Search Results
Overview
| Uniprot ID | Q5M7V8 |
|---|---|
| Protein Name | Thyroid hormone receptor-associated protein 3 |
| Gene Name | Thrap3 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 252 | RERSPALKSPLQSVV |
| 346 | SGGAAYTKRYLEEQK |
| 375 | DKEKLKEKGGFSDAD |
| 384 | GFSDADVKMKSDPFA |
| 386 | SDADVKMKSDPFAPK |
| 418 | LRDDFEKKMADFHKE |
| 439 | KDKCKGRKEPEFDDE |
| 452 | DEPKFISKVIAGASK |
| 459 | KVIAGASKNQEEEKS |
| 468 | QEEEKSGKWESLHAG |
| 476 | WESLHAGKEKQRKAE |
| 481 | AGKEKQRKAEELEEE |
| 516 | HRGFVPEKNFRVTAY |
| 524 | NFRVTAYKAVQEKSS |
| 548 | SRDKLGNKGDFSSGK |
| 555 | KGDFSSGKSSFSITR |
| 599 | RDLVHSNKKEQEFRS |
| 685 | ISPSTFRKHGLTHEE |
| 694 | GLTHEELKSPREPGY |
| 702 | SPREPGYKAEGKYKD |
| 706 | PGYKAEGKYKDDPVD |
| 708 | YKAEGKYKDDPVDLR |
| 872 | WDPEYTPKSKKYYLH |
| 875 | EYTPKSKKYYLHDDR |
| 917 | RKSSTSPKWAHDKFS |
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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0003712 | transcription coregulator activity |
| Cellular Component | GO:0035145 | exon-exon junction complex |
| Cellular Component | GO:0016592 | mediator complex |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0046966 | nuclear thyroid hormone receptor binding |
| Molecular Function | GO:0051219 | phosphoprotein binding |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Biological Process | GO:0007623 | circadian rhythm |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0048255 | mRNA stabilization |
| Biological Process | GO:0000956 | nuclear-transcribed mRNA catabolic process |
| Biological Process | GO:0042753 | positive regulation of circadian rhythm |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:0048026 | positive regulation of mRNA splicing, via spliceosome |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0000381 | regulation of alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0008380 | RNA splicing |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.
[2] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.