Protein detail
TRPM4
Transient receptor potential cation channel subfamily M member 4 (hTRPM4) (Calcium-activated non-selective cation channel 1) (Long transient receptor potential channel 4) (LTrpC-4) (LTrpC4) (Melastatin-4)
Protein symbol TRPM4 | UniProt ID | EVMP score 0.63 |
Frequency 6 | Transmembrane count 6 | Protein classification Disease related genesHuman disease related genesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransportersVoltage-gated ion channels |
Basic Information
Protein Names
Transient receptor potential cation channel subfamily M member 4 (hTRPM4) (Calcium-activated non-selective cation channel 1) (Long transient receptor potential channel 4) (LTrpC-4) (LTrpC4) (Melastatin-4)
Protein Class
Disease related genesHuman disease related genesPotential drug targetsPredicted intracellular proteinsPredicted membrane proteinsTransportersVoltage-gated ion channels
Protein Function
- Voltage-gated ion channels:Transient Receptor Potential Channels
- Predicted intracellular proteins
- Potential drug targets
- Transporters:Transporter channels and pores
- Human disease related genes:Congenital malformations:Congenital malformations of skin
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
Transmembrane
783..803; Helical; 815..835; Helical; 864..884; Helical; 887..910; Helical; 931..951; Helical; 1020..1040; Helical
Transmembrane Count
6
Ensembl
Entrez Gene Symbol
Gene Synonym
FLJ20041
Gene Description
Transient receptor potential cation channel subfamily M member 4
Chromosome
19
Position
49157741-49211836
Frequency
6
EVMP Score
0.63
Fluorescence & Localization
Tissue SpecificesophagusCell SpecificEndometrial ciliated cellsSingle-Nuclei Brain Specificependymal cell
Function & Pathway
Protein Function
- Voltage-gated ion channels:Transient Receptor Potential Channels
- Predicted intracellular proteins
- Potential drug targets
- Transporters:Transporter channels and pores
- Human disease related genes:Congenital malformations:Congenital malformations of skin
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
Cellular Component
Molecular Function
Biological Process
Reactome
Mediation Categories
Fusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
5 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| TRPM4 | PRKCA | P17252 | S | 1,152 | phosphorylation | PhosphoSite_MIMPMIMPSIGNORProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:15590641SIGNOR:15590641 |
| TRPM4 | PRKCA | P17252 | S | 1,145 | phosphorylation | PhosphoSite_MIMPMIMPSIGNORProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:15590641SIGNOR:15590641 |
| TRPM4 | CSNK1E | P49674 | S | 839 | phosphorylation | PhosphoSitePhosphoSite_ProtMapperProtMapper | |
| TRPM4 | KRT1 | P04264 | S | 839 | phosphorylation | REACH_ProtMapperProtMapper | ProtMapper:25441424 |
| TRPM4 | CSNK1A1L | Q8N752 | S | 839 | phosphorylation | RLIMS-P_ProtMapperProtMapper | ProtMapper:25231975 |
Ligand-Receptor Signaling
22 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| transmembrane | transmembrane | UniProt_location | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | No | No |
| transmembrane | transmembrane | TopDB | No | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
| peripheral | peripheral | UniProt_topology | No | No | No | No | No |
| peripheral | peripheral | OmniPath | No | No | No | No | No |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
| plasma_membrane | plasma_membrane | OmniPath | No | No | No | No | No |
Regulatory Interaction Network
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| KPCA | P17252 | TRPM4 | Q8TD43 | Yes | Yes | No | PhosphoSite_MIMPMIMPPhosphoSite_norefSIGNORiPTMnetProtMapperSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | ProtMapper:15590641SIGNOR:15590641PhosphoSite:15590641 |
| KC1E | P49674 | TRPM4 | Q8TD43 | Yes | No | No | iPTMnetProtMapperELMPhosphoSitePhosphoSite_ProtMapper | PhosphoSite:25231975ELM:25231975 |
Protein Complex Composition
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyImmunoaffinity Capture | R SequencingMass spectrometry | 18 | 337183423994949037702715327954143873186831222168268019194078452922106071376863664009834641201090412168844031161639835386400914553953270341315767 |
Sequence, Structure & Domains
Sequences
Length
1,214
Mass
134,301
Sequence
MVVPEKEQSWIPKIFKKKTCTTFIVDSTDPGGTLCQCGRPRTAHPAVAMEDAFGAAVVTVWDSDAHTTEKPTDAYGELDFTGAGRKHSNFLRLSDRTDPAAVYSLVTRTWGFRAPNLVVSVLGGSGGPVLQTWLQDLLRRGLVRAAQSTGAWIVTGGLHTGIGRHVGVAVRDHQMASTGGTKVVAMGVAPWGVVRNRDTLINPKGSFPARYRWRGDPEDGVQFPLDYNYSAFFLVDDGTHGCLGGENRFRLRLESYISQQKTGVGGTGIDIPVLLLLIDGDEKMLTRIENATQAQLPCLLVAGSGGAADCLAETLEDTLAPGSGGARQGEARDRIRRFFPKGDLEVLQAQVERIMTRKELLTVYSSEDGSEEFETIVLKALVKACGSSEASAYLDELRLAVAWNRVDIAQSELFRGDIQWRSFHLEASLMDALLNDRPEFVRLLISHGLSLGHFLTPMRLAQLYSAAPSNSLIRNLLDQASHSAGTKAPALKGGAAELRPPDVGHVLRMLLGKMCAPRYPSGGAWDPHPGQGFGESMYLLSDKATSPLSLDAGLGQAPWSDLLLWALLLNRAQMAMYFWEMGSNAVSSALGACLLLRVMARLEPDAEEAARRKDLAFKFEGMGVDLFGECYRSSEVRAARLLLRRCPLWGDATCLQLAMQADARAFFAQDGVQSLLTQKWWGDMASTTPIWALVLAFFCPPLIYTRLITFRKSEEEPTREELEFDMDSVINGEGPVGTADPAEKTPLGVPRQSGRPGCCGGRCGGRRCLRRWFHFWGAPVTIFMGNVVSYLLFLLLFSRVLLVDFQPAPPGSLELLLYFWAFTLLCEELRQGLSGGGGSLASGGPGPGHASLSQRLRLYLADSWNQCDLVALTCFLLGVGCRLTPGLYHLGRTVLCIDFMVFTVRLLHIFTVNKQLGPKIVIVSKMMKDVFFFLFFLGVWLVAYGVATEGLLRPRDSDFPSILRRVFYRPYLQIFGQIPQEDMDVALMEHSNCSSEPGFWAHPPGAQAGTCVSQYANWLVVLLLVIFLLVANILLVNLLIAMFSYTFGKVQGNSDLYWKAQRYRLIREFHSRPALAPPFIVISHLRLLLRQLCRRPRSPQPSSPALEHFRVYLSKEAERKLLTWESVHKENFLLARARDKRESDSERLKRTSQKVDLALKQLGHIREYEQRLKVLEREVQQCSRVLGWVAEALSRSALLPPGGPPPPDLPGSKD
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; Synonyms=TRPM4b; IsoId=Q8TD43-1; Sequence=Displayed; Name=2; Synonyms=TRPM4a; IsoId=Q8TD43-2; Sequence=VSP_021442; Name=3; Synonyms=TRPM4c; IsoId=Q8TD43-3; Sequence=VSP_021443
Alternative Sequence
1..174; Missing (in isoform 2); 738..882; Missing (in isoform 3)
3D Structural Models
Turn
63..66; 197..200; 202..205; 306..308; 323..325; 340..342; 356..360; 367..369; 648..650; 681..683; 914..916; 1089..1092
Helix
8..10; 11..14; 99..108; 132..149; 161..175; 247..258; 265..267; 282..293; 309..316; 326..335; 346..355; 374..385; 391..393; 394..402; 407..411; 422..434; 438..446; 451..454; 457..465; 472..479; 503..511; 558..569; 572..580; 585..602; 608..633; 635..641; 654..661; 664..668; 670..680; 690..698; 700..704; 767..777; 779..802; 812..833; 852..860; 863..883; 888..905; 906..911; 917..925; 927..952; 959..974; 980..983; 985..987; 1017..1032; 1034..1049; 1051..1070; 1077..1079; 1080..1087; 1116..1141; 1144..1176
Beta Strand
16..19; 36..38; 41..44; 68..71; 76..78; 79..84; 89..96; 118..122; 127..129; 155..160; 177..179; 187..190; 193..195; 206..208; 230..236; 238..240; 261..263; 268..270; 273..277; 298..301; 343..345; 362..364; 370..372; 416..418; 604..607; 705..708; 807..809; 884..886; 988..990; 995..998; 1000..1002; 1006..1008
3D Structure
Electron microscopy (16)
Domain & Motif Annotations
Motif
975..977; Selectivity filter
Coiled Coil
1134..1187
Domain (CC)
TRPM4, is a temperature-sensitive ion channel, it adopts distinct conformations at different temperatures, markedly influencing where and how ligands interact with it. Decavanadate (a positive modulator), ATP (an inhibitor) and Ca(2+) bind to different locations of TRPM4 at physiological temperatures or at lower temperatures.
Region
1076..1176; Calmodulin-binding; 1136..1141; Mediates modulation by decavanadate and PIP2-binding
Protein Families
- Transient receptor (TC 1.A.4) family
- LTrpC subfamily
- TRPM4 sub-subfamily
Sequence Similarities
Belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM4 sub-subfamily.