Thyroid hormone receptor-associated protein 3

Contribute

Send feedback

Read comments (?) or add your own

Q569Z6 (TR150_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	951 AA.
Sequence status	Complete.
Protein existence	Evidence 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 indepenedent 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 By similarity.
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 By similarity.
Subcellular location	Nucleus By similarity.

Ontologies

Keywords
Biological process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Activator Receptor
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara
Cellular_component	mediator complex Inferred from direct assay PubMed 12093747 PubMed 15340084. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA polymerase II transcription cofactor activity Inferred from electronic annotation. Source: Compara phosphoprotein binding Inferred from sequence or structural similarity. Source: UniProtKB receptor activity Inferred from electronic annotation. Source: Compara transcription coactivator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 951

951

Thyroid hormone receptor-associated protein 3

PRO_0000235980

Regions

Nucleotide binding

549 – 556

ATP Potential

Region

1 – 190

190

Required for mRNA splicing activation By similarity

Region

359 – 951

593

Required for mRNA decay activity By similarity

Compositional bias

7 – 339

333

Ser-rich

Compositional bias

12 – 161

150

Arg-rich

Amino acid modifications

Modified residue

Dimethylated arginine By similarity

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine Ref.7

Modified residue

119

Phosphoserine Ref.8

Modified residue

134

Phosphoserine Ref.8

Modified residue

221

N6-acetyllysine By similarity

Modified residue

233

Phosphoserine By similarity

Modified residue

238

Phosphoserine Ref.8

Modified residue

240

Phosphoserine By similarity

Modified residue

243

Phosphoserine Ref.6 Ref.8 Ref.9

Modified residue

248

Phosphoserine Ref.4 Ref.5 Ref.8 Ref.9

Modified residue

253

Phosphoserine Ref.4 Ref.5 Ref.9

Modified residue

257

Phosphoserine By similarity

Modified residue

264

Phosphoserine Ref.7

Modified residue

268

Phosphoserine Ref.7

Modified residue

315

Phosphoserine Ref.5 Ref.7

Modified residue

320

Phosphoserine Ref.5 Ref.7

Modified residue

324

Phosphothreonine Ref.5

Modified residue

339

Phosphoserine By similarity

Modified residue

379

Phosphoserine Ref.8

Modified residue

403

Phosphoserine Ref.7

Modified residue

405

Phosphoserine Ref.7

Modified residue

452

N6-acetyllysine By similarity

Modified residue

516

N6-acetyllysine By similarity

Modified residue

532

Phosphoserine By similarity

Modified residue

572

Phosphoserine Ref.2 Ref.3 Ref.7 Ref.8 Ref.9

Modified residue

619

Phosphoserine By similarity

Modified residue

669

Phosphoserine By similarity

Modified residue

679

Phosphoserine Ref.5 Ref.6 Ref.8 Ref.9

Modified residue

681

Phosphoserine By similarity

Modified residue

695

Phosphoserine Ref.8

Modified residue

808

N6-acetyllysine By similarity

Modified residue

860

Phosphoserine Ref.7

Modified residue

870

Phosphothreonine By similarity

Modified residue

924

Phosphoserine Ref.5 Ref.7 Ref.8

Modified residue

935

Phosphoserine Ref.3 Ref.5

Modified residue

937

Phosphothreonine Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q569Z6 [UniParc].

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

FASTA

951

108,178

        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

[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, MASS SPECTROMETRY. Tissue: Brain.
[3]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 AND SER-935, MASS SPECTROMETRY. Tissue: Liver.
[4]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-253, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
[5]	"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-248; SER-253; SER-315; SER-320; THR-324; SER-679; SER-924; SER-935 AND THR-937, MASS SPECTROMETRY. Tissue: Liver.
[6]	"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, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-53; SER-55; SER-264; SER-268; SER-315; SER-320; SER-403; SER-405; SER-572; SER-860 AND SER-924, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"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-119; SER-134; SER-238; SER-243; SER-248; SER-379; SER-572; SER-679; SER-695 AND SER-924, MASS SPECTROMETRY. Tissue: Macrophage.
[9]	"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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC092239 mRNA. Translation: AAH92239.1.
IPI	IPI00556768.
RefSeq	NP_666265.3. NM_146153.3.
UniGene	Mm.236211. Mm.29813.
3D structure databases
ProteinModelPortal	Q569Z6.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q569Z6. 3 interactions.
STRING	10090.ENSMUSP00000079722.
PTM databases
PhosphoSite	Q569Z6.
Proteomic databases
PaxDb	Q569Z6.
PRIDE	Q569Z6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
GeneID	230753.
KEGG	mmu:230753.
Organism-specific databases
CTD	9967.
MGI	MGI:2442637. Thrap3.
Phylogenomic databases
eggNOG	NOG43306.
GeneTree	ENSGT00530000063211.
HOGENOM	HOG000231570.
HOVERGEN	HBG054554.
InParanoid	Q569Z6.
KO	K13112.
OMA	KMKEKGS.
OrthoDB	EOG4NKBVJ.
Gene expression databases
ArrayExpress	Q569Z6.
Bgee	Q569Z6.
CleanEx	MM_THRAP3.
Genevestigator	Q569Z6.
GermOnline	ENSMUSG00000043962. Mus musculus.
Family and domain databases
InterPro	IPR026667. THRAP3. [Graphical view]
PANTHER	PTHR15268:SF7. PTHR15268:SF7. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	THRAP3. mouse.
NextBio	380111.
SOURCE	Search...

Entry information

Entry name

TR150_MOUSE

Accession

Primary (citable) accession number: Q569Z6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2006
Last sequence update:	May 10, 2005
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents