H2B1J_HUMAN
ID H2B1J_HUMAN Reviewed; 126 AA.
AC P06899; B2R4J4; O60816;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Histone H2B type 1-J;
DE AltName: Full=Histone H2B.1;
DE AltName: Full=Histone H2B.r;
DE Short=H2B/r;
GN Name=H2BC11 {ECO:0000312|HGNC:HGNC:4761};
GN Synonyms=H2BFR {ECO:0000312|HGNC:HGNC:4761},
GN HIST1H2BJ {ECO:0000312|HGNC:HGNC:4761};
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=6647026; DOI=10.1093/nar/11.21.7409;
RA Zhong R., Roeder R.G., Heintz N.;
RT "The primary structure and expression of four cloned human histone genes.";
RL Nucleic Acids Res. 11:7409-7425(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
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 MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
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., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., 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., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA 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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-27.
RX PubMed=2917990; DOI=10.1016/s0021-9258(19)84968-2;
RA Alnemri E.S., Litwack G.;
RT "Glucocorticoid-induced lymphocytolysis is not mediated by an induced
RT endonuclease.";
RL J. Biol. Chem. 264:4104-4111(1989).
RN [7]
RP PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
RX PubMed=11859126; DOI=10.4049/jimmunol.168.5.2356;
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 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 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 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; LYS-16;
RP 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., Finn P.,
RA Grauslund M., Hansen A.M., Jensen O.N.;
RT "Quantitative proteomic analysis of post-translational modifications of
RT human histones.";
RL Mol. Cell. Proteomics 5:1314-1325(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION.
RX PubMed=11709551; DOI=10.1074/jbc.m107894200;
RA Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
RT "Global regulation of post-translational modifications on core histones.";
RL J. Biol. Chem. 277:2579-2588(2002).
RN [13]
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 sterile
RT twenty kinase.";
RL Cell 113:507-517(2003).
RN [14]
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., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [15]
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 [16]
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., 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 [17]
RP CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; 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., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [18]
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 ligase
RT for H2B K34 and is involved in crosstalk with H3 K4 and K79 methylation.";
RL Mol. Cell 43:132-144(2011).
RN [19]
RP SUCCINYLATION AT LYS-35; LYS-117 AND LYS-121, AND MALONYLATION AT LYS-117.
RX PubMed=22389435; DOI=10.1074/mcp.m111.015875;
RA Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
RT "Lysine succinylation and lysine malonylation in histones.";
RL Mol. Cell. Proteomics 11:100-107(2012).
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 pre-mRNA
RT splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 31-126 IN COMPLEX WITH H2AZ1 AND
RP ANP32E.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
RN [22] {ECO:0007744|PDB:5AY8}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH H2A; H3.Y AND H4.
RX PubMed=27016736; DOI=10.1093/nar/gkw202;
RA Kujirai T., Horikoshi N., Sato K., Maehara K., Machida S., Osakabe A.,
RA Kimura H., Ohkawa Y., Kurumizaka H.;
RT "Structure and function of human histone H3.Y nucleosome.";
RL Nucleic Acids Res. 44:6127-6141(2016).
RN [23]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-13; LYS-21; LYS-24; LYS-25; LYS-35;
RP LYS-44; LYS-47; LYS-58; LYS-86; LYS-109; LYS-117 AND LYS-121.
RX PubMed=24681537; DOI=10.1038/nchembio.1497;
RA Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H., Debernardi A.,
RA Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z., Allis C.D., Ren B.,
RA Khochbin S., Zhao Y.;
RT "Lysine 2-hydroxyisobutyrylation is a widely distributed active histone
RT mark.";
RL Nat. Chem. Biol. 10:365-370(2014).
RN [24]
RP BUTYRYLATION AT LYS-6 AND LYS-21.
RX PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
RA Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
RA Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
RA Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C., Panne D.,
RA Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
RT "Dynamic competing histone H4 K5K8 acetylation and butyrylation are
RT hallmarks of highly active gene promoters.";
RL Mol. Cell 62:169-180(2016).
RN [25]
RP HYDROXYBUTYRYLATION AT LYS-6; LYS-12; LYS-17; LYS-21; LYS-35; LYS-86;
RP LYS-117 AND LYS-121.
RX PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
RA Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
RA Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
RA Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
RA White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lysine beta-
RT hydroxybutyrylation.";
RL Mol. Cell 62:194-206(2016).
RN [26]
RP GLUTARYLATION AT LYS-17; LYS-35; LYS-44; LYS-47; LYS-109; LYS-117 AND
RP LYS-121.
RX PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL Mol. Cell 0:0-0(2019).
RN [27]
RP LACTYLATION AT LYS-6; LYS-12; LYS-16; LYS-17; LYS-21; LYS-24; LYS-44;
RP LYS-86; LYS-109; LYS-117 AND LYS-121.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 31-126 IN COMPLEX WITH H2AZ1 AND
RP VPS72, AND INTERACTION WITH H2AZ1 AND VPS72.
RX PubMed=26974126; DOI=10.1038/nsmb.3189;
RA Latrick C.M., Marek M., Ouararhni K., Papin C., Stoll I., Ignatyeva M.,
RA Obri A., Ennifar E., Dimitrov S., Romier C., Hamiche A.;
RT "Molecular basis and specificity of H2A.Z-H2B recognition and deposition by
RT the histone chaperone YL1.";
RL Nat. Struct. Mol. Biol. 23:309-316(2016).
RN [29] {ECO:0007744|PDB:7CCQ, ECO:0007744|PDB:7CCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF 33-125 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=33051594; DOI=10.1038/s41422-020-00422-4;
RA Cao D., Han X., Fan X., Xu R.M., Zhang X.;
RT "Structural basis for nucleosome-mediated inhibition of cGAS activity.";
RL Cell Res. 30:1088-1097(2020).
RN [30] {ECO:0007744|PDB:6USJ}
RP STRUCTURE BY ELECTRON MICROSCOPY (10.50 ANGSTROMS) OF NUCLEOSOME CORE
RP COMPLEX IN COMPLEX WITH PARP2.
RX PubMed=33141820; DOI=10.1371/journal.pone.0240932;
RA Gaullier G., Roberts G., Muthurajan U.M., Bowerman S., Rudolph J.,
RA Mahadevan J., Jha A., Rae P.S., Luger K.;
RT "Bridging of nucleosome-proximal DNA double-strand breaks by PARP2 enhances
RT its interaction with HPF1.";
RL PLoS ONE 15:e0240932-e0240932(2020).
RN [31] {ECO:0007744|PDB:7C0M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 2-126 IN COMPLEX WITH
RP NUCLEOSOME CORE AND CGAS.
RX PubMed=32912999; DOI=10.1126/science.abd0237;
RA Kujirai T., Zierhut C., Takizawa Y., Kim R., Negishi L., Uruma N.,
RA Hirai S., Funabiki H., Kurumizaka H.;
RT "Structural basis for the inhibition of cGAS by nucleosomes.";
RL Science 370:455-458(2020).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and 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 molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA. Heterodimer H2BC11 and H2AZ1 interacts with VPS72 (via N-terminal
CC domain) (PubMed:26974126). {ECO:0000269|PubMed:24463511,
CC ECO:0000269|PubMed:26974126}.
CC -!- INTERACTION:
CC P06899; P04908: H2AC8; NbExp=11; IntAct=EBI-6150252, EBI-358971;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is
CC required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me)
CC methylation and transcription activation at specific gene loci, such as
CC HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121
CC (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with
CC the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub
CC also acts as a regulator of mRNA splicing: deubiquitination by USP49 is
CC required for efficient cotranscriptional splicing of a large set of
CC exons. {ECO:0000269|PubMed:11709551, ECO:0000269|PubMed:16627869}.
CC -!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress
CC promotes transcription (By similarity). Phosphorylated on Ser-15
CC (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic
CC chromatin condensation. Also phosphorylated on Ser-15 in response to
CC DNA double strand breaks (DSBs), and in correlation with somatic
CC hypermutation and immunoglobulin class-switch recombination.
CC {ECO:0000250|UniProtKB:Q64475, ECO:0000269|PubMed:12757711}.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000269|PubMed:21925322}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000269|PubMed:31645732}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; X00088; CAA24950.1; -; Genomic_DNA.
DR EMBL; AF531293; AAN06693.1; -; Genomic_DNA.
DR EMBL; AK311849; BAG34791.1; -; mRNA.
DR EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03080.1; -; Genomic_DNA.
DR CCDS; CCDS4618.1; -.
DR PIR; A26318; HSHUB1.
DR PIR; S65409; S65409.
DR RefSeq; NP_066402.2; NM_021058.3.
DR PDB; 2RVQ; NMR; -; D=1-126.
DR PDB; 3A6N; X-ray; 2.70 A; D/H=1-126.
DR PDB; 3AFA; X-ray; 2.50 A; D/H=1-126.
DR PDB; 3AN2; X-ray; 3.60 A; D/H=1-126.
DR PDB; 3AV1; X-ray; 2.50 A; D/H=1-126.
DR PDB; 3AV2; X-ray; 2.80 A; D/H=1-126.
DR PDB; 3AYW; X-ray; 2.90 A; D/H=1-126.
DR PDB; 3AZE; X-ray; 3.00 A; D/H=1-126.
DR PDB; 3AZF; X-ray; 2.70 A; D/H=1-126.
DR PDB; 3AZG; X-ray; 2.40 A; D/H=1-126.
DR PDB; 3AZH; X-ray; 3.49 A; D/H=1-126.
DR PDB; 3AZI; X-ray; 2.70 A; D/H=1-126.
DR PDB; 3AZJ; X-ray; 2.89 A; D/H=1-126.
DR PDB; 3AZK; X-ray; 3.20 A; D/H=1-126.
DR PDB; 3AZL; X-ray; 2.70 A; D/H=1-126.
DR PDB; 3AZM; X-ray; 2.89 A; D/H=1-126.
DR PDB; 3AZN; X-ray; 3.00 A; D/H=1-126.
DR PDB; 3W96; X-ray; 3.00 A; D/H=1-126.
DR PDB; 3W97; X-ray; 3.20 A; D/H=26-126.
DR PDB; 3W98; X-ray; 3.42 A; D/H=1-126.
DR PDB; 3W99; X-ray; 3.00 A; D/H=1-126.
DR PDB; 3WA9; X-ray; 3.07 A; D/H=1-126.
DR PDB; 3WAA; X-ray; 3.20 A; D/H=1-126.
DR PDB; 3WTP; X-ray; 2.67 A; D/H=1-126.
DR PDB; 4CAY; X-ray; 1.48 A; B=31-126.
DR PDB; 4YM5; X-ray; 4.00 A; D/H=1-126.
DR PDB; 4YM6; X-ray; 3.51 A; D/H=1-126.
DR PDB; 4Z5T; X-ray; 2.80 A; D/H=1-126.
DR PDB; 5AV5; X-ray; 2.40 A; D/H=1-126.
DR PDB; 5AV6; X-ray; 2.20 A; D/H=1-126.
DR PDB; 5AV8; X-ray; 2.20 A; D/H=1-126.
DR PDB; 5AV9; X-ray; 2.20 A; D/H=1-126.
DR PDB; 5AVB; X-ray; 2.40 A; D/H=1-126.
DR PDB; 5AVC; X-ray; 2.40 A; D/H=1-126.
DR PDB; 5AY8; X-ray; 2.80 A; D/H=1-126.
DR PDB; 5B0Y; X-ray; 2.56 A; D/H=1-126.
DR PDB; 5B0Z; X-ray; 1.99 A; D/H=1-126.
DR PDB; 5B24; X-ray; 3.60 A; D/H=1-126.
DR PDB; 5B2I; X-ray; 3.00 A; D/H=1-126.
DR PDB; 5B2J; X-ray; 2.60 A; D/H=1-126.
DR PDB; 5B31; X-ray; 2.20 A; D/H=1-126.
DR PDB; 5B32; X-ray; 2.35 A; D/H=1-126.
DR PDB; 5B33; X-ray; 2.92 A; D/H=1-126.
DR PDB; 5B40; X-ray; 3.33 A; D/H=1-126.
DR PDB; 5CPI; X-ray; 2.90 A; D/H=1-126.
DR PDB; 5CPJ; X-ray; 3.15 A; D/H=1-126.
DR PDB; 5CPK; X-ray; 2.63 A; D/H=1-126.
DR PDB; 5FUG; X-ray; 2.70 A; B/E/H/K=31-126.
DR PDB; 5GSE; X-ray; 3.14 A; D/H/N=1-126.
DR PDB; 5GTC; X-ray; 2.70 A; D/H=1-126.
DR PDB; 5GXQ; X-ray; 2.85 A; D/H=1-126.
DR PDB; 5JRG; X-ray; 2.50 A; D/H=1-126.
DR PDB; 5VEY; NMR; -; A=34-124.
DR PDB; 5X7X; X-ray; 2.18 A; D/H=1-126.
DR PDB; 5XF3; X-ray; 2.60 A; D/H=1-126.
DR PDB; 5XF4; X-ray; 2.87 A; D/H=1-126.
DR PDB; 5XF5; X-ray; 2.82 A; D/H=1-126.
DR PDB; 5Y0C; X-ray; 2.09 A; D/H=1-126.
DR PDB; 5Y0D; X-ray; 1.99 A; D/H=1-126.
DR PDB; 5Z23; X-ray; 2.73 A; D/H=1-126.
DR PDB; 5Z30; X-ray; 2.45 A; D/H=1-126.
DR PDB; 5ZBX; X-ray; 2.58 A; D/H=1-126.
DR PDB; 6A5L; EM; 5.60 A; d/h=1-126.
DR PDB; 6A5O; EM; 9.90 A; d/h=1-126.
DR PDB; 6A5P; EM; 7.00 A; d/h=1-126.
DR PDB; 6A5R; EM; 8.70 A; d/h=1-126.
DR PDB; 6A5T; EM; 6.70 A; d/h=1-126.
DR PDB; 6A5U; EM; 7.60 A; d/h=1-126.
DR PDB; 6BUZ; EM; 3.92 A; D/H=1-126.
DR PDB; 6E0C; EM; 2.63 A; D/H=1-126.
DR PDB; 6E0P; EM; 2.60 A; D/H=1-126.
DR PDB; 6HKT; X-ray; 9.70 A; 1/3/D/H/N/R/X/d/h/n/r/x=1-126.
DR PDB; 6HTS; EM; 4.80 A; L/P=1-126.
DR PDB; 6INQ; EM; 6.90 A; d/h=1-126.
DR PDB; 6IPU; X-ray; 1.99 A; D/H=32-126.
DR PDB; 6IQ4; X-ray; 2.25 A; D/H=32-126.
DR PDB; 6IR9; EM; 3.80 A; d/h=1-126.
DR PDB; 6J4W; EM; 7.90 A; d/h=1-126.
DR PDB; 6J4X; EM; 4.30 A; d/h=1-126.
DR PDB; 6J4Y; EM; 4.30 A; d/h=1-126.
DR PDB; 6J4Z; EM; 4.10 A; d/h=1-126.
DR PDB; 6J50; EM; 4.70 A; d/h=1-126.
DR PDB; 6J51; EM; 4.20 A; d/h=1-126.
DR PDB; 6JOU; X-ray; 2.17 A; D/H=1-126.
DR PDB; 6JR0; X-ray; 2.50 A; D/H=1-126.
DR PDB; 6JR1; X-ray; 2.40 A; D/H=1-126.
DR PDB; 6JXD; X-ray; 2.25 A; D/H=30-126.
DR PDB; 6K1I; X-ray; 2.75 A; D/H=1-126.
DR PDB; 6K1J; X-ray; 2.85 A; D/H=1-126.
DR PDB; 6K1K; X-ray; 2.20 A; D/H=1-126.
DR PDB; 6KVD; X-ray; 2.21 A; D/H=1-126.
DR PDB; 6KXV; X-ray; 3.63 A; D/H=1-126.
DR PDB; 6L49; EM; 18.90 A; D/H/N/R/V/Z=1-126.
DR PDB; 6L4A; EM; 12.30 A; D/H/N/R/V/Z=1-126.
DR PDB; 6L9Z; X-ray; 2.50 A; D/H/N/R=1-126.
DR PDB; 6LA2; X-ray; 3.89 A; D/H/N/R/X/b/h/l=1-126.
DR PDB; 6LA8; X-ray; 3.40 A; D/H/N/R=1-126.
DR PDB; 6LA9; X-ray; 3.70 A; D/H/N/R=1-126.
DR PDB; 6LAB; X-ray; 3.20 A; D/H/N/R=1-126.
DR PDB; 6LER; X-ray; 3.00 A; D/H/N/R=1-126.
DR PDB; 6M3V; X-ray; 4.60 A; D/H/N/R=1-126.
DR PDB; 6M44; X-ray; 3.81 A; D/H/N/R=1-126.
DR PDB; 6O1D; EM; 3.40 A; D/H=1-126.
DR PDB; 6R8Y; EM; 4.30 A; D/H=1-126.
DR PDB; 6R8Z; EM; 3.90 A; D/H=1-126.
DR PDB; 6R90; EM; 4.50 A; D/H=1-126.
DR PDB; 6R91; EM; 4.10 A; D/H=1-126.
DR PDB; 6R92; EM; 4.80 A; D/H=1-126.
DR PDB; 6R93; EM; 4.00 A; D/H=1-126.
DR PDB; 6R94; EM; 3.50 A; D/H=1-126.
DR PDB; 6T90; EM; 3.05 A; D/H=1-125.
DR PDB; 6T93; EM; 3.49 A; D/H=1-126.
DR PDB; 6USJ; EM; 10.50 A; D/H/N/R=1-126.
DR PDB; 6V2K; X-ray; 2.60 A; D/H=1-126.
DR PDB; 6YOV; EM; 3.42 A; D/H=1-125.
DR PDB; 7BY0; EM; 4.50 A; D/H=1-126.
DR PDB; 7C0M; EM; 3.90 A; D/H/d/h=2-126.
DR PDB; 7CCQ; EM; 3.80 A; D/H=33-125.
DR PDB; 7CCR; EM; 4.90 A; D/H/O/S=33-125.
DR PDB; 7COW; X-ray; 2.86 A; D/H/N/R=1-126.
DR PDB; 7D1Z; EM; 3.15 A; D/H=2-126.
DR PDB; 7D20; EM; 3.00 A; D/H=2-126.
DR PDB; 7E8D; EM; 2.80 A; D/H=2-126.
DR PDB; 7K5X; EM; 2.93 A; D/H=1-126.
DR PDB; 7K5Y; EM; 2.76 A; D/H=1-126.
DR PDB; 7K60; EM; 3.12 A; D/H=1-126.
DR PDB; 7K61; EM; 2.85 A; D/H=1-126.
DR PDB; 7K63; EM; 3.03 A; D/H=1-126.
DR PDB; 7LYA; EM; 2.91 A; D/H=1-124.
DR PDB; 7LYB; EM; 3.28 A; D/H=1-124.
DR PDB; 7LYC; EM; 2.94 A; D/H=1-124.
DR PDB; 7NL0; EM; 3.50 A; D/H=1-126.
DR PDB; 7SCY; EM; 4.10 A; D/H=1-126.
DR PDB; 7SCZ; EM; 3.50 A; D/H=1-126.
DR PDBsum; 2RVQ; -.
DR PDBsum; 3A6N; -.
DR PDBsum; 3AFA; -.
DR PDBsum; 3AN2; -.
DR PDBsum; 3AV1; -.
DR PDBsum; 3AV2; -.
DR PDBsum; 3AYW; -.
DR PDBsum; 3AZE; -.
DR PDBsum; 3AZF; -.
DR PDBsum; 3AZG; -.
DR PDBsum; 3AZH; -.
DR PDBsum; 3AZI; -.
DR PDBsum; 3AZJ; -.
DR PDBsum; 3AZK; -.
DR PDBsum; 3AZL; -.
DR PDBsum; 3AZM; -.
DR PDBsum; 3AZN; -.
DR PDBsum; 3W96; -.
DR PDBsum; 3W97; -.
DR PDBsum; 3W98; -.
DR PDBsum; 3W99; -.
DR PDBsum; 3WA9; -.
DR PDBsum; 3WAA; -.
DR PDBsum; 3WTP; -.
DR PDBsum; 4CAY; -.
DR PDBsum; 4YM5; -.
DR PDBsum; 4YM6; -.
DR PDBsum; 4Z5T; -.
DR PDBsum; 5AV5; -.
DR PDBsum; 5AV6; -.
DR PDBsum; 5AV8; -.
DR PDBsum; 5AV9; -.
DR PDBsum; 5AVB; -.
DR PDBsum; 5AVC; -.
DR PDBsum; 5AY8; -.
DR PDBsum; 5B0Y; -.
DR PDBsum; 5B0Z; -.
DR PDBsum; 5B24; -.
DR PDBsum; 5B2I; -.
DR PDBsum; 5B2J; -.
DR PDBsum; 5B31; -.
DR PDBsum; 5B32; -.
DR PDBsum; 5B33; -.
DR PDBsum; 5B40; -.
DR PDBsum; 5CPI; -.
DR PDBsum; 5CPJ; -.
DR PDBsum; 5CPK; -.
DR PDBsum; 5FUG; -.
DR PDBsum; 5GSE; -.
DR PDBsum; 5GTC; -.
DR PDBsum; 5GXQ; -.
DR PDBsum; 5JRG; -.
DR PDBsum; 5VEY; -.
DR PDBsum; 5X7X; -.
DR PDBsum; 5XF3; -.
DR PDBsum; 5XF4; -.
DR PDBsum; 5XF5; -.
DR PDBsum; 5Y0C; -.
DR PDBsum; 5Y0D; -.
DR PDBsum; 5Z23; -.
DR PDBsum; 5Z30; -.
DR PDBsum; 5ZBX; -.
DR PDBsum; 6A5L; -.
DR PDBsum; 6A5O; -.
DR PDBsum; 6A5P; -.
DR PDBsum; 6A5R; -.
DR PDBsum; 6A5T; -.
DR PDBsum; 6A5U; -.
DR PDBsum; 6BUZ; -.
DR PDBsum; 6E0C; -.
DR PDBsum; 6E0P; -.
DR PDBsum; 6HKT; -.
DR PDBsum; 6HTS; -.
DR PDBsum; 6INQ; -.
DR PDBsum; 6IPU; -.
DR PDBsum; 6IQ4; -.
DR PDBsum; 6IR9; -.
DR PDBsum; 6J4W; -.
DR PDBsum; 6J4X; -.
DR PDBsum; 6J4Y; -.
DR PDBsum; 6J4Z; -.
DR PDBsum; 6J50; -.
DR PDBsum; 6J51; -.
DR PDBsum; 6JOU; -.
DR PDBsum; 6JR0; -.
DR PDBsum; 6JR1; -.
DR PDBsum; 6JXD; -.
DR PDBsum; 6K1I; -.
DR PDBsum; 6K1J; -.
DR PDBsum; 6K1K; -.
DR PDBsum; 6KVD; -.
DR PDBsum; 6KXV; -.
DR PDBsum; 6L49; -.
DR PDBsum; 6L4A; -.
DR PDBsum; 6L9Z; -.
DR PDBsum; 6LA2; -.
DR PDBsum; 6LA8; -.
DR PDBsum; 6LA9; -.
DR PDBsum; 6LAB; -.
DR PDBsum; 6LER; -.
DR PDBsum; 6M3V; -.
DR PDBsum; 6M44; -.
DR PDBsum; 6O1D; -.
DR PDBsum; 6R8Y; -.
DR PDBsum; 6R8Z; -.
DR PDBsum; 6R90; -.
DR PDBsum; 6R91; -.
DR PDBsum; 6R92; -.
DR PDBsum; 6R93; -.
DR PDBsum; 6R94; -.
DR PDBsum; 6T90; -.
DR PDBsum; 6T93; -.
DR PDBsum; 6USJ; -.
DR PDBsum; 6V2K; -.
DR PDBsum; 6YOV; -.
DR PDBsum; 7BY0; -.
DR PDBsum; 7C0M; -.
DR PDBsum; 7CCQ; -.
DR PDBsum; 7CCR; -.
DR PDBsum; 7COW; -.
DR PDBsum; 7D1Z; -.
DR PDBsum; 7D20; -.
DR PDBsum; 7E8D; -.
DR PDBsum; 7K5X; -.
DR PDBsum; 7K5Y; -.
DR PDBsum; 7K60; -.
DR PDBsum; 7K61; -.
DR PDBsum; 7K63; -.
DR PDBsum; 7LYA; -.
DR PDBsum; 7LYB; -.
DR PDBsum; 7LYC; -.
DR PDBsum; 7NL0; -.
DR PDBsum; 7SCY; -.
DR PDBsum; 7SCZ; -.
DR AlphaFoldDB; P06899; -.
DR SMR; P06899; -.
DR BioGRID; 114460; 108.
DR ComplexPortal; CPX-2556; Nucleosome, variant H3.1-H2A.2-H2B.1.
DR ComplexPortal; CPX-2564; Nucleosome, variant H3.1t-H2A.2-H2B.1.
DR ComplexPortal; CPX-5647; CENP-A nucleosome complex.
DR ComplexPortal; CPX-5668; Nucleosome, variant H3.2-H2A.2-H2B.1.
DR ComplexPortal; CPX-5670; Nucleosome, variant H3.1-H2A.Z-H2B.1.
DR ComplexPortal; CPX-5671; Nucleosome, variant H3.1-H2A.V-H2B.1.
DR DIP; DIP-421N; -.
DR IntAct; P06899; 40.
DR MINT; P06899; -.
DR STRING; 9606.ENSP00000476136; -.
DR GlyGen; P06899; 1 site.
DR iPTMnet; P06899; -.
DR PhosphoSitePlus; P06899; -.
DR SwissPalm; P06899; -.
DR BioMuta; HIST1H2BJ; -.
DR DMDM; 7404367; -.
DR EPD; P06899; -.
DR jPOST; P06899; -.
DR MassIVE; P06899; -.
DR MaxQB; P06899; -.
DR PaxDb; P06899; -.
DR PeptideAtlas; P06899; -.
DR PRIDE; P06899; -.
DR TopDownProteomics; P06899; -.
DR ABCD; P06899; 1 sequenced antibody.
DR Antibodypedia; 58726; 202 antibodies from 15 providers.
DR DNASU; 8970; -.
DR Ensembl; ENST00000339812.3; ENSP00000342886.3; ENSG00000124635.9.
DR Ensembl; ENST00000607124.1; ENSP00000476136.1; ENSG00000124635.9.
DR GeneID; 8970; -.
DR KEGG; hsa:8970; -.
DR MANE-Select; ENST00000339812.3; ENSP00000342886.3; NM_021058.4; NP_066402.2.
DR UCSC; uc003niv.4; human.
DR CTD; 8970; -.
DR DisGeNET; 8970; -.
DR GeneCards; H2BC11; -.
DR HGNC; HGNC:4761; H2BC11.
DR HPA; ENSG00000124635; Tissue enhanced (testis).
DR MIM; 615044; gene.
DR neXtProt; NX_P06899; -.
DR OpenTargets; ENSG00000124635; -.
DR VEuPathDB; HostDB:ENSG00000124635; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244832; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P06899; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P06899; -.
DR TreeFam; TF300212; -.
DR PathwayCommons; P06899; -.
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-3214815; HDACs deacetylate histones.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
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-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
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-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
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-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
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 SignaLink; P06899; -.
DR SIGNOR; P06899; -.
DR BioGRID-ORCS; 8970; 663 hits in 1020 CRISPR screens.
DR EvolutionaryTrace; P06899; -.
DR GeneWiki; HIST1H2BJ; -.
DR GenomeRNAi; 8970; -.
DR Pharos; P06899; Tbio.
DR PRO; PR:P06899; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P06899; protein.
DR Bgee; ENSG00000124635; Expressed in bone marrow cell and 103 other tissues.
DR ExpressionAtlas; P06899; baseline and differential.
DR GO; GO:0043505; C:CENP-A containing nucleosome; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IPI:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR GO; GO:0061644; P:protein localization to CENP-A containing chromatin; IC:ComplexPortal.
DR DisProt; DP01158; -.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
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 3D-structure; Acetylation; Antibiotic; Antimicrobial; Chromosome;
KW Direct protein sequencing; DNA-binding; Glycoprotein; Hydroxylation;
KW Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527,
FT ECO:0000269|PubMed:11859126, ECO:0000269|PubMed:12860195,
FT ECO:0000269|PubMed:15019208, ECO:0000269|PubMed:2917990,
FT ECO:0000269|PubMed:8620898"
FT CHAIN 2..126
FT /note="Histone H2B type 1-J"
FT /id="PRO_0000071836"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT MOD_RES 6
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 6
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:16627869"
FT MOD_RES 6
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 6
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 6
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 12
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 12
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16627869"
FT MOD_RES 12
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 13
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:16627869"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 15
FT /note="Phosphoserine; by STK4/MST1"
FT /evidence="ECO:0000269|PubMed:12757711"
FT MOD_RES 16
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:16627869"
FT MOD_RES 16
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 16
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 17
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16627869"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 17
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 21
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 21
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16283522,
FT ECO:0000269|PubMed:16627869"
FT MOD_RES 21
FT /note="N6-butyryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105113"
FT MOD_RES 21
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 21
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 24
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 24
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 24
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 25
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 35
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 35
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 35
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 35
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 35
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 37
FT /note="Phosphoserine; by AMPK"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 44
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 44
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 44
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 47
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 47
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 47
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16627869"
FT MOD_RES 58
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16627869"
FT MOD_RES 58
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 80
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 86
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 86
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 86
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 87
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 93
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 109
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 109
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 109
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 109
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:16627869"
FT MOD_RES 116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 117
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 117
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 117
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 117
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 117
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 117
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT MOD_RES 121
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:24681537"
FT MOD_RES 121
FT /note="N6-(beta-hydroxybutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:27105115"
FT MOD_RES 121
FT /note="N6-glutaryllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31542297"
FT MOD_RES 121
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 121
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:22389435"
FT CARBOHYD 113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P58876"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:21726816"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000269|PubMed:16307923,
FT ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563"
FT CONFLICT 29..33
FT /note="KRKRS -> SAAH (in Ref. 1; CAA24950)"
FT /evidence="ECO:0000305"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:4CAY"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7D1Z"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4CAY"
FT HELIX 57..83
FT /evidence="ECO:0007829|PDB:4CAY"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:5B33"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5B0Z"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:4CAY"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:4CAY"
SQ SEQUENCE 126 AA; 13904 MW; 0408C881ABBE6647 CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSAK
