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Protein

Thyroid hormone receptor-associated protein 3

Gene

Thrap3

Organism
Mus musculus (Mouse)
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).2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi549 – 556ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2442637. Thrap3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002359802 – 951Thyroid hormone receptor-associated protein 3Add BLAST950

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei17Dimethylated arginineBy similarity1
Modified residuei66Asymmetric dimethylarginineBy similarity1
Modified residuei101Asymmetric dimethylarginineCombined sources1
Modified residuei108Asymmetric dimethylarginineCombined sources1
Cross-linki202Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei220PhosphoserineBy similarity1
Modified residuei221N6-acetyllysineBy similarity1
Modified residuei233PhosphoserineCombined sources1
Modified residuei238PhosphoserineCombined sources1
Modified residuei240PhosphoserineBy similarity1
Modified residuei243PhosphoserineCombined sources1
Modified residuei248PhosphoserineCombined sources1
Modified residuei252N6-methyllysineBy similarity1
Modified residuei253PhosphoserineCombined sources1
Modified residuei257PhosphoserineBy similarity1
Modified residuei315PhosphoserineCombined sources1
Modified residuei320PhosphoserineCombined sources1
Modified residuei324PhosphothreonineCombined sources1
Modified residuei326PhosphoserineBy similarity1
Modified residuei328PhosphotyrosineCombined sources1
Modified residuei339PhosphoserineBy similarity1
Modified residuei346N6-acetyllysineCombined sources1
Modified residuei379PhosphoserineCombined sources1
Cross-linki384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei394PhosphothreonineBy similarity1
Modified residuei403PhosphoserineBy similarity1
Modified residuei405PhosphoserineBy similarity1
Cross-linki424Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki448Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei452N6-acetyllysineCombined sources1
Cross-linki465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei466PhosphoserineBy similarity1
Modified residuei468N6-acetyllysine; alternateCombined sources1
Cross-linki468Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei476N6-acetyllysineCombined sources1
Cross-linki481Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei516N6-acetyllysineBy similarity1
Modified residuei524N6-acetyllysine; alternateCombined sources1
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei532PhosphoserineBy similarity1
Modified residuei555N6-acetyllysineCombined sources1
Modified residuei557PhosphoserineBy similarity1
Modified residuei559PhosphoserineBy similarity1
Modified residuei572PhosphoserineCombined sources1
Modified residuei616PhosphoserineBy similarity1
Modified residuei619PhosphoserineBy similarity1
Modified residuei669PhosphoserineBy similarity1
Modified residuei679PhosphoserineCombined sources1
Modified residuei681PhosphoserineBy similarity1
Cross-linki694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei695PhosphoserineBy similarity1
Cross-linki702Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki708Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki753Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei808N6-acetyllysineBy similarity1
Modified residuei841Asymmetric dimethylarginineCombined sources1
Modified residuei860PhosphoserineBy similarity1
Modified residuei870PhosphothreonineCombined sources1
Modified residuei924PhosphoserineCombined sources1
Modified residuei935PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ569Z6.
MaxQBiQ569Z6.
PaxDbiQ569Z6.
PeptideAtlasiQ569Z6.
PRIDEiQ569Z6.

PTM databases

iPTMnetiQ569Z6.
PhosphoSitePlusiQ569Z6.

Expressioni

Inductioni

Expressed in a circadian manner in the liver with a peak at approximately circadian time (CT) 8 hours (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000043962.
CleanExiMM_THRAP3.
ExpressionAtlasiQ569Z6. baseline and differential.
GenevisibleiQ569Z6. MM.

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 similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi231014. 3 interactors.
IntActiQ569Z6. 6 interactors.
STRINGi10090.ENSMUSP00000079722.

Structurei

3D structure databases

ProteinModelPortaliQ569Z6.
SMRiQ569Z6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 190Required for mRNA splicing activationBy similarityAdd BLAST189
Regioni359 – 951Required for mRNA decay activityBy similarityAdd BLAST593

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.
InParanoidiQ569Z6.
KOiK13112.
OMAiRSTEKTE.
OrthoDBiEOG091G03HU.
PhylomeDBiQ569Z6.
TreeFamiTF335939.

Family and domain databases

InterProiIPR026667. THRAP3.
IPR029199. THRAP3_BCLAF1.
[Graphical view]
PANTHERiPTHR15268:SF16. PTHR15268:SF16. 1 hit.
PfamiPF15440. THRAP3_BCLAF1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q569Z6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS 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 SSKRKSTKEK KSSSKDSRPS QAAGDNQGDE
210 220 230 240 250
AKEQTFSGGT SQDIKGSESS KPWPDATTYG AGSASRASVS DLSPRERSPA
260 270 280 290 300
LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG
310 320 330 340 350
QFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYSKRYLE
360 370 380 390 400
EQKTENGKDK EQKQTNADKE KLKEKGGFSD ADVKMKSDPF APKTDSEKPF
410 420 430 440 450
RGSQSPKRYK LRDDFEKKMA DFHKEELDEH DKDKSKGRKE PEFDDEPKFM
460 470 480 490 500
SKVIAGASKN QEEEKSGKWE SLHTGKEKQR KAEEMEDEPF TERSRKEERG
510 520 530 540 550
GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE SRDKLGSKGD
560 570 580 590 600
FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK
610 620 630 640 650
EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER
660 670 680 690 700
FTKYLKRGNE QEAAKNKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG
710 720 730 740 750
YKAEGKYKDD PVDLRLDIER RKKHKERDLK RGKSRESVDS RDSSHSRERS
760 770 780 790 800
TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS SQSSHSYKAE EYPEEAEERE
810 820 830 840 850
ESTSGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG RGNYSGNNNN
860 870 880 890 900
NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MGRGRGRGAF
910 920 930 940 950
PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA

E
Length:951
Mass (Da):108,178
Last modified:May 10, 2005 - v1
Checksum:i40DF483027363B4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC092239 mRNA. Translation: AAH92239.1.
CCDSiCCDS18645.1.
RefSeqiNP_666265.3. NM_146153.3.
XP_006503104.1. XM_006503041.3.
XP_011238805.1. XM_011240503.2.
UniGeneiMm.236211.
Mm.29813.

Genome annotation databases

EnsembliENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
GeneIDi230753.
KEGGimmu:230753.
UCSCiuc008usv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC092239 mRNA. Translation: AAH92239.1.
CCDSiCCDS18645.1.
RefSeqiNP_666265.3. NM_146153.3.
XP_006503104.1. XM_006503041.3.
XP_011238805.1. XM_011240503.2.
UniGeneiMm.236211.
Mm.29813.

3D structure databases

ProteinModelPortaliQ569Z6.
SMRiQ569Z6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231014. 3 interactors.
IntActiQ569Z6. 6 interactors.
STRINGi10090.ENSMUSP00000079722.

PTM databases

iPTMnetiQ569Z6.
PhosphoSitePlusiQ569Z6.

Proteomic databases

EPDiQ569Z6.
MaxQBiQ569Z6.
PaxDbiQ569Z6.
PeptideAtlasiQ569Z6.
PRIDEiQ569Z6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
GeneIDi230753.
KEGGimmu:230753.
UCSCiuc008usv.1. mouse.

Organism-specific databases

CTDi9967.
MGIiMGI:2442637. Thrap3.

Phylogenomic databases

eggNOGiENOG410IE11. Eukaryota.
ENOG410ZR5P. LUCA.
GeneTreeiENSGT00530000063211.
HOGENOMiHOG000231570.
HOVERGENiHBG054554.
InParanoidiQ569Z6.
KOiK13112.
OMAiRSTEKTE.
OrthoDBiEOG091G03HU.
PhylomeDBiQ569Z6.
TreeFamiTF335939.

Enzyme and pathway databases

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

ChiTaRSiThrap3. mouse.
PROiQ569Z6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000043962.
CleanExiMM_THRAP3.
ExpressionAtlasiQ569Z6. baseline and differential.
GenevisibleiQ569Z6. MM.

Family and domain databases

InterProiIPR026667. THRAP3.
IPR029199. THRAP3_BCLAF1.
[Graphical view]
PANTHERiPTHR15268:SF16. PTHR15268:SF16. 1 hit.
PfamiPF15440. THRAP3_BCLAF1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTR150_MOUSE
AccessioniPrimary (citable) accession number: Q569Z6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) 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.