H2A_DROME
ID H2A_DROME Reviewed; 124 AA.
AC P84051; P02267; Q4ABC7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Histone H2A;
GN Name=His2A; Synonyms=H2a;
GN and
GN Name=His2A:CG31618; ORFNames=CG31618;
GN and
GN Name=His2A:CG33808; ORFNames=CG33808;
GN and
GN Name=His2A:CG33814; ORFNames=CG33814;
GN and
GN Name=His2A:CG33817; ORFNames=CG33817;
GN and
GN Name=His2A:CG33820; ORFNames=CG33820;
GN and
GN Name=His2A:CG33823; ORFNames=CG33823;
GN and
GN Name=His2A:CG33826; ORFNames=CG33826;
GN and
GN Name=His2A:CG33829; ORFNames=CG33829;
GN and
GN Name=His2A:CG33832; ORFNames=CG33832;
GN and
GN Name=His2A:CG33835; ORFNames=CG33835;
GN and
GN Name=His2A:CG33838; ORFNames=CG33838;
GN and
GN Name=His2A:CG33841; ORFNames=CG33841;
GN and
GN Name=His2A:CG33844; ORFNames=CG33844;
GN and
GN Name=His2A:CG33847; ORFNames=CG33847;
GN and
GN Name=His2A:CG33850; ORFNames=CG33850;
GN and
GN Name=His2A:CG33862; ORFNames=CG33862;
GN and
GN Name=His2A:CG33865; ORFNames=CG33865;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2A).
RC STRAIN=AK-194;
RX PubMed=2536150; DOI=10.1093/nar/17.1.225;
RA Matsuo Y., Yamazaki T.;
RT "tRNA derived insertion element in histone gene repeating unit of
RT Drosophila melanogaster.";
RL Nucleic Acids Res. 17:225-238(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS2A:CG31618;
RP HIS2A:CG33808; HIS2A:CG33814; HIS2A:CG33817; HIS2A:CG33820; HIS2A:CG33823;
RP HIS2A:CG33826; HIS2A:CG33829; HIS2A:CG33832; HIS2A:CG33835; HIS2A:CG33838;
RP HIS2A:CG33841; HIS2A:CG33844; HIS2A:CG33847; HIS2A:CG33850; HIS2A:CG33862
RP AND HIS2A:CG33865).
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PROTEIN SEQUENCE OF 96-122, AND PHOSPHORYLATION AT THR-120.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=15078818; DOI=10.1101/gad.1184604;
RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N., Takio K.,
RA Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in
RT the early Drosophila embryo.";
RL Genes Dev. 18:877-888(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122 (HIS2A).
RA Goldberg M.L.;
RL Thesis (1979), University of Stanford, United States.
RN [6]
RP PHOSPHORYLATION AT SER-2.
RX PubMed=15133681; DOI=10.1007/s00412-004-0281-9;
RA Barber C.M., Turner F.B., Wang Y., Hagstrom K., Taverna S.D., Mollah S.,
RA Ueberheide B., Meyer B.J., Hunt D.F., Cheung P., Allis C.D.;
RT "The enhancement of histone H4 and H2A serine 1 phosphorylation during
RT mitosis and S-phase is evolutionarily conserved.";
RL Chromosoma 112:360-371(2004).
RN [7]
RP UBIQUITINATION.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P., Jones R.S.,
RA Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [8]
RP PHOSPHORYLATION AT THR-120.
RX PubMed=16230526; DOI=10.1101/gad.1348905;
RA Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
RT "A histone code in meiosis: the histone kinase, NHK-1, is required for
RT proper chromosomal architecture in Drosophila oocytes.";
RL Genes Dev. 19:2571-2582(2005).
RN [9]
RP SUCCINYLATION AT LYS-36.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
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 -!- INTERACTION:
CC P84051; Q9V6Q2: cid; NbExp=2; IntAct=EBI-182580, EBI-129287;
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. {ECO:0000269|PubMed:15078818,
CC ECO:0000269|PubMed:15133681, ECO:0000269|PubMed:16230526}.
CC -!- PTM: Monoubiquitination of Lys-119 by sce/dRING gives a specific tag
CC for epigenetic transcriptional repression.
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; X14215; CAA32431.1; -; Genomic_DNA.
DR EMBL; X14215; CAA32436.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN11125.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66488.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66497.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66502.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66507.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66512.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66517.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66522.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66527.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66532.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66537.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66542.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66547.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66552.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66557.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66577.1; -; Genomic_DNA.
DR EMBL; AE014134; AAZ66582.1; -; Genomic_DNA.
DR PIR; S10094; HSFF2.
DR RefSeq; NP_001027292.1; NM_001032121.2.
DR RefSeq; NP_001027301.1; NM_001032130.2.
DR RefSeq; NP_001027306.1; NM_001032135.2.
DR RefSeq; NP_001027311.1; NM_001032140.2.
DR RefSeq; NP_001027316.1; NM_001032145.2.
DR RefSeq; NP_001027321.1; NM_001032150.2.
DR RefSeq; NP_001027326.1; NM_001032155.2.
DR RefSeq; NP_001027331.1; NM_001032160.2.
DR RefSeq; NP_001027336.1; NM_001032165.2.
DR RefSeq; NP_001027341.1; NM_001032170.2.
DR RefSeq; NP_001027346.1; NM_001032175.2.
DR RefSeq; NP_001027351.1; NM_001032180.2.
DR RefSeq; NP_001027356.1; NM_001032185.2.
DR RefSeq; NP_001027361.1; NM_001032190.2.
DR RefSeq; NP_001027381.1; NM_001032210.2.
DR RefSeq; NP_001027386.1; NM_001032215.2.
DR RefSeq; NP_724343.1; NM_165382.3.
DR PDB; 2NQB; X-ray; 2.30 A; C/G=2-124.
DR PDB; 2PYO; X-ray; 2.43 A; C/G=2-121.
DR PDB; 4QLC; X-ray; 3.50 A; C/G=2-124.
DR PDB; 4X23; X-ray; 3.50 A; C/G/M/Q=16-117.
DR PDB; 5WCU; X-ray; 5.53 A; C/G/M/Q=15-118.
DR PDB; 6DZT; EM; 2.99 A; C/G=1-124.
DR PDB; 6PWE; EM; 3.95 A; C/G=1-124.
DR PDB; 6PWF; EM; 4.07 A; C/G=1-124.
DR PDB; 7PJ1; NMR; -; A=2-124.
DR PDBsum; 2NQB; -.
DR PDBsum; 2PYO; -.
DR PDBsum; 4QLC; -.
DR PDBsum; 4X23; -.
DR PDBsum; 5WCU; -.
DR PDBsum; 6DZT; -.
DR PDBsum; 6PWE; -.
DR PDBsum; 6PWF; -.
DR PDBsum; 7PJ1; -.
DR AlphaFoldDB; P84051; -.
DR SMR; P84051; -.
DR BioGRID; 534102; 1.
DR BioGRID; 77146; 35.
DR DIP; DIP-29504N; -.
DR IntAct; P84051; 9.
DR MINT; P84051; -.
DR STRING; 7227.FBpp0085249; -.
DR iPTMnet; P84051; -.
DR PaxDb; P84051; -.
DR PRIDE; P84051; -.
DR ABCD; P84051; 1 sequenced antibody.
DR EnsemblMetazoa; FBtr0085893; FBpp0085249; FBgn0051618.
DR EnsemblMetazoa; FBtr0091812; FBpp0091055; FBgn0053808.
DR EnsemblMetazoa; FBtr0091818; FBpp0091060; FBgn0053814.
DR EnsemblMetazoa; FBtr0091821; FBpp0091063; FBgn0053817.
DR EnsemblMetazoa; FBtr0091824; FBpp0091066; FBgn0053820.
DR EnsemblMetazoa; FBtr0091827; FBpp0091069; FBgn0053823.
DR EnsemblMetazoa; FBtr0091830; FBpp0091072; FBgn0053826.
DR EnsemblMetazoa; FBtr0091833; FBpp0091075; FBgn0053829.
DR EnsemblMetazoa; FBtr0091836; FBpp0091078; FBgn0053832.
DR EnsemblMetazoa; FBtr0091839; FBpp0091081; FBgn0053835.
DR EnsemblMetazoa; FBtr0091842; FBpp0091084; FBgn0053838.
DR EnsemblMetazoa; FBtr0091845; FBpp0091087; FBgn0053841.
DR EnsemblMetazoa; FBtr0091848; FBpp0091090; FBgn0053844.
DR EnsemblMetazoa; FBtr0091851; FBpp0091093; FBgn0053847.
DR EnsemblMetazoa; FBtr0091854; FBpp0091096; FBgn0053850.
DR EnsemblMetazoa; FBtr0091866; FBpp0091108; FBgn0053862.
DR EnsemblMetazoa; FBtr0091869; FBpp0091111; FBgn0053865.
DR GeneID; 318855; -.
DR GeneID; 3771774; -.
DR GeneID; 3771783; -.
DR GeneID; 3771785; -.
DR GeneID; 3772148; -.
DR GeneID; 3772278; -.
DR GeneID; 3772282; -.
DR GeneID; 3772345; -.
DR GeneID; 3772351; -.
DR GeneID; 3772360; -.
DR GeneID; 3772447; -.
DR GeneID; 3772448; -.
DR GeneID; 3772505; -.
DR GeneID; 3772541; -.
DR GeneID; 3772565; -.
DR GeneID; 3772618; -.
DR GeneID; 3772632; -.
DR KEGG; dme:Dmel_CG31618; -.
DR KEGG; dme:Dmel_CG33808; -.
DR KEGG; dme:Dmel_CG33814; -.
DR KEGG; dme:Dmel_CG33817; -.
DR KEGG; dme:Dmel_CG33820; -.
DR KEGG; dme:Dmel_CG33823; -.
DR KEGG; dme:Dmel_CG33826; -.
DR KEGG; dme:Dmel_CG33829; -.
DR KEGG; dme:Dmel_CG33832; -.
DR KEGG; dme:Dmel_CG33835; -.
DR KEGG; dme:Dmel_CG33838; -.
DR KEGG; dme:Dmel_CG33841; -.
DR KEGG; dme:Dmel_CG33844; -.
DR KEGG; dme:Dmel_CG33847; -.
DR KEGG; dme:Dmel_CG33850; -.
DR KEGG; dme:Dmel_CG33862; -.
DR KEGG; dme:Dmel_CG33865; -.
DR UCSC; CG31618-RA; d. melanogaster.
DR CTD; 318855; -.
DR CTD; 3771774; -.
DR CTD; 3771783; -.
DR CTD; 3771785; -.
DR CTD; 3772148; -.
DR CTD; 3772278; -.
DR CTD; 3772282; -.
DR CTD; 3772345; -.
DR CTD; 3772351; -.
DR CTD; 3772360; -.
DR CTD; 3772447; -.
DR CTD; 3772448; -.
DR CTD; 3772505; -.
DR CTD; 3772541; -.
DR CTD; 3772565; -.
DR CTD; 3772618; -.
DR CTD; 3772632; -.
DR FlyBase; FBgn0001196; His2A.
DR FlyBase; FBgn0051618; His2A:CG31618.
DR FlyBase; FBgn0053808; His2A:CG33808.
DR FlyBase; FBgn0053814; His2A:CG33814.
DR FlyBase; FBgn0053817; His2A:CG33817.
DR FlyBase; FBgn0053820; His2A:CG33820.
DR FlyBase; FBgn0053823; His2A:CG33823.
DR FlyBase; FBgn0053826; His2A:CG33826.
DR FlyBase; FBgn0053829; His2A:CG33829.
DR FlyBase; FBgn0053832; His2A:CG33832.
DR FlyBase; FBgn0053835; His2A:CG33835.
DR FlyBase; FBgn0053838; His2A:CG33838.
DR FlyBase; FBgn0053841; His2A:CG33841.
DR FlyBase; FBgn0053844; His2A:CG33844.
DR FlyBase; FBgn0053847; His2A:CG33847.
DR FlyBase; FBgn0053850; His2A:CG33850.
DR FlyBase; FBgn0053862; His2A:CG33862.
DR FlyBase; FBgn0053865; His2A:CG33865.
DR VEuPathDB; VectorBase:FBgn0051618; -.
DR VEuPathDB; VectorBase:FBgn0053808; -.
DR VEuPathDB; VectorBase:FBgn0053814; -.
DR VEuPathDB; VectorBase:FBgn0053817; -.
DR VEuPathDB; VectorBase:FBgn0053820; -.
DR VEuPathDB; VectorBase:FBgn0053823; -.
DR VEuPathDB; VectorBase:FBgn0053826; -.
DR VEuPathDB; VectorBase:FBgn0053829; -.
DR VEuPathDB; VectorBase:FBgn0053832; -.
DR VEuPathDB; VectorBase:FBgn0053835; -.
DR VEuPathDB; VectorBase:FBgn0053838; -.
DR VEuPathDB; VectorBase:FBgn0053841; -.
DR VEuPathDB; VectorBase:FBgn0053844; -.
DR VEuPathDB; VectorBase:FBgn0053847; -.
DR VEuPathDB; VectorBase:FBgn0053850; -.
DR VEuPathDB; VectorBase:FBgn0053862; -.
DR VEuPathDB; VectorBase:FBgn0053865; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000164494; -.
DR HOGENOM; CLU_062828_3_3_1; -.
DR InParanoid; P84051; -.
DR OMA; RTEGKHE; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P84051; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-3214847; HATs acetylate histones.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR Reactome; R-DME-5689901; Metalloprotease DUBs.
DR Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; P84051; -.
DR ChiTaRS; His2Av; fly.
DR EvolutionaryTrace; P84051; -.
DR PRO; PR:P84051; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0051618; Expressed in midgut and 10 other tissues.
DR Genevisible; P84051; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000786; C:nucleosome; ISS:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; ISS:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; ISS:FlyBase.
DR GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR CDD; cd00074; H2A; 1.
DR DisProt; DP01546; -.
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 3D-structure; Acetylation; Chromosome; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..124
FT /note="Histone H2A"
FT /id="PRO_0000055222"
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:0000305|PubMed:15133681"
FT MOD_RES 36
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 104
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15078818,
FT ECO:0000269|PubMed:16230526"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:15386022"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:7PJ1"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 46..72
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:2NQB"
FT HELIX 91..96
FT /evidence="ECO:0007829|PDB:2NQB"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2NQB"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7PJ1"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2NQB"
SQ SEQUENCE 124 AA; 13363 MW; 725BA63C393155F6 CRC64;
MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA
EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
EKKA
