H2B1A_HUMAN
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 03-AUG-2022, entry version 165.
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},
GN TSH2B {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=10.1006/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=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}.
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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; 125.
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; Q96A08; -.
DR PeptideAtlas; Q96A08; -.
DR PRIDE; Q96A08; -.
DR ProteomicsDB; 75889; -.
DR TopDownProteomics; Q96A08; -.
DR Antibodypedia; 3172; 319 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 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; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; Q96A08; -.
DR OMA; YLQIAFX; -.
DR OrthoDB; 1536672at2759; -.
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 SignaLink; Q96A08; -.
DR SIGNOR; Q96A08; -.
DR BioGRID-ORCS; 255626; 10 hits in 1064 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 left testis and 19 other tissues.
DR Genevisible; Q96A08; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
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; IBA:GO_Central.
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: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:0051099; P:positive regulation of binding; IEA:Ensembl.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; ISS:UniProtKB.
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; 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
