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Q8TEL6 (TP4AP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-associated protein

Short name=Trp4-associated protein
Short name=Trpc4-associated protein
Alternative name(s):
Protein TAP1
TNF-receptor ubiquitous scaffolding/signaling protein
Short name=Protein TRUSS
Gene names
Name:TRPC4AP
Synonyms:C20orf188, TRRP4AP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length797 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control. The DCX(TRUSS) complex specifically mediates the polyubiquitination and subsequent degradation of MYC. Also participates in the activation of NFKB1 in response to ligation of TNFRSF1A, possibly by linking TNFRSF1A to the IKK signalosome. Involved in JNK activation via its interaction with TRAF2. Also involved in elevation of endoplasmic reticulum Ca2+ storage reduction in response to CHRM1. Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Constitutively associated with TNFRSF1A. Directly interacts with TRADD, TRAF2, CHUK, IKBKB and IKBKG. Interacts with TRPC1, TRPC4 and TRPC5 By similarity. Component of the DCX(TRUSS) E3 ubiquitin ligase complex, at least composed of CUL4A, DDB1, TRPC4AP/TRUSS and RBX1. Interacts with MYC. Ref.6

Sequence caution

The sequence BAB84932.1 differs from that shown. Reason: Frameshift at position 43.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein ubiquitination

Inferred from direct assay Ref.6. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.6. Source: UniProtKB

   Cellular_componentCul4A-RING ubiquitin ligase complex

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionphosphatase binding

Inferred from direct assay PubMed 19389623. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP1CAP621362EBI-2559060,EBI-357253

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TEL6-1)

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 2 (identifier: Q8TEL6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     533-797: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 797797Short transient receptor potential channel 4-associated protein
PRO_0000072641

Regions

Region1 – 400400Interaction with TNFRSF1A By similarity

Natural variations

Alternative sequence533 – 797265Missing in isoform 2.
VSP_003982

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: 999A8CA3B0D2CEEE

FASTA79790,852
        10         20         30         40         50         60 
MAAAPVAAGS GAGRGRRSAA TVAAWGGWGG RPRPGNILLQ LRQGQLTGRG LVRAVQFTET 

        70         80         90        100        110        120 
FLTERDKQSK WSGIPQLLLK LHTTSHLHSD FVECQNILKE ISPLLSMEAM AFVTEERKLT 

       130        140        150        160        170        180 
QETTYPNTYI FDLFGGVDLL VEILMRPTIS IRGQKLKISD EMSKDCLSIL YNTCVCTEGV 

       190        200        210        220        230        240 
TKRLAEKNDF VIFLFTLMTS KKTFLQTATL IEDILGVKKE MIRLDEVPNL SSLVSNFDQQ 

       250        260        270        280        290        300 
QLANFCRILA VTISEMDTGN DDKHTLLAKN AQQKKSLSLG PSAAEINQAA LLSIPGFVER 

       310        320        330        340        350        360 
LCKLATRKVS ESTGTASFLQ ELEEWYTWLD NALVLDALMR VANEESEHNQ ASIVFPPPGA 

       370        380        390        400        410        420 
SEENGLPHTS ARTQLPQSMK IMHEIMYKLE VLYVLCVLLM GRQRNQVHRM IAEFKLIPGL 

       430        440        450        460        470        480 
NNLFDKLIWR KHSASALVLH GHNQNCDCSP DITLKIQFLR LLQSFSDHHE NKYLLLNNQE 

       490        500        510        520        530        540 
LNELSAISLK ANIPEVEAVL NTDRSLVCDG KRGLLTRLLQ VMKKEPAESS FRFWQARAVE 

       550        560        570        580        590        600 
SFLRGTTSYA DQMFLLKRGL LEHILYCIVD SECKSRDVLQ SYFDLLGELM KFNVDAFKRF 

       610        620        630        640        650        660 
NKYINTDAKF QVFLKQINSS LVDSNMLVRC VTLSLDRFEN QVDMKVAEVL SECRLLAYIS 

       670        680        690        700        710        720 
QVPTQMSFLF RLINIIHVQT LTQENVSCLN TSLVILMLAR RKERLPLYLR LLQRMEHSKK 

       730        740        750        760        770        780 
YPGFLLNNFH NLLRFWQQHY LHKDKDSTCL ENSSCISFSY WKETVSILLN PDRQSPSALV 

       790 
SYIEEPYMDI DRDFTEE 

« Hide

Isoform 2 [UniParc].

Checksum: D9E123C910E93950
Show »

FASTA53259,547

References

« Hide 'large scale' references
[1]"Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones."
Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N., Ohara O.
DNA Res. 10:49-57(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Spleen.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Cervix, Muscle and Prostate.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-797 (ISOFORM 1).
Tissue: Mammary cancer.
[6]"Myc protein is stabilized by suppression of a novel E3 ligase complex in cancer cells."
Choi S.H., Wright J.B., Gerber S.A., Cole M.D.
Genes Dev. 24:1236-1241(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, INTERACTION WITH MYC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK074106 mRNA. Translation: BAB84932.1. Frameshift.
AL132825 Genomic DNA. Translation: CAC14946.1.
CH471077 Genomic DNA. Translation: EAW76229.1.
CH471077 Genomic DNA. Translation: EAW76234.1.
BC001323 mRNA. Translation: AAH01323.1.
BC008836 mRNA. Translation: AAH08836.2.
BC013144 mRNA. Translation: AAH13144.1.
AL117480 mRNA. Translation: CAB55953.1.
IPIIPI00152769.
IPI00219534.
PIRT17263.
RefSeqNP_056453.1. NM_015638.2.
NP_955400.1. NM_199368.1.
UniGeneHs.168073.

3D structure databases

ProteinModelPortalQ8TEL6.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-42719N.
IntActQ8TEL6. 3 interactions.
MINTMINT-2844857.
STRING9606.ENSP00000252015.

PTM databases

PhosphoSiteQ8TEL6.

Polymorphism databases

DMDM25091357.

Proteomic databases

PaxDbQ8TEL6.
PRIDEQ8TEL6.

Protocols and materials databases

DNASU26133.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252015; ENSP00000252015; ENSG00000100991.
GeneID26133.
KEGGhsa:26133.
UCSCuc002xbk.3. human.

Organism-specific databases

CTD26133.
GeneCardsGC20M033590.
HGNCHGNC:16181. TRPC4AP.
HPAHPA051197.
MIM608430. gene.
neXtProtNX_Q8TEL6.
PharmGKBPA25730.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42180.
HOGENOMHOG000231794.
HOVERGENHBG059886.
InParanoidQ8TEL6.
KOK11796.
OMAQESTFPN.
OrthoDBEOG49KFQ0.
PhylomeDBQ8TEL6.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ8TEL6.
BgeeQ8TEL6.
CleanExHS_TRPC4AP.
GenevestigatorQ8TEL6.
GermOnlineENSG00000100991. Homo sapiens.

Family and domain databases

InterProIPR022162. DUF3689.
[Graphical view]
PfamPF12463. DUF3689. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTRPC4AP. human.
GenomeRNAi26133.
NextBio48157.
SOURCESearch...

Entry information

Entry nameTP4AP_HUMAN
AccessionPrimary (citable) accession number: Q8TEL6
Secondary accession number(s): E1P5Q1 expand/collapse secondary AC list , Q96H82, Q9BVB8, Q9H429, Q9UFS6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: May 1, 2013
This is version 97 of the entry and version 2 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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways