THRAP3
entrez
9967
canonical
uniprot
Q9Y2W1
canonical
ensembl
ENSG00000054118
resolver
ensp
ENSP00000346634
resolver
ensp
ENSP00000433825
resolver
ensp
ENSP00000554238
resolver
ensp
ENSP00000554239
resolver
ensp
ENSP00000554240
resolver
ensp
ENSP00000554241
resolver
ensp
ENSP00000554242
resolver
ensp
ENSP00000609562
resolver
ensp
ENSP00000609563
resolver
ensp
ENSP00000609564
resolver
ensp
ENSP00000609565
resolver
ensp
ENSP00000609568
resolver
ensp
ENSP00000609570
resolver
ensp
ENSP00000609571
resolver
ensp
ENSP00000609573
resolver
ensp
ENSP00000624177
resolver
ensp
ENSP00000624179
resolver
enst
ENST00000354618
resolver
enst
ENST00000469141
resolver
enst
ENST00000884179
resolver
enst
ENST00000884182
resolver
enst
ENST00000884183
resolver
enst
ENST00000939504
resolver
enst
ENST00000939505
resolver
enst
ENST00000939509
resolver
enst
ENST00000939512
resolver
enst
ENST00000939514
resolver
enst
ENST00000954118
resolver
enst
ENST00000954120
resolver
genesymbol
THRAP3
resolver
genesymbol_syn
BCLAF2
resolver
genesymbol_syn
TRAP150
resolver
hgnc
HGNC:22964
resolver
uniprot
D3DPS5
resolver
uniprot
Q5VTK6
resolver
uniprot_entry
TR150_HUMAN
resolver
uniprot_sec
D3DPS5
resolver
uniprot_sec
Q5VTK6
resolver
amino_acid_sequence
MSKTNKSKSGSRSSRSRSASRSRSRSFSKSRSRSRSLSRSRKRRLSSRSRSRSYSPAHNRERNHPRVYQNRDFRGHNRGYRRPYYFRGRNRGFYPWGQYNRGGYGNYRSNWQNYRQAYSPRRGRSRSRSPKRRSPSPRSRSHSRNSDKSSSDRSRRSSSSRSSSNHSRVESSKRKSAKEKKSSSKDSRPSQAAGDNQGDEAKEQTFSGGTSQDTKASESSKPWPDATYGTGSASRASAVSELSPRERSPALKSPLQSVVVRRRSPRPSPVPKPSPPLSSTSQMGSTLPSGAGYQSGTHQGQFDHGSGSLSPSKKSPVGKSPPSTGSTYGSSQKEESAASGGAAYTKRYLEEQKTENGKDKEQKQTNTDKEKIKEKGSFSDTGLGDGKMKSDSFAPKTDSEKPFRGSQSPKRYKLRDDFEKKMADFHKEEMDDQDKDKAKGRKESEFDDEPKFMSKVIGANKNQEEEKSGKWEGLVYAPPGKEKQRKTEELEEESFPERSKKEDRGKRSEGGHRGFVPEKNFRVTAYKAVQEKSSSPPPRKTSESRDKLGAKGDFPTGKSSFSITREAQVNVRMDSFDEDLARPSGLLAQERKLCRDLVHSNKKEQEFRSIFQHIQSAQSQRSPSELFAQHIVTIVHHVKEHHFGSSGMTLHERFTKYLKRGTEQEAAKNKKSPEIHRRIDISPSTFRKHGLAHDEMKSPREPGYKAEGKYKDDPVDLRLDIERRKKHKERDLKRGKSRESVDSRDSSHSRERSAEKTEKTHKGSKKQKKHRRARDRSRSSSSSSQSSHSYKAEEYTEETEEREESTTGFDKSRLGTKDFVGPSERGGGRARGTFQFRARGRGWGRGNYSGNNNNNSNNDFQKRNREEEWDPEYTPKSKKYYLHDDREGEGSDKWVSRGRGRGAFPRGRGRFMFRKSSTSPKWAHDKFSGEEGEIEDDESGTENREEKDNIQPTTE
uniprot
proteins
function
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. Plays a role in the positive regulation of the circadian clock. Acts as a coactivator of the CLOCK-BMAL1 heterodimer and promotes its transcriptional activator activity and binding to circadian target genes (PubMed:24043798). {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:20932480, ECO:0000269|PubMed:22424773, ECO:0000269|PubMed:23525231, ECO:0000269|PubMed:24043798}.
uniprot
proteins
mass_dalton
108666
uniprot
proteins
mutagenesis
MUTAGEN 406; /note="S->A: Reduces phosphorylation upon DNA damage; when associated with A-408."; /evidence="ECO:0000269|PubMed:22424773"; MUTAGEN 408; /note="S->A: Reduces phosphorylation upon DNA damage; when associated with A-406."; /evidence="ECO:0000269|PubMed:22424773
uniprot
proteins
post_translational_modification
PTM: ADP-ribosylation during genotoxic stress promotes accumulation in nuclear speckles.
uniprot
proteins
protein_family
BCLAF1/THRAP3 family
uniprot
proteins
pubmed
10198638
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17095540
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18794151
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20123736
uniprot
proteins
pubmed
20932480
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22424773
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23525231
uniprot
proteins
pubmed
24043798
uniprot
proteins
pubmed
24055347
uniprot
proteins
pubmed
24100041
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
sequence_length
955
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20123736, ECO:0000269|PubMed:23525231}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24100041}. Nucleus speckle {ECO:0000269|PubMed:24100041}.
uniprot
proteins