    3. protein binding Source: UniProtKB
    4. store-operated calcium channel activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. calcium ion transmembrane transport Source: Reactome
    3. calcium ion transport Source: ProtInc
    4. ion transmembrane transport Source: Reactome
    5. nervous system development Source: ProtInc
    6. transmembrane transport Source: Reactome

    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.
    REACT_22228. Role of second messengers in netrin-1 signaling.

    Protein family/group databases

    TCDBi1.A.4.1.7. the transient receptor potential ca(2+) channel (trp-cc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short transient receptor potential channel 5
    Short name:
    TrpC5
    Alternative name(s):
    Transient receptor protein 5
    Short name:
    TRP-5
    Short name:
    hTRP-5
    Short name:
    hTRP5
    Gene namesi
    Name:TRPC5
    Synonyms:TRP5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12337. TRPC5.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. calcium channel complex Source: UniProtKB
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37010.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 973973Short transient receptor potential channel 5PRO_0000215318Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ9UL62.
    PRIDEiQ9UL62.

    PTM databases

    PhosphoSiteiQ9UL62.

    Expressioni

    Tissue specificityi

    Expressed in brain with higher levels in fetal brain. Found in cerebellum and occipital pole.1 Publication

    Gene expression databases

    BgeeiQ9UL62.
    CleanExiHS_TRPC5.
    GenevestigatoriQ9UL62.

    Organism-specific databases

    HPAiHPA000510.

    Interactioni

    Subunit structurei

    Interacts with TRPC4AP By similarity. Homotetramer and heterotetramer with TRPC1 and/or TRPC4. Interacts with NHERF By similarity. Interacts with MX1 and RNF24. Interacts (via C-terminus) with CABP1. Interacts with SESTD1 (via the spectrin 1 repeat).By similarity5 Publications

    Protein-protein interaction databases

    BioGridi113075. 17 interactions.
    IntActiQ9UL62. 1 interaction.
    STRINGi9606.ENSP00000262839.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UL62.
    SMRiQ9UL62. Positions 35-170.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 330330CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini352 – 39847ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini420 – 43718CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini459 – 47012ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini492 – 51221CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini534 – 60370ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini625 – 973349CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei331 – 35121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei399 – 41921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei438 – 45821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei471 – 49121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei513 – 53321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei604 – 62421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati31 – 6030ANK 1Add
    BLAST
    Repeati69 – 9729ANK 2Add
    BLAST
    Repeati98 – 12427ANK 3Add
    BLAST
    Repeati141 – 17030ANK 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni971 – 9733Essential for binding to NHERF PDZ domainBy similarity

    Sequence similaritiesi

    Contains 4 ANK repeats.Curated

    Keywords - Domaini

    ANK repeat, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG254238.
    HOGENOMiHOG000020589.
    HOVERGENiHBG068337.
    InParanoidiQ9UL62.
    KOiK04968.
    OMAiPPLIRTM.
    OrthoDBiEOG72G17P.
    PhylomeDBiQ9UL62.
    TreeFamiTF313147.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR013555. TRP_dom.
    IPR005461. TRPC5_channel.
    IPR002153. TRPC_channel.
    [Graphical view]
    PANTHERiPTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF24. PTHR10117:SF24. 1 hit.
    PfamiPF00023. Ank. 1 hit.
    PF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF08344. TRP_2. 1 hit.
    [Graphical view]
    PRINTSiPR01097. TRNSRECEPTRP.
    PR01646. TRPCHANNEL5.
    SMARTiSM00248. ANK. 2 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9UL62-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQLYYKKVN YSPYRDRIPL QIVRAETELS AEEKAFLNAV EKGDYATVKQ    50
    ALQEAEIYYN VNINCMDPLG RSALLIAIEN ENLEIMELLL NHSVYVGDAL 100
    LYAIRKEVVG AVELLLSYRR PSGEKQVPTL MMDTQFSEFT PDITPIMLAA 150
    HTNNYEIIKL LVQKRVTIPR PHQIRCNCVE CVSSSEVDSL RHSRSRLNIY 200
    KALASPSLIA LSSEDPILTA FRLGWELKEL SKVENEFKAE YEELSQQCKL 250
    FAKDLLDQAR SSRELEIILN HRDDHSEELD PQKYHDLAKL KVAIKYHQKE 300
    FVAQPNCQQL LATLWYDGFP GWRRKHWVVK LLTCMTIGFL FPMLSIAYLI 350
    SPRSNLGLFI KKPFIKFICH TASYLTFLFM LLLASQHIVR TDLHVQGPPP 400
    TVVEWMILPW VLGFIWGEIK EMWDGGFTEY IHDWWNLMDF AMNSLYLATI 450
    SLKIVAYVKY NGSRPREEWE MWHPTLIAEA LFAISNILSS LRLISLFTAN 500
    SHLGPLQISL GRMLLDILKF LFIYCLVLLA FANGLNQLYF YYETRAIDEP 550
    NNCKGIRCEK QNNAFSTLFE TLQSLFWSVF GLLNLYVTNV KARHEFTEFV 600
    GATMFGTYNV ISLVVLLNML IAMMNNSYQL IADHADIEWK FARTKLWMSY 650
    FDEGGTLPPP FNIIPSPKSF LYLGNWFNNT FCPKRDPDGR RRRRNLRSFT 700
    ERNADSLIQN QHYQEVIRNL VKRYVAAMIR NSKTHEGLTE ENFKELKQDI 750
    SSFRYEVLDL LGNRKHPRSF STSSTELSQR DDNNDGSGGA RAKSKSVSFN 800
    LGCKKKTCHG PPLIRTMPRS SGAQGKSKAE SSSKRSFMGP SLKKLGLLFS 850
    KFNGHMSEPS SEPMYTISDG IVQQHCMWQD IRYSQMEKGK AEACSQSEIN 900
    LSEVELGEVQ GAAQSSECPL ACSSSLHCAS SICSSNSKLL DSSEDVFETW 950
    GEACDLLMHK WGDGQEEQVT TRL 973
    Length:973
    Mass (Da):111,412
    Last modified:May 1, 2000 - v1
    Checksum:iFBC8CBF17BE42166
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti667 – 6671P → T Found in a patient with severe delayed speech, autism spectrum and Gilles de la Tourette disorders. 1 Publication
    VAR_069415
    Natural varianti702 – 7021R → H.
    Corresponds to variant rs36047478 [ dbSNP | Ensembl ].
    VAR_052369

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF054568 mRNA. Translation: AAF00002.1.
    AC005191 Genomic DNA. Translation: AAC24563.1.
    AL049563, AC005191 Genomic DNA. Translation: CAI43017.1.
    CH471120 Genomic DNA. Translation: EAX02630.1.
    BC137271 mRNA. Translation: AAI37272.1.
    BC137274 mRNA. Translation: AAI37275.1.
    CCDSiCCDS14561.1.
    RefSeqiNP_036603.1. NM_012471.2.
    UniGeneiHs.657709.

    Genome annotation databases

    EnsembliENST00000262839; ENSP00000262839; ENSG00000072315.
    GeneIDi7224.
    KEGGihsa:7224.
    UCSCiuc004epl.1. human.

    Polymorphism databases

    DMDMi10720321.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF054568 mRNA. Translation: AAF00002.1 .
    AC005191 Genomic DNA. Translation: AAC24563.1 .
    AL049563 , AC005191 Genomic DNA. Translation: CAI43017.1 .
    CH471120 Genomic DNA. Translation: EAX02630.1 .
    BC137271 mRNA. Translation: AAI37272.1 .
    BC137274 mRNA. Translation: AAI37275.1 .
    CCDSi CCDS14561.1.
    RefSeqi NP_036603.1. NM_012471.2.
    UniGenei Hs.657709.

    3D structure databases

    ProteinModelPortali Q9UL62.
    SMRi Q9UL62. Positions 35-170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113075. 17 interactions.
    IntActi Q9UL62. 1 interaction.
    STRINGi 9606.ENSP00000262839.

    Chemistry

    ChEMBLi CHEMBL1250411.
    GuidetoPHARMACOLOGYi 490.

    Protein family/group databases

    TCDBi 1.A.4.1.7. the transient receptor potential ca(2+) channel (trp-cc) family.

    PTM databases

    PhosphoSitei Q9UL62.

    Polymorphism databases

    DMDMi 10720321.

    Proteomic databases

    PaxDbi Q9UL62.
    PRIDEi Q9UL62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262839 ; ENSP00000262839 ; ENSG00000072315 .
    GeneIDi 7224.
    KEGGi hsa:7224.
    UCSCi uc004epl.1. human.

    Organism-specific databases

    CTDi 7224.
    GeneCardsi GC0XM111017.
    HGNCi HGNC:12337. TRPC5.
    HPAi HPA000510.
    MIMi 300334. gene.
    neXtProti NX_Q9UL62.
    PharmGKBi PA37010.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254238.
    HOGENOMi HOG000020589.
    HOVERGENi HBG068337.
    InParanoidi Q9UL62.
    KOi K04968.
    OMAi PPLIRTM.
    OrthoDBi EOG72G17P.
    PhylomeDBi Q9UL62.
    TreeFami TF313147.

    Enzyme and pathway databases

    Reactomei REACT_169333. TRP channels.
    REACT_22228. Role of second messengers in netrin-1 signaling.

    Miscellaneous databases

    GeneWikii TRPC5.
    GenomeRNAii 7224.
    NextBioi 28291.
    PROi Q9UL62.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UL62.
    CleanExi HS_TRPC5.
    Genevestigatori Q9UL62.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR005821. Ion_trans_dom.
    IPR004729. TRP_channel.
    IPR013555. TRP_dom.
    IPR005461. TRPC5_channel.
    IPR002153. TRPC_channel.
    [Graphical view ]
    PANTHERi PTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF24. PTHR10117:SF24. 1 hit.
    Pfami PF00023. Ank. 1 hit.
    PF12796. Ank_2. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF08344. TRP_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01097. TRNSRECEPTRP.
    PR01646. TRPCHANNEL5.
    SMARTi SM00248. ANK. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    TIGRFAMsi TIGR00870. trp. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca(2+) entry channel."
      Sossey-Alaoui K., Lyon J.A., Jones L., Abidi F.E., Hartung A.J., Hane B., Schwartz C.E., Stevenson R.E., Srivastava A.K.
      Genomics 60:330-340(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain.
    5. "A novel capacitative calcium entry channel expressed in excitable cells."
      Philipp S., Hambrecht J., Braslavski L., Schroth G., Freichel M., Murakami M., Cavalie A., Flockerzi V.
      EMBO J. 17:4274-4282(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Subunit composition of mammalian transient receptor potential channels in living cells."
      Hofmann T., Schaefer M., Schultz G., Gudermann T.
      Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    7. "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC."
      Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., St-Hilaire M., Pinard M., Boulay G.
      J. Biol. Chem. 280:19393-19400(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MX1.
    8. "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus oocytes."
      Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.
      Pflugers Arch. 450:345-354(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CABP1.
    9. "Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells."
      Shimizu S., Yoshida T., Wakamori M., Ishii M., Okada T., Takahashi M., Seto M., Sakurada K., Kiuchi Y., Mori Y.
      J. Physiol. (Lond.) 570:219-235(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS CALCIUM CHANNEL, ENZYME REGULATION, SUBCELLULAR LOCATION.
    10. "RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC."
      Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.
      Cell Calcium 43:432-443(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF24.
    11. "The phospholipid-binding protein SESTD1 is a novel regulator of the transient receptor potential channels TRPC4 and TRPC5."
      Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H., Strubing C.
      J. Biol. Chem. 285:12426-12434(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SESTD1.
    12. Cited for: VARIANT THR-667.

    Entry informationi

    Entry nameiTRPC5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UL62
    Secondary accession number(s): B2RP53
    , O75233, Q5JXY8, Q9Y514
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 128 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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