H2A_DROSI
ID H2A_DROSI Reviewed; 124 AA.
AC P84054; B4NUX3; P02267;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Histone H2A;
GN Name=His2A; Synonyms=H2a;
GN and
GN ORFNames=GD24469;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2A).
RC STRAIN=s2;
RX PubMed=11922104; DOI=10.1266/ggs.76.355;
RA Tsunemoto K., Matsuo Y.;
RT "Molecular evolutionary analysis of a histone gene repeating unit from
RT Drosophila simulans.";
RL Genes Genet. Syst. 76:355-361(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (GD24469).
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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; AB055959; BAC54548.1; -; Genomic_DNA.
DR EMBL; CH984460; EDX15909.1; -; Genomic_DNA.
DR EMBL; CH987256; EDX16003.1; -; Genomic_DNA.
DR EMBL; CH989013; EDX16129.1; -; Genomic_DNA.
DR EMBL; CH989564; EDX16175.1; -; Genomic_DNA.
DR EMBL; CH989728; EDX16187.1; -; Genomic_DNA.
DR EMBL; CH990890; EDX16244.1; -; Genomic_DNA.
DR EMBL; CH991512; EDX16267.1; -; Genomic_DNA.
DR EMBL; CM000366; EDX17492.1; -; Genomic_DNA.
DR RefSeq; XP_002077189.2; XM_002077153.2.
DR AlphaFoldDB; P84054; -.
DR SMR; P84054; -.
DR STRING; 7240.P84054; -.
DR EnsemblMetazoa; FBtr0224379; FBpp0222871; FBgn0195804.
DR GeneID; 6740317; -.
DR HOGENOM; CLU_062828_3_3_1; -.
DR OMA; RTEGKHE; -.
DR PhylomeDB; P84054; -.
DR ChiTaRS; His2Av; fly.
DR Proteomes; UP000000304; Chromosome x.
DR Proteomes; UP000000304; Unassembled WGS sequence.
DR Bgee; FBgn0195804; Expressed in embryo and 3 other tissues.
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 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..124
FT /note="Histone H2A"
FT /id="PRO_0000055223"
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
