Full text data of HIST1H2AB
HIST1H2AB
(H2AFA)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histone H2A type 1-B/E (Histone H2A.2; Histone H2A/a; Histone H2A/m)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H2A type 1-B/E (Histone H2A.2; Histone H2A/a; Histone H2A/m)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P04908
ID H2A1B_HUMAN Reviewed; 130 AA.
AC P04908; P28001; Q76P63;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Histone H2A type 1-B/E;
DE AltName: Full=Histone H2A.2;
DE AltName: Full=Histone H2A/a;
DE AltName: Full=Histone H2A/m;
GN Name=HIST1H2AB; Synonyms=H2AFM;
GN and
GN Name=HIST1H2AE; Synonyms=H2AFA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB).
RX PubMed=6647026; DOI=10.1093/nar/11.21.7409;
RA Zhong R., Roeder R.G., Heintz N.;
RT "The primary structure and expression of four cloned human histone
RT genes.";
RL Nucleic Acids Res. 11:7409-7425(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
RX PubMed=1916825; DOI=10.1016/0888-7543(91)90183-F;
RA Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
RT "Isolation and characterization of two human H1 histone genes within
RT clusters of core histone genes.";
RL Genomics 10:940-948(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
RX PubMed=9439656; DOI=10.1007/s004390050630;
RA Albig W., Doenecke D.;
RT "The human histone gene cluster at the D6S105 locus.";
RL Hum. Genet. 101:284-294(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB AND HIST1H2AE).
RX PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H2AE).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=15078818; DOI=10.1101/gad.1184604;
RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,
RA Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during
RT mitosis in the early Drosophila embryo.";
RL Genes Dev. 18:877-888(2004).
RN [8]
RP PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
RX PubMed=15010469; DOI=10.1074/jbc.M400099200;
RA Zhang Y., Griffin K., Mondal N., Parvin J.D.;
RT "Phosphorylation of histone H2A inhibits transcription on chromatin
RT templates.";
RL J. Biol. Chem. 279:21866-21872(2004).
RN [9]
RP UBIQUITINATION AT LYS-120.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
RA Jones R.S., Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, AND
RP ACETYLATION AT SER-2.
RX PubMed=11709551; DOI=10.1074/jbc.M107894200;
RA Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
RT "Global regulation of post-translational modifications on core
RT histones.";
RL J. Biol. Chem. 277:2579-2588(2002).
RN [11]
RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY.
RX PubMed=15823041; DOI=10.1021/bi047505c;
RA Hagiwara T., Hidaka Y., Yamada M.;
RT "Deimination of histone H2A and H4 at arginine 3 in HL-60
RT granulocytes.";
RL Biochemistry 44:5827-5834(2005).
RN [12]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene
RT silencing.";
RL Mol. Cell 20:845-854(2005).
RN [13]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16702407; DOI=10.1101/gad.373706;
RA Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,
RA de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,
RA Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
RT "DNA damage triggers nucleotide excision repair-dependent
RT monoubiquitylation of histone H2A.";
RL Genes Dev. 20:1343-1352(2006).
RN [14]
RP MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by
RT top down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
RN [15]
RP UBIQUITINATION.
RX PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
RA Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
RA Lukas C., Lukas J.;
RT "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
RT assembly of repair proteins.";
RL Cell 131:887-900(2007).
RN [16]
RP UBIQUITINATION.
RX PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
RA Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
RT "RNF8 transduces the DNA-damage signal via histone ubiquitylation and
RT checkpoint protein assembly.";
RL Cell 131:901-914(2007).
RN [17]
RP UBIQUITINATION.
RX PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
RA Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
RA Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
RA Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
RA Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
RA Durocher D.;
RT "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
RT cascade at sites of DNA damage.";
RL Cell 136:420-434(2009).
RN [18]
RP UBIQUITINATION.
RX PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
RA Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
RA Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J.,
RA Lukas J., Lukas C.;
RT "RNF168 binds and amplifies ubiquitin conjugates on damaged
RT chromosomes to allow accumulation of repair proteins.";
RL Cell 136:435-446(2009).
RN [19]
RP CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [20]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
RA Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
RA Vermeulen W., Marteijn J.A., Sixma T.K.;
RT "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage
RT signaling.";
RL Cell 150:1182-1195(2012).
RN [21]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22713238; DOI=10.4161/cc.20919;
RA Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.;
RT "A novel ubiquitin mark at the N-terminal tail of histone H2As
RT targeted by RNF168 ubiquitin ligase.";
RL Cell Cycle 11:2538-2544(2012).
RN [22]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=24140421; DOI=10.1016/j.molcel.2013.09.017;
RA Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S.,
RA Heo K., An W.;
RT "VprBP has intrinsic kinase activity targeting histone H2A and
RT represses gene transcription.";
RL Mol. Cell 0:0-0(2013).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones
CC thereby play a central role in transcription regulation, DNA
CC repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and
CC nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and
CC RNF2/RING2 complex gives a specific tag for epigenetic
CC transcriptional repression and participates in X chromosome
CC inactivation of female mammals. It is involved in the initiation
CC of both imprinted and random X inactivation. Ubiquitinated H2A is
CC enriched in inactive X chromosome chromatin. Ubiquitination of H2A
CC functions downstream of methylation of 'Lys-27' of histone H3
CC (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by
CC ultraviolet and may be involved in DNA repair. Following DNA
CC double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
CC linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3
CC ligases RNF8 and RNF168, leading to the recruitment of repair
CC proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-
CC 16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage
CC is initiated by RNF168 that mediates monoubiquitination at these 2
CC sites, and 'Lys-63'-linked ubiquitin are then conjugated to
CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin
CC chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-
CC 63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct
CC events.
CC -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during
CC mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly
CC represses transcription. Acetylation of H3 inhibits Ser-2
CC phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121
CC (H2AT120ph) by VPRBP is present in the regulatory region of many
CC tumor suppresor genes and down-regulates their transcription.
CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex
CC may play a crucial role in the germ-cell lineage (By similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- MASS SPECTROMETRY: Mass=14037.9; Method=Electrospray; Range=2-130;
CC Note=Monoisotopic with N-acetylserine; Source=PubMed:16457589;
CC -!- SIMILARITY: Belongs to the histone H2A family.
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DR EMBL; X00089; CAA24951.1; -; Genomic_DNA.
DR EMBL; M60752; AAA63191.1; -; Genomic_DNA.
DR EMBL; Z83741; CAB06036.1; -; Genomic_DNA.
DR EMBL; AY131983; AAN59964.1; -; Genomic_DNA.
DR EMBL; AY131986; AAN59967.1; -; Genomic_DNA.
DR EMBL; AL031777; CAB39192.1; -; Genomic_DNA.
DR EMBL; BC093836; AAH93836.1; -; mRNA.
DR EMBL; BC093862; AAH93862.1; -; mRNA.
DR PIR; B26318; HSHUA5.
DR PIR; G40335; G40335.
DR RefSeq; NP_003504.2; NM_003513.2.
DR RefSeq; NP_066390.1; NM_021052.2.
DR UniGene; Hs.121017; -.
DR UniGene; Hs.248174; -.
DR PDB; 2CV5; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3A6N; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AFA; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3AN2; X-ray; 3.60 A; C/G=1-130.
DR PDB; 3AV1; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3AV2; X-ray; 2.80 A; C/G=1-130.
DR PDB; 3AYW; X-ray; 2.90 A; C/G=1-130.
DR PDB; 3AZE; X-ray; 3.00 A; C/G=1-130.
DR PDB; 3AZF; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZG; X-ray; 2.40 A; C/G=1-130.
DR PDB; 3AZH; X-ray; 3.49 A; C/G=1-130.
DR PDB; 3AZI; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZJ; X-ray; 2.89 A; C/G=1-130.
DR PDB; 3AZK; X-ray; 3.20 A; C/G=1-130.
DR PDB; 3AZL; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZM; X-ray; 2.89 A; C/G=1-130.
DR PDB; 3AZN; X-ray; 3.00 A; C/G=1-130.
DR PDB; 3W96; X-ray; 3.00 A; C/G=11-130.
DR PDB; 3W97; X-ray; 3.20 A; C/G=1-130.
DR PDB; 3W98; X-ray; 3.42 A; C/G=1-130.
DR PDB; 3W99; X-ray; 3.00 A; C/G=1-130.
DR PDBsum; 2CV5; -.
DR PDBsum; 3A6N; -.
DR PDBsum; 3AFA; -.
DR PDBsum; 3AN2; -.
DR PDBsum; 3AV1; -.
DR PDBsum; 3AV2; -.
DR PDBsum; 3AYW; -.
DR PDBsum; 3AZE; -.
DR PDBsum; 3AZF; -.
DR PDBsum; 3AZG; -.
DR PDBsum; 3AZH; -.
DR PDBsum; 3AZI; -.
DR PDBsum; 3AZJ; -.
DR PDBsum; 3AZK; -.
DR PDBsum; 3AZL; -.
DR PDBsum; 3AZM; -.
DR PDBsum; 3AZN; -.
DR PDBsum; 3W96; -.
DR PDBsum; 3W97; -.
DR PDBsum; 3W98; -.
DR PDBsum; 3W99; -.
DR ProteinModelPortal; P04908; -.
DR SMR; P04908; 12-119.
DR DIP; DIP-44197N; -.
DR IntAct; P04908; 26.
DR MINT; MINT-1139478; -.
DR STRING; 9606.ENSP00000259791; -.
DR PhosphoSite; P04908; -.
DR PaxDb; P04908; -.
DR PRIDE; P04908; -.
DR DNASU; 3012; -.
DR DNASU; 8335; -.
DR Ensembl; ENST00000259791; ENSP00000259791; ENSG00000137259.
DR Ensembl; ENST00000303910; ENSP00000303373; ENSG00000168274.
DR GeneID; 3012; -.
DR GeneID; 8335; -.
DR KEGG; hsa:3012; -.
DR KEGG; hsa:8335; -.
DR UCSC; uc003nft.1; human.
DR CTD; 3012; -.
DR CTD; 8335; -.
DR GeneCards; GC06M026033; -.
DR GeneCards; GC06P026255; -.
DR HGNC; HGNC:4734; HIST1H2AB.
DR HGNC; HGNC:4724; HIST1H2AE.
DR HPA; CAB011483; -.
DR HPA; CAB012242; -.
DR MIM; 602786; gene.
DR MIM; 602795; gene.
DR neXtProt; NX_P04908; -.
DR PharmGKB; PA29111; -.
DR eggNOG; COG5262; -.
DR HOGENOM; HOG000234652; -.
DR HOVERGEN; HBG009342; -.
DR InParanoid; P04908; -.
DR KO; K11251; -.
DR OMA; TKNAQSR; -.
DR OrthoDB; EOG7M0NTR; -.
DR PhylomeDB; P04908; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR EvolutionaryTrace; P04908; -.
DR GeneWiki; HIST1H2AB; -.
DR GeneWiki; HIST1H2AE; -.
DR NextBio; 11940; -.
DR PRO; PR:P04908; -.
DR ArrayExpress; P04908; -.
DR Bgee; P04908; -.
DR CleanEx; HS_HIST1H2AB; -.
DR CleanEx; HS_HIST1H2AE; -.
DR Genevestigator; P04908; -.
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:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR002119; Histone_H2A.
DR Pfam; PF00125; Histone; 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; Citrullination;
KW Complete proteome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 130 Histone H2A type 1-B/E.
FT /FTId=PRO_0000055237.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine; by RPS6KA5.
FT MOD_RES 4 4 Citrulline.
FT MOD_RES 6 6 N6-acetyllysine (By similarity).
FT MOD_RES 37 37 N6-crotonyl-L-lysine.
FT MOD_RES 119 119 N6-crotonyl-L-lysine.
FT MOD_RES 120 120 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 121 121 Phosphothreonine; by VPRBP.
FT MOD_RES 126 126 N6-crotonyl-L-lysine.
FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT MUTAGEN 2 2 S->A: Blocks the inhibition of
FT transcription by RPS6KA5/MSK1.
FT CONFLICT 38 39 GN -> AH (in Ref. 1; CAA24951).
FT HELIX 18 22
FT HELIX 28 36
FT TURN 37 39
FT STRAND 42 44
FT HELIX 47 73
FT STRAND 77 79
FT HELIX 81 89
FT HELIX 92 97
FT TURN 98 100
FT STRAND 101 103
FT HELIX 114 116
SQ SEQUENCE 130 AA; 14135 MW; 9CFE6184B2CC89F5 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK
//
ID H2A1B_HUMAN Reviewed; 130 AA.
AC P04908; P28001; Q76P63;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 144.
DE RecName: Full=Histone H2A type 1-B/E;
DE AltName: Full=Histone H2A.2;
DE AltName: Full=Histone H2A/a;
DE AltName: Full=Histone H2A/m;
GN Name=HIST1H2AB; Synonyms=H2AFM;
GN and
GN Name=HIST1H2AE; Synonyms=H2AFA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB).
RX PubMed=6647026; DOI=10.1093/nar/11.21.7409;
RA Zhong R., Roeder R.G., Heintz N.;
RT "The primary structure and expression of four cloned human histone
RT genes.";
RL Nucleic Acids Res. 11:7409-7425(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
RX PubMed=1916825; DOI=10.1016/0888-7543(91)90183-F;
RA Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
RT "Isolation and characterization of two human H1 histone genes within
RT clusters of core histone genes.";
RL Genomics 10:940-948(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AE).
RX PubMed=9439656; DOI=10.1007/s004390050630;
RA Albig W., Doenecke D.;
RT "The human histone gene cluster at the D6S105 locus.";
RL Hum. Genet. 101:284-294(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2AB AND HIST1H2AE).
RX PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST1H2AE).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=15078818; DOI=10.1101/gad.1184604;
RA Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,
RA Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
RT "Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during
RT mitosis in the early Drosophila embryo.";
RL Genes Dev. 18:877-888(2004).
RN [8]
RP PHOSPHORYLATION AT SER-2, AND MUTAGENESIS OF SER-2.
RX PubMed=15010469; DOI=10.1074/jbc.M400099200;
RA Zhang Y., Griffin K., Mondal N., Parvin J.D.;
RT "Phosphorylation of histone H2A inhibits transcription on chromatin
RT templates.";
RL J. Biol. Chem. 279:21866-21872(2004).
RN [9]
RP UBIQUITINATION AT LYS-120.
RX PubMed=15386022; DOI=10.1038/nature02985;
RA Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
RA Jones R.S., Zhang Y.;
RT "Role of histone H2A ubiquitination in Polycomb silencing.";
RL Nature 431:873-878(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-2, AND
RP ACETYLATION AT SER-2.
RX PubMed=11709551; DOI=10.1074/jbc.M107894200;
RA Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
RT "Global regulation of post-translational modifications on core
RT histones.";
RL J. Biol. Chem. 277:2579-2588(2002).
RN [11]
RP ACETYLATION AT SER-2, CITRULLINATION AT ARG-4, AND MASS SPECTROMETRY.
RX PubMed=15823041; DOI=10.1021/bi047505c;
RA Hagiwara T., Hidaka Y., Yamada M.;
RT "Deimination of histone H2A and H4 at arginine 3 in HL-60
RT granulocytes.";
RL Biochemistry 44:5827-5834(2005).
RN [12]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16359901; DOI=10.1016/j.molcel.2005.12.002;
RA Cao R., Tsukada Y., Zhang Y.;
RT "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene
RT silencing.";
RL Mol. Cell 20:845-854(2005).
RN [13]
RP UBIQUITINATION AT LYS-120.
RX PubMed=16702407; DOI=10.1101/gad.373706;
RA Bergink S., Salomons F.A., Hoogstraten D., Groothuis T.A.M.,
RA de Waard H., Wu J., Yuan L., Citterio E., Houtsmuller A.B.,
RA Neefjes J., Hoeijmakers J.H.J., Vermeulen W., Dantuma N.P.;
RT "DNA damage triggers nucleotide excision repair-dependent
RT monoubiquitylation of histone H2A.";
RL Genes Dev. 20:1343-1352(2006).
RN [14]
RP MASS SPECTROMETRY, AND ACETYLATION AT SER-2.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by
RT top down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
RN [15]
RP UBIQUITINATION.
RX PubMed=18001824; DOI=10.1016/j.cell.2007.09.040;
RA Mailand N., Bekker-Jensen S., Faustrup H., Melander F., Bartek J.,
RA Lukas C., Lukas J.;
RT "RNF8 ubiquitylates histones at DNA double-strand breaks and promotes
RT assembly of repair proteins.";
RL Cell 131:887-900(2007).
RN [16]
RP UBIQUITINATION.
RX PubMed=18001825; DOI=10.1016/j.cell.2007.09.041;
RA Huen M.S.Y., Grant R., Manke I., Minn K., Yu X., Yaffe M.B., Chen J.;
RT "RNF8 transduces the DNA-damage signal via histone ubiquitylation and
RT checkpoint protein assembly.";
RL Cell 131:901-914(2007).
RN [17]
RP UBIQUITINATION.
RX PubMed=19203578; DOI=10.1016/j.cell.2008.12.042;
RA Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K.,
RA Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M.,
RA Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L.,
RA Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R.,
RA Durocher D.;
RT "The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling
RT cascade at sites of DNA damage.";
RL Cell 136:420-434(2009).
RN [18]
RP UBIQUITINATION.
RX PubMed=19203579; DOI=10.1016/j.cell.2008.12.041;
RA Doil C., Mailand N., Bekker-Jensen S., Menard P., Larsen D.H.,
RA Pepperkok R., Ellenberg J., Panier S., Durocher D., Bartek J.,
RA Lukas J., Lukas C.;
RT "RNF168 binds and amplifies ubiquitin conjugates on damaged
RT chromosomes to allow accumulation of repair proteins.";
RL Cell 136:435-446(2009).
RN [19]
RP CROTONYLATION AT LYS-37; LYS-119; LYS-120 AND LYS-126.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [20]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22980979; DOI=10.1016/j.cell.2012.08.005;
RA Mattiroli F., Vissers J.H., van Dijk W.J., Ikpa P., Citterio E.,
RA Vermeulen W., Marteijn J.A., Sixma T.K.;
RT "RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA Damage
RT signaling.";
RL Cell 150:1182-1195(2012).
RN [21]
RP UBIQUITINATION AT LYS-14 AND LYS-16 BY RNF168.
RX PubMed=22713238; DOI=10.4161/cc.20919;
RA Gatti M., Pinato S., Maspero E., Soffientini P., Polo S., Penengo L.;
RT "A novel ubiquitin mark at the N-terminal tail of histone H2As
RT targeted by RNF168 ubiquitin ligase.";
RL Cell Cycle 11:2538-2544(2012).
RN [22]
RP PHOSPHORYLATION AT THR-121.
RX PubMed=24140421; DOI=10.1016/j.molcel.2013.09.017;
RA Kim K., Kim J.M., Kim J.S., Choi J., Lee Y.S., Neamati N., Song J.S.,
RA Heo K., An W.;
RT "VprBP has intrinsic kinase activity targeting histone H2A and
RT represses gene transcription.";
RL Mol. Cell 0:0-0(2013).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones
CC thereby play a central role in transcription regulation, DNA
CC repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and
CC nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
CC -!- PTM: Monoubiquitination of Lys-120 (H2AK119Ub) by RING1 and
CC RNF2/RING2 complex gives a specific tag for epigenetic
CC transcriptional repression and participates in X chromosome
CC inactivation of female mammals. It is involved in the initiation
CC of both imprinted and random X inactivation. Ubiquitinated H2A is
CC enriched in inactive X chromosome chromatin. Ubiquitination of H2A
CC functions downstream of methylation of 'Lys-27' of histone H3
CC (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by
CC ultraviolet and may be involved in DNA repair. Following DNA
CC double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63'
CC linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3
CC ligases RNF8 and RNF168, leading to the recruitment of repair
CC proteins to sites of DNA damage. Ubiquitination at Lys-14 and Lys-
CC 16 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage
CC is initiated by RNF168 that mediates monoubiquitination at these 2
CC sites, and 'Lys-63'-linked ubiquitin are then conjugated to
CC monoubiquitin; RNF8 is able to extend 'Lys-63'-linked ubiquitin
CC chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-
CC 63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct
CC events.
CC -!- PTM: Phosphorylation on Ser-2 (H2AS1ph) is enhanced during
CC mitosis. Phosphorylation on Ser-2 by RPS6KA5/MSK1 directly
CC represses transcription. Acetylation of H3 inhibits Ser-2
CC phosphorylation by RPS6KA5/MSK1. Phosphorylation at Thr-121
CC (H2AT120ph) by VPRBP is present in the regulatory region of many
CC tumor suppresor genes and down-regulates their transcription.
CC -!- PTM: Symmetric dimethylation on Arg-4 by the PRDM1/PRMT5 complex
CC may play a crucial role in the germ-cell lineage (By similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- MASS SPECTROMETRY: Mass=14037.9; Method=Electrospray; Range=2-130;
CC Note=Monoisotopic with N-acetylserine; Source=PubMed:16457589;
CC -!- SIMILARITY: Belongs to the histone H2A family.
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DR EMBL; X00089; CAA24951.1; -; Genomic_DNA.
DR EMBL; M60752; AAA63191.1; -; Genomic_DNA.
DR EMBL; Z83741; CAB06036.1; -; Genomic_DNA.
DR EMBL; AY131983; AAN59964.1; -; Genomic_DNA.
DR EMBL; AY131986; AAN59967.1; -; Genomic_DNA.
DR EMBL; AL031777; CAB39192.1; -; Genomic_DNA.
DR EMBL; BC093836; AAH93836.1; -; mRNA.
DR EMBL; BC093862; AAH93862.1; -; mRNA.
DR PIR; B26318; HSHUA5.
DR PIR; G40335; G40335.
DR RefSeq; NP_003504.2; NM_003513.2.
DR RefSeq; NP_066390.1; NM_021052.2.
DR UniGene; Hs.121017; -.
DR UniGene; Hs.248174; -.
DR PDB; 2CV5; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3A6N; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AFA; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3AN2; X-ray; 3.60 A; C/G=1-130.
DR PDB; 3AV1; X-ray; 2.50 A; C/G=1-130.
DR PDB; 3AV2; X-ray; 2.80 A; C/G=1-130.
DR PDB; 3AYW; X-ray; 2.90 A; C/G=1-130.
DR PDB; 3AZE; X-ray; 3.00 A; C/G=1-130.
DR PDB; 3AZF; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZG; X-ray; 2.40 A; C/G=1-130.
DR PDB; 3AZH; X-ray; 3.49 A; C/G=1-130.
DR PDB; 3AZI; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZJ; X-ray; 2.89 A; C/G=1-130.
DR PDB; 3AZK; X-ray; 3.20 A; C/G=1-130.
DR PDB; 3AZL; X-ray; 2.70 A; C/G=1-130.
DR PDB; 3AZM; X-ray; 2.89 A; C/G=1-130.
DR PDB; 3AZN; X-ray; 3.00 A; C/G=1-130.
DR PDB; 3W96; X-ray; 3.00 A; C/G=11-130.
DR PDB; 3W97; X-ray; 3.20 A; C/G=1-130.
DR PDB; 3W98; X-ray; 3.42 A; C/G=1-130.
DR PDB; 3W99; X-ray; 3.00 A; C/G=1-130.
DR PDBsum; 2CV5; -.
DR PDBsum; 3A6N; -.
DR PDBsum; 3AFA; -.
DR PDBsum; 3AN2; -.
DR PDBsum; 3AV1; -.
DR PDBsum; 3AV2; -.
DR PDBsum; 3AYW; -.
DR PDBsum; 3AZE; -.
DR PDBsum; 3AZF; -.
DR PDBsum; 3AZG; -.
DR PDBsum; 3AZH; -.
DR PDBsum; 3AZI; -.
DR PDBsum; 3AZJ; -.
DR PDBsum; 3AZK; -.
DR PDBsum; 3AZL; -.
DR PDBsum; 3AZM; -.
DR PDBsum; 3AZN; -.
DR PDBsum; 3W96; -.
DR PDBsum; 3W97; -.
DR PDBsum; 3W98; -.
DR PDBsum; 3W99; -.
DR ProteinModelPortal; P04908; -.
DR SMR; P04908; 12-119.
DR DIP; DIP-44197N; -.
DR IntAct; P04908; 26.
DR MINT; MINT-1139478; -.
DR STRING; 9606.ENSP00000259791; -.
DR PhosphoSite; P04908; -.
DR PaxDb; P04908; -.
DR PRIDE; P04908; -.
DR DNASU; 3012; -.
DR DNASU; 8335; -.
DR Ensembl; ENST00000259791; ENSP00000259791; ENSG00000137259.
DR Ensembl; ENST00000303910; ENSP00000303373; ENSG00000168274.
DR GeneID; 3012; -.
DR GeneID; 8335; -.
DR KEGG; hsa:3012; -.
DR KEGG; hsa:8335; -.
DR UCSC; uc003nft.1; human.
DR CTD; 3012; -.
DR CTD; 8335; -.
DR GeneCards; GC06M026033; -.
DR GeneCards; GC06P026255; -.
DR HGNC; HGNC:4734; HIST1H2AB.
DR HGNC; HGNC:4724; HIST1H2AE.
DR HPA; CAB011483; -.
DR HPA; CAB012242; -.
DR MIM; 602786; gene.
DR MIM; 602795; gene.
DR neXtProt; NX_P04908; -.
DR PharmGKB; PA29111; -.
DR eggNOG; COG5262; -.
DR HOGENOM; HOG000234652; -.
DR HOVERGEN; HBG009342; -.
DR InParanoid; P04908; -.
DR KO; K11251; -.
DR OMA; TKNAQSR; -.
DR OrthoDB; EOG7M0NTR; -.
DR PhylomeDB; P04908; -.
DR Reactome; REACT_111183; Meiosis.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_120956; Cellular responses to stress.
DR EvolutionaryTrace; P04908; -.
DR GeneWiki; HIST1H2AB; -.
DR GeneWiki; HIST1H2AE; -.
DR NextBio; 11940; -.
DR PRO; PR:P04908; -.
DR ArrayExpress; P04908; -.
DR Bgee; P04908; -.
DR CleanEx; HS_HIST1H2AB; -.
DR CleanEx; HS_HIST1H2AE; -.
DR Genevestigator; P04908; -.
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:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR002119; Histone_H2A.
DR Pfam; PF00125; Histone; 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; Citrullination;
KW Complete proteome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 130 Histone H2A type 1-B/E.
FT /FTId=PRO_0000055237.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 2 2 Phosphoserine; by RPS6KA5.
FT MOD_RES 4 4 Citrulline.
FT MOD_RES 6 6 N6-acetyllysine (By similarity).
FT MOD_RES 37 37 N6-crotonyl-L-lysine.
FT MOD_RES 119 119 N6-crotonyl-L-lysine.
FT MOD_RES 120 120 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 121 121 Phosphothreonine; by VPRBP.
FT MOD_RES 126 126 N6-crotonyl-L-lysine.
FT CROSSLNK 14 14 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 16 16 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 120 120 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT MUTAGEN 2 2 S->A: Blocks the inhibition of
FT transcription by RPS6KA5/MSK1.
FT CONFLICT 38 39 GN -> AH (in Ref. 1; CAA24951).
FT HELIX 18 22
FT HELIX 28 36
FT TURN 37 39
FT STRAND 42 44
FT HELIX 47 73
FT STRAND 77 79
FT HELIX 81 89
FT HELIX 92 97
FT TURN 98 100
FT STRAND 101 103
FT HELIX 114 116
SQ SEQUENCE 130 AA; 14135 MW; 9CFE6184B2CC89F5 CRC64;
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT
AEILELAGNA ARDNKKTRII PRHLQLAIRN DEELNKLLGR VTIAQGGVLP NIQAVLLPKK
TESHHKAKGK
//
MIM
602786
*RECORD*
*FIELD* NO
602786
*FIELD* TI
*602786 HISTONE GENE CLUSTER 1, H2A HISTONE FAMILY, MEMBER E; HIST1H2AE
;;HISTONE GENE CLUSTER 1, H2AE;;
read moreHIST1 CLUSTER, H2AE;;
H2A HISTONE FAMILY, MEMBER A; H2AFA;;
H2A/A;;
H2A.1
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2A histone family, see HIST1H2AA (613499).
CLONING
Albig et al. (1991) identified a gene encoding a member of the H2A class
of histones and designated it H2A.1. Albig and Doenecke (1997)
designated this gene H2A/a.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2A/a gene
to chromosome 6p21.3, within a cluster of 35 histone genes.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H2AE.
GENE FUNCTION
See HIST1H2AA (613499) for functional information on H2A histones.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; Doenecke, D.
: Isolation and characterization of two human H1 histone genes within
clusters of core histone genes. Genomics 10: 940-948, 1991.
3. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
4. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 01/11/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/11/2013
mgross: 7/19/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602786
*FIELD* TI
*602786 HISTONE GENE CLUSTER 1, H2A HISTONE FAMILY, MEMBER E; HIST1H2AE
;;HISTONE GENE CLUSTER 1, H2AE;;
read moreHIST1 CLUSTER, H2AE;;
H2A HISTONE FAMILY, MEMBER A; H2AFA;;
H2A/A;;
H2A.1
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2A histone family, see HIST1H2AA (613499).
CLONING
Albig et al. (1991) identified a gene encoding a member of the H2A class
of histones and designated it H2A.1. Albig and Doenecke (1997)
designated this gene H2A/a.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2A/a gene
to chromosome 6p21.3, within a cluster of 35 histone genes.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H2AE.
GENE FUNCTION
See HIST1H2AA (613499) for functional information on H2A histones.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Kardalinou, E.; Drabent, B.; Zimmer, A.; Doenecke, D.
: Isolation and characterization of two human H1 histone genes within
clusters of core histone genes. Genomics 10: 940-948, 1991.
3. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
4. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
*FIELD* CN
Matthew B. Gross - updated: 01/11/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/11/2013
mgross: 7/19/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/9/1998
MIM
602795
*RECORD*
*FIELD* NO
602795
*FIELD* TI
*602795 HISTONE GENE CLUSTER 1, H2A HISTONE FAMILY, MEMBER B; HIST1H2AB
;;HISTONE GENE CLUSTER 1, H2AB;;
read moreHIST1 CLUSTER, H2AB;;
H2A HISTONE FAMILY, MEMBER M; H2AFM;;
H2A/M
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2A histone family, see HIST1H2AA (613499).
CLONING
Zhong et al. (1983) identified a gene encoding a member of the H2A class
of histones. Albig and Doenecke (1997) designated this gene H2A/m.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2A/m gene
to chromosome 6p21.3, within a cluster of 35 histone genes.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H2AB.
GENE FUNCTION
See HIST1H2AA (613499) for functional information on H2A histones.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
3. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
4. Zhong, R.; Roeder, R. G.; Heintz, N.: The primary structure and
expression of four cloned human histone genes. Nucleic Acids Res. 11:
7409-7425, 1983.
*FIELD* CN
Matthew B. Gross - updated: 01/11/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/11/2013
mgross: 7/19/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602795
*FIELD* TI
*602795 HISTONE GENE CLUSTER 1, H2A HISTONE FAMILY, MEMBER B; HIST1H2AB
;;HISTONE GENE CLUSTER 1, H2AB;;
read moreHIST1 CLUSTER, H2AB;;
H2A HISTONE FAMILY, MEMBER M; H2AFM;;
H2A/M
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2A histone family, see HIST1H2AA (613499).
CLONING
Zhong et al. (1983) identified a gene encoding a member of the H2A class
of histones. Albig and Doenecke (1997) designated this gene H2A/m.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2A/m gene
to chromosome 6p21.3, within a cluster of 35 histone genes.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H2AB.
GENE FUNCTION
See HIST1H2AA (613499) for functional information on H2A histones.
*FIELD* RF
1. Albig, W.; Doenecke, D.: The human histone gene cluster at the
D6S105 locus. Hum. Genet. 101: 284-294, 1997.
2. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
3. Marzluff, W. F.; Gongidi, P.; Woods, K. R.; Jin, J.; Maltais, L.
J.: The human and mouse replication-dependent histone genes. Genomics 80:
487-498, 2002.
4. Zhong, R.; Roeder, R. G.; Heintz, N.: The primary structure and
expression of four cloned human histone genes. Nucleic Acids Res. 11:
7409-7425, 1983.
*FIELD* CN
Matthew B. Gross - updated: 01/11/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/11/2013
mgross: 7/19/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998