Search Results

Overview

Uniprot ID	Q9BQA1
Protein Name	Methylosome protein WDR77
Gene Name	WDR77
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
3	*****MRKETPPPLV

Function

Non-catalytic component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A, which modifies specific arginines to dimethylarginines in several spliceosomal Sm proteins and histones (PubMed:11756452). This modification targets Sm proteins to the survival of motor neurons (SMN) complex for assembly into small nuclear ribonucleoprotein core particles. Might play a role in transcription regulation. The methylosome complex also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (PubMed:23071334)

Protein Sequence

10 MRKETPPPLV 20 PPAAREWNLP 30 PNAPACMERQ 40 LEAARYRSDG 50 ALLLGASSLS 60 GRCWAGSLWL 70 FKDPCAAPNE 80 GFCSAGVQTE 90 AGVADLTWVG 100 ERGILVASDS 110 GAVELWELDE 120 NETLIVSKFC 130 KYEHDDIVST 140 VSVLSSGTQA 150 VSGSKDICIK 160 VWDLAQQVVL 170 SSYRAHAAQV 180 TCVAASPHKD 190 SVFLSCSEDN 200 RILLWDTRCP 210 KPASQIGCSA 220 PGYLPTSLAW 230 HPQQSEVFVF 240 GDENGTVSLV 250 DTKSTSCVLS 260 SAVHSQCVTG 270 LVFSPHSVPF 280 LASLSEDCSL 290 AVLDSSLSEL 300 FRSQAHRDFV 310 RDATWSPLNH 320 SLLTTVGWDH 330 QVVHHVVPTE 340 PLPAPGPASV TE

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0031465	Cul4B-RING E3 ubiquitin ligase complex
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005794	Golgi apparatus
Cellular Component	GO:0034709	methylosome
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0008327	methyl-CpG binding
Molecular Function	GO:0003713	transcription coactivator activity
Molecular Function	GO:1990756	ubiquitin-like ligase-substrate adaptor activity
Biological Process	GO:0048026	positive regulation of mRNA splicing, via spliceosome
Biological Process	GO:2000234	positive regulation of rRNA processing
Biological Process	GO:0000209	protein polyubiquitination
Biological Process	GO:0000387	spliceosomal snRNP assembly
Biological Process	GO:0006511	ubiquitin-dependent protein catabolic process

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] 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.

[5] 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.

[6] 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.

[7] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[8] 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.