Macroh2a1
entrez
29384
canonical
uniprot
Q02874
canonical
ensembl
ENSRNOG00000011523
resolver
ensp
ENSRNOP00000015632
resolver
ensp
ENSRNOP00000049143
resolver
enst
ENSRNOT00000015632
resolver
genesymbol
Macroh2a1
resolver
genesymbol_syn
H2afy
resolver
uniprot
A0A140TAB4
resolver
uniprot
O09140
resolver
uniprot
Q63325
resolver
uniprot_entry
A0A140TAB4_RAT
resolver
uniprot_entry
H2AY_RAT
resolver
uniprot_sec
O09140
resolver
uniprot_sec
Q63325
resolver
amino_acid_sequence
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVAKKTGGKKGARKSKKQGEVSKAASADSTTEGAPTDGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNADFYIGGEVGSTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDRKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
uniprot
proteins
function
FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template (PubMed:16107708). Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability (PubMed:16107708). DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling (PubMed:16107708). Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors, including NF-kappa-B, and interferes with the activity of remodeling SWI/SNF complexes (By similarity). Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin (By similarity). {ECO:0000250|UniProtKB:O75367, ECO:0000250|UniProtKB:Q9QZQ8, ECO:0000269|PubMed:16107708}.; FUNCTION: [Isoform 1]: Isoform that specifically binds poly-ADP-ribose and O-acetyl-ADP-ribose and plays a key role in NAD(+) metabolism. Able to bind to the ends of poly-ADP-ribose chains created by PARP1 and cap them. This prevents PARP1 from further addition of ADP-ribose and thus limits the consumption of nuclear NAD(+), allowing the cell to maintain proper NAD(+) levels in both the nucleus and the mitochondria to promote proper mitochondrial respiration. Increases the expression of genes involved in redox metabolism, including SOD3. {ECO:0000250|UniProtKB:Q9QZQ8}.; FUNCTION: [Isoform 2]: In contrast to isoform 1, does not bind poly-ADP-ribose. Represses SOD3 gene expression. {ECO:0000250|UniProtKB:Q9QZQ8}.
uniprot
proteins
mass_dalton
39040
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin. {ECO:0000250|UniProtKB:O75367}.
uniprot
proteins
protein_family
Histone H2A family
uniprot
proteins
pubmed
1529340
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16107708
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
9138085
uniprot
proteins
sequence_length
368
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O75367}. Chromosome {ECO:0000250|UniProtKB:O75367}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin. Recruited to DNA damage sites in an APLF-dependent manner. {ECO:0000250|UniProtKB:O75367}.
uniprot
proteins