H2A_CAEEL
ID H2A_CAEEL Reviewed; 127 AA.
AC P09588; Q7JKF5;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Histone H2A;
GN Name=his-3; ORFNames=T10C6.12;
GN and
GN Name=his-7; ORFNames=F45F2.4;
GN and
GN Name=his-12; ORFNames=ZK131.6;
GN and
GN Name=his-16; ORFNames=ZK131.10;
GN and
GN Name=his-19; ORFNames=K06C4.11;
GN and
GN Name=his-21; ORFNames=K06C4.3;
GN and
GN Name=his-30; ORFNames=F35H10.1;
GN and
GN Name=his-33; ORFNames=F17E9.13;
GN and
GN Name=his-43; ORFNames=F08G2.2;
GN and
GN Name=his-47; ORFNames=B0035.7;
GN and
GN Name=his-51; ORFNames=F07B7.10;
GN and
GN Name=his-53; ORFNames=F07B7.3;
GN and
GN Name=his-57; ORFNames=F54E12.5;
GN and
GN Name=his-61; ORFNames=F55G1.10;
GN and
GN Name=his-65; ORFNames=H02I12.7;
GN and
GN Name=his-68; ORFNames=T23D8.6;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544730; DOI=10.1016/0022-2836(89)90566-4;
RA Roberts S.B., Emmons S.W., Childs G.;
RT "Nucleotide sequences of Caenorhabditis elegans core histone genes. Genes
RT for different histone classes share common flanking sequence elements.";
RL J. Mol. Biol. 206:567-577(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PROTEIN SEQUENCE OF 2-127, AND ACETYLATION AT SER-2; LYS-6; LYS-9 AND
RP LYS-11.
RC STRAIN=DR27;
RX PubMed=3606579; DOI=10.1042/bj2430297;
RA Vanfleteren J.R., van Bun S.M., van Beeumen J.J.;
RT "The primary structure of histone H2A from the nematode Caenorhabditis
RT elegans.";
RL Biochem. J. 243:297-300(1987).
RN [4]
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 [5]
RP UBIQUITINATION.
RX PubMed=15525528; DOI=10.1016/j.devcel.2004.10.005;
RA de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R.,
RA Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.;
RT "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to
RT heritable gene silencing and X inactivation.";
RL Dev. Cell 7:663-676(2004).
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: Monoubiquitination of Lys-121 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000305}.
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; X15633; CAA33641.1; -; Genomic_DNA.
DR EMBL; FO081169; CCD69634.1; -; Genomic_DNA.
DR EMBL; FO081135; CCD69397.1; -; Genomic_DNA.
DR EMBL; FO081551; CCD72371.1; -; Genomic_DNA.
DR EMBL; FO081551; CCD72361.1; -; Genomic_DNA.
DR EMBL; FO081223; CCD70021.1; -; Genomic_DNA.
DR EMBL; Z73102; CAA97414.1; -; Genomic_DNA.
DR EMBL; Z81128; CAB03399.1; -; Genomic_DNA.
DR EMBL; Z81495; CAB04056.1; -; Genomic_DNA.
DR EMBL; Z82271; CAB05212.1; -; Genomic_DNA.
DR EMBL; Z83245; CAB05836.1; -; Genomic_DNA.
DR EMBL; Z83245; CAB05838.1; -; Genomic_DNA.
DR EMBL; Z92789; CAB07221.1; -; Genomic_DNA.
DR EMBL; Z93388; CAB07656.1; -; Genomic_DNA.
DR EMBL; FO081059; CCD68872.1; -; Genomic_DNA.
DR EMBL; FO081059; CCD68866.1; -; Genomic_DNA.
DR EMBL; FO081018; CCD68534.1; -; Genomic_DNA.
DR PIR; S04238; HSKW2A.
DR RefSeq; NP_492642.1; NM_060241.4.
DR RefSeq; NP_496887.1; NM_064486.3.
DR RefSeq; NP_496891.1; NM_064490.1.
DR RefSeq; NP_496898.1; NM_064497.1.
DR RefSeq; NP_501201.1; NM_068800.3.
DR RefSeq; NP_501404.1; NM_069003.1.
DR RefSeq; NP_501408.1; NM_069007.1.
DR RefSeq; NP_502131.1; NM_069730.4.
DR RefSeq; NP_502141.1; NM_069740.1.
DR RefSeq; NP_502150.1; NM_069749.1.
DR RefSeq; NP_505198.1; NM_072797.1.
DR RefSeq; NP_505277.1; NM_072876.1.
DR RefSeq; NP_505280.1; NM_072879.1.
DR RefSeq; NP_505293.1; NM_072892.1.
DR RefSeq; NP_505296.1; NM_072895.1.
DR RefSeq; NP_507032.1; NM_074631.3.
DR PDB; 6K00; X-ray; 2.20 A; D=10-121.
DR PDB; 6K03; X-ray; 2.86 A; D=10-121.
DR PDB; 6K09; X-ray; 2.25 A; D=10-121.
DR PDBsum; 6K00; -.
DR PDBsum; 6K03; -.
DR PDBsum; 6K09; -.
DR AlphaFoldDB; P09588; -.
DR SMR; P09588; -.
DR BioGRID; 38282; 2.
DR BioGRID; 40311; 1.
DR BioGRID; 40314; 1.
DR BioGRID; 40320; 1.
DR BioGRID; 42639; 2.
DR BioGRID; 43147; 2.
DR BioGRID; 43154; 1.
DR BioGRID; 44299; 1.
DR BioGRID; 44303; 1.
DR BioGRID; 45064; 6.
DR BioGRID; 48911; 1.
DR BioGRID; 51394; 2.
DR BioGRID; 56170; 2.
DR BioGRID; 56176; 1.
DR BioGRID; 56178; 2.
DR BioGRID; 56827; 1.
DR STRING; 6239.B0035.7; -.
DR iPTMnet; P09588; -.
DR EPD; P09588; -.
DR PaxDb; P09588; -.
DR PRIDE; P09588; -.
DR EnsemblMetazoa; B0035.7.1; B0035.7.1; WBGene00001921.
DR EnsemblMetazoa; F07B7.10.1; F07B7.10.1; WBGene00001925.
DR EnsemblMetazoa; F07B7.3.1; F07B7.3.1; WBGene00001927.
DR EnsemblMetazoa; F08G2.2.1; F08G2.2.1; WBGene00001917.
DR EnsemblMetazoa; F17E9.13.1; F17E9.13.1; WBGene00001907.
DR EnsemblMetazoa; F35H10.1.1; F35H10.1.1; WBGene00001904.
DR EnsemblMetazoa; F45F2.4.1; F45F2.4.1; WBGene00001881.
DR EnsemblMetazoa; F54E12.5a.1; F54E12.5a.1; WBGene00001931.
DR EnsemblMetazoa; F55G1.10.1; F55G1.10.1; WBGene00001935.
DR EnsemblMetazoa; H02I12.7.1; H02I12.7.1; WBGene00001939.
DR EnsemblMetazoa; K06C4.11.1; K06C4.11.1; WBGene00001893.
DR EnsemblMetazoa; K06C4.3.1; K06C4.3.1; WBGene00001895.
DR EnsemblMetazoa; T10C6.12.1; T10C6.12.1; WBGene00001877.
DR EnsemblMetazoa; T23D8.6.1; T23D8.6.1; WBGene00001942.
DR EnsemblMetazoa; ZK131.10.1; ZK131.10.1; WBGene00001890.
DR EnsemblMetazoa; ZK131.6.1; ZK131.6.1; WBGene00001886.
DR GeneID; 172860; -.
DR GeneID; 175025; -.
DR GeneID; 175028; -.
DR GeneID; 175034; -.
DR GeneID; 177521; -.
DR GeneID; 178048; -.
DR GeneID; 178056; -.
DR GeneID; 179261; -.
DR GeneID; 179265; -.
DR GeneID; 180073; -.
DR GeneID; 184112; -.
DR GeneID; 186671; -.
DR GeneID; 191669; -.
DR GeneID; 191676; -.
DR GeneID; 191678; -.
DR GeneID; 259800; -.
DR KEGG; cel:CELE_B0035.7; -.
DR KEGG; cel:CELE_F07B7.10; -.
DR KEGG; cel:CELE_F07B7.3; -.
DR KEGG; cel:CELE_F08G2.2; -.
DR KEGG; cel:CELE_F17E9.13; -.
DR KEGG; cel:CELE_F35H10.1; -.
DR KEGG; cel:CELE_F45F2.4; -.
DR KEGG; cel:CELE_F55G1.10; -.
DR KEGG; cel:CELE_H02I12.7; -.
DR KEGG; cel:CELE_K06C4.11; -.
DR KEGG; cel:CELE_K06C4.3; -.
DR KEGG; cel:CELE_T10C6.12; -.
DR KEGG; cel:CELE_T23D8.6; -.
DR KEGG; cel:CELE_ZK131.10; -.
DR KEGG; cel:CELE_ZK131.6; -.
DR UCSC; T23D8.6; c. elegans.
DR CTD; 172860; -.
DR CTD; 175025; -.
DR CTD; 175028; -.
DR CTD; 175034; -.
DR CTD; 177521; -.
DR CTD; 178048; -.
DR CTD; 178056; -.
DR CTD; 179261; -.
DR CTD; 179265; -.
DR CTD; 180073; -.
DR CTD; 184112; -.
DR CTD; 186671; -.
DR CTD; 191669; -.
DR CTD; 191676; -.
DR CTD; 191678; -.
DR CTD; 259800; -.
DR WormBase; B0035.7; CE04501; WBGene00001921; his-47.
DR WormBase; F07B7.10; CE04501; WBGene00001925; his-51.
DR WormBase; F07B7.3; CE04501; WBGene00001927; his-53.
DR WormBase; F08G2.2; CE04501; WBGene00001917; his-43.
DR WormBase; F17E9.13; CE04501; WBGene00001907; his-33.
DR WormBase; F35H10.1; CE04501; WBGene00001904; his-30.
DR WormBase; F45F2.4; CE04501; WBGene00001881; his-7.
DR WormBase; F54E12.5; CE04501; WBGene00001931; his-57.
DR WormBase; F55G1.10; CE04501; WBGene00001935; his-61.
DR WormBase; H02I12.7; CE04501; WBGene00001939; his-65.
DR WormBase; K06C4.11; CE04501; WBGene00001893; his-19.
DR WormBase; K06C4.3; CE04501; WBGene00001895; his-21.
DR WormBase; T10C6.12; CE04501; WBGene00001877; his-3.
DR WormBase; T23D8.6; CE04501; WBGene00001942; his-68.
DR WormBase; ZK131.10; CE04501; WBGene00001890; his-16.
DR WormBase; ZK131.6; CE04501; WBGene00001886; his-12.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT01020000230360; -.
DR HOGENOM; CLU_062828_3_1_1; -.
DR InParanoid; P09588; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P09588; -.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-3214847; HATs acetylate histones.
DR Reactome; R-CEL-3214858; RMTs methylate histone arginines.
DR Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-CEL-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CEL-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-5689901; Metalloprotease DUBs.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P09588; -.
DR Proteomes; UP000001940; Chromosome I.
DR Proteomes; UP000001940; Chromosome II.
DR Proteomes; UP000001940; Chromosome IV.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00001877; Expressed in pharyngeal muscle cell (C elegans) 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; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 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:0000269|PubMed:3606579"
FT CHAIN 2..127
FT /note="Histone H2A"
FT /id="PRO_0000055210"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000305|PubMed:3606579"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:15133681"
FT MOD_RES 6
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:3606579"
FT MOD_RES 9
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:3606579"
FT MOD_RES 11
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:3606579"
FT MOD_RES 106
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000250"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:15525528"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:6K00"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:6K00"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:6K00"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6K03"
FT HELIX 48..74
FT /evidence="ECO:0007829|PDB:6K00"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6K00"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:6K00"
FT HELIX 93..98
FT /evidence="ECO:0007829|PDB:6K00"
SQ SEQUENCE 127 AA; 13405 MW; FBF085558F1BD340 CRC64;
MSGRGKGGKA KTGGKAKSRS SRAGLQFPVG RLHRILRKGN YAQRVGAGAP VYLAAVLEYL
AAEVLELAGN AARDNKKTRI APRHLQLAVR NDEELNKLLA GVTIAQGGVL PNIQAVLLPK
KTGGDKE
