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Q8TD43

- TRPM4_HUMAN

UniProt

Q8TD43 - TRPM4_HUMAN

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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

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. cardiac conduction Source: InterPro
  3. dendritic cell chemotaxis Source: UniProtKB
  4. ion transmembrane transport Source: Reactome
  5. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  6. positive regulation of cell proliferation Source: UniProtKB
  7. protein sumoylation Source: UniProtKB
  8. regulation of membrane potential Source: InterPro
  9. regulation of T cell cytokine production Source: UniProtKB
  10. transmembrane transport Source: Reactome
  11. vasoconstriction Source: InterPro
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 683683CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei684 – 70421HelicalSequence AnalysisAdd
BLAST
Topological domaini705 – 77672ExtracellularSequence AnalysisAdd
BLAST
Transmembranei777 – 79721HelicalSequence AnalysisAdd
BLAST
Topological domaini798 – 86871CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei869 – 88921HelicalSequence AnalysisAdd
BLAST
Topological domaini890 – 8923ExtracellularSequence Analysis
Transmembranei893 – 91321HelicalSequence AnalysisAdd
BLAST
Topological domaini914 – 92916CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei930 – 95021HelicalSequence AnalysisAdd
BLAST
Topological domaini951 – 96515ExtracellularSequence AnalysisAdd
BLAST
Intramembranei966 – 99328Pore-formingSequence AnalysisAdd
BLAST
Topological domaini994 – 101926ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1020 – 104021HelicalSequence AnalysisAdd
BLAST
Topological domaini1041 – 1214174CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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. 1 Publication
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

BgeeiQ8TD43.
CleanExiHS_TRPM4.
ExpressionAtlasiQ8TD43. baseline and differential.
GenevestigatoriQ8TD43.

Organism-specific databases

HPAiHPA041169.

Interactioni

Subunit structurei

Homomultimer.1 Publication

Protein-protein interaction databases

BioGridi120154. 4 interactions.
STRINGi9606.ENSP00000252826.

Structurei

3D structure databases

ProteinModelPortaliQ8TD43.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119127.
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

        10         20         30         40         50
MVVPEKEQSW IPKIFKKKTC TTFIVDSTDP GGTLCQCGRP RTAHPAVAME
60 70 80 90 100
DAFGAAVVTV WDSDAHTTEK PTDAYGELDF TGAGRKHSNF LRLSDRTDPA
110 120 130 140 150
AVYSLVTRTW GFRAPNLVVS VLGGSGGPVL QTWLQDLLRR GLVRAAQSTG
160 170 180 190 200
AWIVTGGLHT GIGRHVGVAV RDHQMASTGG TKVVAMGVAP WGVVRNRDTL
210 220 230 240 250
INPKGSFPAR YRWRGDPEDG VQFPLDYNYS AFFLVDDGTH GCLGGENRFR
260 270 280 290 300
LRLESYISQQ KTGVGGTGID IPVLLLLIDG DEKMLTRIEN ATQAQLPCLL
310 320 330 340 350
VAGSGGAADC LAETLEDTLA PGSGGARQGE ARDRIRRFFP KGDLEVLQAQ
360 370 380 390 400
VERIMTRKEL LTVYSSEDGS EEFETIVLKA LVKACGSSEA SAYLDELRLA
410 420 430 440 450
VAWNRVDIAQ SELFRGDIQW RSFHLEASLM DALLNDRPEF VRLLISHGLS
460 470 480 490 500
LGHFLTPMRL AQLYSAAPSN SLIRNLLDQA SHSAGTKAPA LKGGAAELRP
510 520 530 540 550
PDVGHVLRML LGKMCAPRYP SGGAWDPHPG QGFGESMYLL SDKATSPLSL
560 570 580 590 600
DAGLGQAPWS DLLLWALLLN RAQMAMYFWE MGSNAVSSAL GACLLLRVMA
610 620 630 640 650
RLEPDAEEAA RRKDLAFKFE GMGVDLFGEC YRSSEVRAAR LLLRRCPLWG
660 670 680 690 700
DATCLQLAMQ ADARAFFAQD GVQSLLTQKW WGDMASTTPI WALVLAFFCP
710 720 730 740 750
PLIYTRLITF RKSEEEPTRE ELEFDMDSVI NGEGPVGTAD PAEKTPLGVP
760 770 780 790 800
RQSGRPGCCG GRCGGRRCLR RWFHFWGAPV TIFMGNVVSY LLFLLLFSRV
810 820 830 840 850
LLVDFQPAPP GSLELLLYFW AFTLLCEELR QGLSGGGGSL ASGGPGPGHA
860 870 880 890 900
SLSQRLRLYL ADSWNQCDLV ALTCFLLGVG CRLTPGLYHL GRTVLCIDFM
910 920 930 940 950
VFTVRLLHIF TVNKQLGPKI VIVSKMMKDV FFFLFFLGVW LVAYGVATEG
960 970 980 990 1000
LLRPRDSDFP SILRRVFYRP YLQIFGQIPQ EDMDVALMEH SNCSSEPGFW
1010 1020 1030 1040 1050
AHPPGAQAGT CVSQYANWLV VLLLVIFLLV ANILLVNLLI AMFSYTFGKV
1060 1070 1080 1090 1100
QGNSDLYWKA QRYRLIREFH SRPALAPPFI VISHLRLLLR QLCRRPRSPQ
1110 1120 1130 1140 1150
PSSPALEHFR VYLSKEAERK LLTWESVHKE NFLLARARDK RESDSERLKR
1160 1170 1180 1190 1200
TSQKVDLALK QLGHIREYEQ RLKVLEREVQ QCSRVLGWVA EALSRSALLP
1210
PGGPPPPDLP GSKD
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 4 interactions.
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.
GeneTreei ENSGT00760000119127.
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

Bgeei Q8TD43.
CleanExi HS_TRPM4.
ExpressionAtlasi Q8TD43. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 101 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

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