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Q9UBN4 (TRPC4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TRPC4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length977 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.16

Subunit structure

Interacts with TRPC4AP By similarity. Homotetramer and heterotetramer with TRPC1 and/or TRPC5. Isoform alphabut not isoform betaassociates 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Enhanced insertion into the cell membrane after activation of the EGF receptor. Ref.3 Ref.8 Ref.10 Ref.12

Tissue specificity

Strongly expressed in placenta. Expressed at lower levels in heart, pancreas, kidney and brain. Expressed in endothelial cells. Isoform alphawas found to be the predominant isoform. Isoform betawas not found in pancreas and brain. Ref.16

Domain

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.

Post-translational modification

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

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.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. STrpC subfamily. TRPC4 sub-subfamily. [View classification]

Contains 4 ANK repeats.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Coiled coil
Repeat
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionCalcium channel
Ion channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

calcium ion import

Inferred from direct assay Ref.16. Source: BHF-UCL

calcium ion transmembrane transport

Traceable author statement. Source: Reactome

calcium ion transport

Traceable author statement Ref.7. Source: ProtInc

gamma-aminobutyric acid secretion

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentbasolateral plasma membrane

Inferred from direct assay Ref.16. Source: BHF-UCL

calcium channel complex

Inferred from direct assay Ref.15. Source: UniProtKB

caveola

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay Ref.16. Source: BHF-UCL

cortical cytoskeleton

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from physical interaction Ref.16. Source: BHF-UCL

cadherin binding

Inferred from physical interaction Ref.16. Source: BHF-UCL

inositol 1,4,5 trisphosphate binding

Inferred from electronic annotation. Source: Ensembl

store-operated calcium channel activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MX1P205912EBI-929504,EBI-929476

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform Alpha (identifier: Q9UBN4-1)

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.
Isoform Beta (identifier: Q9UBN4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     785-868: Missing.
Isoform Delta (identifier: Q9UBN4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     730-870: Missing.
Isoform Gamma (identifier: Q9UBN4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     629-693: Missing.
     785-868: Missing.
Isoform Epsilon (identifier: Q9UBN4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     693-693: G → GVRTQH
Isoform Zeta (identifier: Q9UBN4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     127-299: Missing.
Isoform Eta (identifier: Q9UBN4-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 977977Short transient receptor potential channel 4
PRO_0000215314

Regions

Topological domain1 – 329329Cytoplasmic Potential
Transmembrane330 – 35021Helical; Potential
Topological domain351 – 36212Extracellular Potential
Transmembrane363 – 38321Helical; Potential
Topological domain384 – 43653Cytoplasmic Potential
Transmembrane437 – 45721Helical; Potential
Topological domain458 – 46912Extracellular Potential
Transmembrane470 – 49021Helical; Potential
Topological domain491 – 51121Cytoplasmic Potential
Transmembrane512 – 53221Helical; Potential
Topological domain533 – 59967Extracellular Potential
Transmembrane600 – 62021Helical; Potential
Topological domain621 – 977357Cytoplasmic Potential
Repeat31 – 6030ANK 1
Repeat69 – 9729ANK 2
Repeat98 – 12427ANK 3
Repeat141 – 17030ANK 4
Region87 – 17286Multimerization domain By similarity
Region254 – 30451Multimerization domain By similarity
Region615 – 977363Binds to ITPR1, ITPR2 and ITPR3
Region975 – 9773PDZ-binding domain
Coiled coil223 – 26038 Potential
Compositional bias377 – 3826Poly-Leu

Amino acid modifications

Modified residue9591Phosphotyrosine; by FYN Ref.12
Modified residue9721Phosphotyrosine; by FYN Ref.12

Natural variations

Alternative sequence127 – 299173Missing in isoform Zeta.
VSP_041439
Alternative sequence300 – 32324FVAQP…PGWRR → ASYGEKLNRCGMADFRTTSM IGGI in isoform Eta.
VSP_047747
Alternative sequence324 – 977654Missing in isoform Eta.
VSP_047748
Alternative sequence629 – 69365Missing in isoform Gamma.
VSP_006567
Alternative sequence6931G → GVRTQH in isoform Epsilon.
VSP_041262
Alternative sequence730 – 870141Missing in isoform Delta.
VSP_006568
Alternative sequence785 – 86884Missing in isoform Beta and isoform Gamma.
VSP_006569
Natural variant1381E → K in a breast cancer sample; somatic mutation. Ref.17
VAR_036452

Experimental info

Mutagenesis9591Y → 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. Ref.12
Mutagenesis9721Y → 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. Ref.12
Mutagenesis975 – 9773Missing: Loss of interaction with SLC9A3R1/NHERF. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform Alpha [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 77E4D27C374D660E

FASTA977112,101
        10         20         30         40         50         60 
MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK 

        70         80         90        100        110        120 
ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK 

       130        140        150        160        170        180 
PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE 

       190        200        210        220        230        240 
CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE 

       250        260        270        280        290        300 
YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF 

       310        320        330        340        350        360 
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR 

       370        380        390        400        410        420 
KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ 

       430        440        450        460        470        480 
MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL 

       490        500        510        520        530        540 
FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY 

       550        560        570        580        590        600 
YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM 

       610        620        630        640        650        660 
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI 

       670        680        690        700        710        720 
PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA 

       730        740        750        760        770        780 
MIRDAKTEEG LTEENFKELK QDISSFRFEV LGLLRGSKLS TIQSANASKE SSNSADSDEK 

       790        800        810        820        830        840 
SDSEGNSKDK KKNFSLFDLT TLIHPRSAAI ASERHNISNG SALVVQEPPR EKQRKVNFVT 

       850        860        870        880        890        900 
DIKNFGLFHR RSKQNAAEQN ANQIFSVSEE VARQQAAGPL ERNIQLESRG LASRGDLSIP 

       910        920        930        940        950        960 
GLSEQCVLVD HRERNTDTLG LQVGKRVCPF KSEKVVVEDT VPIIPKEKHA KEEDSSIDYD 

       970 
LNLPDTVTHE DYVTTRL 

« Hide

Isoform Beta [UniParc].

Checksum: 20E5FE3C93B47BB5
Show »

FASTA893102,640
Isoform Delta [UniParc].

Checksum: 1BAE1CA946ED6DAF
Show »

FASTA83696,389
Isoform Gamma [UniParc].

Checksum: C01141A15CCA516C
Show »

FASTA82894,859
Isoform Epsilon [UniParc].

Checksum: 7F4500A57F38B8BD
Show »

FASTA982112,723
Isoform Zeta [UniParc].

Checksum: 30F8E11810A76888
Show »

FASTA80492,221
Isoform Eta [UniParc].

Checksum: 39B4E28D03534CDD
Show »

FASTA32336,759

References

« Hide 'large scale' references
[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]"Functional differences between TRPC4 splice variants."
Schaefer M., Plant T.D., Stresow N., Albrecht N., Schultz G.
J. Biol. Chem. 277:3752-3759(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-138.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001129427.1. NM_001135955.1.
NP_001129428.1. NM_001135956.1.
NP_001129429.1. NM_001135957.1.
NP_001129430.1. NM_001135958.1.
NP_003297.1. NM_003306.1.
NP_057263.1. NM_016179.2.
UniGeneHs.262960.

3D structure databases

ProteinModelPortalQ9UBN4.
SMRQ9UBN4. Positions 36-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113074. 13 interactions.
IntActQ9UBN4. 2 interactions.
MINTMINT-157838.
STRING9606.ENSP00000369003.

Chemistry

GuidetoPHARMACOLOGY489.

PTM databases

PhosphoSiteQ9UBN4.

Polymorphism databases

DMDM13633994.

Proteomic databases

PaxDbQ9UBN4.
PRIDEQ9UBN4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338947; ENSP00000342580; ENSG00000133107. [Q9UBN4-6]
ENST00000355779; ENSP00000348025; ENSG00000133107. [Q9UBN4-3]
ENST00000358477; ENSP00000351264; ENSG00000133107. [Q9UBN4-2]
ENST00000379673; ENSP00000368995; ENSG00000133107. [Q9UBN4-4]
ENST00000379679; ENSP00000369001; ENSG00000133107. [Q9UBN4-6]
ENST00000379681; ENSP00000369003; ENSG00000133107. [Q9UBN4-5]
ENST00000379705; ENSP00000369027; ENSG00000133107. [Q9UBN4-1]
ENST00000447043; ENSP00000414316; ENSG00000133107. [Q9UBN4-3]
ENST00000488717; ENSP00000435969; ENSG00000133107. [Q9UBN4-7]
GeneID7223.
KEGGhsa:7223.
UCSCuc001uws.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

CTD7223.
GeneCardsGC13M038210.
HGNCHGNC:12336. TRPC4.
MIM603651. gene.
neXtProtNX_Q9UBN4.
PharmGKBPA37009.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG254238.
HOVERGENHBG068337.
KOK04967.
OMAGLSEQCI.
OrthoDBEOG72G17P.
PhylomeDBQ9UBN4.
TreeFamTF313147.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ9UBN4.
BgeeQ9UBN4.
CleanExHS_TRPC4.
GenevestigatorQ9UBN4.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. 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]
PANTHERPTHR10117. PTHR10117. 1 hit.
PTHR10117:SF25. PTHR10117:SF25. 1 hit.
PfamPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF08344. TRP_2. 1 hit.
[Graphical view]
PRINTSPR01097. TRNSRECEPTRP.
PR01645. TRPCHANNEL4.
SMARTSM00248. ANK. 2 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
TIGRFAMsTIGR00870. trp. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRPC4. human.
GeneWikiTRPC4.
GenomeRNAi7223.
NextBio28287.
PROQ9UBN4.
SOURCESearch...

Entry information

Entry nameTRPC4_HUMAN
AccessionPrimary (citable) accession number: Q9UBN4
Secondary accession number(s): B1ALE0 expand/collapse secondary AC list , B1ALE1, B1ALE2, Q15721, Q3SWS6, Q96P03, Q96P04, Q96P05, Q9UIB0, Q9UIB1, Q9UIB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM