H2AB2_HUMAN
ID H2AB2_HUMAN Reviewed; 115 AA.
AC P0C5Z0; A1L4E4; 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 110.
DE RecName: Full=Histone H2A-Bbd type 2/3;
DE AltName: Full=H2A Barr body-deficient;
DE Short=H2A.Bbd;
GN Name=H2AB2 {ECO:0000312|HGNC:HGNC:18298};
GN Synonyms=H2AFB2 {ECO:0000312|HGNC:HGNC:18298};
GN and
GN Name=H2AB3 {ECO:0000312|HGNC:HGNC:14455};
GN Synonyms=H2ABBD, H2AFB, H2AFB3 {ECO:0000312|HGNC:HGNC:14455};
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 [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=11266453; DOI=10.1083/jcb.152.2.375;
RA Chadwick B.P., Willard H.F.;
RT "A novel chromatin protein, distantly related to histone H2A, is largely
RT excluded from the inactive X chromosome.";
RL J. Cell Biol. 152:375-384(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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, AND DOMAIN.
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.
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).
CC -!- FUNCTION: Atypical histone H2A which can replace conventional H2A in
CC some nucleosomes and is associated with active transcription and mRNA
CC processing. Nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability.
CC Nucleosomes containing this histone are less rigid and organize less
CC DNA than canonical nucleosomes in vivo. They are enriched in actively
CC transcribed genes and associate with the elongating form of RNA
CC polymerase. They associate with spliceosome components and are required
CC for mRNA splicing. May participate in spermatogenesis.
CC {ECO:0000269|PubMed:15257289, ECO:0000269|PubMed:16287874,
CC ECO:0000269|PubMed:16957777, ECO:0000269|PubMed:17591702,
CC ECO:0000269|PubMed:17726088, ECO:0000269|PubMed:18329190,
CC ECO:0000269|PubMed:22795134}.
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 -!- INTERACTION:
CC P0C5Z0; Q99880: H2BC13; NbExp=3; IntAct=EBI-13318575, EBI-1237119;
CC P0C5Z0; U3KQK0: H2BC15; NbExp=3; IntAct=EBI-13318575, EBI-12142839;
CC P0C5Z0; Q14696: MESD; NbExp=3; IntAct=EBI-13318575, EBI-6165891;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20008104}. Chromosome
CC {ECO:0000269|PubMed:20008104, ECO:0000269|PubMed:22795134}.
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.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Histone H2A entry;
CC URL="https://en.wikipedia.org/wiki/Histone_H2A";
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DR EMBL; AF254576; AAL01652.1; -; mRNA.
DR EMBL; BX276110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX682237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72649.1; -; Genomic_DNA.
DR EMBL; BC101409; AAI01410.1; -; mRNA.
DR EMBL; BC101415; AAI01416.1; -; mRNA.
DR EMBL; BC101417; AAI01418.1; -; mRNA.
DR EMBL; BC101418; AAI01419.1; -; mRNA.
DR EMBL; BC130510; AAI30511.1; -; mRNA.
DR EMBL; BC130512; AAI30513.1; -; mRNA.
DR EMBL; BC134365; AAI34366.1; -; mRNA.
DR CCDS; CCDS35461.1; -.
DR CCDS; CCDS35464.1; -.
DR RefSeq; NP_001017991.1; NM_001017991.2.
DR RefSeq; NP_542451.1; NM_080720.1.
DR PDB; 6A7U; X-ray; 2.60 A; A=2-115.
DR PDB; 6M4G; EM; 2.80 A; C/G=1-115.
DR PDB; 6M4H; EM; 3.90 A; C/G=1-115.
DR PDBsum; 6A7U; -.
DR PDBsum; 6M4G; -.
DR PDBsum; 6M4H; -.
DR AlphaFoldDB; P0C5Z0; -.
DR SMR; P0C5Z0; -.
DR BioGRID; 123748; 202.
DR BioGRID; 138882; 148.
DR IntAct; P0C5Z0; 4.
DR STRING; 9606.ENSP00000346509; -.
DR iPTMnet; P0C5Z0; -.
DR PhosphoSitePlus; P0C5Z0; -.
DR BioMuta; H2AFB3; -.
DR DMDM; 161784333; -.
DR MassIVE; P0C5Z0; -.
DR PaxDb; P0C5Z0; -.
DR PRIDE; P0C5Z0; -.
DR ProteomicsDB; 52314; -.
DR Antibodypedia; 72622; 17 antibodies from 2 providers.
DR Antibodypedia; 75346; 3 antibodies from 3 providers.
DR DNASU; 474381; -.
DR Ensembl; ENST00000354514.6; ENSP00000346509.5; ENSG00000277858.2.
DR Ensembl; ENST00000615853.1; ENSP00000482564.1; ENSG00000277745.1.
DR GeneID; 474381; -.
DR GeneID; 83740; -.
DR KEGG; hsa:474381; -.
DR KEGG; hsa:83740; -.
DR MANE-Select; ENST00000354514.6; ENSP00000346509.5; NM_001017991.3; NP_001017991.1.
DR MANE-Select; ENST00000615853.1; ENSP00000482564.1; NM_080720.3; NP_542451.1.
DR UCSC; uc004fnh.5; human.
DR CTD; 474381; -.
DR CTD; 83740; -.
DR GeneCards; H2AB2; -.
DR GeneCards; H2AB3; -.
DR HGNC; HGNC:18298; H2AB2.
DR HGNC; HGNC:14455; H2AB3.
DR HPA; ENSG00000277745; Tissue enriched (testis).
DR HPA; ENSG00000277858; Tissue enriched (testis).
DR MIM; 300445; gene.
DR MIM; 301038; gene.
DR neXtProt; NX_P0C5Z0; -.
DR VEuPathDB; HostDB:ENSG00000277745; -.
DR VEuPathDB; HostDB:ENSG00000277858; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000163020; -.
DR HOGENOM; CLU_062828_3_2_1; -.
DR InParanoid; P0C5Z0; -.
DR OMA; MAVHNNR; -.
DR OrthoDB; 1516933at2759; -.
DR PhylomeDB; P0C5Z0; -.
DR TreeFam; TF300137; -.
DR PathwayCommons; P0C5Z0; -.
DR SignaLink; P0C5Z0; -.
DR SIGNOR; P0C5Z0; -.
DR BioGRID-ORCS; 474381; 20 hits in 582 CRISPR screens.
DR BioGRID-ORCS; 83740; 47 hits in 592 CRISPR screens.
DR GeneWiki; H2AFB2; -.
DR GeneWiki; H2AFB3; -.
DR Pharos; P0C5Z0; Tdark.
DR PRO; PR:P0C5Z0; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P0C5Z0; protein.
DR Bgee; ENSG00000277745; Expressed in right coronary artery and 74 other tissues.
DR Genevisible; P0C5Z0; 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 3D-structure; Chromosome; DNA-binding; mRNA processing; Nucleosome core;
KW Nucleus; Reference proteome.
FT CHAIN 1..115
FT /note="Histone H2A-Bbd type 2/3"
FT /id="PRO_0000055321"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..115
FT /note="Docking domain"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:6A7U"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:6A7U"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6A7U"
FT HELIX 51..77
FT /evidence="ECO:0007829|PDB:6A7U"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6A7U"
FT HELIX 85..92
FT /evidence="ECO:0007829|PDB:6A7U"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6A7U"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6A7U"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6M4G"
SQ SEQUENCE 115 AA; 12713 MW; F7CA7588C2F57451 CRC64;
MPRRRRRRGS SGAGGRGRTC SRTVRAELSF SVSQVERSLR EGHYAQRLSR TAPVYLAAVI
EYLTAKVLEL AGNEAQNSGE RNITPLLLDM VVHNDRLLST LFNTTTISQV APGED
