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Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C0S6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11101893"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20473270"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24463511"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26237645"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26974126"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28645917"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30327463"}],"value":"The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. H2A or its variant H2AZ1 forms a heterodimer with H2B. H2AZ1 interacts with INCENP (By similarity). Interacts (via M6 cassette) with ANP32E; leading to removal of H2A.Z/H2AZ1 from the nucleosome. Heterodimer H2BC11 and H2AZ1 interacts with VPS72 (via N-terminal domain) (PubMed:26974126). The interaction of HZAZ1 and VPS72 is enhanced by VPS72 phosphorylation which is promoted by ZNHIT1 (By similarity). Interacts with PWWP2A (PubMed:28645917, PubMed:30327463). Interacts with FH (when phosphorylated by PRKDC) (PubMed:26237645). Interacts with ZNHIT1; the interaction results in recruitment of H2AZ1 to the MYOG promoter region which is required for muscle-specific gene expression (PubMed:20473270)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"P01023","geneName":"A2M","intActId":"EBI-640741"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"Q9GZN1","geneName":"ACTR6","intActId":"EBI-769329"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"P50570-2","geneName":"DNM2","intActId":"EBI-10968534"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"P07954","geneName":"FH","intActId":"EBI-1050358"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"Q16778","geneName":"H2BC21","intActId":"EBI-1056125"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"P58876","geneName":"H2BC5","intActId":"EBI-4409942"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"O14656-2","geneName":"TOR1A","intActId":"EBI-25847109"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0C0S5","intActId":"EBI-1199859"},"interactantTwo":{"uniProtKBAccession":"O43257","geneName":"ZNHIT1","intActId":"EBI-347522"},"numberOfExperiments":9,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Nucleus","id":"SL-0191"}},{"location":{"value":"Chromosome","id":"SL-0468"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11835281"}],"value":"Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C0S6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31527837"}],"value":"Acetylated on Lys-5, Lys-8, Lys-12 and Lys-14 by KAT2A; KAT2A is recruited by the XPC complex in absence of DNA damage (PubMed:31527837). Acetylated on Lys-5, Lys-8 and Lys-12 during interphase; acetylation disappears at mitosis (By similarity). Acetylation by the NuA4 histone acetyltransferase complex is required for hematopoietic stem cell maintenance (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23324626"}],"value":"Monomethylated on Lys-5 and Lys-8 by SETD6. SETD6 predominantly methylates Lys-8, lys-5 being a possible secondary site"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P0C0S4"}],"value":"Not phosphorylated"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31645732"}],"value":"Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription"}],"commentType":"PTM"},{"commentType":"MASS SPECTROMETRY","method":"Electrospray","molWeight":13413.4,"molWeightError":0.0,"note":"Monoisotopic, not modified.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16457589"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the histone H2A family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000305"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Histone H2A.Z","featureId":"PRO_0000055297"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Required for interaction with INCENP","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Region","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"M6 cassette"},{"type":"Region","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Required for interaction with INCENP","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Region","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"Required for interaction with PWWP2A","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28645917"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"N6-acetyllysine; 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