MACROH2A1
entrez
9555
canonical
uniprot
O75367
canonical
ensembl
ENSG00000113648
resolver
ensp
ENSP00000302572
resolver
ensp
ENSP00000310169
resolver
ensp
ENSP00000415121
resolver
ensp
ENSP00000423563
resolver
ensp
ENSP00000424971
resolver
ensp
ENSP00000515857
resolver
ensp
ENSP00000547679
resolver
ensp
ENSP00000547680
resolver
ensp
ENSP00000593093
resolver
ensp
ENSP00000623795
resolver
ensp
ENSP00000665137
resolver
ensp
ENSP00000771106
resolver
enst
ENST00000423969
resolver
enst
ENST00000513210
resolver
enst
ENST00000953736
resolver
genesymbol
MACROH2A1
resolver
genesymbol_syn
H2AFY
resolver
hgnc
HGNC:4740
resolver
uniprot
A0A994J4J7
resolver
uniprot
A0ACI8UWE3
resolver
uniprot
B4DJC3
resolver
uniprot
O75377
resolver
uniprot
Q503A8
resolver
uniprot
Q7Z5E3
resolver
uniprot
Q96D41
resolver
uniprot
Q9H8P3
resolver
uniprot
Q9UP96
resolver
uniprot_entry
A0A994J4J7_HUMAN
resolver
uniprot_entry
A0ACI8UWE3_HUMAN
resolver
uniprot_entry
B4DJC3_HUMAN
resolver
uniprot_entry
H2AY_HUMAN
resolver
uniprot_sec
O75377
resolver
uniprot_sec
Q503A8
resolver
uniprot_sec
Q7Z5E3
resolver
uniprot_sec
Q96D41
resolver
uniprot_sec
Q9H8P3
resolver
uniprot_sec
Q9UP96
resolver
amino_acid_sequence
MSSRGGKKKSTKTSRSAKAGVIFPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNKKGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKGKLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASADSTTEGTPADGFTVLSTKSLFLGQKLQVVQADIASIDSDAVVHPTNTDFYIGGEVGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKFVIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFPKQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
uniprot
proteins
function
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). {ECO:0000269|PubMed:12718888, ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:16107708, ECO:0000269|PubMed:16428466}.; FUNCTION: [Isoform 1]: Isoform that specifically binds poly-ADP-ribose and O-acetyl-ADP-ribose and plays a key role in NAD(+) metabolism (PubMed:15902274). Able to bind to the ends of poly-ADP-ribose chains created by PARP1 and cap them (By similarity). 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 (By similarity). Increases the expression of genes involved in redox metabolism, including SOD3 (PubMed:23022728). {ECO:0000250|UniProtKB:Q9QZQ8, ECO:0000269|PubMed:15902274, ECO:0000269|PubMed:23022728}.; FUNCTION: [Isoform 2]: In contrast to isoform 1, does not bind poly-ADP-ribose (PubMed:15902274). Represses SOD3 gene expression (PubMed:23022728). {ECO:0000269|PubMed:15902274, ECO:0000269|PubMed:23022728}.
uniprot
proteins
mass_dalton
39184
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:0000269|PubMed:15897469, ECO:0000269|PubMed:16129414, ECO:0000269|PubMed:19818708}.
uniprot
proteins
protein_family
Histone H2A family
uniprot
proteins
pubmed
12718888
uniprot
proteins
pubmed
12800201
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15621527
uniprot
proteins
pubmed
15897469
uniprot
proteins
pubmed
15902274
uniprot
proteins
pubmed
15965484
uniprot
proteins
pubmed
16107708
uniprot
proteins
pubmed
16129414
uniprot
proteins
pubmed
16210244
uniprot
proteins
pubmed
16428466
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19818708
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21211722
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23022728
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23474714
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29905837
uniprot
proteins
pubmed
9634239
uniprot
proteins
pubmed
9653160
uniprot
proteins
pubmed
9714746
uniprot
proteins
sequence_length
369
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9634239}. Chromosome {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}. Note=Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin (PubMed:15621527, PubMed:15897469, PubMed:9634239). Recruited to DNA damage sites in an APLF-dependent manner (PubMed:21211722, PubMed:29905837). {ECO:0000269|PubMed:15621527, ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:21211722, ECO:0000269|PubMed:29905837, ECO:0000269|PubMed:9634239}.
uniprot
proteins