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Overview

Uniprot IDP51608
Protein NameMethyl-CpG-binding protein 2
Gene NameMECP2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
200 GSGTTRPKAATSEGV
210 TSEGVQVKRVLEKSP
215 QVKRVLEKSPGKLLV
219 VLEKSPGKLLVKMPF
22 DQDLQGLKDKPLKFK
223 SPGKLLVKMPFQTSP
249 STQVMVIKRPGRKRK
256 KRPGRKRKAEADPQA
266 ADPQAIPKKRGRKPG
27 GLKDKPLKFKKVKKD
271 IPKKRGRKPGSVVAA
284 AAAAAEAKKKAVKES
289 EAKKKAVKESSIRSV
304 QETVLPIKKRKTRET
305 ETVLPIKKRKTRETV
331 LVSTLGEKSGKGLKT
435 GCPKEPAKTQPAVAT
449 TAATAAEKYKHRGEG
451 ATAAEKYKHRGEGER
459 HRGEGERKDIVSSSM

Function

Chromosomal protein that binds to methylated DNA. It can bind specifically to a single methyl-CpG pair. It is not influenced by sequences flanking the methyl-CpGs. Mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A. Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference for 5-methylcytosine (5mC)

Protein Sequence

10 MVAGMLGLRE 20 EKSEDQDLQG 30 LKDKPLKFKK 40 VKKDKKEEKE 50 GKHEPVQPSA 60 HHSAEPAEAG 70 KAETSEGSGS 80 APAVPEASAS 90 PKQRRSIIRD 100 RGPMYDDPTL 110 PEGWTRKLKQ 120 RKSGRSAGKY 130 DVYLINPQGK 140 AFRSKVELIA 150 YFEKVGDTSL 160 DPNDFDFTVT 170 GRGSPSRREQ 180 KPPKKPKSPK 190 APGTGRGRGR 200 PKGSGTTRPK 210 AATSEGVQVK 220 RVLEKSPGKL 230 LVKMPFQTSP 240 GGKAEGGGAT 250 TSTQVMVIKR 260 PGRKRKAEAD 270 PQAIPKKRGR 280 KPGSVVAAAA 290 AEAKKKAVKE 300 SSIRSVQETV 310 LPIKKRKTRE 320 TVSIEVKEVV 330 KPLLVSTLGE 340 KSGKGLKTCK 350 SPGRKSKESS 360 PKGRSSSASS 370 PPKKEHHHHH 380 HHSESPKAPV 390 PLLPPLPPPP 400 PEPESSEDPT 410 SPPEPQDLSS 420 SVCKEEKMPR 430 GGSLESDGCP 440 KEPAKTQPAV 450 ATAATAAEKY 460 KHRGEGERKD 470 IVSSSMPRPN 480 REEPVDSRTP VTERVS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0010385 double-stranded methylated DNA binding
Molecular Function GO:0140566 histone reader activity
Molecular Function GO:0008327 methyl-CpG binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0140693 molecular condensate scaffold activity
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003676 nucleic acid binding
Molecular Function GO:1990841 promoter-specific chromatin binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0035197 siRNA binding
Molecular Function GO:0003714 transcription corepressor activity
Biological Process GO:0008306 associative learning
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0071514 genomic imprinting
Biological Process GO:0016525 negative regulation of angiogenesis
Biological Process GO:0043537 negative regulation of blood vessel endothelial cell migration
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0010629 negative regulation of gene expression
Biological Process GO:0044027 negative regulation of gene expression via chromosomal CpG island methylation
Biological Process GO:0051151 negative regulation of smooth muscle cell differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0030182 neuron differentiation
Biological Process GO:0007219 Notch signaling pathway
Biological Process GO:0090063 positive regulation of microtubule nucleation

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] 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] 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.

[9] 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.