Full text data of HIST1H2BC
HIST1H2BC
(H2BFK)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histone H2B type 1-C/E/F/G/I (Histone H2B.1 A; Histone H2B.a; H2B/a; Histone H2B.g; H2B/g; Histone H2B.h; H2B/h; Histone H2B.k; H2B/k; Histone H2B.l; H2B/l)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H2B type 1-C/E/F/G/I (Histone H2B.1 A; Histone H2B.a; H2B/a; Histone H2B.g; H2B/g; Histone H2B.h; H2B/h; Histone H2B.k; H2B/k; Histone H2B.l; H2B/l)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62807
ID H2B1C_HUMAN Reviewed; 126 AA.
AC P62807; P02278; Q3B872; Q4VB69; Q93078; Q93080;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Histone H2B type 1-C/E/F/G/I;
DE AltName: Full=Histone H2B.1 A;
DE AltName: Full=Histone H2B.a;
DE Short=H2B/a;
DE AltName: Full=Histone H2B.g;
DE Short=H2B/g;
DE AltName: Full=Histone H2B.h;
DE Short=H2B/h;
DE AltName: Full=Histone H2B.k;
DE Short=H2B/k;
DE AltName: Full=Histone H2B.l;
DE Short=H2B/l;
GN Name=HIST1H2BC; Synonyms=H2BFL;
GN and
GN Name=HIST1H2BE; Synonyms=H2BFH;
GN and
GN Name=HIST1H2BF; Synonyms=H2BFG;
GN and
GN Name=HIST1H2BG; Synonyms=H2BFA;
GN and
GN Name=HIST1H2BI; Synonyms=H2BFK;
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] (HIST1H2BG).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF AND
RP HIST1H2BI), AND VARIANT SER-27.
RX PubMed=9119399; DOI=10.1006/geno.1996.4592;
RA Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
RT "Human histone gene organization: nonregular arrangement within a
RT large cluster.";
RL Genomics 40:314-322(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF;
RP HIST1H2BG AND HIST1H2BI).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H2BC; HIST1H2BE;
RP HIST1H2BF; HIST1H2BG AND HIST1H2BI).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 2-126.
RC TISSUE=Spleen;
RX PubMed=422550;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H2B. Isolation and amino acid sequence.";
RL J. Biochem. 85:615-624(1979).
RN [7]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=11859126;
RA Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.;
RT "Endotoxin-neutralizing antimicrobial proteins of the human
RT placenta.";
RL J. Immunol. 168:2356-2364(2002).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RX PubMed=8620898; DOI=10.1111/j.1432-1033.1996.0086n.x;
RA Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A.,
RA Liden S., Joernvall H., Boman H.G.;
RT "Biochemical and antibacterial analysis of human wound and blister
RT fluid.";
RL Eur. J. Biochem. 237:86-92(1996).
RN [9]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=12860195; DOI=10.1016/S0196-9781(03)00114-1;
RA Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H.,
RA Agerberth B.;
RT "Antimicrobial peptides in the first line defence of human colon
RT mucosa.";
RL Peptides 24:523-530(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=15019208; DOI=10.1016/j.peptides.2003.07.028;
RA Howell S.J., Wilk D., Yadav S.P., Bevins C.L.;
RT "Antimicrobial polypeptides of the human colonic epithelium.";
RL Peptides 24:1763-1770(2003).
RN [11]
RP PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;
RP LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,
RP UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY.
RX PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
RA Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
RT "Quantitative proteomic analysis of post-translational modifications
RT of human histones.";
RL Mol. Cell. Proteomics 5:1314-1325(2006).
RN [12]
RP PHOSPHORYLATION AT SER-15.
RX PubMed=12757711; DOI=10.1016/S0092-8674(03)00355-6;
RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian
RT sterile twenty kinase.";
RL Cell 113:507-517(2003).
RN [13]
RP UBIQUITINATION AT LYS-121.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
RA Tempst P., Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and
RT their roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [14]
RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1;
RA Golebiowski F., Kasprzak K.S.;
RT "Inhibition of core histones acetylation by carcinogenic nickel(II).";
RL Mol. Cell. Biochem. 279:133-139(2005).
RN [15]
RP UBIQUITINATION AT LYS-121.
RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029;
RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A.,
RA Reinberg D.;
RT "Histone H2B monoubiquitination functions cooperatively with FACT to
RT regulate elongation by RNA polymerase II.";
RL Cell 125:703-717(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16457587; DOI=10.1021/pr050268v;
RA Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.;
RT "Gene-specific characterization of human histone H2B by electron
RT capture dissociation.";
RL J. Proteome Res. 5:233-239(2006).
RN [17]
RP UBIQUITINATION AT LYS-35.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin
RT ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79
RT methylation.";
RL Mol. Cell 43:132-144(2011).
RN [18]
RP GLYCOSYLATION AT SER-113, AND UBIQUITINATION AT LYS-121.
RX PubMed=22121020; DOI=10.1038/nature10656;
RA Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
RA Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,
RA Kitagawa H., Roeder R.G., Brown M., Kato S.;
RT "GlcNAcylation of histone H2B facilitates its monoubiquitination.";
RL Nature 480:557-560(2011).
RN [19]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND
RP LYS-35.
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, AND DEUBIQUITINATION BY USP49.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(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 -!- FUNCTION: Has broad antibacterial activity. May contribute to the
CC formation of the functional antimicrobial barrier of the colonic
CC epithelium, and to the bactericidal activity of amniotic fluid.
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: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2
CC dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79'
CC (H3K79me) methylation and transcription activation at specific
CC gene loci, such as HOXA9 and MEIS1 loci. Similarly,
CC monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex
CC gives a specific tag for epigenetic transcriptional activation and
CC is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer
CC to stimulate elongation by RNA polymerase II. H2BK120Ub also acts
CC as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set
CC of exons.
CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to
CC stress promotes transcription (By similarity). Phosphorylated on
CC Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates
CC apoptotic chromatin condensation. Also phosphorylated on Ser-15 in
CC response to DNA double strand breaks (DSBs), and in correlation
CC with somatic hypermutation and immunoglobulin class-switch
CC recombination.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-
CC 121. It fluctuates in response to extracellular glucose, and
CC associates with transcribed genes.
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 -!- SIMILARITY: Belongs to the histone H2B family.
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DR EMBL; M60750; AAA63189.1; -; Genomic_DNA.
DR EMBL; Z80782; CAB02544.1; -; Genomic_DNA.
DR EMBL; Z80779; CAB02541.1; -; Genomic_DNA.
DR EMBL; Z80780; CAB02542.1; -; Genomic_DNA.
DR EMBL; Z80783; CAB02545.1; -; Genomic_DNA.
DR EMBL; AF531286; AAN06686.1; -; Genomic_DNA.
DR EMBL; AF531288; AAN06688.1; -; Genomic_DNA.
DR EMBL; AF531289; AAN06689.1; -; Genomic_DNA.
DR EMBL; AF531290; AAN06690.1; -; Genomic_DNA.
DR EMBL; AF531292; AAN06692.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03411.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03417.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03420.1; -; Genomic_DNA.
DR EMBL; AL353759; CAC04130.1; -; Genomic_DNA.
DR EMBL; BC001131; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC009612; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC096120; AAH96120.1; -; mRNA.
DR EMBL; BC096122; AAH96122.1; -; mRNA.
DR EMBL; BC096123; AAH96123.1; -; mRNA.
DR EMBL; BC101653; AAI01654.1; -; mRNA.
DR EMBL; BC101655; AAI01656.1; -; mRNA.
DR EMBL; BC101748; AAI01749.1; -; mRNA.
DR EMBL; BC101750; AAI01751.1; -; mRNA.
DR EMBL; BC106899; AAI06900.1; -; mRNA.
DR PIR; E40335; HSHUB2.
DR PIR; S65409; S65409.
DR RefSeq; NP_003509.1; NM_003518.3.
DR RefSeq; NP_003513.1; NM_003522.3.
DR RefSeq; NP_003514.2; NM_003523.2.
DR RefSeq; NP_003516.1; NM_003525.2.
DR RefSeq; NP_003517.2; NM_003526.2.
DR RefSeq; NP_066407.1; NM_021063.3.
DR RefSeq; XP_005249497.1; XM_005249440.1.
DR UniGene; Hs.182137; -.
DR UniGene; Hs.534369; -.
DR UniGene; Hs.553506; -.
DR UniGene; Hs.591797; -.
DR UniGene; Hs.591809; -.
DR UniGene; Hs.658713; -.
DR UniGene; Hs.726509; -.
DR ProteinModelPortal; P62807; -.
DR SMR; P62807; 5-126.
DR DIP; DIP-32890N; -.
DR IntAct; P62807; 18.
DR MINT; MINT-276222; -.
DR STRING; 9606.ENSP00000321744; -.
DR PhosphoSite; P62807; -.
DR PaxDb; P62807; -.
DR PRIDE; P62807; -.
DR DNASU; 8339; -.
DR DNASU; 8344; -.
DR DNASU; 8347; -.
DR Ensembl; ENST00000244601; ENSP00000244601; ENSG00000187990.
DR Ensembl; ENST00000314332; ENSP00000321744; ENSG00000180596.
DR Ensembl; ENST00000356530; ENSP00000348924; ENSG00000197697.
DR Ensembl; ENST00000359985; ENSP00000353074; ENSG00000197846.
DR Ensembl; ENST00000377733; ENSP00000366962; ENSG00000168242.
DR Ensembl; ENST00000396984; ENSP00000380180; ENSG00000180596.
DR GeneID; 3017; -.
DR GeneID; 8339; -.
DR GeneID; 8343; -.
DR GeneID; 8344; -.
DR GeneID; 8346; -.
DR GeneID; 8347; -.
DR KEGG; hsa:3017; -.
DR KEGG; hsa:8339; -.
DR KEGG; hsa:8343; -.
DR KEGG; hsa:8344; -.
DR KEGG; hsa:8346; -.
DR KEGG; hsa:8347; -.
DR UCSC; uc003ngk.4; human.
DR CTD; 3017; -.
DR CTD; 8339; -.
DR CTD; 8343; -.
DR CTD; 8344; -.
DR CTD; 8346; -.
DR CTD; 8347; -.
DR GeneCards; GC06M026115; -.
DR GeneCards; GC06M026216; -.
DR GeneCards; GC06P026183; -.
DR GeneCards; GC06P026199; -.
DR GeneCards; GC06P026273; -.
DR HGNC; HGNC:4757; HIST1H2BC.
DR HGNC; HGNC:4753; HIST1H2BE.
DR HGNC; HGNC:4752; HIST1H2BF.
DR HGNC; HGNC:4746; HIST1H2BG.
DR HGNC; HGNC:4756; HIST1H2BI.
DR MIM; 602798; gene.
DR MIM; 602804; gene.
DR MIM; 602805; gene.
DR MIM; 602807; gene.
DR MIM; 602847; gene.
DR neXtProt; NX_P62807; -.
DR PharmGKB; PA29132; -.
DR eggNOG; NOG289161; -.
DR HOGENOM; HOG000231213; -.
DR HOVERGEN; HBG007774; -.
DR InParanoid; P62807; -.
DR KO; K11252; -.
DR OMA; TSAKTIY; -.
DR OrthoDB; EOG72VH8J; -.
DR PhylomeDB; P62807; -.
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 ChiTaRS; HIST1H2BC; human.
DR GeneWiki; HIST1H2BE; -.
DR GeneWiki; HIST1H2BF; -.
DR GeneWiki; HIST1H2BG; -.
DR GeneWiki; HIST1H2BI; -.
DR GeneWiki; Histone_H2B_type_1-C; -.
DR NextBio; 11956; -.
DR PRO; PR:P62807; -.
DR ArrayExpress; P62807; -.
DR Bgee; P62807; -.
DR CleanEx; HS_HIST1H2BC; -.
DR CleanEx; HS_HIST1H2BE; -.
DR CleanEx; HS_HIST1H2BF; -.
DR CleanEx; HS_HIST1H2BG; -.
DR CleanEx; HS_HIST1H2BI; -.
DR Genevestigator; P62807; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Histone H2B type 1-C/E/F/G/I.
FT /FTId=PRO_0000071826.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT MOD_RES 6 6 N6-acetyllysine; alternate.
FT MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 12 12 N6-acetyllysine; alternate.
FT MOD_RES 12 12 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 13 13 N6-acetyllysine; alternate.
FT MOD_RES 13 13 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 15 15 Phosphoserine; by STK4/MST1.
FT MOD_RES 16 16 N6-acetyllysine; alternate.
FT MOD_RES 16 16 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 17 17 N6-acetyllysine; alternate.
FT MOD_RES 17 17 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 21 21 N6-acetyllysine; alternate.
FT MOD_RES 21 21 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 35 35 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 37 37 Phosphoserine; by AMPK (By similarity).
FT MOD_RES 47 47 N6-methyllysine.
FT MOD_RES 58 58 N6,N6-dimethyllysine.
FT MOD_RES 80 80 Dimethylated arginine (By similarity).
FT MOD_RES 86 86 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 86 86 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 87 87 Omega-N-methylarginine (By similarity).
FT MOD_RES 93 93 Omega-N-methylarginine (By similarity).
FT MOD_RES 109 109 N6-methyllysine.
FT MOD_RES 116 116 Phosphothreonine (By similarity).
FT MOD_RES 117 117 N6-methylated lysine (By similarity).
FT CARBOHYD 113 113 O-linked (GlcNAc).
FT CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 27 27 G -> S (in dbSNP:rs7766641).
FT /FTId=VAR_055887.
FT CONFLICT 5 5 A -> S (in Ref. 2; CAB02545).
FT CONFLICT 33 33 S -> T (in Ref. 2; CAB02545).
SQ SEQUENCE 126 AA; 13906 MW; FAE1479F44BE703D CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
//
ID H2B1C_HUMAN Reviewed; 126 AA.
AC P62807; P02278; Q3B872; Q4VB69; Q93078; Q93080;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
read moreDT 02-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Histone H2B type 1-C/E/F/G/I;
DE AltName: Full=Histone H2B.1 A;
DE AltName: Full=Histone H2B.a;
DE Short=H2B/a;
DE AltName: Full=Histone H2B.g;
DE Short=H2B/g;
DE AltName: Full=Histone H2B.h;
DE Short=H2B/h;
DE AltName: Full=Histone H2B.k;
DE Short=H2B/k;
DE AltName: Full=Histone H2B.l;
DE Short=H2B/l;
GN Name=HIST1H2BC; Synonyms=H2BFL;
GN and
GN Name=HIST1H2BE; Synonyms=H2BFH;
GN and
GN Name=HIST1H2BF; Synonyms=H2BFG;
GN and
GN Name=HIST1H2BG; Synonyms=H2BFA;
GN and
GN Name=HIST1H2BI; Synonyms=H2BFK;
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] (HIST1H2BG).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF AND
RP HIST1H2BI), AND VARIANT SER-27.
RX PubMed=9119399; DOI=10.1006/geno.1996.4592;
RA Albig W., Kioschis P., Poustka A., Meergans K., Doenecke D.;
RT "Human histone gene organization: nonregular arrangement within a
RT large cluster.";
RL Genomics 40:314-322(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H2BC; HIST1H2BE; HIST1H2BF;
RP HIST1H2BG AND HIST1H2BI).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIST1H2BC; HIST1H2BE;
RP HIST1H2BF; HIST1H2BG AND HIST1H2BI).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 2-126.
RC TISSUE=Spleen;
RX PubMed=422550;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H2B. Isolation and amino acid sequence.";
RL J. Biochem. 85:615-624(1979).
RN [7]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=11859126;
RA Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.;
RT "Endotoxin-neutralizing antimicrobial proteins of the human
RT placenta.";
RL J. Immunol. 168:2356-2364(2002).
RN [8]
RP PROTEIN SEQUENCE OF 2-13.
RX PubMed=8620898; DOI=10.1111/j.1432-1033.1996.0086n.x;
RA Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A.,
RA Liden S., Joernvall H., Boman H.G.;
RT "Biochemical and antibacterial analysis of human wound and blister
RT fluid.";
RL Eur. J. Biochem. 237:86-92(1996).
RN [9]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=12860195; DOI=10.1016/S0196-9781(03)00114-1;
RA Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H.,
RA Agerberth B.;
RT "Antimicrobial peptides in the first line defence of human colon
RT mucosa.";
RL Peptides 24:523-530(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
RX PubMed=15019208; DOI=10.1016/j.peptides.2003.07.028;
RA Howell S.J., Wilk D., Yadav S.P., Bevins C.L.;
RT "Antimicrobial polypeptides of the human colonic epithelium.";
RL Peptides 24:1763-1770(2003).
RN [11]
RP PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;
RP LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,
RP UBIQUITINATION AT LYS-121, AND MASS SPECTROMETRY.
RX PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
RA Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
RA Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
RT "Quantitative proteomic analysis of post-translational modifications
RT of human histones.";
RL Mol. Cell. Proteomics 5:1314-1325(2006).
RN [12]
RP PHOSPHORYLATION AT SER-15.
RX PubMed=12757711; DOI=10.1016/S0092-8674(03)00355-6;
RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian
RT sterile twenty kinase.";
RL Cell 113:507-517(2003).
RN [13]
RP UBIQUITINATION AT LYS-121.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
RA Tempst P., Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and
RT their roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [14]
RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
RX PubMed=16283522; DOI=10.1007/s11010-005-8285-1;
RA Golebiowski F., Kasprzak K.S.;
RT "Inhibition of core histones acetylation by carcinogenic nickel(II).";
RL Mol. Cell. Biochem. 279:133-139(2005).
RN [15]
RP UBIQUITINATION AT LYS-121.
RX PubMed=16713563; DOI=10.1016/j.cell.2006.04.029;
RA Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A.,
RA Reinberg D.;
RT "Histone H2B monoubiquitination functions cooperatively with FACT to
RT regulate elongation by RNA polymerase II.";
RL Cell 125:703-717(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16457587; DOI=10.1021/pr050268v;
RA Siuti N., Roth M.J., Mizzen C.A., Kelleher N.L., Pesavento J.J.;
RT "Gene-specific characterization of human histone H2B by electron
RT capture dissociation.";
RL J. Proteome Res. 5:233-239(2006).
RN [17]
RP UBIQUITINATION AT LYS-35.
RX PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
RA Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
RT "The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin
RT ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79
RT methylation.";
RL Mol. Cell 43:132-144(2011).
RN [18]
RP GLYCOSYLATION AT SER-113, AND UBIQUITINATION AT LYS-121.
RX PubMed=22121020; DOI=10.1038/nature10656;
RA Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
RA Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,
RA Kitagawa H., Roeder R.G., Brown M., Kato S.;
RT "GlcNAcylation of histone H2B facilitates its monoubiquitination.";
RL Nature 480:557-560(2011).
RN [19]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-24 AND
RP LYS-35.
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, AND DEUBIQUITINATION BY USP49.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(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 -!- FUNCTION: Has broad antibacterial activity. May contribute to the
CC formation of the functional antimicrobial barrier of the colonic
CC epithelium, and to the bactericidal activity of amniotic fluid.
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: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2
CC dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79'
CC (H3K79me) methylation and transcription activation at specific
CC gene loci, such as HOXA9 and MEIS1 loci. Similarly,
CC monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex
CC gives a specific tag for epigenetic transcriptional activation and
CC is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer
CC to stimulate elongation by RNA polymerase II. H2BK120Ub also acts
CC as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set
CC of exons.
CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to
CC stress promotes transcription (By similarity). Phosphorylated on
CC Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates
CC apoptotic chromatin condensation. Also phosphorylated on Ser-15 in
CC response to DNA double strand breaks (DSBs), and in correlation
CC with somatic hypermutation and immunoglobulin class-switch
CC recombination.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-
CC 121. It fluctuates in response to extracellular glucose, and
CC associates with transcribed genes.
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 -!- SIMILARITY: Belongs to the histone H2B family.
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DR EMBL; M60750; AAA63189.1; -; Genomic_DNA.
DR EMBL; Z80782; CAB02544.1; -; Genomic_DNA.
DR EMBL; Z80779; CAB02541.1; -; Genomic_DNA.
DR EMBL; Z80780; CAB02542.1; -; Genomic_DNA.
DR EMBL; Z80783; CAB02545.1; -; Genomic_DNA.
DR EMBL; AF531286; AAN06686.1; -; Genomic_DNA.
DR EMBL; AF531288; AAN06688.1; -; Genomic_DNA.
DR EMBL; AF531289; AAN06689.1; -; Genomic_DNA.
DR EMBL; AF531290; AAN06690.1; -; Genomic_DNA.
DR EMBL; AF531292; AAN06692.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03411.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03417.1; -; Genomic_DNA.
DR EMBL; AL031777; CAC03420.1; -; Genomic_DNA.
DR EMBL; AL353759; CAC04130.1; -; Genomic_DNA.
DR EMBL; BC001131; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC009612; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC096120; AAH96120.1; -; mRNA.
DR EMBL; BC096122; AAH96122.1; -; mRNA.
DR EMBL; BC096123; AAH96123.1; -; mRNA.
DR EMBL; BC101653; AAI01654.1; -; mRNA.
DR EMBL; BC101655; AAI01656.1; -; mRNA.
DR EMBL; BC101748; AAI01749.1; -; mRNA.
DR EMBL; BC101750; AAI01751.1; -; mRNA.
DR EMBL; BC106899; AAI06900.1; -; mRNA.
DR PIR; E40335; HSHUB2.
DR PIR; S65409; S65409.
DR RefSeq; NP_003509.1; NM_003518.3.
DR RefSeq; NP_003513.1; NM_003522.3.
DR RefSeq; NP_003514.2; NM_003523.2.
DR RefSeq; NP_003516.1; NM_003525.2.
DR RefSeq; NP_003517.2; NM_003526.2.
DR RefSeq; NP_066407.1; NM_021063.3.
DR RefSeq; XP_005249497.1; XM_005249440.1.
DR UniGene; Hs.182137; -.
DR UniGene; Hs.534369; -.
DR UniGene; Hs.553506; -.
DR UniGene; Hs.591797; -.
DR UniGene; Hs.591809; -.
DR UniGene; Hs.658713; -.
DR UniGene; Hs.726509; -.
DR ProteinModelPortal; P62807; -.
DR SMR; P62807; 5-126.
DR DIP; DIP-32890N; -.
DR IntAct; P62807; 18.
DR MINT; MINT-276222; -.
DR STRING; 9606.ENSP00000321744; -.
DR PhosphoSite; P62807; -.
DR PaxDb; P62807; -.
DR PRIDE; P62807; -.
DR DNASU; 8339; -.
DR DNASU; 8344; -.
DR DNASU; 8347; -.
DR Ensembl; ENST00000244601; ENSP00000244601; ENSG00000187990.
DR Ensembl; ENST00000314332; ENSP00000321744; ENSG00000180596.
DR Ensembl; ENST00000356530; ENSP00000348924; ENSG00000197697.
DR Ensembl; ENST00000359985; ENSP00000353074; ENSG00000197846.
DR Ensembl; ENST00000377733; ENSP00000366962; ENSG00000168242.
DR Ensembl; ENST00000396984; ENSP00000380180; ENSG00000180596.
DR GeneID; 3017; -.
DR GeneID; 8339; -.
DR GeneID; 8343; -.
DR GeneID; 8344; -.
DR GeneID; 8346; -.
DR GeneID; 8347; -.
DR KEGG; hsa:3017; -.
DR KEGG; hsa:8339; -.
DR KEGG; hsa:8343; -.
DR KEGG; hsa:8344; -.
DR KEGG; hsa:8346; -.
DR KEGG; hsa:8347; -.
DR UCSC; uc003ngk.4; human.
DR CTD; 3017; -.
DR CTD; 8339; -.
DR CTD; 8343; -.
DR CTD; 8344; -.
DR CTD; 8346; -.
DR CTD; 8347; -.
DR GeneCards; GC06M026115; -.
DR GeneCards; GC06M026216; -.
DR GeneCards; GC06P026183; -.
DR GeneCards; GC06P026199; -.
DR GeneCards; GC06P026273; -.
DR HGNC; HGNC:4757; HIST1H2BC.
DR HGNC; HGNC:4753; HIST1H2BE.
DR HGNC; HGNC:4752; HIST1H2BF.
DR HGNC; HGNC:4746; HIST1H2BG.
DR HGNC; HGNC:4756; HIST1H2BI.
DR MIM; 602798; gene.
DR MIM; 602804; gene.
DR MIM; 602805; gene.
DR MIM; 602807; gene.
DR MIM; 602847; gene.
DR neXtProt; NX_P62807; -.
DR PharmGKB; PA29132; -.
DR eggNOG; NOG289161; -.
DR HOGENOM; HOG000231213; -.
DR HOVERGEN; HBG007774; -.
DR InParanoid; P62807; -.
DR KO; K11252; -.
DR OMA; TSAKTIY; -.
DR OrthoDB; EOG72VH8J; -.
DR PhylomeDB; P62807; -.
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 ChiTaRS; HIST1H2BC; human.
DR GeneWiki; HIST1H2BE; -.
DR GeneWiki; HIST1H2BF; -.
DR GeneWiki; HIST1H2BG; -.
DR GeneWiki; HIST1H2BI; -.
DR GeneWiki; Histone_H2B_type_1-C; -.
DR NextBio; 11956; -.
DR PRO; PR:P62807; -.
DR ArrayExpress; P62807; -.
DR Bgee; P62807; -.
DR CleanEx; HS_HIST1H2BC; -.
DR CleanEx; HS_HIST1H2BE; -.
DR CleanEx; HS_HIST1H2BF; -.
DR CleanEx; HS_HIST1H2BG; -.
DR CleanEx; HS_HIST1H2BI; -.
DR Genevestigator; P62807; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antibiotic; Antimicrobial; Chromosome; Complete proteome;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 126 Histone H2B type 1-C/E/F/G/I.
FT /FTId=PRO_0000071826.
FT MOD_RES 2 2 N-acetylproline (By similarity).
FT MOD_RES 6 6 N6-acetyllysine; alternate.
FT MOD_RES 6 6 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 12 12 N6-acetyllysine; alternate.
FT MOD_RES 12 12 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 13 13 N6-acetyllysine; alternate.
FT MOD_RES 13 13 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 15 15 Phosphoserine; by STK4/MST1.
FT MOD_RES 16 16 N6-acetyllysine; alternate.
FT MOD_RES 16 16 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 17 17 N6-acetyllysine; alternate.
FT MOD_RES 17 17 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 21 21 N6-acetyllysine; alternate.
FT MOD_RES 21 21 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 24 24 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 24 24 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 35 35 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 37 37 Phosphoserine; by AMPK (By similarity).
FT MOD_RES 47 47 N6-methyllysine.
FT MOD_RES 58 58 N6,N6-dimethyllysine.
FT MOD_RES 80 80 Dimethylated arginine (By similarity).
FT MOD_RES 86 86 N6,N6,N6-trimethyllysine; alternate (By
FT similarity).
FT MOD_RES 86 86 N6-acetyllysine; alternate (By
FT similarity).
FT MOD_RES 87 87 Omega-N-methylarginine (By similarity).
FT MOD_RES 93 93 Omega-N-methylarginine (By similarity).
FT MOD_RES 109 109 N6-methyllysine.
FT MOD_RES 116 116 Phosphothreonine (By similarity).
FT MOD_RES 117 117 N6-methylated lysine (By similarity).
FT CARBOHYD 113 113 O-linked (GlcNAc).
FT CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin);
FT alternate.
FT CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 27 27 G -> S (in dbSNP:rs7766641).
FT /FTId=VAR_055887.
FT CONFLICT 5 5 A -> S (in Ref. 2; CAB02545).
FT CONFLICT 33 33 S -> T (in Ref. 2; CAB02545).
SQ SEQUENCE 126 AA; 13906 MW; FAE1479F44BE703D CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
//
MIM
602798
*RECORD*
*FIELD* NO
602798
*FIELD* TI
*602798 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER G; HIST1H2BG
;;HISTONE GENE CLUSTER 1, H2BG;;
read moreHIST1 CLUSTER, H2BG;;
H2B HISTONE FAMILY, MEMBER A; H2BFA;;
H2B/A;;
H2B.1A
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
CLONING
Albig et al. (1991) identified a gene encoding a member of the H2B class
of histones and designated it H2B.1A. Albig and Doenecke (1997)
designated this gene H2B/a.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2B/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 HIST1H2BG.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602798
*FIELD* TI
*602798 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER G; HIST1H2BG
;;HISTONE GENE CLUSTER 1, H2BG;;
read moreHIST1 CLUSTER, H2BG;;
H2B HISTONE FAMILY, MEMBER A; H2BFA;;
H2B/A;;
H2B.1A
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
CLONING
Albig et al. (1991) identified a gene encoding a member of the H2B class
of histones and designated it H2B.1A. Albig and Doenecke (1997)
designated this gene H2B/a.
MAPPING
By analysis of a YAC contig, Albig et al. (1997) mapped the H2B/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 HIST1H2BG.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
MIM
602804
*RECORD*
*FIELD* NO
602804
*FIELD* TI
*602804 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER F; HIST1H2BF
;;HISTONE GENE CLUSTER 1, H2BF;;
read moreHIST1 CLUSTER, H2BF;;
H2B HISTONE FAMILY, MEMBER G; H2BFG;;
H2B/G
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/g.
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 HIST1H2BF.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 4/3/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602804
*FIELD* TI
*602804 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER F; HIST1H2BF
;;HISTONE GENE CLUSTER 1, H2BF;;
read moreHIST1 CLUSTER, H2BF;;
H2B HISTONE FAMILY, MEMBER G; H2BFG;;
H2B/G
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/g.
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 HIST1H2BF.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 4/3/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
MIM
602805
*RECORD*
*FIELD* NO
602805
*FIELD* TI
*602805 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER E; HIST1H2BE
;;HISTONE GENE CLUSTER 1, H2BE;;
read moreHIST1 CLUSTER, H2BE;;
H2B HISTONE FAMILY, MEMBER H; H2BFH;;
H2B/H
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/h.
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 HIST1H2BE.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602805
*FIELD* TI
*602805 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER E; HIST1H2BE
;;HISTONE GENE CLUSTER 1, H2BE;;
read moreHIST1 CLUSTER, H2BE;;
H2B HISTONE FAMILY, MEMBER H; H2BFH;;
H2B/H
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/h.
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 HIST1H2BE.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
MIM
602807
*RECORD*
*FIELD* NO
602807
*FIELD* TI
*602807 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER I; HIST1H2BI
;;HISTONE GENE CLUSTER 1, H2BI;;
read moreHIST1 CLUSTER, H2BI;;
H2B HISTONE FAMILY, MEMBER K; H2BFK;;
H2B/K
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/k.
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 HIST1H2BI.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
*RECORD*
*FIELD* NO
602807
*FIELD* TI
*602807 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER I; HIST1H2BI
;;HISTONE GENE CLUSTER 1, H2BI;;
read moreHIST1 CLUSTER, H2BI;;
H2B HISTONE FAMILY, MEMBER K; H2BFK;;
H2B/K
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes that included H2B/k.
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 HIST1H2BI.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/9/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
alopez: 7/9/1998
MIM
602847
*RECORD*
*FIELD* NO
602847
*FIELD* TI
*602847 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER C; HIST1H2BC
;;HISTONE GENE CLUSTER 1, H2BC;;
read moreHIST1 CLUSTER, H2BC;;
H2B HISTONE FAMILY, MEMBER L; H2BFL;;
H2B/L
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes, including H2B/l.
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 HIST1H2BC.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/14/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998
*RECORD*
*FIELD* NO
602847
*FIELD* TI
*602847 HISTONE GENE CLUSTER 1, H2B HISTONE FAMILY, MEMBER C; HIST1H2BC
;;HISTONE GENE CLUSTER 1, H2BC;;
read moreHIST1 CLUSTER, H2BC;;
H2B HISTONE FAMILY, MEMBER L; H2BFL;;
H2B/L
*FIELD* TX
For background information on histones, histone gene clusters, and the
H2B histone family, see HIST1H2BA (609904).
MAPPING
By analysis of a YAC contig from chromosome 6p21.3, Albig et al. (1997)
characterized a cluster of 35 histone genes, including H2B/l.
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 HIST1H2BC.
GENE FUNCTION
See HIST1H2BA (609904) for functional information on H2B histones.
*FIELD* RF
1. 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.
2. 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: 01/29/2013
*FIELD* CD
Rebekah S. Rasooly: 7/14/1998
*FIELD* ED
mgross: 01/29/2013
mgross: 7/22/2010
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/14/1998