H2A_DROYA
ID H2A_DROYA Reviewed; 124 AA.
AC P84055; B4IW80; D5MP57; P02267; Q6XHF1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Histone H2A;
GN Name=His2A; Synonyms=H2a;
GN and
GN ORFNames=GE14578;
GN and
GN ORFNames=GE15127;
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2A).
RC STRAIN=y6;
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 [GENOMIC DNA] (HIS2A).
RX PubMed=14676429; DOI=10.1266/ggs.78.383;
RA Kakita M., Shimizu T., Emoto M., Nagai M., Takeguchi M., Hosono Y.,
RA Kume N., Ozawa T., Ueda M., Bhuiyan M.S., Matsuo Y.;
RT "Divergence and heterogeneity of the histone gene repeating units in the
RT Drosophila melanogaster species subgroup.";
RL Genes Genet. Syst. 78:383-389(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (GE14578 AND GE15127).
RC STRAIN=Tai18E2 / Tucson 14021-0261.01;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (HIS2A).
RX PubMed=14525923; DOI=10.1101/gr.1311003;
RA Domazet-Loso T., Tautz D.;
RT "An evolutionary analysis of orphan genes in Drosophila.";
RL Genome Res. 13:2213-2219(2003).
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; AB073635; BAC54556.1; -; Genomic_DNA.
DR EMBL; AB073636; BAJ06136.1; -; Genomic_DNA.
DR EMBL; AB105179; BAD02421.1; -; Genomic_DNA.
DR EMBL; CH897169; EDX00543.1; -; Genomic_DNA.
DR EMBL; CH899414; EDX00670.1; -; Genomic_DNA.
DR EMBL; AY232232; AAR10255.1; -; mRNA.
DR RefSeq; XP_002087242.1; XM_002087206.2.
DR RefSeq; XP_002087253.1; XM_002087217.2.
DR RefSeq; XP_002087344.1; XM_002087308.2.
DR RefSeq; XP_002087349.2; XM_002087313.2.
DR AlphaFoldDB; P84055; -.
DR SMR; P84055; -.
DR STRING; 7245.FBpp0259588; -.
DR EnsemblMetazoa; FBtr0261096; FBpp0259588; FBgn0232174.
DR EnsemblMetazoa; FBtr0261645; FBpp0260137; FBgn0232716.
DR GeneID; 6540447; -.
DR GeneID; 6540554; -.
DR GeneID; 6540563; -.
DR KEGG; dya:Dyak_GE14578; -.
DR KEGG; dya:Dyak_GE15127; -.
DR FlyBase; FBgn0028752; Dyak\His2A.
DR eggNOG; KOG1756; Eukaryota.
DR HOGENOM; CLU_062828_3_3_1; -.
DR OMA; RTEGKHE; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P84055; -.
DR ChiTaRS; His2Av; fly.
DR Proteomes; UP000002282; Unassembled WGS sequence.
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 2: Evidence at transcript level;
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_0000055224"
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
