Search Results

Overview

Uniprot IDO95983
Protein NameMethyl-CpG-binding domain protein 3
Gene NameMBD3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 RQTASIFKQPVTKIT
114 IFKQPVTKITNHPSN
41 FYYSPSGKKFRSKPQ
42 YYSPSGKKFRSKPQL
68 TFDFRTGKMLMSKMN
73 TGKMLMSKMNKSRQR
90 YDSSNQVKGKPDLNT

Function

Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:12124384, PubMed:16428440, PubMed:28977666). Acts as transcriptional repressor and plays a role in gene silencing (PubMed:10947852, PubMed:18644863). Does not bind to methylated DNA by itself (PubMed:12124384, PubMed:16428440). Binds to a lesser degree DNA containing unmethylated CpG dinucleotides (PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases

Protein Sequence

10 MERKRWECPA 20 LPQGWEREEV 30 PRRSGLSAGH 40 RDVFYYSPSG 50 KKFRSKPQLA 60 RYLGGSMDLS 70 TFDFRTGKML 80 MSKMNKSRQR 90 VRYDSSNQVK 100 GKPDLNTALP 110 VRQTASIFKQ 120 PVTKITNHPS 130 NKVKSDPQKA 140 VDQPRQLFWE 150 KKLSGLNAFD 160 IAEELVKTMD 170 LPKGLQGVGP 180 GCTDETLLSA 190 IASALHTSTM 200 PITGQLSAAV 210 EKNPGVWLNT 220 TQPLCKAFMV 230 TDEDIRKQEE 240 LVQQVRKRLE 250 EALMADMLAH 260 VEELARDGEA 270 PLDKACAEDD 280 DEEDEEEEEE 290 EPDPDPEMEH V

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0016581 NuRD complex
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0008327 methyl-CpG binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006346 DNA methylation-dependent constitutive heterochromatin formation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0048568 embryonic organ development
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0042659 regulation of cell fate specification
Biological Process GO:2000736 regulation of stem cell differentiation
Biological Process GO:1903925 response to bisphenol A
Biological Process GO:0032355 response to estradiol
Biological Process GO:0031667 response to nutrient levels
Biological Process GO:0003229 ventricular cardiac muscle tissue development

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] 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.

[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] 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.

[5] 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.

[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] 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.