Search Results

Overview

Uniprot IDO15541
Protein NameE3 ubiquitin-protein ligase RNF113A
Gene NameRNF113A
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
139 AIFERSQKIQEELRG
161 RGINNYQKYMKPKDT
166 YQKYMKPKDTSMGNA
20 QVCTFLFKKPGRKGA
21 VCTFLFKKPGRKGAA
69 THNPMIQKTRDSGKQ

Function

Required for pre-mRNA splicing as component of the spliceosome (PubMed:29360106, PubMed:29361316). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins (PubMed:28978524, PubMed:29144457). Catalyzes polyubiquitination of SNRNP200/BRR2 with non-canonical 'Lys-63'-linked polyubiquitin chains (PubMed:29144457). Plays a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit ALKBH3 and the ASCC complex to sites of DNA damage by alkylating agents (PubMed:29144457). Ubiquitinates CXCR4, leading to its degradation, and thereby contributes to the termination of CXCR4 signaling (PubMed:28978524)

Protein Sequence

10 MAEQLSPGKA 20 VDQVCTFLFK 30 KPGRKGAAGR 40 RKRPACDPEP 50 GESGSSSDEG 60 CTVVRPEKKR 70 VTHNPMIQKT 80 RDSGKQKAAY 90 GDLSSEEEEE 100 NEPESLGVVY 110 KSTRSAKPVG 120 PEDMGATAVY 130 ELDTEKERDA 140 QAIFERSQKI 150 QEELRGKEDD 160 KIYRGINNYQ 170 KYMKPKDTSM 180 GNASSGMVRK 190 GPIRAPEHLR 200 ATVRWDYQPD 210 ICKDYKETGF 220 CGFGDSCKFL 230 HDRSDYKHGW 240 QIERELDEGR 250 YGVYEDENYE 260 VGSDDEEIPF 270 KCFICRQSFQ 280 NPVVTKCRHY 290 FCESCALQHF 300 RTTPRCYVCD 310 QQTNGVFNPA 320 KELIAKLEKH 330 RATGEGGASD 340 LPEDPDEDAI PIT

Gene Ontology

Classification GO ID Description
Cellular Component GO:0016607 nuclear speck
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0071005 U2-type precatalytic spliceosome
Cellular Component GO:0005684 U2-type spliceosomal complex
Molecular Function GO:0061630 ubiquitin protein ligase activity
Molecular Function GO:0004842 ubiquitin-protein transferase activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0000398 mRNA splicing, via spliceosome
Biological Process GO:0070100 negative regulation of chemokine-mediated signaling pathway
Biological Process GO:0016567 protein ubiquitination

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] 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.

[4] 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.

[5] 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.

[6] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[7] 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.