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Q8TEL6

- TP4AP_HUMAN

UniProt

Q8TEL6 - TP4AP_HUMAN

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Protein
Short transient receptor potential channel 4-associated protein
Gene
TRPC4AP, C20orf188, TRRP4AP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 CHRM1.1 Publication

Pathwayi

GO - Molecular functioni

  1. phosphatase binding Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane transport Source: Reactome
  2. ion transmembrane transport Source: Reactome
  3. protein ubiquitination Source: UniProtKB
  4. transmembrane transport Source: Reactome
  5. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_169333. TRP channels.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:TRPC4AP
Synonyms:C20orf188, TRRP4AP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:16181. TRPC4AP.

Subcellular locationi

GO - Cellular componenti

  1. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  2. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 797796Short transient receptor potential channel 4-associated protein
PRO_0000072641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8TEL6.
PaxDbiQ8TEL6.
PRIDEiQ8TEL6.

PTM databases

PhosphoSiteiQ8TEL6.

Expressioni

Gene expression databases

ArrayExpressiQ8TEL6.
BgeeiQ8TEL6.
CleanExiHS_TRPC4AP.
GenevestigatoriQ8TEL6.

Organism-specific databases

HPAiHPA051197.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1CAP621362EBI-2559060,EBI-357253

Protein-protein interaction databases

BioGridi117569. 21 interactions.
DIPiDIP-42719N.
IntActiQ8TEL6. 5 interactions.
MINTiMINT-2844857.
STRINGi9606.ENSP00000252015.

Structurei

3D structure databases

ProteinModelPortaliQ8TEL6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 400399Interaction with TNFRSF1A By similarity
Add
BLAST

Phylogenomic databases

eggNOGiNOG42180.
HOGENOMiHOG000231794.
HOVERGENiHBG059886.
InParanoidiQ8TEL6.
KOiK11796.
OMAiHYLNKDK.
OrthoDBiEOG7P02H9.
PhylomeDBiQ8TEL6.
TreeFamiTF329145.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR022162. DUF3689.
[Graphical view]
PfamiPF12463. DUF3689. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8TEL6-1) [UniParc]FASTAAdd to Basket

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

MAAAPVAAGS GAGRGRRSAA TVAAWGGWGG RPRPGNILLQ LRQGQLTGRG    50
LVRAVQFTET FLTERDKQSK WSGIPQLLLK LHTTSHLHSD FVECQNILKE 100
ISPLLSMEAM AFVTEERKLT QETTYPNTYI FDLFGGVDLL VEILMRPTIS 150
IRGQKLKISD EMSKDCLSIL YNTCVCTEGV TKRLAEKNDF VIFLFTLMTS 200
KKTFLQTATL IEDILGVKKE MIRLDEVPNL SSLVSNFDQQ QLANFCRILA 250
VTISEMDTGN DDKHTLLAKN AQQKKSLSLG PSAAEINQAA LLSIPGFVER 300
LCKLATRKVS ESTGTASFLQ ELEEWYTWLD NALVLDALMR VANEESEHNQ 350
ASIVFPPPGA SEENGLPHTS ARTQLPQSMK IMHEIMYKLE VLYVLCVLLM 400
GRQRNQVHRM IAEFKLIPGL NNLFDKLIWR KHSASALVLH GHNQNCDCSP 450
DITLKIQFLR LLQSFSDHHE NKYLLLNNQE LNELSAISLK ANIPEVEAVL 500
NTDRSLVCDG KRGLLTRLLQ VMKKEPAESS FRFWQARAVE SFLRGTTSYA 550
DQMFLLKRGL LEHILYCIVD SECKSRDVLQ SYFDLLGELM KFNVDAFKRF 600
NKYINTDAKF QVFLKQINSS LVDSNMLVRC VTLSLDRFEN QVDMKVAEVL 650
SECRLLAYIS QVPTQMSFLF RLINIIHVQT LTQENVSCLN TSLVILMLAR 700
RKERLPLYLR LLQRMEHSKK YPGFLLNNFH NLLRFWQQHY LHKDKDSTCL 750
ENSSCISFSY WKETVSILLN PDRQSPSALV SYIEEPYMDI DRDFTEE 797
Length:797
Mass (Da):90,852
Last modified:November 15, 2002 - v2
Checksum:i999A8CA3B0D2CEEE
GO
Isoform 2 (identifier: Q8TEL6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     533-797: Missing.

Note: No experimental confirmation available.

Show »
Length:532
Mass (Da):59,547
Checksum:iD9E123C910E93950
GO
Isoform 3 (identifier: Q8TEL6-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     351-358: Missing.

Show »
Length:789
Mass (Da):90,043
Checksum:i8FF952722B28B257
GO

Sequence cautioni

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 3588Missing in isoform 3.
VSP_054231
Alternative sequencei533 – 797265Missing in isoform 2.
VSP_003982Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK074106 mRNA. Translation: BAB84932.1. Frameshift.
AB590540 mRNA. Translation: BAJ20695.1.
AL132825 Genomic DNA. Translation: CAC14946.1.
CH471077 Genomic DNA. Translation: EAW76233.1.
CH471077 Genomic DNA. Translation: EAW76235.1.
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.
CCDSiCCDS13246.1. [Q8TEL6-1]
CCDS46591.1. [Q8TEL6-3]
PIRiT17263.
RefSeqiNP_056453.1. NM_015638.2. [Q8TEL6-1]
NP_955400.1. NM_199368.1. [Q8TEL6-3]
UniGeneiHs.168073.

Genome annotation databases

EnsembliENST00000252015; ENSP00000252015; ENSG00000100991. [Q8TEL6-1]
ENST00000451813; ENSP00000400614; ENSG00000100991.
GeneIDi26133.
KEGGihsa:26133.
UCSCiuc002xbk.3. human. [Q8TEL6-1]
uc002xbl.3. human.

Polymorphism databases

DMDMi25091357.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK074106 mRNA. Translation: BAB84932.1 . Frameshift.
AB590540 mRNA. Translation: BAJ20695.1 .
AL132825 Genomic DNA. Translation: CAC14946.1 .
CH471077 Genomic DNA. Translation: EAW76233.1 .
CH471077 Genomic DNA. Translation: EAW76235.1 .
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 .
CCDSi CCDS13246.1. [Q8TEL6-1 ]
CCDS46591.1. [Q8TEL6-3 ]
PIRi T17263.
RefSeqi NP_056453.1. NM_015638.2. [Q8TEL6-1 ]
NP_955400.1. NM_199368.1. [Q8TEL6-3 ]
UniGenei Hs.168073.

3D structure databases

ProteinModelPortali Q8TEL6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117569. 21 interactions.
DIPi DIP-42719N.
IntActi Q8TEL6. 5 interactions.
MINTi MINT-2844857.
STRINGi 9606.ENSP00000252015.

PTM databases

PhosphoSitei Q8TEL6.

Polymorphism databases

DMDMi 25091357.

Proteomic databases

MaxQBi Q8TEL6.
PaxDbi Q8TEL6.
PRIDEi Q8TEL6.

Protocols and materials databases

DNASUi 26133.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252015 ; ENSP00000252015 ; ENSG00000100991 . [Q8TEL6-1 ]
ENST00000451813 ; ENSP00000400614 ; ENSG00000100991 .
GeneIDi 26133.
KEGGi hsa:26133.
UCSCi uc002xbk.3. human. [Q8TEL6-1 ]
uc002xbl.3. human.

Organism-specific databases

CTDi 26133.
GeneCardsi GC20M033590.
HGNCi HGNC:16181. TRPC4AP.
HPAi HPA051197.
MIMi 608430. gene.
neXtProti NX_Q8TEL6.
PharmGKBi PA25730.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42180.
HOGENOMi HOG000231794.
HOVERGENi HBG059886.
InParanoidi Q8TEL6.
KOi K11796.
OMAi HYLNKDK.
OrthoDBi EOG7P02H9.
PhylomeDBi Q8TEL6.
TreeFami TF329145.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_169333. TRP channels.

Miscellaneous databases

ChiTaRSi TRPC4AP. human.
GeneWikii TRPC4AP.
GenomeRNAii 26133.
NextBioi 48157.
PROi Q8TEL6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8TEL6.
Bgeei Q8TEL6.
CleanExi HS_TRPC4AP.
Genevestigatori Q8TEL6.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR022162. DUF3689.
[Graphical view ]
Pfami PF12463. DUF3689. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 2 AND 3).
  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.
    , 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. 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. 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.
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTP4AP_HUMAN
AccessioniPrimary (citable) accession number: Q8TEL6
Secondary accession number(s): E1P5Q0
, E1P5Q1, Q96H82, Q9BVB8, Q9H429, Q9UFS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: September 3, 2014
This is version 108 of the entry and version 2 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 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways

External Data

Dasty 3

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