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Q8TD43

- TRPM4_HUMAN

UniProt

Q8TD43 - TRPM4_HUMAN

Protein

Transient receptor potential cation channel subfamily M member 4

Gene

TRPM4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      Previous versions | rss
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    Functioni

    Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca2+, it is impermeable to it. Mediates transport of monovalent cations (Na+ > K+ > Cs+ > Li+), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca2+ oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca2+ overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway.8 Publications

    Enzyme regulationi

    Gating is voltage-dependent and repressed by decavanadate. Calmodulin-binding confers the Ca2+ sensitivity. ATP is able to restore Ca2+ sensitivity after desensitization. Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances activity, by increasing the channel's Ca2+ sensitivity and shifting its voltage dependence of activation towards negative potentials. Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole derivative (BTP2).5 Publications

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium activated cation channel activity Source: UniProtKB
    3. calcium channel activity Source: Ensembl

    GO - Biological processi

    1. calcium ion transmembrane transport Source: Reactome
    2. dendritic cell chemotaxis Source: UniProtKB
    3. ion transmembrane transport Source: Reactome
    4. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    5. positive regulation of cell proliferation Source: UniProtKB
    6. protein sumoylation Source: UniProtKB
    7. regulation of T cell cytokine production Source: UniProtKB
    8. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Ion channel

    Keywords - Biological processi

    Adaptive immunity, Immunity, Ion transport, Transport

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_169333. TRP channels.

    Protein family/group databases

    TCDBi1.A.4.5.4. the transient receptor potential ca(2+) channel (trp-cc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transient receptor potential cation channel subfamily M member 4
    Short name:
    hTRPM4
    Alternative name(s):
    Calcium-activated non-selective cation channel 1
    Long transient receptor potential channel 4
    Short name:
    LTrpC-4
    Short name:
    LTrpC4
    Melastatin-4
    Gene namesi
    Name:TRPM4
    Synonyms:LTRPC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17993. TRPM4.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. Golgi apparatus Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Golgi apparatus, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Progressive familial heart block 1B (PFHB1B) [MIM:604559]: A cardiac bundle branch disorder characterized by progressive alteration of cardiac conduction through the His-Purkinje system, with a pattern of a right bundle-branch block and/or left anterior hemiblock occurring individually or together. It leads to complete atrio-ventricular block causing syncope and sudden death.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71E → K in PFHB1B; attenuated desumoylation of TRPM4 resulting in constitutive sumoylation of the channel leading to impaired endocytosis and elevated channel density at the cell surface. 1 Publication
    VAR_064042
    Natural varianti131 – 1311Q → H in PFHB1B; incomplete right bundle-branch block. 1 Publication
    VAR_066763
    Natural varianti164 – 1641R → W in PFHB1B. 1 Publication
    VAR_066764
    Natural varianti293 – 2931Q → R in PFHB1B; right bundle-branch block. 1 Publication
    Corresponds to variant rs172147855 [ dbSNP | Ensembl ].
    VAR_066766
    Natural varianti432 – 4321A → T in PFHB1B; atrioventricular block. 2 Publications
    Corresponds to variant rs201907325 [ dbSNP | Ensembl ].
    VAR_066767
    Natural varianti582 – 5821G → S in PFHB1B; atrioventricular block. 1 Publication
    Corresponds to variant rs172149856 [ dbSNP | Ensembl ].
    VAR_066770
    Natural varianti790 – 7901Y → H in PFHB1B; atrioventricular block. 1 Publication
    VAR_066771
    Natural varianti844 – 8441G → D in PFHB1B; right bundle-branch block. 2 Publications
    Corresponds to variant rs200038418 [ dbSNP | Ensembl ].
    VAR_066772
    Natural varianti914 – 9141K → R in PFHB1B; atrioventricular block. 1 Publication
    VAR_066774
    Natural varianti970 – 9701P → S in PFHB1B; incomplete right bundle-branch block. 1 Publication
    VAR_066775

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi275 – 2751L → A or C: Abolishes ability to restore sensitivity to Ca(2+) after desensitization. 1 Publication
    Mutagenesisi278 – 2781I → N: No effect. 1 Publication
    Mutagenesisi279 – 2791D → N: No effect. 1 Publication
    Mutagenesisi324 – 3241G → A: No effect. 1 Publication
    Mutagenesisi325 – 3251G → A: Abolishes ability to restore sensitivity to Ca(2+) after desensitization. 1 Publication
    Mutagenesisi327 – 3271R → A: No effect. 1 Publication
    Mutagenesisi977 – 9771Q → E: Alters the monovalent cation permeability sequence and results in a pore with moderate Ca(2+) permeability. 1 Publication
    Mutagenesisi981 – 9866EDMDVA → TIIDGP: Induces a functional channel that combines the gating hallmarks of TRPM4 (activation by Ca(2+)) with TRPV6-like sensitivity to block by extracellular Ca(2+) and Mg(2+) as well as Ca(2+) permeation. 1 Publication
    Mutagenesisi981 – 9811E → A: Results in a channel with normal permeability properties but with a reduced sensitivity to block by intracellular spermine. 1 Publication
    Mutagenesisi982 – 9821D → A: Results in a functional channel that exhibits extremely fast desensitization, possibly indicating destabilization of the pore. 1 Publication
    Mutagenesisi984 – 9841D → A: Results in a non-functional channel with a dominant negative phenotype. 1 Publication
    Mutagenesisi1059 – 10591K → Q: Does not affect PIP2-binding. 1 Publication
    Mutagenesisi1072 – 10721R → Q: Does not affect PIP2-binding. 1 Publication
    Mutagenesisi1136 – 11416Missing: Results in a channel with very rapid desensitization and highly reduced sensitivity to PIP2.
    Mutagenesisi1145 – 11451S → A: Decreases the sensitivity to Ca(2+). 1 Publication
    Mutagenesisi1152 – 11521S → A: Decreases the sensitivity to Ca(2+). 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi604559. phenotype.
    Orphaneti130. Brugada syndrome.
    871. Familial progressive cardiac conduction defect.
    PharmGKBiPA38272.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12141214Transient receptor potential cation channel subfamily M member 4PRO_0000259529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1145 – 11451Phosphoserine; by PKC1 Publication
    Modified residuei1152 – 11521Phosphoserine; by PKC1 Publication

    Post-translational modificationi

    Phosphorylation by PKC leads to increase the sensitivity to Ca2+.1 Publication
    Sumoylated. Desumoylated by SENP1.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8TD43.
    PaxDbiQ8TD43.
    PRIDEiQ8TD43.

    PTM databases

    PhosphoSiteiQ8TD43.

    Expressioni

    Tissue specificityi

    Widely expressed with a high expression in intestine and prostate. In brain, it is both expressed in whole cerebral arteries and isolated vascular smooth muscle cells. Prominently expressed in Purkinje fibers. Expressed at higher levels in T-helper 2 (Th2) cells as compared to T-helper 1 (Th1) cells.7 Publications

    Gene expression databases

    ArrayExpressiQ8TD43.
    BgeeiQ8TD43.
    CleanExiHS_TRPM4.
    GenevestigatoriQ8TD43.

    Organism-specific databases

    HPAiHPA041169.

    Interactioni

    Subunit structurei

    Homomultimer.1 Publication

    Protein-protein interaction databases

    BioGridi120154. 1 interaction.
    STRINGi9606.ENSP00000252826.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8TD43.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 683683CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini705 – 77672ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini798 – 86871CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini890 – 8923ExtracellularSequence Analysis
    Topological domaini914 – 92916CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini951 – 96515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini994 – 101926ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1041 – 1214174CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei966 – 99328Pore-formingSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei684 – 70421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei777 – 79721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei869 – 88921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei893 – 91321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei930 – 95021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1020 – 104021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1076 – 1176101Calmodulin-bindingAdd
    BLAST
    Regioni1136 – 11416Mediates modulation by decavanadate and PIP2-binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1134 – 118754Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi981 – 9866Selectivity filter

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG253824.
    HOGENOMiHOG000236350.
    HOVERGENiHBG108337.
    InParanoidiQ8TD43.
    KOiK04979.
    OMAiRTWGFRA.
    OrthoDBiEOG725DH1.
    PhylomeDBiQ8TD43.
    TreeFamiTF314204.

    Family and domain databases

    InterProiIPR005821. Ion_trans_dom.
    IPR029581. TRPM4.
    [Graphical view]
    PANTHERiPTHR13800:SF6. PTHR13800:SF6. 1 hit.
    PfamiPF00520. Ion_trans. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TD43-1) [UniParc]FASTAAdd to Basket

    Also known as: TRPM4b

    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

    MVVPEKEQSW IPKIFKKKTC TTFIVDSTDP GGTLCQCGRP RTAHPAVAME     50
    DAFGAAVVTV WDSDAHTTEK PTDAYGELDF TGAGRKHSNF LRLSDRTDPA 100
    AVYSLVTRTW GFRAPNLVVS VLGGSGGPVL QTWLQDLLRR GLVRAAQSTG 150
    AWIVTGGLHT GIGRHVGVAV RDHQMASTGG TKVVAMGVAP WGVVRNRDTL 200
    INPKGSFPAR YRWRGDPEDG VQFPLDYNYS AFFLVDDGTH GCLGGENRFR 250
    LRLESYISQQ KTGVGGTGID IPVLLLLIDG DEKMLTRIEN ATQAQLPCLL 300
    VAGSGGAADC LAETLEDTLA PGSGGARQGE ARDRIRRFFP KGDLEVLQAQ 350
    VERIMTRKEL LTVYSSEDGS EEFETIVLKA LVKACGSSEA SAYLDELRLA 400
    VAWNRVDIAQ SELFRGDIQW RSFHLEASLM DALLNDRPEF VRLLISHGLS 450
    LGHFLTPMRL AQLYSAAPSN SLIRNLLDQA SHSAGTKAPA LKGGAAELRP 500
    PDVGHVLRML LGKMCAPRYP SGGAWDPHPG QGFGESMYLL SDKATSPLSL 550
    DAGLGQAPWS DLLLWALLLN RAQMAMYFWE MGSNAVSSAL GACLLLRVMA 600
    RLEPDAEEAA RRKDLAFKFE GMGVDLFGEC YRSSEVRAAR LLLRRCPLWG 650
    DATCLQLAMQ ADARAFFAQD GVQSLLTQKW WGDMASTTPI WALVLAFFCP 700
    PLIYTRLITF RKSEEEPTRE ELEFDMDSVI NGEGPVGTAD PAEKTPLGVP 750
    RQSGRPGCCG GRCGGRRCLR RWFHFWGAPV TIFMGNVVSY LLFLLLFSRV 800
    LLVDFQPAPP GSLELLLYFW AFTLLCEELR QGLSGGGGSL ASGGPGPGHA 850
    SLSQRLRLYL ADSWNQCDLV ALTCFLLGVG CRLTPGLYHL GRTVLCIDFM 900
    VFTVRLLHIF TVNKQLGPKI VIVSKMMKDV FFFLFFLGVW LVAYGVATEG 950
    LLRPRDSDFP SILRRVFYRP YLQIFGQIPQ EDMDVALMEH SNCSSEPGFW 1000
    AHPPGAQAGT CVSQYANWLV VLLLVIFLLV ANILLVNLLI AMFSYTFGKV 1050
    QGNSDLYWKA QRYRLIREFH SRPALAPPFI VISHLRLLLR QLCRRPRSPQ 1100
    PSSPALEHFR VYLSKEAERK LLTWESVHKE NFLLARARDK RESDSERLKR 1150
    TSQKVDLALK QLGHIREYEQ RLKVLEREVQ QCSRVLGWVA EALSRSALLP 1200
    PGGPPPPDLP GSKD 1214
    Length:1,214
    Mass (Da):134,301
    Last modified:June 1, 2002 - v1
    Checksum:i76ADA452690ED8F5
    GO
    Isoform 2 (identifier: Q8TD43-2) [UniParc]FASTAAdd to Basket

    Also known as: TRPM4a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-174: Missing.

    Show »
    Length:1,040
    Mass (Da):115,566
    Checksum:i684A8C554B2B0F2E
    GO
    Isoform 3 (identifier: Q8TD43-3) [UniParc]FASTAAdd to Basket

    Also known as: TRPM4c

    The sequence of this isoform differs from the canonical sequence as follows:
         738-882: Missing.

    Show »
    Length:1,069
    Mass (Da):118,630
    Checksum:i80DEBD935A55F200
    GO

    Sequence cautioni

    The sequence BAA90907.1 differs from that shown. Reason: Erroneous termination at position 1191. Translated as Glu.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1149 – 11491K → E in BAA90907. (PubMed:14702039)Curated
    Sequence conflicti1207 – 12071P → L in BAA90907. (PubMed:14702039)Curated
    Sequence conflicti1210 – 12101P → H in BAA90907. (PubMed:14702039)Curated
    Sequence conflicti1214 – 12141D → E in BAA90907. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71E → K in PFHB1B; attenuated desumoylation of TRPM4 resulting in constitutive sumoylation of the channel leading to impaired endocytosis and elevated channel density at the cell surface. 1 Publication
    VAR_064042
    Natural varianti101 – 1011A → T.1 Publication
    Corresponds to variant rs113984787 [ dbSNP | Ensembl ].
    VAR_066761
    Natural varianti103 – 1031Y → C.1 Publication
    VAR_066762
    Natural varianti131 – 1311Q → H in PFHB1B; incomplete right bundle-branch block. 1 Publication
    VAR_066763
    Natural varianti164 – 1641R → W in PFHB1B. 1 Publication
    VAR_066764
    Natural varianti252 – 2521R → H.1 Publication
    VAR_066765
    Natural varianti293 – 2931Q → R in PFHB1B; right bundle-branch block. 1 Publication
    Corresponds to variant rs172147855 [ dbSNP | Ensembl ].
    VAR_066766
    Natural varianti432 – 4321A → T in PFHB1B; atrioventricular block. 2 Publications
    Corresponds to variant rs201907325 [ dbSNP | Ensembl ].
    VAR_066767
    Natural varianti487 – 49812Missing.
    VAR_066768Add
    BLAST
    Natural varianti561 – 5611D → A.1 Publication
    Corresponds to variant rs56355369 [ dbSNP | Ensembl ].
    VAR_066769
    Natural varianti582 – 5821G → S in PFHB1B; atrioventricular block. 1 Publication
    Corresponds to variant rs172149856 [ dbSNP | Ensembl ].
    VAR_066770
    Natural varianti790 – 7901Y → H in PFHB1B; atrioventricular block. 1 Publication
    VAR_066771
    Natural varianti844 – 8441G → D in PFHB1B; right bundle-branch block. 2 Publications
    Corresponds to variant rs200038418 [ dbSNP | Ensembl ].
    VAR_066772
    Natural varianti854 – 8541Q → R.1 Publication
    Corresponds to variant rs172155862 [ dbSNP | Ensembl ].
    VAR_066773
    Natural varianti914 – 9141K → R in PFHB1B; atrioventricular block. 1 Publication
    VAR_066774
    Natural varianti970 – 9701P → S in PFHB1B; incomplete right bundle-branch block. 1 Publication
    VAR_066775
    Natural varianti1204 – 12041P → L.1 Publication
    Corresponds to variant rs150391806 [ dbSNP | Ensembl ].
    VAR_066776

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 174174Missing in isoform 2. 2 PublicationsVSP_021442Add
    BLAST
    Alternative sequencei738 – 882145Missing in isoform 3. 1 PublicationVSP_021443Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY046396 mRNA. Translation: AAL02142.1.
    AF497623 mRNA. Translation: AAM18083.1.
    AY297044 mRNA. Translation: AAP44473.1.
    AY297045 mRNA. Translation: AAP44474.1.
    AY297046 mRNA. Translation: AAP44475.1.
    AJ575813 mRNA. Translation: CAE05941.1.
    AK000048 mRNA. Translation: BAA90907.1. Sequence problems.
    AK292862 mRNA. Translation: BAF85551.1.
    BC132727 mRNA. Translation: AAI32728.1.
    CCDSiCCDS33073.1. [Q8TD43-1]
    CCDS56098.1. [Q8TD43-3]
    RefSeqiNP_001182156.1. NM_001195227.1. [Q8TD43-3]
    NP_060106.2. NM_017636.3. [Q8TD43-1]
    UniGeneiHs.467101.

    Genome annotation databases

    EnsembliENST00000252826; ENSP00000252826; ENSG00000130529. [Q8TD43-1]
    ENST00000427978; ENSP00000407492; ENSG00000130529. [Q8TD43-3]
    GeneIDi54795.
    KEGGihsa:54795.
    UCSCiuc002pmw.3. human. [Q8TD43-1]
    uc010emu.3. human. [Q8TD43-3]

    Polymorphism databases

    DMDMi74715868.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY046396 mRNA. Translation: AAL02142.1 .
    AF497623 mRNA. Translation: AAM18083.1 .
    AY297044 mRNA. Translation: AAP44473.1 .
    AY297045 mRNA. Translation: AAP44474.1 .
    AY297046 mRNA. Translation: AAP44475.1 .
    AJ575813 mRNA. Translation: CAE05941.1 .
    AK000048 mRNA. Translation: BAA90907.1 . Sequence problems.
    AK292862 mRNA. Translation: BAF85551.1 .
    BC132727 mRNA. Translation: AAI32728.1 .
    CCDSi CCDS33073.1. [Q8TD43-1 ]
    CCDS56098.1. [Q8TD43-3 ]
    RefSeqi NP_001182156.1. NM_001195227.1. [Q8TD43-3 ]
    NP_060106.2. NM_017636.3. [Q8TD43-1 ]
    UniGenei Hs.467101.

    3D structure databases

    ProteinModelPortali Q8TD43.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120154. 1 interaction.
    STRINGi 9606.ENSP00000252826.

    Chemistry

    ChEMBLi CHEMBL1628469.
    GuidetoPHARMACOLOGYi 496.

    Protein family/group databases

    TCDBi 1.A.4.5.4. the transient receptor potential ca(2+) channel (trp-cc) family.

    PTM databases

    PhosphoSitei Q8TD43.

    Polymorphism databases

    DMDMi 74715868.

    Proteomic databases

    MaxQBi Q8TD43.
    PaxDbi Q8TD43.
    PRIDEi Q8TD43.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252826 ; ENSP00000252826 ; ENSG00000130529 . [Q8TD43-1 ]
    ENST00000427978 ; ENSP00000407492 ; ENSG00000130529 . [Q8TD43-3 ]
    GeneIDi 54795.
    KEGGi hsa:54795.
    UCSCi uc002pmw.3. human. [Q8TD43-1 ]
    uc010emu.3. human. [Q8TD43-3 ]

    Organism-specific databases

    CTDi 54795.
    GeneCardsi GC19P049661.
    HGNCi HGNC:17993. TRPM4.
    HPAi HPA041169.
    MIMi 604559. phenotype.
    606936. gene.
    neXtProti NX_Q8TD43.
    Orphaneti 130. Brugada syndrome.
    871. Familial progressive cardiac conduction defect.
    PharmGKBi PA38272.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253824.
    HOGENOMi HOG000236350.
    HOVERGENi HBG108337.
    InParanoidi Q8TD43.
    KOi K04979.
    OMAi RTWGFRA.
    OrthoDBi EOG725DH1.
    PhylomeDBi Q8TD43.
    TreeFami TF314204.

    Enzyme and pathway databases

    Reactomei REACT_169333. TRP channels.

    Miscellaneous databases

    GeneWikii TRPM4.
    GenomeRNAii 54795.
    NextBioi 57471.
    PROi Q8TD43.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TD43.
    Bgeei Q8TD43.
    CleanExi HS_TRPM4.
    Genevestigatori Q8TD43.

    Family and domain databases

    InterProi IPR005821. Ion_trans_dom.
    IPR029581. TRPM4.
    [Graphical view ]
    PANTHERi PTHR13800:SF6. PTHR13800:SF6. 1 hit.
    Pfami PF00520. Ion_trans. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform."
      Xu X.-Z.S., Moebius F., Gill D.L., Montell C.
      Proc. Natl. Acad. Sci. U.S.A. 98:10692-10697(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "TRPM4 is a Ca2+-activated nonselective cation channel mediating cell membrane depolarization."
      Launay P., Fleig A., Perraud A.-L., Scharenberg A.M., Penner R., Kinet J.-P.
      Cell 109:397-407(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
    3. "TRPM5 is a voltage-modulated and Ca(2+)-activated monovalent selective cation channel."
      Hofmann T., Chubanov V., Gudermann T., Montell C.
      Curr. Biol. 13:1153-1158(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Prostate.
    5. "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: Trachea.
    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 1).
      Tissue: Brain.
    7. "Critical role for transient receptor potential channel TRPM4 in myogenic constriction of cerebral arteries."
      Earley S., Waldron B.J., Brayden J.E.
      Circ. Res. 95:922-929(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    8. "Functional characterization of a Ca(2+)-activated non-selective cation channel in human atrial cardiomyocytes."
      Guinamard R., Chatelier A., Demion M., Potreau D., Patri S., Rahmati M., Bois P.
      J. Physiol. (Lond.) 558:75-83(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Decavanadate modulates gating of TRPM4 cation channels."
      Nilius B., Prenen J., Janssens A., Voets T., Droogmans G.
      J. Physiol. (Lond.) 560:753-765(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    10. "Intracellular nucleotides and polyamines inhibit the Ca2+-activated cation channel TRPM4b."
      Nilius B., Prenen J., Voets T., Droogmans G.
      Pflugers Arch. 448:70-75(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: ATP-BINDING, ENZYME REGULATION.
    11. "TRPM4 regulates calcium oscillations after T cell activation."
      Launay P., Cheng H., Srivatsan S., Penner R., Fleig A., Kinet J.-P.
      Science 306:1374-1377(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Regulation of the Ca2+ sensitivity of the nonselective cation channel TRPM4."
      Nilius B., Prenen J., Tang J., Wang C., Owsianik G., Janssens A., Voets T., Zhu M.X.
      J. Biol. Chem. 280:6423-6433(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1145 AND SER-1152, ATP-BINDING, CALMODULIN-BINDING, MUTAGENESIS OF LEU-275; ILE-278; ASP-279; GLY-324; GLY-325; ARG-327; SER-1145 AND SER-1152.
    13. Cited for: SELECTIVITY FILTER MOTIF, MUTAGENESIS OF GLN-977; GLU-981; 981-GLU--ALA-986; ASP-982 AND ASP-984.
    14. "Phosphatidylinositol 4,5-bisphosphate rescues TRPM4 channels from desensitization."
      Zhang Z., Okawa H., Wang Y., Liman E.R.
      J. Biol. Chem. 280:39185-39192(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PIP2-BINDING.
    15. "TRPM4 controls insulin secretion in pancreatic beta-cells."
      Cheng H., Beck A., Launay P., Gross S.A., Stokes A.J., Kinet J.-P., Fleig A., Penner R.
      Cell Calcium 41:51-61(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The Ca2+-activated cation channel TRPM4 is regulated by phosphatidylinositol 4,5-biphosphate."
      Nilius B., Mahieu F., Prenen J., Janssens A., Owsianik G., Vennekens R., Voets T.
      EMBO J. 25:467-478(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PIP2-BINDING, MUTAGENESIS OF LYS-1059; ARG-1072 AND 1136-ARG--ARG-1141.
    17. "Tissue distribution profiles of the human TRPM cation channel family."
      Fonfria E., Murdock P.R., Cusdin F.S., Benham C.D., Kelsell R.E., McNulty S.
      J. Recept. Signal Transduct. 26:159-178(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    18. "A pyrazole derivative potently inhibits lymphocyte Ca2+ influx and cytokine production by facilitating transient receptor potential melastatin 4 channel activity."
      Takezawa R., Cheng H., Beck A., Ishikawa J., Launay P., Kubota H., Kinet J.-P., Fleig A., Yamada T., Penner R.
      Mol. Pharmacol. 69:1413-1420(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    19. "Cloning and characterization of rat transient receptor potential-melastatin 4 (TRPM4)."
      Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N., Hong S.G., Park J.Y.
      Biochem. Biophys. Res. Commun. 391:806-811(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    20. "TRPM4 enhances cell proliferation through up-regulation of the beta-catenin signaling pathway."
      Armisen R., Marcelain K., Simon F., Tapia J.C., Toro J., Quest A.F., Stutzin A.
      J. Cell. Physiol. 226:103-109(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Trpm4 differentially regulates Th1 and th2 function by altering calcium signaling and NFAT localization."
      Weber K.S., Hildner K., Murphy K.M., Allen P.M.
      J. Immunol. 185:2836-2846(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    22. "Impaired endocytosis of the ion channel TRPM4 is associated with human progressive familial heart block type I."
      Kruse M., Schulze-Bahr E., Corfield V., Beckmann A., Stallmeyer B., Kurtbay G., Ohmert I., Schulze-Bahr E., Brink P., Pongs O.
      J. Clin. Invest. 119:2737-2744(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PFHB1B LYS-7, CHARACTERIZATION OF VARIANT PFHB1B LYS-7, SUMOYLATION, TISSUE SPECIFICITY.
    23. "Gain-of-function mutations in TRPM4 cause autosomal dominant isolated cardiac conduction disease."
      Liu H., El Zein L., Kruse M., Guinamard R., Beckmann A., Bozio A., Kurtbay G., Megarbane A., Ohmert I., Blaysat G., Villain E., Pongs O., Bouvagnet P.
      Circ. Cardiovasc. Genet. 3:374-385(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PFHB1B TRP-164; THR-432 AND ASP-844.
    24. "Mutational spectrum in the Ca(2+) -activated cation channel gene TRPM4 in patients with cardiac conductance disturbances."
      Stallmeyer B., Zumhagen S., Denjoy I., Duthoit G., Hebert J.L., Ferrer X., Maugenre S., Schmitz W., Kirchhefer U., Schulze-Bahr E., Guicheney P., Schulze-Bahr E.
      Hum. Mutat. 33:109-117(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PFHB1B HIS-131; ARG-293; THR-432; SER-582; HIS-790; ASP-844; ARG-914 AND SER-970, VARIANTS THR-101; CYS-103; HIS-252; LYS-487 DEL; ALA-561; ARG-854 AND LEU-1204.

    Entry informationi

    Entry nameiTRPM4_HUMAN
    AccessioniPrimary (citable) accession number: Q8TD43
    Secondary accession number(s): A2RU25
    , Q7Z5D9, Q96L84, Q9NXV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 100 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 19
      Human chromosome 19: 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