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Protein

Thyroid hormone receptor-associated protein 3

Gene

THRAP3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing. Remains associated with spliced mRNA after splicing which probably involves interactions with the exon junction complex (EJC). Can trigger mRNA decay which seems to be independent of nonsense-mediated decay involving premature stop codons (PTC) recognition. May be involved in nuclear mRNA decay. Involved in regulation of signal-induced alternative splicing. During splicing of PTPRC/CD45 is proposed to sequester phosphorylated SFPQ from PTPRC/CD45 pre-mRNA in resting T-cells. Involved in cyclin-D1/CCND1 mRNA stability probably by acting as component of the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in response to DNA damage. Is excluced from DNA damage sites in a manner that parallels transcription inhibition; the function may involve the SNARP complex. Initially thought to play a role in transcriptional coactivation through its association with the TRAP complex; however, it is not regarded as a stable Mediator complex subunit. Cooperatively with HELZ2, enhances the transcriptional activation mediated by PPARG, maybe through the stabilization of the PPARG binding to DNA in presence of ligand. May play a role in the terminal stage of adipocyte differentiation. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-ARNTL/BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798).5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi552 – 559ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • core promoter sequence-specific DNA binding Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • phosphoprotein binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • receptor activity Source: UniProtKB
  • RNA polymerase II transcription cofactor activity Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription coactivator activity Source: MGI
  • transcription cofactor activity Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

GO - Biological processi

  • androgen receptor signaling pathway Source: UniProtKB
  • circadian rhythm Source: Ensembl
  • intracellular steroid hormone receptor signaling pathway Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
  • mRNA stabilization Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process Source: UniProtKB
  • positive regulation of circadian rhythm Source: UniProtKB
  • positive regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  • RNA splicing Source: UniProtKB-KW
  • transcription initiation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000054118-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9Y2W1.
SIGNORiQ9Y2W1.

Names & Taxonomyi

Protein namesi
Recommended name:
Thyroid hormone receptor-associated protein 3
Alternative name(s):
Thyroid hormone receptor-associated protein complex 150 kDa component
Short name:
Trap150
Gene namesi
Name:THRAP3
Synonyms:TRAP150
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:22964. THRAP3.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • mediator complex Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi406S → A: Reduces phosphorylation upon DNA damage; when associated with A-408. 1 Publication1
Mutagenesisi408S → A: Reduces phosphorylation upon DNA damage; when associated with A-406. 1 Publication1

Organism-specific databases

DisGeNETi9967.
OpenTargetsiENSG00000054118.
PharmGKBiPA134893249.

Polymorphism and mutation databases

BioMutaiTHRAP3.
DMDMi97537467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000655832 – 955Thyroid hormone receptor-associated protein 3Add BLAST954

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei17Dimethylated arginine1 Publication1
Modified residuei66Asymmetric dimethylarginineCombined sources1
Modified residuei101Asymmetric dimethylarginineCombined sources1
Modified residuei108Asymmetric dimethylarginineCombined sources1
Cross-linki202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei220PhosphoserineCombined sources1
Modified residuei221N6-acetyllysineCombined sources1
Modified residuei232PhosphoserineCombined sources1
Modified residuei237PhosphoserineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei243PhosphoserineCombined sources1 Publication1
Modified residuei248PhosphoserineCombined sources1
Modified residuei252N6-methyllysineCombined sources1
Modified residuei253PhosphoserineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei315PhosphoserineCombined sources1
Modified residuei320PhosphoserineCombined sources1 Publication1
Modified residuei323PhosphoserineCombined sources1
Modified residuei324PhosphothreonineBy similarity1
Modified residuei326PhosphoserineCombined sources1
Modified residuei328PhosphotyrosineBy similarity1
Modified residuei339PhosphoserineCombined sources1
Modified residuei346N6-acetyllysineBy similarity1
Modified residuei377PhosphoserineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Cross-linki387Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki396Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei397PhosphothreonineCombined sources1
Modified residuei406PhosphoserineCombined sources1
Modified residuei408PhosphoserineCombined sources1
Cross-linki427Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei444PhosphoserineCombined sources1
Cross-linki451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki451Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei455N6-acetyllysineCombined sources1
Cross-linki467Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei468PhosphoserineCombined sources1
Modified residuei470N6-acetyllysine; alternateBy similarity1
Cross-linki470Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei481N6-acetyllysineBy similarity1
Cross-linki486Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei519N6-acetyllysineCombined sources1
Modified residuei527N6-acetyllysine; alternateBy similarity1
Cross-linki527Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei535PhosphoserineCombined sources1
Modified residuei558N6-acetyllysineBy similarity1
Modified residuei560PhosphoserineCombined sources1
Modified residuei562PhosphoserineCombined sources1
Modified residuei575PhosphoserineCombined sources1
Modified residuei619PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
Modified residuei672PhosphoserineCombined sources1
Modified residuei682PhosphoserineCombined sources1 Publication1
Modified residuei684PhosphoserineCombined sources1
Cross-linki697Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei698PhosphoserineCombined sources1
Cross-linki705Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki711Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki759Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei811N6-acetyllysineCombined sources1
Modified residuei845Asymmetric dimethylarginineBy similarity1
Modified residuei874PhosphothreonineCombined sources1
Modified residuei928PhosphoserineCombined sources1
Modified residuei939PhosphoserineCombined sources1

Post-translational modificationi

ADP-ribosylation during genotoxic stress promotes accumulation in nuclear speckles.

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y2W1.
MaxQBiQ9Y2W1.
PaxDbiQ9Y2W1.
PeptideAtlasiQ9Y2W1.
PRIDEiQ9Y2W1.
TopDownProteomicsiQ9Y2W1.

PTM databases

iPTMnetiQ9Y2W1.
PhosphoSitePlusiQ9Y2W1.
SwissPalmiQ9Y2W1.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000054118.
CleanExiHS_THRAP3.
ExpressionAtlasiQ9Y2W1. baseline and differential.
GenevisibleiQ9Y2W1. HS.

Organism-specific databases

HPAiCAB017472.
HPA012041.
HPA063765.

Interactioni

Subunit structurei

Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of SFPQ to an ESS1 exonic splicing silencer element-containing RNA. Interacts with NXF1. Component of the SNARP complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN. Associated with spliced mRNP complexes. Interacts with HELZ2 and PPARG. Interacts with CLOCK and ARNTL/BMAL1 (By similarity). Component of the WTAP complex composed of WTAP, ZC3H13, CBLL1, KIAA1429, RBM15, BCLAF1 and THRAP3.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4A3P389192EBI-352039,EBI-299104
NXF1Q9UBU94EBI-352039,EBI-398874
SFPQP232466EBI-352039,EBI-355453
SNW1Q135734EBI-352039,EBI-632715

GO - Molecular functioni

  • phosphoprotein binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB
  • vitamin D receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115292. 127 interactors.
IntActiQ9Y2W1. 47 interactors.
MINTiMINT-1684118.
STRINGi9606.ENSP00000346634.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2W1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 190Required for mRNA splicing activationAdd BLAST189
Regioni359 – 955Required for mRNA decay activityAdd BLAST597

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 339Ser-richAdd BLAST333
Compositional biasi12 – 161Arg-richAdd BLAST150

Phylogenomic databases

eggNOGiENOG410IE11. Eukaryota.
ENOG410ZR5P. LUCA.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000231570.
HOVERGENiHBG054554.
InParanoidiQ9Y2W1.
KOiK13112.
OMAiRSTEKTE.
OrthoDBiEOG091G03HU.
PhylomeDBiQ9Y2W1.
TreeFamiTF335939.

Family and domain databases

InterProiIPR029199. THRAP3_BCLAF1.
[Graphical view]
PfamiPF15440. THRAP3_BCLAF1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Y2W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSLSRS RKRRLSSRSR
60 70 80 90 100
SRSYSPAHNR ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN
110 120 130 140 150
RGGYGNYRSN WQNYRQAYSP RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS
160 170 180 190 200
SDRSRRSSSS RSSSNHSRVE SSKRKSAKEK KSSSKDSRPS QAAGDNQGDE
210 220 230 240 250
AKEQTFSGGT SQDTKASESS KPWPDATYGT GSASRASAVS ELSPRERSPA
260 270 280 290 300
LKSPLQSVVV RRRSPRPSPV PKPSPPLSST SQMGSTLPSG AGYQSGTHQG
310 320 330 340 350
QFDHGSGSLS PSKKSPVGKS PPSTGSTYGS SQKEESAASG GAAYTKRYLE
360 370 380 390 400
EQKTENGKDK EQKQTNTDKE KIKEKGSFSD TGLGDGKMKS DSFAPKTDSE
410 420 430 440 450
KPFRGSQSPK RYKLRDDFEK KMADFHKEEM DDQDKDKAKG RKESEFDDEP
460 470 480 490 500
KFMSKVIGAN KNQEEEKSGK WEGLVYAPPG KEKQRKTEEL EEESFPERSK
510 520 530 540 550
KEDRGKRSEG GHRGFVPEKN FRVTAYKAVQ EKSSSPPPRK TSESRDKLGA
560 570 580 590 600
KGDFPTGKSS FSITREAQVN VRMDSFDEDL ARPSGLLAQE RKLCRDLVHS
610 620 630 640 650
NKKEQEFRSI FQHIQSAQSQ RSPSELFAQH IVTIVHHVKE HHFGSSGMTL
660 670 680 690 700
HERFTKYLKR GTEQEAAKNK KSPEIHRRID ISPSTFRKHG LAHDEMKSPR
710 720 730 740 750
EPGYKAEGKY KDDPVDLRLD IERRKKHKER DLKRGKSRES VDSRDSSHSR
760 770 780 790 800
ERSAEKTEKT HKGSKKQKKH RRARDRSRSS SSSSQSSHSY KAEEYTEETE
810 820 830 840 850
EREESTTGFD KSRLGTKDFV GPSERGGGRA RGTFQFRARG RGWGRGNYSG
860 870 880 890 900
NNNNNSNNDF QKRNREEEWD PEYTPKSKKY YLHDDREGEG SDKWVSRGRG
910 920 930 940 950
RGAFPRGRGR FMFRKSSTSP KWAHDKFSGE EGEIEDDESG TENREEKDNI

QPTTE
Length:955
Mass (Da):108,666
Last modified:May 16, 2006 - v2
Checksum:i01131D2479B8C0F4
GO

Sequence cautioni

The sequence AAH37554 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_024552201A → V.3 PublicationsCorresponds to variant rs6425977dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117756 mRNA. Translation: AAD22034.1.
AL591845 Genomic DNA. Translation: CAH71859.1.
CH471059 Genomic DNA. Translation: EAX07379.1.
CH471059 Genomic DNA. Translation: EAX07380.1.
BC037554 mRNA. Translation: AAH37554.1. Sequence problems.
BC112330 mRNA. Translation: AAI12331.1.
BC112350 mRNA. Translation: AAI12351.1.
CCDSiCCDS405.1.
RefSeqiNP_001308400.1. NM_001321471.1.
NP_001308402.1. NM_001321473.1.
NP_005110.2. NM_005119.3.
UniGeneiHs.744057.

Genome annotation databases

EnsembliENST00000354618; ENSP00000346634; ENSG00000054118.
ENST00000469141; ENSP00000433825; ENSG00000054118.
GeneIDi9967.
KEGGihsa:9967.
UCSCiuc001cae.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF117756 mRNA. Translation: AAD22034.1.
AL591845 Genomic DNA. Translation: CAH71859.1.
CH471059 Genomic DNA. Translation: EAX07379.1.
CH471059 Genomic DNA. Translation: EAX07380.1.
BC037554 mRNA. Translation: AAH37554.1. Sequence problems.
BC112330 mRNA. Translation: AAI12331.1.
BC112350 mRNA. Translation: AAI12351.1.
CCDSiCCDS405.1.
RefSeqiNP_001308400.1. NM_001321471.1.
NP_001308402.1. NM_001321473.1.
NP_005110.2. NM_005119.3.
UniGeneiHs.744057.

3D structure databases

ProteinModelPortaliQ9Y2W1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115292. 127 interactors.
IntActiQ9Y2W1. 47 interactors.
MINTiMINT-1684118.
STRINGi9606.ENSP00000346634.

PTM databases

iPTMnetiQ9Y2W1.
PhosphoSitePlusiQ9Y2W1.
SwissPalmiQ9Y2W1.

Polymorphism and mutation databases

BioMutaiTHRAP3.
DMDMi97537467.

Proteomic databases

EPDiQ9Y2W1.
MaxQBiQ9Y2W1.
PaxDbiQ9Y2W1.
PeptideAtlasiQ9Y2W1.
PRIDEiQ9Y2W1.
TopDownProteomicsiQ9Y2W1.

Protocols and materials databases

DNASUi9967.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354618; ENSP00000346634; ENSG00000054118.
ENST00000469141; ENSP00000433825; ENSG00000054118.
GeneIDi9967.
KEGGihsa:9967.
UCSCiuc001cae.5. human.

Organism-specific databases

CTDi9967.
DisGeNETi9967.
GeneCardsiTHRAP3.
HGNCiHGNC:22964. THRAP3.
HPAiCAB017472.
HPA012041.
HPA063765.
MIMi603809. gene.
neXtProtiNX_Q9Y2W1.
OpenTargetsiENSG00000054118.
PharmGKBiPA134893249.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IE11. Eukaryota.
ENOG410ZR5P. LUCA.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000231570.
HOVERGENiHBG054554.
InParanoidiQ9Y2W1.
KOiK13112.
OMAiRSTEKTE.
OrthoDBiEOG091G03HU.
PhylomeDBiQ9Y2W1.
TreeFamiTF335939.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000054118-MONOMER.
ReactomeiR-HSA-1989781. PPARA activates gene expression.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiQ9Y2W1.
SIGNORiQ9Y2W1.

Miscellaneous databases

ChiTaRSiTHRAP3. human.
GeneWikiiTHRAP3.
GenomeRNAii9967.
PROiQ9Y2W1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000054118.
CleanExiHS_THRAP3.
ExpressionAtlasiQ9Y2W1. baseline and differential.
GenevisibleiQ9Y2W1. HS.

Family and domain databases

InterProiIPR029199. THRAP3_BCLAF1.
[Graphical view]
PfamiPF15440. THRAP3_BCLAF1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTR150_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2W1
Secondary accession number(s): D3DPS5, Q5VTK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: May 16, 2006
Last modified: November 30, 2016
This is version 163 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.