H2A_PODAS
ID H2A_PODAS Reviewed; 135 AA.
AC Q875B8;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Histone H2A;
GN Name=HTA1; ORFNames=Pa5D0006;
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s;
RX PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT "Characterization of the genomic organization of the region bordering the
RT centromere of chromosome V of Podospora anserina by direct sequencing.";
RL Fungal Genet. Biol. 39:250-263(2003).
CC -!- FUNCTION: Core component of nucleosome which plays a central role in
CC DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA
CC double-strand breaks (DSBs) generated by exogenous genotoxic agents and
CC by stalled replication forks. Phosphorylation is dependent on the DNA
CC damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side
CC of a detected DSB site and may mark the surrounding chromatin for
CC recruitment of proteins required for DNA damage signaling and repair.
CC Gamma-H2A is removed from the DNA prior to the strand invasion-primer
CC extension step of the repair process and subsequently dephosphorylated.
CC Dephosphorylation is necessary for efficient recovery from the DNA
CC damage checkpoint (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylated by ESA1 to form H2AK4ac and H2AK7ac. {ECO:0000250}.
CC -!- MISCELLANEOUS: In contrast to vertebrates and insects, its C-terminus
CC is not monoubiquitinated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H2AK4ac =
CC acetylated Lys-6; H2AK7ac = acetylated Lys-10; H2AS128ph =
CC phosphorylated Ser-132. {ECO:0000305}.
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DR EMBL; BX088700; CAD60693.1; -; Genomic_DNA.
DR AlphaFoldDB; Q875B8; -.
DR SMR; Q875B8; -.
DR VEuPathDB; FungiDB:PODANS_5_5390; -.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 3: Inferred from homology;
KW Acetylation; Chromosome; DNA damage; DNA repair; DNA-binding; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..135
FT /note="Histone H2A"
FT /id="PRO_0000228733"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..133
FT /note="[ST]-Q motif"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 121
FT /note="Not ubiquitinated"
FT /evidence="ECO:0000305"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 107
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 135 AA; 14251 MW; 90785684E485DF3F CRC64;
MTGGGKSGGK ASSGKNAQSR SSKAGLAFPV GRVHRLLRKG NYAQRVGAGA PVYLAAVLEY
LAAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL GHVTIAQGGV LPNIHQNLLP
KKTGTKPGKN ASQEL
