H2AB1_HUMAN
ID H2AB1_HUMAN Reviewed; 115 AA.
AC P0C5Y9; A0PK90; P98176; Q5TZB2; Q6FG78; Q96PR7;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histone H2A-Bbd type 1 {ECO:0000305};
DE AltName: Full=H2A Barr body-deficient {ECO:0000303|PubMed:20008104};
DE Short=H2A.B {ECO:0000303|PubMed:24336483};
DE Short=H2A.Bbd {ECO:0000303|PubMed:20008104};
GN Name=H2AB1 {ECO:0000312|HGNC:HGNC:22516};
GN Synonyms=H2AFB1 {ECO:0000312|HGNC:HGNC:22516};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8528212; DOI=10.1093/hmg/4.7.1217;
RA Naylor J.A., Buck D., Green P.M., Williamson H., Bentley D., Giannelli F.;
RT "Investigation of the factor VIII intron 22 repeated region (int22h) and
RT the associated inversion junctions.";
RL Hum. Mol. Genet. 4:1217-1224(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, DOMAIN, AND SUBUNIT.
RX PubMed=15257289; DOI=10.1038/sj.emboj.7600316;
RA Bao Y., Konesky K., Park Y.-J., Rosu S., Dyer P.N., Rangasamy D.,
RA Tremethick D.J., Laybourn P.J., Luger K.;
RT "Nucleosomes containing the histone variant H2A.Bbd organize only 118 base
RT pairs of DNA.";
RL EMBO J. 23:3314-3324(2004).
RN [6]
RP FUNCTION.
RX PubMed=16287874; DOI=10.1128/mcb.25.23.10639-10651.2005;
RA Okuwaki M., Kato K., Shimahara H., Tate S., Nagata K.;
RT "Assembly and disassembly of nucleosome core particles containing histone
RT variants by human nucleosome assembly protein I.";
RL Mol. Cell. Biol. 25:10639-10651(2005).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16957777; DOI=10.1038/sj.emboj.7601310;
RA Doyen C.M., Montel F., Gautier T., Menoni H., Claudet C.,
RA Delacour-Larose M., Angelov D., Hamiche A., Bednar J.,
RA Faivre-Moskalenko C., Bouvet P., Dimitrov S.;
RT "Dissection of the unusual structural and functional properties of the
RT variant H2A.Bbd nucleosome.";
RL EMBO J. 25:4234-4244(2006).
RN [8]
RP FUNCTION.
RX PubMed=17591702; DOI=10.1128/mcb.00376-07;
RA Menoni H., Gasparutto D., Hamiche A., Cadet J., Dimitrov S., Bouvet P.,
RA Angelov D.;
RT "ATP-dependent chromatin remodeling is required for base excision repair in
RT conventional but not in variant H2A.Bbd nucleosomes.";
RL Mol. Cell. Biol. 27:5949-5956(2007).
RN [9]
RP FUNCTION.
RX PubMed=17726088; DOI=10.1096/fj.07-9255com;
RA Eirin-Lopez J.M., Ishibashi T., Ausio J.;
RT "H2A.Bbd: a quickly evolving hypervariable mammalian histone that
RT destabilizes nucleosomes in an acetylation-independent way.";
RL FASEB J. 22:316-326(2008).
RN [10]
RP FUNCTION.
RX PubMed=18329190; DOI=10.1016/j.gene.2008.02.003;
RA Gonzalez-Romero R., Mendez J., Ausio J., Eirin-Lopez J.M.;
RT "Quickly evolving histones, nucleosome stability and chromatin folding: all
RT about histone H2A.Bbd.";
RL Gene 413:1-7(2008).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20008104; DOI=10.1093/nar/gkp1129;
RA Ishibashi T., Li A., Eirin-Lopez J.M., Zhao M., Missiaen K., Abbott D.W.,
RA Meistrich M., Hendzel M.J., Ausio J.;
RT "H2A.Bbd: an X-chromosome-encoded histone involved in mammalian
RT spermiogenesis.";
RL Nucleic Acids Res. 38:1780-1789(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22795134; DOI=10.1016/j.molcel.2012.06.011;
RA Tolstorukov M.Y., Goldman J.A., Gilbert C., Ogryzko V., Kingston R.E.,
RA Park P.J.;
RT "Histone variant H2A.Bbd is associated with active transcription and mRNA
RT processing in human cells.";
RL Mol. Cell 47:596-607(2012).
RN [13]
RP FUNCTION.
RX PubMed=24753410; DOI=10.1093/nar/gku303;
RA Sansoni V., Casas-Delucchi C.S., Rajan M., Schmidt A., Boenisch C.,
RA Thomae A.W., Staege M.S., Hake S.B., Cardoso M.C., Imhof A.;
RT "The histone variant H2A.Bbd is enriched at sites of DNA synthesis.";
RL Nucleic Acids Res. 42:6405-6420(2014).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=24336483; DOI=10.1038/srep03510;
RA Arimura Y., Kimura H., Oda T., Sato K., Osakabe A., Tachiwana H., Sato Y.,
RA Kinugasa Y., Ikura T., Sugiyama M., Sato M., Kurumizaka H.;
RT "Structural basis of a nucleosome containing histone H2A.B/H2A.Bbd that
RT transiently associates with reorganized chromatin.";
RL Sci. Rep. 3:3510-3510(2013).
RN [15]
RP ERRATUM OF PUBMED:24336483.
RX PubMed=26166249; DOI=10.1038/srep09628;
RA Arimura Y., Kimura H., Oda T., Sato K., Osakabe A., Tachiwana H., Sato Y.,
RA Kinugasa Y., Ikura T., Sugiyama M., Sato M., Kurumizaka H.;
RT "Corrigendum: Structural basis of a nucleosome containing histone
RT H2A.B/H2A.Bbd that transiently associates with reorganized chromatin.";
RL Sci. Rep. 5:9628-9628(2015).
CC -!- FUNCTION: Atypical histone H2A which can replace conventional H2A in
CC some nucleosomes and is associated with active transcription and mRNA
CC processing (PubMed:22795134). Nucleosomes wrap and compact DNA into
CC chromatin, limiting DNA accessibility to the cellular machineries which
CC require DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability (PubMed:15257289, PubMed:16287874, PubMed:16957777,
CC PubMed:17591702, PubMed:17726088, PubMed:18329190, PubMed:22795134).
CC Nucleosomes containing this histone are less rigid and organize less
CC DNA than canonical nucleosomes in vivo (PubMed:15257289,
CC PubMed:16957777, PubMed:17591702, PubMed:24336483). They are enriched
CC in actively transcribed genes and associate with the elongating form of
CC RNA polymerase (PubMed:17591702, PubMed:24753410). They associate with
CC spliceosome components and are required for mRNA splicing
CC (PubMed:22795134). {ECO:0000269|PubMed:15257289,
CC ECO:0000269|PubMed:16287874, ECO:0000269|PubMed:16957777,
CC ECO:0000269|PubMed:17591702, ECO:0000269|PubMed:17726088,
CC ECO:0000269|PubMed:18329190, ECO:0000269|PubMed:22795134,
CC ECO:0000269|PubMed:24336483, ECO:0000269|PubMed:24753410}.
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. May be incorporated into a proportion of
CC nucleosomes, replacing one or more H2A molecules.
CC {ECO:0000269|PubMed:15257289, ECO:0000269|PubMed:16957777}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20008104,
CC ECO:0000269|PubMed:24336483}. Chromosome {ECO:0000269|PubMed:20008104,
CC ECO:0000269|PubMed:22795134, ECO:0000269|PubMed:24336483}.
CC Note=Associated with the active X chromosome and with autosomes, while
CC it is absent from the inactive X chromosome and excluded from Barr
CC bodies. {ECO:0000269|PubMed:20008104}.
CC -!- TISSUE SPECIFICITY: Present in mature sperm.
CC {ECO:0000269|PubMed:20008104}.
CC -!- DOMAIN: The docking domain is responsible for the weaker
CC heterodimerization with H2B. {ECO:0000269|PubMed:15257289}.
CC -!- MISCELLANEOUS: In contrast to other H2A histones, it does not contain
CC the conserved residues that are the target of post-translational
CC modifications. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: Although related to variant histone H2AB1 in mouse (AC
CC Q9CQ70), it is unclear whether human and mouse H2AB1 proteins are
CC involved in similar processes. In mouse, variant histone H2AB1 is
CC specifically required to direct the transformation of dissociating
CC nucleosomes to protamine in male germ cells during spermatogenesis. It
CC is however unclear whether human protein, which participates in mRNA
CC processing and is associated with active transcription, is also
CC involved in nucleosomes to protamine replacement (PubMed:22795134).
CC {ECO:0000269|PubMed:22795134}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Histone H2A entry;
CC URL="https://en.wikipedia.org/wiki/Histone_H2A";
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DR EMBL; X86012; CAA59998.1; -; Genomic_DNA.
DR EMBL; CR542230; CAG47026.1; -; mRNA.
DR EMBL; BX842559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128034; AAI28035.1; -; mRNA.
DR CCDS; CCDS35458.1; -.
DR PIR; I37901; I37901.
DR RefSeq; NP_001017990.1; NM_001017990.1.
DR AlphaFoldDB; P0C5Y9; -.
DR SMR; P0C5Y9; -.
DR BioGRID; 138883; 24.
DR STRING; 9606.ENSP00000484261; -.
DR iPTMnet; P0C5Y9; -.
DR PhosphoSitePlus; P0C5Y9; -.
DR BioMuta; H2AFB1; -.
DR DMDM; 161784332; -.
DR MassIVE; P0C5Y9; -.
DR PaxDb; P0C5Y9; -.
DR PeptideAtlas; P0C5Y9; -.
DR PRIDE; P0C5Y9; -.
DR Antibodypedia; 74717; 56 antibodies from 13 providers.
DR DNASU; 474382; -.
DR Ensembl; ENST00000620016.2; ENSP00000484261.2; ENSG00000274183.2.
DR GeneID; 474382; -.
DR KEGG; hsa:474382; -.
DR MANE-Select; ENST00000620016.2; ENSP00000484261.2; NM_001017990.2; NP_001017990.1.
DR UCSC; uc004fmu.5; human.
DR CTD; 474382; -.
DR DisGeNET; 474382; -.
DR GeneCards; H2AB1; -.
DR HGNC; HGNC:22516; H2AB1.
DR HPA; ENSG00000274183; Tissue enriched (testis).
DR MIM; 301037; gene.
DR neXtProt; NX_P0C5Y9; -.
DR VEuPathDB; HostDB:ENSG00000274183; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000163020; -.
DR HOGENOM; CLU_062828_3_2_1; -.
DR InParanoid; P0C5Y9; -.
DR OMA; QMERGLW; -.
DR OrthoDB; 1516933at2759; -.
DR PhylomeDB; P0C5Y9; -.
DR TreeFam; TF300137; -.
DR PathwayCommons; P0C5Y9; -.
DR Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
DR Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-HSA-110331; Cleavage of the damaged purine.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-171306; Packaging Of Telomere Ends.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5334118; DNA methylation.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-HSA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-912446; Meiotic recombination.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR Reactome; R-HSA-9710421; Defective pyroptosis.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR SIGNOR; P0C5Y9; -.
DR BioGRID-ORCS; 474382; 99 hits in 593 CRISPR screens.
DR GeneWiki; H2AFB1; -.
DR GenomeRNAi; 474382; -.
DR Pharos; P0C5Y9; Tbio.
DR PRO; PR:P0C5Y9; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P0C5Y9; protein.
DR Bgee; ENSG00000274183; Expressed in lower esophagus mucosa and 85 other tissues.
DR Genevisible; P0C5Y9; HS.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; mRNA processing; Nucleosome core; Nucleus;
KW Reference proteome.
FT CHAIN 1..115
FT /note="Histone H2A-Bbd type 1"
FT /id="PRO_0000312805"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..115
FT /note="Docking domain"
FT /evidence="ECO:0000269|PubMed:15257289"
FT CONFLICT 109
FT /note="Q -> K (in Ref. 4; AAI28035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 115 AA; 12697 MW; 57CA60C8C2F5744B CRC64;
MPRRRRRRGS SGAGGRGRTC SRTVRAELSF SVSQVERSLR EGHYAQRLSR TAPVYLAAVI
EYLTAKVPEL AGNEAQNSGE RNITPLLLDM VVHNDRLLST LFNTTTISQV APGED
