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Q569Z6 (TR150_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thyroid hormone receptor-associated protein 3
Alternative name(s):
Thyroid hormone receptor-associated protein complex 150 kDa component
Short name=Trap150
Gene names
Name:Thrap3
Synonyms:Trap150
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length951 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

Associated with the large multiprotein complex TRAP (Mediator complex-like). Interacts with SFPQ; the interaction is dependent on SFPQ phosphorylation at 'Thr-679' 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. Ref.8

Subcellular location

Nucleus Ref.8.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Receptor
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear-transcribed mRNA catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of alternative mRNA splicing, via spliceosome

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred by curator PubMed 12093747. Source: MGI

transcription initiation from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentexon-exon junction complex

Inferred from electronic annotation. Source: Ensembl

mediator complex

Inferred from direct assay PubMed 12093747PubMed 15340084. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription cofactor activity

Inferred from electronic annotation. Source: Ensembl

phosphoprotein binding

Inferred from sequence or structural similarity. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: Ensembl

transcription coactivator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 951950Thyroid hormone receptor-associated protein 3
PRO_0000235980

Regions

Nucleotide binding549 – 5568ATP Potential
Region2 – 190189Required for mRNA splicing activation By similarity
Region359 – 951593Required for mRNA decay activity By similarity
Compositional bias7 – 339333Ser-rich
Compositional bias12 – 161150Arg-rich

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue171Dimethylated arginine By similarity
Modified residue2211N6-acetyllysine By similarity
Modified residue2331Phosphoserine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2401Phosphoserine By similarity
Modified residue2431Phosphoserine Ref.3 Ref.4 Ref.6
Modified residue2481Phosphoserine Ref.6
Modified residue2531Phosphoserine Ref.6
Modified residue2571Phosphoserine By similarity
Modified residue3151Phosphoserine Ref.3
Modified residue3201Phosphoserine Ref.3
Modified residue3391Phosphoserine By similarity
Modified residue3461N6-acetyllysine
Modified residue3791Phosphoserine Ref.3 Ref.5
Modified residue4031Phosphoserine By similarity
Modified residue4051Phosphoserine By similarity
Modified residue4521N6-acetyllysine
Modified residue4681N6-acetyllysine
Modified residue4761N6-acetyllysine
Modified residue5161N6-acetyllysine By similarity
Modified residue5241N6-acetyllysine
Modified residue5321Phosphoserine By similarity
Modified residue5551N6-acetyllysine
Modified residue5721Phosphoserine Ref.2 Ref.5 Ref.6
Modified residue6191Phosphoserine By similarity
Modified residue6691Phosphoserine By similarity
Modified residue6791Phosphoserine Ref.4 Ref.5 Ref.6
Modified residue6951Phosphoserine By similarity
Modified residue8081N6-acetyllysine By similarity
Modified residue8701Phosphothreonine By similarity
Modified residue9241Phosphoserine Ref.3 Ref.5
Modified residue9351Phosphoserine Ref.3 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q569Z6 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 40DF483027363B4E

FASTA951108,178
        10         20         30         40         50         60 
MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS RKRRLSSRSR SRSYSPAHNR 

        70         80         90        100        110        120 
ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP 

       130        140        150        160        170        180 
RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSTKEK 

       190        200        210        220        230        240 
KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDIKGSESS KPWPDATTYG AGSASRASVS 

       250        260        270        280        290        300 
DLSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG 

       310        320        330        340        350        360 
QFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYSKRYLE EQKTENGKDK 

       370        380        390        400        410        420 
EQKQTNADKE KLKEKGGFSD ADVKMKSDPF APKTDSEKPF RGSQSPKRYK LRDDFEKKMA 

       430        440        450        460        470        480 
DFHKEELDEH DKDKSKGRKE PEFDDEPKFM SKVIAGASKN QEEEKSGKWE SLHTGKEKQR 

       490        500        510        520        530        540 
KAEEMEDEPF TERSRKEERG GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE 

       550        560        570        580        590        600 
SRDKLGSKGD FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK 

       610        620        630        640        650        660 
EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER FTKYLKRGNE 

       670        680        690        700        710        720 
QEAAKNKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG YKAEGKYKDD PVDLRLDIER 

       730        740        750        760        770        780 
RKKHKERDLK RGKSRESVDS RDSSHSRERS TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS 

       790        800        810        820        830        840 
SQSSHSYKAE EYPEEAEERE ESTSGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG 

       850        860        870        880        890        900 
RGNYSGNNNN NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MGRGRGRGAF 

       910        920        930        940        950 
PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA E 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: C57BL/6.
Tissue: Head.
[2]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-315; SER-320; SER-379; SER-924 AND SER-935, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379; SER-572; SER-679; SER-924 AND SER-935, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248; SER-253; SER-572 AND SER-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[7]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-346; LYS-452; LYS-468; LYS-476; LYS-524 AND LYS-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[8]"THRAP3 interacts with HELZ2 and plays a novel role in adipocyte differentiation."
Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S., Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K., Okada S., Yamada M., Mori M.
Mol. Endocrinol. 27:769-780(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HELZ2 AND PPARG, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC092239 mRNA. Translation: AAH92239.1.
RefSeqNP_666265.3. NM_146153.3.
XP_006503104.1. XM_006503041.1.
UniGeneMm.236211.
Mm.29813.

3D structure databases

ProteinModelPortalQ569Z6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid231014. 2 interactions.
IntActQ569Z6. 4 interactions.
STRING10090.ENSMUSP00000079722.

PTM databases

PhosphoSiteQ569Z6.

Proteomic databases

PaxDbQ569Z6.
PRIDEQ569Z6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
GeneID230753.
KEGGmmu:230753.
UCSCuc008usv.1. mouse.

Organism-specific databases

CTD9967.
MGIMGI:2442637. Thrap3.

Phylogenomic databases

eggNOGNOG43306.
GeneTreeENSGT00530000063211.
HOGENOMHOG000231570.
HOVERGENHBG054554.
InParanoidQ569Z6.
KOK13112.
OMARSTEKTE.
OrthoDBEOG7RBZ7X.
TreeFamTF335939.

Gene expression databases

ArrayExpressQ569Z6.
BgeeQ569Z6.
CleanExMM_THRAP3.
GenevestigatorQ569Z6.

Family and domain databases

InterProIPR026667. THRAP3.
[Graphical view]
PANTHERPTHR15268:SF7. PTHR15268:SF7. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTHRAP3. mouse.
NextBio380111.
PROQ569Z6.
SOURCESearch...

Entry information

Entry nameTR150_MOUSE
AccessionPrimary (citable) accession number: Q569Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 10, 2005
Last modified: March 19, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot