ID   H2A_DROHY               Reviewed;         124 AA.
AC   P84053; P02267;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Histone H2A;
GN   Name=His2A; Synonyms=H2a;
OS   Drosophila hydei (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2109309; DOI=10.1093/nar/18.6.1573;
RA   Kremer H., Hennig W.;
RT   "Isolation and characterization of a Drosophila hydei histone DNA repeat
RT   unit.";
RL   Nucleic Acids Res. 18:1573-1580(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Strausbaugh L.D., Fitch D.H.A., Barrett V.;
RL   Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
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   -!- PTM: The chromatin-associated form, but not the free cytoplasmic form,
CC       is phosphorylated on Thr-120 by NHK-1 during mitosis, and
CC       dephosphorylated during S-phase. Also phosphorylated on Thr-120 by NHK-
CC       1 during prophase I of meiosis; which is required for acetylation of H3
CC       'Lys-14' and H4 'Lys-5', diassembly of the synaptonemal complex, and
CC       karyosome formation (By similarity). {ECO:0000250}.
CC   -!- PTM: Monoubiquitination of Lys-119 by sce/dRING gives a specific tag
CC       for epigenetic transcriptional repression. {ECO:0000250}.
CC   -!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
CC       Phosphorylation on Ser-2 directly represses transcription (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; X17072; CAA34921.1; -; Genomic_DNA.
DR   EMBL; X52576; CAA36807.1; -; Genomic_DNA.
DR   PIR; S21938; S21938.
DR   AlphaFoldDB; P84053; -.
DR   SMR; P84053; -.
DR   FlyBase; FBgn0012375; Dhyd\His2A.
DR   GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
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-binding; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..124
FT                   /note="Histone H2A"
FT                   /id="PRO_0000055221"
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:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         36
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P84051"
FT   MOD_RES         104
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         120
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   124 AA;  13363 MW;  725BA63C393155F6 CRC64;
     MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA
     EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
     EKKA