ID H2B1A_HUMAN Reviewed; 127 AA. AC Q96A08; B2R544; Q6NZ98; Q6NZA0; Q6NZA1; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 174. DE RecName: Full=Histone H2B type 1-A; DE AltName: Full=Histone H2B, testis {ECO:0000303|PubMed:12213818}; DE Short=TSH2B.1; DE Short=hTSH2B {ECO:0000303|PubMed:12213818}; DE AltName: Full=Testis-specific histone H2B {ECO:0000303|PubMed:12213818}; GN Name=H2BC1 {ECO:0000312|HGNC:HGNC:18730}; GN Synonyms=HIST1H2BA {ECO:0000312|HGNC:HGNC:18730}, TSH2B GN {ECO:0000303|PubMed:12213818}; 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], AND TISSUE SPECIFICITY. RX PubMed=12213818; DOI=10.1074/jbc.m206065200; RA Zalensky A.O., Siino J.S., Gineitis A.A., Zalenskaya I.A., Tomilin N.V., RA Yau P., Bradbury E.M.; RT "Human testis/sperm-specific histone H2B (hTSH2B). Molecular cloning and RT characterization."; RL J. Biol. Chem. 277:43474-43480(2002). 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 MRNA]. RC TISSUE=Testis; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP UBIQUITINATION AT LYS-122. 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 [8] RP ACETYLATION AT LYS-7; LYS-14; LYS-17 AND LYS-22. 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 [9] RP UBIQUITINATION AT LYS-122. 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 [10] RP CROTONYLATION AT LYS-7; LYS-13; LYS-14; LYS-17; LYS-18; LYS-22; LYS-25 AND RP LYS-36. 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 [11] RP UBIQUITINATION AT LYS-36. 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 [12] RP ACETYLATION AT LYS-87, METHYLATION AT ARG-81; LYS-87; ARG-88 AND ARG-94, RP PHOSPHORYLATION AT SER-86, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=21249133; DOI=10.1371/journal.pone.0015960; RA Jufvas A., Stralfors P., Vener A.V.; RT "Histone variants and their post-translational modifications in primary RT human fat cells."; RL PLoS ONE 6:E15960-E15960(2011). RN [13] 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). CC -!- FUNCTION: Variant histone specifically required to direct the CC transformation of dissociating nucleosomes to protamine in male germ CC cells (By similarity). Entirely replaces classical histone H2B prior CC nucleosome to protamine transition and probably acts as a nucleosome CC dissociating factor that creates a more dynamic chromatin, facilitating CC the large-scale exchange of histones (By similarity). Core component of CC nucleosome (By similarity). Nucleosomes wrap and compact DNA into CC chromatin, limiting DNA accessibility to the cellular machineries which CC require DNA as a template (By similarity). Histones thereby play a CC central role in transcription regulation, DNA repair, DNA replication CC and chromosomal stability (By similarity). DNA accessibility is CC regulated via a complex set of post-translational modifications of CC histones, also called histone code, and nucleosome remodeling (By CC similarity). Also found in fat cells, its function and the presence of CC post-translational modifications specific to such cells are still CC unclear (PubMed:21249133). {ECO:0000250|UniProtKB:P70696, CC ECO:0000269|PubMed:21249133}. 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. {ECO:0000250|UniProtKB:P70696}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P70696}. CC Chromosome {ECO:0000250|UniProtKB:P70696}. CC -!- TISSUE SPECIFICITY: Mainly expressed in testis, and the corresponding CC protein is also present in mature sperm (at protein level). Also found CC in some fat cells. {ECO:0000269|PubMed:12213818, CC ECO:0000269|PubMed:21249133}. CC -!- PTM: Monoubiquitination at Lys-36 (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-122 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:16307923, ECO:0000269|PubMed:16713563}. 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: Acetylated during spermatogenesis. Acetylated form is most CC abundant in spermatogonia compared to spermatocytes and round CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q00729}. CC -!- PTM: Phosphorylated at Thr-117 in spermatogonia, spermatocytes and CC round spermatids. {ECO:0000250|UniProtKB:Q00729}. CC -!- PTM: Methylated at Lys-118 in spermatogonia, spermatocytes and round CC spermatids. {ECO:0000250|UniProtKB:Q00729}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF397301; AAK84040.1; -; Genomic_DNA. DR EMBL; AF531284; AAN06684.1; -; Genomic_DNA. DR EMBL; AK312055; BAG34991.1; -; mRNA. DR EMBL; AL512384; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55490.1; -; Genomic_DNA. DR EMBL; BC066238; AAH66238.1; -; mRNA. DR EMBL; BC066239; AAH66239.1; -; mRNA. DR EMBL; BC066240; AAH66240.1; -; mRNA. DR EMBL; BC066241; AAH66241.1; -; mRNA. DR EMBL; BC066242; AAH66242.1; -; mRNA. DR EMBL; BC066243; AAH66243.1; -; mRNA. DR CCDS; CCDS4563.1; -. DR RefSeq; NP_733759.1; NM_170610.2. DR PDB; 3WKJ; X-ray; 2.80 A; D/H=1-127. DR PDB; 5GSU; X-ray; 3.10 A; D/H=2-127. DR PDB; 5GT3; X-ray; 2.91 A; D/H=2-127. DR PDB; 6BIY; X-ray; 2.05 A; C=70-82. DR PDBsum; 3WKJ; -. DR PDBsum; 5GSU; -. DR PDBsum; 5GT3; -. DR PDBsum; 6BIY; -. DR AlphaFoldDB; Q96A08; -. DR SMR; Q96A08; -. DR BioGRID; 129111; 129. DR IntAct; Q96A08; 85. DR MINT; Q96A08; -. DR STRING; 9606.ENSP00000274764; -. DR GlyGen; Q96A08; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96A08; -. DR MetOSite; Q96A08; -. DR PhosphoSitePlus; Q96A08; -. DR SwissPalm; Q96A08; -. DR BioMuta; HIST1H2BA; -. DR DMDM; 51316070; -. DR EPD; Q96A08; -. DR jPOST; Q96A08; -. DR MassIVE; Q96A08; -. DR MaxQB; Q96A08; -. DR PaxDb; 9606-ENSP00000274764; -. DR PeptideAtlas; Q96A08; -. DR ProteomicsDB; 75889; -. DR Pumba; Q96A08; -. DR TopDownProteomics; Q96A08; -. DR ABCD; Q96A08; 4 sequenced antibodies. DR Antibodypedia; 3172; 352 antibodies from 21 providers. DR DNASU; 255626; -. DR Ensembl; ENST00000274764.5; ENSP00000274764.3; ENSG00000146047.7. DR GeneID; 255626; -. DR KEGG; hsa:255626; -. DR MANE-Select; ENST00000274764.5; ENSP00000274764.3; NM_170610.3; NP_733759.1. DR UCSC; uc003nfd.4; human. DR AGR; HGNC:18730; -. DR CTD; 255626; -. DR DisGeNET; 255626; -. DR GeneCards; H2BC1; -. DR HGNC; HGNC:18730; H2BC1. DR HPA; ENSG00000146047; Tissue enriched (testis). DR MIM; 609904; gene. DR neXtProt; NX_Q96A08; -. DR OpenTargets; ENSG00000146047; -. DR VEuPathDB; HostDB:ENSG00000146047; -. DR eggNOG; KOG1744; Eukaryota. DR GeneTree; ENSGT01100000263474; -. DR HOGENOM; CLU_075666_2_1_1; -. DR InParanoid; Q96A08; -. DR OMA; ITSRKVQ; -. DR OrthoDB; 4736903at2759; -. DR PhylomeDB; Q96A08; -. DR TreeFam; TF300212; -. DR PathwayCommons; Q96A08; -. 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 Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT). DR Reactome; R-HSA-9821993; Replacement of protamines by nucleosomes in the male pronucleus. DR SignaLink; Q96A08; -. DR SIGNOR; Q96A08; -. DR BioGRID-ORCS; 255626; 12 hits in 1131 CRISPR screens. DR GeneWiki; HIST1H2BA; -. DR GenomeRNAi; 255626; -. DR Pharos; Q96A08; Tbio. DR PRO; PR:Q96A08; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q96A08; Protein. DR Bgee; ENSG00000146047; Expressed in primordial germ cell in gonad and 21 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0001674; C:female germ cell nucleus; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0042393; F:histone binding; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0071674; P:mononuclear cell migration; IEA:Ensembl. DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB. DR GO; GO:0006337; P:nucleosome disassembly; ISS:UniProtKB. DR GO; GO:0031639; P:plasminogen activation; IEA:Ensembl. DR GO; GO:0035092; P:sperm DNA condensation; ISS:UniProtKB. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000558; Histone_H2B. DR PANTHER; PTHR23428; HISTONE H2B; 1. DR PANTHER; PTHR23428:SF77; HISTONE H2B TYPE 1-A; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. DR Genevisible; Q96A08; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; DNA-binding; Isopeptide bond; KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P23527" FT CHAIN 2..127 FT /note="Histone H2B type 1-A" FT /id="PRO_0000071842" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..36 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 7 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16283522" FT MOD_RES 7 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 7 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 13 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 13 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 13 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 14 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16283522" FT MOD_RES 14 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 17 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16283522" FT MOD_RES 17 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 17 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 18 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q00729" FT MOD_RES 18 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 18 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 22 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:16283522" FT MOD_RES 22 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 22 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 25 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 25 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 25 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 36 FT /note="N6-crotonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21925322" FT MOD_RES 36 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 38 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q64475" FT MOD_RES 45 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 48 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 59 FT /note="N6,N6-dimethyllysine" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 81 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 86 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 87 FT /note="N6,N6,N6-trimethyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 87 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 87 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 88 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 94 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:21249133" FT MOD_RES 110 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 110 FT /note="N6-methyllysine" FT /evidence="ECO:0000250|UniProtKB:P62807" FT MOD_RES 117 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q00729" FT MOD_RES 118 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 118 FT /note="N6-methylated lysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q00729" FT MOD_RES 118 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT MOD_RES 122 FT /note="N6-lactoyllysine; alternate" FT /evidence="ECO:0000269|PubMed:31645732" FT MOD_RES 122 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P58876" FT CROSSLNK 22 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:Q5QNW6" FT CROSSLNK 36 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000250|UniProtKB:P33778" FT CROSSLNK 122 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:16713563" FT CONFLICT 2 FT /note="P -> A (in Ref. 6; AAH66243)" FT /evidence="ECO:0000305" FT CONFLICT 22 FT /note="K -> E (in Ref. 6; AAH66241)" FT /evidence="ECO:0000305" FT CONFLICT 80 FT /note="S -> P (in Ref. 6; AAH66240)" FT /evidence="ECO:0000305" FT HELIX 40..50 FT /evidence="ECO:0007829|PDB:3WKJ" FT HELIX 58..85 FT /evidence="ECO:0007829|PDB:3WKJ" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:3WKJ" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:3WKJ" FT HELIX 108..124 FT /evidence="ECO:0007829|PDB:3WKJ" SQ SEQUENCE 127 AA; 14167 MW; 3EE4124DA9B3C3E8 CRC64; MPEVSSKGAT ISKKGFKKAV VKTQKKEGKK RKRTRKESYS IYIYKVLKQV HPDTGISSKA MSIMNSFVTD IFERIASEAS RLAHYSKRST ISSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSSK //