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Q9UBN4

- TRPC4_HUMAN

UniProt

Q9UBN4 - TRPC4_HUMAN

Protein

Short transient receptor potential channel 4

Gene

TRPC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Form a receptor-activated non-selective calcium permeant cation channel. Acts as a cell-cell contact-dependent endothelial calcium entry channel. Probably operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Mediates cation entry, with an enhanced permeability to barium over calcium. May also be activated by intracellular calcium store depletion.2 Publications

    GO - Molecular functioni

    1. beta-catenin binding Source: BHF-UCL
    2. cadherin binding Source: BHF-UCL
    3. inositol 1,4,5 trisphosphate binding Source: Ensembl
    4. protein binding Source: UniProtKB
    5. store-operated calcium channel activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. calcium ion import Source: BHF-UCL
    3. calcium ion transmembrane transport Source: Reactome
    4. calcium ion transport Source: ProtInc
    5. gamma-aminobutyric acid secretion Source: Ensembl
    6. ion transmembrane transport Source: Reactome
    7. 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.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Short transient receptor potential channel 4
    Short name:
    TrpC4
    Alternative name(s):
    Trp-related protein 4
    Short name:
    hTrp-4
    Short name:
    hTrp4
    Gene namesi
    Name:TRPC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:12336. TRPC4.

    Subcellular locationi

    Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein
    Note: Enhanced insertion into the cell membrane after activation of the EGF receptor.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: BHF-UCL
    2. calcium channel complex Source: UniProtKB
    3. caveola Source: Ensembl
    4. cell surface Source: BHF-UCL
    5. cortical cytoskeleton Source: UniProtKB
    6. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi959 – 9591Y → F: Reduced EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF. Loss of EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF; when associated with F-972. 2 Publications
    Mutagenesisi972 – 9721Y → F: Reduced EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF. Loss of EGF-induced phosphorylation and decreased association with SLC9A3R1/NHERF; when associated with F-959. 2 Publications
    Mutagenesisi975 – 9773Missing: Loss of interaction with SLC9A3R1/NHERF. 1 Publication

    Organism-specific databases

    PharmGKBiPA37009.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 977977Short transient receptor potential channel 4PRO_0000215314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei959 – 9591Phosphotyrosine; by FYN1 Publication
    Modified residuei972 – 9721Phosphotyrosine; by FYN1 Publication

    Post-translational modificationi

    Phosphorylation modulates TRPC channel function by regulating the level of TRPC4 at the cell surface and by increasing the association with SLC9A3R1/NHERF.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9UBN4.
    PRIDEiQ9UBN4.

    PTM databases

    PhosphoSiteiQ9UBN4.

    Expressioni

    Tissue specificityi

    Strongly expressed in placenta. Expressed at lower levels in heart, pancreas, kidney and brain. Expressed in endothelial cells. Isoform alpha was found to be the predominant isoform. Isoform beta was not found in pancreas and brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBN4.
    BgeeiQ9UBN4.
    CleanExiHS_TRPC4.
    GenevestigatoriQ9UBN4.

    Interactioni

    Subunit structurei

    Interacts with TRPC4AP By similarity. Homotetramer and heterotetramer with TRPC1 and/or TRPC5. Isoform alpha but not isoform beta associates with inositol 1,4,5-trisphosphate receptor (ITPR). Interacts with (via PDZ-binding domain) with SLC9A3R1/NHERF. Interacts with MX1 and RNF24. Interacts (via CIRB domain) with SESTD1 (via spectrin 1 repeat). Interacts with CDH5 and CTNNB1. Interacts with SPTAN1 (via C-terminal spectrin repeats) and SPTBN5 (via C-terminus). Interacts (via protein 4.1-binding domain) with EPB41L2.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MX1P205912EBI-929504,EBI-929476

    Protein-protein interaction databases

    BioGridi113074. 13 interactions.
    IntActiQ9UBN4. 2 interactions.
    MINTiMINT-157838.
    STRINGi9606.ENSP00000369003.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBN4.
    SMRiQ9UBN4. Positions 35-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 329329CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini351 – 36212ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini384 – 43653CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini458 – 46912ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini491 – 51121CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini533 – 59967ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini621 – 977357CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei330 – 35021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei363 – 38321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei437 – 45721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei470 – 49021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei512 – 53221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei600 – 62021HelicalSequence 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
    Regioni87 – 17286Multimerization domainBy similarityAdd
    BLAST
    Regioni254 – 30451Multimerization domainBy similarityAdd
    BLAST
    Regioni615 – 977363Binds to ITPR1, ITPR2 and ITPR3Add
    BLAST
    Regioni975 – 9773PDZ-binding domain

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili223 – 26038Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi377 – 3826Poly-Leu

    Domaini

    The protein 4.1-binding domain (654-685) is required for binding to EPB41L2 and channel activation.
    The calmodulin- and inositol 1,4,5-trisphosphate receptor-binding (CIRB) domain (695-724) is sufficient for the interaction with SESTD1.
    The spectrin-binding domain (730-758) is required for binding to SPTAN1 and SPTBN5.

    Sequence similaritiesi

    Contains 4 ANK repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Coiled coil, Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG254238.
    HOVERGENiHBG068337.
    KOiK04967.
    OMAiGLSEQCI.
    OrthoDBiEOG72G17P.
    PhylomeDBiQ9UBN4.
    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.
    IPR005460. TRPC4_channel.
    IPR002153. TRPC_channel.
    [Graphical view]
    PANTHERiPTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF25. PTHR10117:SF25. 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.
    PR01645. TRPCHANNEL4.
    SMARTiSM00248. ANK. 2 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    TIGRFAMsiTIGR00870. trp. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform Alpha (identifier: Q9UBN4-1) [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

    MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK    50
    SLEEAEIYFK ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL 100
    LHAIRKEVVG AVELLLNHKK PSGEKQVPPI LLDKQFSEFT PDITPIILAA 150
    HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE CVSSSDVDSL RHSRSRLNIY 200
    KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE YEELSRQCKQ 250
    FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 300
    VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA 350
    PKSPLGLFIR KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT 400
    IVEWMILPWV LGFIWGEIKQ MWDGGLQDYI HDWWNLMDFV MNSLYLATIS 450
    LKIVAFVKYS ALNPRESWDM WHPTLVAEAL FAIANIFSSL RLISLFTANS 500
    HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY YEETKGLTCK 550
    GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 600
    FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG 650
    GTLPTPFNVI PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL 700
    RRHHQYQEVM RNLVKRYVAA MIRDAKTEEG LTEENFKELK QDISSFRFEV 750
    LGLLRGSKLS TIQSANASKE SSNSADSDEK SDSEGNSKDK KKNFSLFDLT 800
    TLIHPRSAAI ASERHNISNG SALVVQEPPR EKQRKVNFVT DIKNFGLFHR 850
    RSKQNAAEQN ANQIFSVSEE VARQQAAGPL ERNIQLESRG LASRGDLSIP 900
    GLSEQCVLVD HRERNTDTLG LQVGKRVCPF KSEKVVVEDT VPIIPKEKHA 950
    KEEDSSIDYD LNLPDTVTHE DYVTTRL 977
    Length:977
    Mass (Da):112,101
    Last modified:May 1, 2000 - v1
    Checksum:i77E4D27C374D660E
    GO
    Isoform Beta (identifier: Q9UBN4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         785-868: Missing.

    Show »
    Length:893
    Mass (Da):102,640
    Checksum:i20E5FE3C93B47BB5
    GO
    Isoform Delta (identifier: Q9UBN4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         730-870: Missing.

    Show »
    Length:836
    Mass (Da):96,389
    Checksum:i1BAE1CA946ED6DAF
    GO
    Isoform Gamma (identifier: Q9UBN4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         629-693: Missing.
         785-868: Missing.

    Show »
    Length:828
    Mass (Da):94,859
    Checksum:iC01141A15CCA516C
    GO
    Isoform Epsilon (identifier: Q9UBN4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         693-693: G → GVRTQH

    Show »
    Length:982
    Mass (Da):112,723
    Checksum:i7F4500A57F38B8BD
    GO
    Isoform Zeta (identifier: Q9UBN4-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         127-299: Missing.

    Show »
    Length:804
    Mass (Da):92,221
    Checksum:i30F8E11810A76888
    GO
    Isoform Eta (identifier: Q9UBN4-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         300-323: FVAQPNCQQLLASRWYDEFPGWRR → ASYGEKLNRCGMADFRTTSMIGGI
         324-977: Missing.

    Show »
    Length:323
    Mass (Da):36,759
    Checksum:i39B4E28D03534CDD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381E → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036452

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei127 – 299173Missing in isoform Zeta. 1 PublicationVSP_041439Add
    BLAST
    Alternative sequencei300 – 32324FVAQP…PGWRR → ASYGEKLNRCGMADFRTTSM IGGI in isoform Eta. 1 PublicationVSP_047747Add
    BLAST
    Alternative sequencei324 – 977654Missing in isoform Eta. 1 PublicationVSP_047748Add
    BLAST
    Alternative sequencei629 – 69365Missing in isoform Gamma. 1 PublicationVSP_006567Add
    BLAST
    Alternative sequencei693 – 6931G → GVRTQH in isoform Epsilon. 1 PublicationVSP_041262
    Alternative sequencei730 – 870141Missing in isoform Delta. 1 PublicationVSP_006568Add
    BLAST
    Alternative sequencei785 – 86884Missing in isoform Beta and isoform Gamma. 2 PublicationsVSP_006569Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063822 mRNA. Translation: AAF22927.1.
    AF063823 mRNA. Translation: AAF22928.1.
    AF063824 mRNA. Translation: AAF22929.1.
    AF063825 mRNA. Translation: AAF22930.1.
    AF175406 mRNA. Translation: AAD51736.1.
    AF421358 mRNA. Translation: AAL24549.1.
    AF421359 mRNA. Translation: AAL24550.1.
    AF421360 mRNA. Translation: AAL24551.1.
    AF421361 mRNA. Translation: AAL24552.1.
    AF421362 mRNA. Translation: AAL24553.1.
    AL138679, AL354802 Genomic DNA. Translation: CAH70109.1.
    AL138679, AL354802 Genomic DNA. Translation: CAH70110.1.
    AL138679, AL354802 Genomic DNA. Translation: CAH70111.1.
    AL138679, AL354802 Genomic DNA. Translation: CAH70114.1.
    AL354802, AL138679 Genomic DNA. Translation: CAI15556.1.
    AL354802, AL138679 Genomic DNA. Translation: CAI15557.1.
    AL354802, AL138679 Genomic DNA. Translation: CAI15558.1.
    AL354802, AL138679 Genomic DNA. Translation: CAI15560.1.
    AL138679, AL354802 Genomic DNA. Translation: CAH70112.1.
    AL354802, AL138679 Genomic DNA. Translation: CAI15561.1.
    CH471075 Genomic DNA. Translation: EAX08595.1.
    CH471075 Genomic DNA. Translation: EAX08596.1.
    CH471075 Genomic DNA. Translation: EAX08597.1.
    CH471075 Genomic DNA. Translation: EAX08598.1.
    CH471075 Genomic DNA. Translation: EAX08600.1.
    CH471075 Genomic DNA. Translation: EAX08601.1.
    BC104725 mRNA. Translation: AAI04726.1.
    U40983 mRNA. Translation: AAC50630.1.
    CCDSiCCDS45035.1. [Q9UBN4-6]
    CCDS45036.1. [Q9UBN4-4]
    CCDS45037.1. [Q9UBN4-5]
    CCDS45038.1. [Q9UBN4-2]
    CCDS45039.1. [Q9UBN4-3]
    CCDS9365.1. [Q9UBN4-1]
    RefSeqiNP_001129427.1. NM_001135955.1. [Q9UBN4-2]
    NP_001129428.1. NM_001135956.1. [Q9UBN4-4]
    NP_001129429.1. NM_001135957.1. [Q9UBN4-3]
    NP_001129430.1. NM_001135958.1. [Q9UBN4-6]
    NP_003297.1. NM_003306.1. [Q9UBN4-5]
    NP_057263.1. NM_016179.2. [Q9UBN4-1]
    UniGeneiHs.262960.

    Genome annotation databases

    EnsembliENST00000338947; ENSP00000342580; ENSG00000133107. [Q9UBN4-6]
    ENST00000355779; ENSP00000348025; ENSG00000133107. [Q9UBN4-3]
    ENST00000358477; ENSP00000351264; ENSG00000133107. [Q9UBN4-2]
    ENST00000379673; ENSP00000368995; ENSG00000133107. [Q9UBN4-4]
    ENST00000379679; ENSP00000369001; ENSG00000133107. [Q9UBN4-6]
    ENST00000379705; ENSP00000369027; ENSG00000133107. [Q9UBN4-1]
    ENST00000488717; ENSP00000435969; ENSG00000133107. [Q9UBN4-7]
    GeneIDi7223.
    KEGGihsa:7223.
    UCSCiuc001uws.3. human. [Q9UBN4-1]
    uc001uwt.3. human. [Q9UBN4-2]
    uc010abw.3. human. [Q9UBN4-6]
    uc010abx.3. human. [Q9UBN4-5]
    uc010aby.3. human. [Q9UBN4-4]
    uc010tey.2. human. [Q9UBN4-3]

    Polymorphism databases

    DMDMi13633994.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF063822 mRNA. Translation: AAF22927.1 .
    AF063823 mRNA. Translation: AAF22928.1 .
    AF063824 mRNA. Translation: AAF22929.1 .
    AF063825 mRNA. Translation: AAF22930.1 .
    AF175406 mRNA. Translation: AAD51736.1 .
    AF421358 mRNA. Translation: AAL24549.1 .
    AF421359 mRNA. Translation: AAL24550.1 .
    AF421360 mRNA. Translation: AAL24551.1 .
    AF421361 mRNA. Translation: AAL24552.1 .
    AF421362 mRNA. Translation: AAL24553.1 .
    AL138679 , AL354802 Genomic DNA. Translation: CAH70109.1 .
    AL138679 , AL354802 Genomic DNA. Translation: CAH70110.1 .
    AL138679 , AL354802 Genomic DNA. Translation: CAH70111.1 .
    AL138679 , AL354802 Genomic DNA. Translation: CAH70114.1 .
    AL354802 , AL138679 Genomic DNA. Translation: CAI15556.1 .
    AL354802 , AL138679 Genomic DNA. Translation: CAI15557.1 .
    AL354802 , AL138679 Genomic DNA. Translation: CAI15558.1 .
    AL354802 , AL138679 Genomic DNA. Translation: CAI15560.1 .
    AL138679 , AL354802 Genomic DNA. Translation: CAH70112.1 .
    AL354802 , AL138679 Genomic DNA. Translation: CAI15561.1 .
    CH471075 Genomic DNA. Translation: EAX08595.1 .
    CH471075 Genomic DNA. Translation: EAX08596.1 .
    CH471075 Genomic DNA. Translation: EAX08597.1 .
    CH471075 Genomic DNA. Translation: EAX08598.1 .
    CH471075 Genomic DNA. Translation: EAX08600.1 .
    CH471075 Genomic DNA. Translation: EAX08601.1 .
    BC104725 mRNA. Translation: AAI04726.1 .
    U40983 mRNA. Translation: AAC50630.1 .
    CCDSi CCDS45035.1. [Q9UBN4-6 ]
    CCDS45036.1. [Q9UBN4-4 ]
    CCDS45037.1. [Q9UBN4-5 ]
    CCDS45038.1. [Q9UBN4-2 ]
    CCDS45039.1. [Q9UBN4-3 ]
    CCDS9365.1. [Q9UBN4-1 ]
    RefSeqi NP_001129427.1. NM_001135955.1. [Q9UBN4-2 ]
    NP_001129428.1. NM_001135956.1. [Q9UBN4-4 ]
    NP_001129429.1. NM_001135957.1. [Q9UBN4-3 ]
    NP_001129430.1. NM_001135958.1. [Q9UBN4-6 ]
    NP_003297.1. NM_003306.1. [Q9UBN4-5 ]
    NP_057263.1. NM_016179.2. [Q9UBN4-1 ]
    UniGenei Hs.262960.

    3D structure databases

    ProteinModelPortali Q9UBN4.
    SMRi Q9UBN4. Positions 35-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113074. 13 interactions.
    IntActi Q9UBN4. 2 interactions.
    MINTi MINT-157838.
    STRINGi 9606.ENSP00000369003.

    Chemistry

    GuidetoPHARMACOLOGYi 489.

    PTM databases

    PhosphoSitei Q9UBN4.

    Polymorphism databases

    DMDMi 13633994.

    Proteomic databases

    PaxDbi Q9UBN4.
    PRIDEi Q9UBN4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338947 ; ENSP00000342580 ; ENSG00000133107 . [Q9UBN4-6 ]
    ENST00000355779 ; ENSP00000348025 ; ENSG00000133107 . [Q9UBN4-3 ]
    ENST00000358477 ; ENSP00000351264 ; ENSG00000133107 . [Q9UBN4-2 ]
    ENST00000379673 ; ENSP00000368995 ; ENSG00000133107 . [Q9UBN4-4 ]
    ENST00000379679 ; ENSP00000369001 ; ENSG00000133107 . [Q9UBN4-6 ]
    ENST00000379705 ; ENSP00000369027 ; ENSG00000133107 . [Q9UBN4-1 ]
    ENST00000488717 ; ENSP00000435969 ; ENSG00000133107 . [Q9UBN4-7 ]
    GeneIDi 7223.
    KEGGi hsa:7223.
    UCSCi uc001uws.3. human. [Q9UBN4-1 ]
    uc001uwt.3. human. [Q9UBN4-2 ]
    uc010abw.3. human. [Q9UBN4-6 ]
    uc010abx.3. human. [Q9UBN4-5 ]
    uc010aby.3. human. [Q9UBN4-4 ]
    uc010tey.2. human. [Q9UBN4-3 ]

    Organism-specific databases

    CTDi 7223.
    GeneCardsi GC13M038210.
    HGNCi HGNC:12336. TRPC4.
    MIMi 603651. gene.
    neXtProti NX_Q9UBN4.
    PharmGKBi PA37009.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254238.
    HOVERGENi HBG068337.
    KOi K04967.
    OMAi GLSEQCI.
    OrthoDBi EOG72G17P.
    PhylomeDBi Q9UBN4.
    TreeFami TF313147.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi TRPC4. human.
    GeneWikii TRPC4.
    GenomeRNAii 7223.
    NextBioi 28287.
    PROi Q9UBN4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBN4.
    Bgeei Q9UBN4.
    CleanExi HS_TRPC4.
    Genevestigatori Q9UBN4.

    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.
    IPR005460. TRPC4_channel.
    IPR002153. TRPC_channel.
    [Graphical view ]
    PANTHERi PTHR10117. PTHR10117. 1 hit.
    PTHR10117:SF25. PTHR10117:SF25. 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.
    PR01645. TRPCHANNEL4.
    SMARTi SM00248. ANK. 2 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

    1. "Cloning and expression of the human transient receptor potential 4 (TRP4) gene: localization and functional expression of human TRP4 and TRP3."
      McKay R.R., Szymeczek-Seay C.L., Lievremont J.-P., Bird G.S., Zitt C., Juengling E., Lueckhoff A., Putney J.W. Jr.
      Biochem. J. 351:735-746(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Kidney.
    2. "Alternative splice variants of hTrp4 differentially interact with the C-terminal portion of the inositol 1,4,5-trisphosphate receptors."
      Mery L., Magnino F., Schmidt K., Krause K.-H., Dufour J.-F.
      FEBS Lett. 487:377-383(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; DELTA AND GAMMA).
      Tissue: Embryonic kidney.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; EPSILON; ETA AND ZETA), SUBCELLULAR LOCATION.
    4. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM ALPHA).
    7. "trp, a novel mammalian gene family essential for agonist-activated capacitative Ca2+ entry."
      Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E., Birnbaumer L.
      Cell 85:661-671(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 514-633.
      Tissue: Kidney.
    8. "The PDZ-interacting domain of TRPC4 controls its localization and surface expression in HEK293 cells."
      Mery L., Strauss B., Dufour J.F., Krause K.H., Hoth M.
      J. Cell Sci. 115:3497-3508(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 975-THR--LEU-977, INTERACTION WITH SLC9A3R1, SUBCELLULAR LOCATION.
    9. "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.
    10. "Activation of the endothelial store-operated ISOC Ca2+ channel requires interaction of protein 4.1 with TRPC4."
      Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.
      Circ. Res. 97:1164-1172(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EPB41L2.
    11. "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.
    12. "Epidermal growth factor induces tyrosine phosphorylation, membrane insertion, and activation of transient receptor potential channel 4."
      Odell A.F., Scott J.L., Van Helden D.F.
      J. Biol. Chem. 280:37974-37987(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-959 AND TYR-972, MUTAGENESIS OF TYR-959 AND TYR-972.
    13. "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.
    14. "The spectrin cytoskeleton influences the surface expression and activation of human transient receptor potential channel 4 channels."
      Odell A.F., Van Helden D.F., Scott J.L.
      J. Biol. Chem. 283:4395-4407(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPTAN1 AND SPTBN5.
    15. "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.
    16. "Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the vascular endothelium: evidence for a regulatory TRPC4-beta-catenin interaction."
      Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M., Drenckhahn D., Romanin C., Baumgartner W., Groschner K.
      J. Biol. Chem. 285:4213-4223(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH CDH5 AND CTNNB1.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-138.

    Entry informationi

    Entry nameiTRPC4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBN4
    Secondary accession number(s): B1ALE0
    , B1ALE1, B1ALE2, Q15721, Q3SWS6, Q96P03, Q96P04, Q96P05, Q9UIB0, Q9UIB1, Q9UIB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 141 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

    Miscellaneous

    The interaction with spectrin is important in controlling the translocation of TRPC4 channels to the plasma membrane following EGF stimulation.
    The cell membrane presentation, the calcium entry function and the interaction with junctional proteins (CTNNB1 and CDH5) are controlled by endothelial cell-cell contacts.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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