Search Results

Overview

Uniprot IDQ9UBB5
Protein NameMethyl-CpG-binding domain protein 2
Gene NameMBD2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
167 KKEEVIRKSGLSAGK
174 KSGLSAGKSDVYYFS
185 YYFSPSGKKFRSKPQ
186 YFSPSGKKFRSKPQL
190 SGKKFRSKPQLARYL
212 SFDFRTGKMMPSKLQ
217 TGKMMPSKLQKNKQR
253 RQTASIFKQPVTKVT
382 RVQQVRKKLEEALMA

Function

Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides (PubMed:9774669). Binds hemimethylated DNA as well (PubMed:10947852, PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases to chromatin (PubMed:10471499, PubMed:10947852). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Acts as a transcriptional repressor and plays a role in gene silencing (PubMed:10471499, PubMed:10947852, PubMed:16415179). Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression (PubMed:16415179). May enhance the activation of some unmethylated cAMP-responsive promoters (PubMed:12665568)

Protein Sequence

10 MRAHPGGGRC 20 CPEQEEGESA 30 AGGSGAGGDS 40 AIEQGGQGSA 50 LAPSPVSGVR 60 REGARGGGRG 70 RGRWKQAGRG 80 GGVCGRGRGR 90 GRGRGRGRGR 100 GRGRGRPPSG 110 GSGLGGDGGG 120 CGGGGSGGGG 130 APRREPVPFP 140 SGSAGPGPRG 150 PRATESGKRM 160 DCPALPPGWK 170 KEEVIRKSGL 180 SAGKSDVYYF 190 SPSGKKFRSK 200 PQLARYLGNT 210 VDLSSFDFRT 220 GKMMPSKLQK 230 NKQRLRNDPL 240 NQNKGKPDLN 250 TTLPIRQTAS 260 IFKQPVTKVT 270 NHPSNKVKSD 280 PQRMNEQPRQ 290 LFWEKRLQGL 300 SASDVTEQII 310 KTMELPKGLQ 320 GVGPGSNDET 330 LLSAVASALH 340 TSSAPITGQV 350 SAAVEKNPAV 360 WLNTSQPLCK 370 AFIVTDEDIR 380 KQEERVQQVR 390 KKLEEALMAD 400 ILSRAADTEE 410 MDIEMDSGDE A

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:0070742 C2H2 zinc finger domain binding
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0008327 methyl-CpG binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0003696 satellite DNA binding
Molecular Function GO:0035197 siRNA binding
Biological Process GO:1904015 cellular response to serotonin
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:0042711 maternal behavior
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:1903925 response to bisphenol A
Biological Process GO:0032355 response to estradiol
Biological Process GO:0009612 response to mechanical stimulus
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] 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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] 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.

[5] 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.

[6] 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.

[7] 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.

[8] 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.

[9] 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.

[10] 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.