ID   H2A_ASTRU               Reviewed;         125 AA.
AC   P02269;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Histone H2A;
OS   Asterias rubens (Common European starfish) (Asterias vulgaris).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Asterozoa; Asteroidea;
OC   Forcipulatacea; Forcipulatida; Asteriidae; Asterias.
OX   NCBI_TaxID=7604;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-125, AND ACETYLATION AT SER-2.
RX   PubMed=6825703; DOI=10.1111/j.1432-1033.1983.tb07173.x;
RA   Martinage A., Belaiche D., Dupressoir T., Sautiere P.;
RT   "Primary structure of histone H2A from gonads of the starfish Asterias
RT   rubens.";
RL   Eur. J. Biochem. 130:465-472(1983).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone 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. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   PIR; A02596; HSSF2.
DR   AlphaFoldDB; P02269; -.
DR   SMR; P02269; -.
DR   iPTMnet; P02269; -.
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   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   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Methylation; Nucleosome core; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6825703"
FT   CHAIN           2..125
FT                   /note="Histone H2A"
FT                   /id="PRO_0000055208"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6825703"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   VARIANT         19
FT                   /note="S -> A"
FT   VARIANT         41
FT                   /note="E -> Q"
FT   VARIANT         51
FT                   /note="L -> N"
SQ   SEQUENCE   125 AA;  13398 MW;  6D261C43384F333F CRC64;
     MSGRGKGGKA RAKAKSRSSR AGLQFPVGRV HRFLRKGNYA ERVGAGAPVY LAAVMEYLAA
     EILELAGNAA RDNKKTRINP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
     AKAAK