Search Results

Overview

Uniprot IDQ9Y2W1
Protein NameThyroid hormone receptor-associated protein 3
Gene NameTHRAP3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
181 RKSAKEKKSSSKDSR
185 KEKKSSSKDSRPSQA
215 GGTSQDTKASESSKP
252 RERSPALKSPLQSVV
346 SGGAAYTKRYLEEQK
373 NTDKEKIKEKGSFSD
375 DKEKIKEKGSFSDTG
387 DTGLGDGKMKSDSFA
389 GLGDGKMKSDSFAPK
396 KSDSFAPKTDSEKPF
420 KLRDDFEKKMADFHK
421 LRDDFEKKMADFHKE
427 KKMADFHKEEMDDQD
442 KDKAKGRKESEFDDE
451 SEFDDEPKFMSKVIG
455 DEPKFMSKVIGANKN
461 SKVIGANKNQEEEKS
470 QEEEKSGKWEGLVYA
481 LVYAPPGKEKQRKTE
486 PGKEKQRKTEELEEE
519 HRGFVPEKNFRVTAY
527 NFRVTAYKAVQEKSS
532 AYKAVQEKSSSPPPR
551 SRDKLGAKGDFPTGK
558 KGDFPTGKSSFSITR
602 RDLVHSNKKEQEFRS
688 ISPSTFRKHGLAHDE
697 GLAHDEMKSPREPGY
705 SPREPGYKAEGKYKD
709 PGYKAEGKYKDDPVD
711 YKAEGKYKDDPVDLR
811 ESTTGFDKSRLGTKD
876 WDPEYTPKSKKYYLH
878 PEYTPKSKKYYLHDD
879 EYTPKSKKYYLHDDR
921 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 (PubMed:24043798)

Protein Sequence

10 MSKTNKSKSG 20 SRSSRSRSAS 30 RSRSRSFSKS 40 RSRSRSLSRS 50 RKRRLSSRSR 60 SRSYSPAHNR 70 ERNHPRVYQN 80 RDFRGHNRGY 90 RRPYYFRGRN 100 RGFYPWGQYN 110 RGGYGNYRSN 120 WQNYRQAYSP 130 RRGRSRSRSP 140 KRRSPSPRSR 150 SHSRNSDKSS 160 SDRSRRSSSS 170 RSSSNHSRVE 180 SSKRKSAKEK 190 KSSSKDSRPS 200 QAAGDNQGDE 210 AKEQTFSGGT 220 SQDTKASESS 230 KPWPDATYGT 240 GSASRASAVS 250 ELSPRERSPA 260 LKSPLQSVVV 270 RRRSPRPSPV 280 PKPSPPLSST 290 SQMGSTLPSG 300 AGYQSGTHQG 310 QFDHGSGSLS 320 PSKKSPVGKS 330 PPSTGSTYGS 340 SQKEESAASG 350 GAAYTKRYLE 360 EQKTENGKDK 370 EQKQTNTDKE 380 KIKEKGSFSD 390 TGLGDGKMKS 400 DSFAPKTDSE 410 KPFRGSQSPK 420 RYKLRDDFEK 430 KMADFHKEEM 440 DDQDKDKAKG 450 RKESEFDDEP 460 KFMSKVIGAN 470 KNQEEEKSGK 480 WEGLVYAPPG 490 KEKQRKTEEL 500 EEESFPERSK 510 KEDRGKRSEG 520 GHRGFVPEKN 530 FRVTAYKAVQ 540 EKSSSPPPRK 550 TSESRDKLGA 560 KGDFPTGKSS 570 FSITREAQVN 580 VRMDSFDEDL 590 ARPSGLLAQE 600 RKLCRDLVHS 610 NKKEQEFRSI 620 FQHIQSAQSQ 630 RSPSELFAQH 640 IVTIVHHVKE 650 HHFGSSGMTL 660 HERFTKYLKR 670 GTEQEAAKNK 680 KSPEIHRRID 690 ISPSTFRKHG 700 LAHDEMKSPR 710 EPGYKAEGKY 720 KDDPVDLRLD 730 IERRKKHKER 740 DLKRGKSRES 750 VDSRDSSHSR 760 ERSAEKTEKT 770 HKGSKKQKKH 780 RRARDRSRSS 790 SSSSQSSHSY 800 KAEEYTEETE 810 EREESTTGFD 820 KSRLGTKDFV 830 GPSERGGGRA 840 RGTFQFRARG 850 RGWGRGNYSG 860 NNNNNSNNDF 870 QKRNREEEWD 880 PEYTPKSKKY 890 YLHDDREGEG 900 SDKWVSRGRG 910 RGAFPRGRGR 920 FMFRKSSTSP 930 KWAHDKFSGE 940 EGEIEDDESG 950 TENREEKDNI QPTTE

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
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:0042809 nuclear vitamin D receptor binding
Molecular Function GO:0051219 phosphoprotein binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0003712 transcription coregulator 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] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[5] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[6] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[7] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[8] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[9] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[10] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[11] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.