Search Results
Overview
| Uniprot ID | O75367 |
|---|---|
| Protein Name | Core histone macro-H2A.1 |
| Gene Name | MACROH2A1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 123 | KKRGSKGKLEAIITP |
| 134 | IITPPPAKKAKSPSQ |
| 135 | ITPPPAKKAKSPSQK |
| 137 | PPPAKKAKSPSQKKP |
| 142 | KAKSPSQKKPVSKKA |
| 161 | GARKSKKKQGEVSKA |
| 167 | KKQGEVSKAASADST |
| 301 | CLALADDKKLKSIAF |
| 302 | LALADDKKLKSIAFP |
| 304 | LADDKKLKSIAFPSI |
Function
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription (PubMed:12718888, PubMed:15621527, PubMed:16428466). Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:15897469). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (PubMed:15897469). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Involved in stable X chromosome inactivation (PubMed:15897469). Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (PubMed:12718888, PubMed:16428466). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (PubMed:16107708, PubMed:16428466)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0001740 | Barr body |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0000793 | condensed chromosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0000228 | nuclear chromosome |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005721 | pericentric heterochromatin |
| Cellular Component | GO:0001739 | sex chromatin |
| Cellular Component | GO:0090734 | site of DNA damage |
| Molecular Function | GO:0072570 | ADP-D-ribose binding |
| Molecular Function | GO:0160002 | ADP-D-ribose modification-dependent protein binding |
| Molecular Function | GO:0031490 | chromatin DNA binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0010385 | double-stranded methylated DNA binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0031492 | nucleosomal DNA binding |
| Molecular Function | GO:0160004 | poly-ADP-D-ribose modification-dependent protein binding |
| Molecular Function | GO:1990841 | promoter-specific chromatin binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0030291 | protein serine/threonine kinase inhibitor activity |
| Molecular Function | GO:0000182 | rDNA binding |
| Molecular Function | GO:0000977 | RNA polymerase II transcription regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Molecular Function | GO:0000976 | transcription cis-regulatory region binding |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0009048 | dosage compensation by inactivation of X chromosome |
| Biological Process | GO:0040029 | epigenetic regulation of gene expression |
| Biological Process | GO:0071169 | establishment of protein localization to chromatin |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:1902750 | negative regulation of cell cycle G2/M phase transition |
| Biological Process | GO:0045814 | negative regulation of gene expression, epigenetic |
| Biological Process | GO:1904815 | negative regulation of protein localization to chromosome, telomeric region |
| Biological Process | GO:1902883 | negative regulation of response to oxidative stress |
| Biological Process | GO:0000122 | negative regulation of transcription by RNA polymerase II |
| Biological Process | GO:1901837 | negative regulation of transcription of nucleolar large rRNA by RNA polymerase I |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:1903226 | positive regulation of endodermal cell differentiation |
| Biological Process | GO:0045618 | positive regulation of keratinocyte differentiation |
| Biological Process | GO:0034184 | positive regulation of maintenance of mitotic sister chromatid cohesion |
| Biological Process | GO:1902884 | positive regulation of response to oxidative stress |
| Biological Process | GO:0019216 | regulation of lipid metabolic process |
| Biological Process | GO:1902688 | regulation of NAD metabolic process |
| Biological Process | GO:0002082 | regulation of oxidative phosphorylation |
| Biological Process | GO:1902882 | regulation of response to oxidative stress |
| Biological Process | GO:0045815 | transcription initiation-coupled chromatin remodeling |
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] 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.
[3] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.
[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.