GenomeNet

Database: UniProt
Entry: P23527
LinkDB: P23527
Original site: P23527 
ID   H2B1O_HUMAN             Reviewed;         126 AA.
AC   P23527; Q3KPI7; Q8TCV6;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   29-OCT-2014, entry version 140.
DE   RecName: Full=Histone H2B type 1-O;
DE   AltName: Full=Histone H2B.2;
DE   AltName: Full=Histone H2B.n;
DE            Short=H2B/n;
GN   Name=HIST1H2BO; Synonyms=H2BFH, H2BFN;
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].
RX   PubMed=1768865;
RA   Dobner T., Wolf I., Mai B., Lipp M.;
RT   "A novel divergently transcribed human histone H2A/H2B gene pair.";
RL   DNA Seq. 1:409-413(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   [3]
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   [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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-12; 35-47; 59-73 AND 110-126, CLEAVAGE OF
RP   INITIATOR METHIONINE, ACETYLATION AT PRO-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Hepatoma;
RA   Bienvenut W.V., Fleming J., Leug H.Y.;
RL   Submitted (JAN-2010) to UniProtKB.
RN   [6]
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 IDENTIFICATION BY 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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
RP   CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24
RP   AND 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   [12]
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   [13]
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   -!- 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. {ECO:0000269|PubMed:16627869}.
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. {ECO:0000250, ECO:0000269|PubMed:12757711}.
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 (By similarity). {ECO:0000250}.
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. {ECO:0000269|PubMed:21925322}.
CC   -!- MISCELLANEOUS: The mouse orthologous protein seems not to exist.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X57138; CAA40416.1; -; Genomic_DNA.
DR   EMBL; AF531298; AAN06698.1; -; Genomic_DNA.
DR   EMBL; Z98744; CAD24078.1; -; Genomic_DNA.
DR   EMBL; BC106720; AAI06721.1; -; mRNA.
DR   CCDS; CCDS4640.1; -.
DR   PIR; A56624; A56624.
DR   RefSeq; NP_003518.2; NM_003527.4.
DR   UniGene; Hs.484991; -.
DR   ProteinModelPortal; P23527; -.
DR   SMR; P23527; 5-126.
DR   BioGrid; 113944; 14.
DR   IntAct; P23527; 7.
DR   MINT; MINT-2801984; -.
DR   STRING; 9606.ENSP00000303408; -.
DR   PhosphoSite; P23527; -.
DR   DMDM; 51338764; -.
DR   MaxQB; P23527; -.
DR   PaxDb; P23527; -.
DR   PRIDE; P23527; -.
DR   DNASU; 8348; -.
DR   Ensembl; ENST00000616182; ENSP00000477527; ENSG00000274641.
DR   GeneID; 8348; -.
DR   KEGG; hsa:8348; -.
DR   UCSC; uc003nkc.1; human.
DR   CTD; 8348; -.
DR   GeneCards; GC06P027861; -.
DR   HGNC; HGNC:4758; HIST1H2BO.
DR   MIM; 602808; gene.
DR   neXtProt; NX_P23527; -.
DR   PharmGKB; PA29133; -.
DR   eggNOG; NOG289161; -.
DR   GeneTree; ENSGT00760000118976; -.
DR   HOGENOM; HOG000231213; -.
DR   HOVERGEN; HBG007774; -.
DR   InParanoid; P23527; -.
DR   KO; K11252; -.
DR   OMA; TTANKAP; -.
DR   OrthoDB; EOG72VH8J; -.
DR   PhylomeDB; P23527; -.
DR   TreeFam; TF300212; -.
DR   Reactome; REACT_169168; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; REACT_169185; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; REACT_169436; Oxidative Stress Induced Senescence.
DR   Reactome; REACT_172610; HATs acetylate histones.
DR   Reactome; REACT_172744; Condensation of Prophase Chromosomes.
DR   Reactome; REACT_200753; formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; REACT_200808; PRC2 methylates histones and DNA.
DR   Reactome; REACT_200827; SIRT1 negatively regulates rRNA Expression.
DR   Reactome; REACT_200856; NoRC negatively regulates rRNA expression.
DR   Reactome; REACT_2204; RNA Polymerase I Chain Elongation.
DR   Reactome; REACT_22186; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; REACT_2232; RNA Polymerase I Promoter Opening.
DR   Reactome; REACT_27271; Meiotic recombination.
DR   Reactome; REACT_75792; Meiotic synapsis.
DR   Reactome; REACT_75925; Amyloids.
DR   Reactome; REACT_7963; Packaging Of Telomere Ends.
DR   GeneWiki; HIST1H2BO; -.
DR   GenomeRNAi; 8348; -.
DR   NextBio; 31264; -.
DR   PRO; PR:P23527; -.
DR   Bgee; P23527; -.
DR   CleanEx; HS_HIST1H2BO; -.
DR   Genevestigator; P23527; -.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProt.
DR   GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; TAS:Reactome.
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; Chromosome; Complete proteome; Direct protein sequencing;
KW   DNA-binding; Glycoprotein; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000269|Ref.5}.
FT   CHAIN         2    126       Histone H2B type 1-O.
FT                                /FTId=PRO_0000071834.
FT   MOD_RES       2      2       N-acetylproline; partial.
FT                                {ECO:0000269|Ref.5}.
FT   MOD_RES       6      6       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16283522,
FT                                ECO:0000269|PubMed:16627869}.
FT   MOD_RES       6      6       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      12     12       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16627869}.
FT   MOD_RES      12     12       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      13     13       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16283522,
FT                                ECO:0000269|PubMed:16627869}.
FT   MOD_RES      13     13       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      15     15       Phosphoserine; by STK4/MST1.
FT                                {ECO:0000269|PubMed:12757711}.
FT   MOD_RES      16     16       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16283522,
FT                                ECO:0000269|PubMed:16627869}.
FT   MOD_RES      16     16       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      17     17       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16627869}.
FT   MOD_RES      17     17       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      21     21       N6-acetyllysine; alternate.
FT                                {ECO:0000269|PubMed:16283522,
FT                                ECO:0000269|PubMed:16627869}.
FT   MOD_RES      21     21       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      24     24       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      35     35       N6-crotonyllysine; alternate.
FT                                {ECO:0000269|PubMed:21925322}.
FT   MOD_RES      37     37       Phosphoserine; by AMPK. {ECO:0000250}.
FT   MOD_RES      47     47       N6-methyllysine.
FT                                {ECO:0000269|PubMed:16627869}.
FT   MOD_RES      58     58       N6,N6-dimethyllysine.
FT                                {ECO:0000269|PubMed:16627869}.
FT   MOD_RES      80     80       Dimethylated arginine. {ECO:0000250}.
FT   MOD_RES      86     86       N6,N6,N6-trimethyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      86     86       N6-acetyllysine; alternate.
FT                                {ECO:0000250}.
FT   MOD_RES      87     87       Omega-N-methylarginine. {ECO:0000250}.
FT   MOD_RES      93     93       Omega-N-methylarginine. {ECO:0000250}.
FT   MOD_RES     109    109       N6-methyllysine.
FT                                {ECO:0000269|PubMed:16627869}.
FT   MOD_RES     116    116       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     117    117       N6-methylated lysine. {ECO:0000250}.
FT   CARBOHYD    113    113       O-linked (GlcNAc). {ECO:0000250}.
FT   CROSSLNK     35     35       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate. {ECO:0000269|PubMed:21726816}.
FT   CROSSLNK    121    121       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16307923,
FT                                ECO:0000269|PubMed:16627869,
FT                                ECO:0000269|PubMed:16713563}.
FT   CONFLICT     29     29       K -> E (in Ref. 1; CAA40416).
FT                                {ECO:0000305}.
SQ   SEQUENCE   126 AA;  13906 MW;  041118811BBF6647 CRC64;
     MPDPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM
     GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
     KYTSSK
//
DBGET integrated database retrieval system