ID H2B2F_HUMAN Reviewed; 126 AA. AC Q5QNW6; A8K0U9; B4DLA9; DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 160. DE RecName: Full=Histone H2B type 2-F; DE AltName: Full=H2B-clustered histone 18 {ECO:0000312|HGNC:HGNC:24700}; GN Name=H2BC18 {ECO:0000312|HGNC:HGNC:24700}; GN Synonyms=HIST2H2BF {ECO:0000312|HGNC:HGNC:24700}; 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala, and Tongue; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pancreas; 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 [4] 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 [5] 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 [6] 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 [7] 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 [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=16319397; DOI=10.1074/mcp.m500288-mcp200; RA Bonenfant D., Coulot M., Towbin H., Schindler P., van Oostrum J.; RT "Characterization of histones H2A and H2B variants and their post- RT translational modifications by mass spectrometry."; RL Mol. Cell. Proteomics 5:541-552(2006). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-17 AND LYS-21, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] 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 [11] 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 [12] 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [14] 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 [15] 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 [16] 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 [17] 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 [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] 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 [20] 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 [21] RP ADP-RIBOSYLATION AT SER-7. RX PubMed=34874266; DOI=10.7554/elife.71502; RA Mohapatra J., Tashiro K., Beckner R.L., Sierra J., Kilgore J.A., RA Williams N.S., Liszczak G.; RT "Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin RT remodeling."; RL Elife 10:0-0(2021). 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 -!- 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. CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5QNW6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5QNW6-2; Sequence=VSP_043431; 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. 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 (PubMed:12757711). Also phosphorylated on Ser-15 CC in response to DNA double strand breaks (DSBs), and in correlation with CC somatic 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: ADP-ribosylated by PARP1 or PARP2 on Ser-7 (H2BS6ADPr) in response CC to DNA damage (PubMed:34874266). H2BS6ADPr promotes recruitment of CC CHD1L (PubMed:34874266). Poly ADP-ribosylation on Glu-36 (H2BE35ADPr) CC by PARP1 regulates adipogenesis: it inhibits phosphorylation at Ser-37 CC (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By CC similarity). {ECO:0000250|UniProtKB:Q6ZWY9, CC ECO:0000269|PubMed:34874266}. 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}. 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; AK289664; BAF82353.1; -; mRNA. DR EMBL; AK296916; BAG59471.1; -; mRNA. DR EMBL; AL591493; CAI12558.1; -; Genomic_DNA. DR EMBL; BC110793; AAI10794.1; -; mRNA. DR CCDS; CCDS30846.1; -. [Q5QNW6-1] DR CCDS; CCDS53359.1; -. [Q5QNW6-2] DR RefSeq; NP_001019770.1; NM_001024599.4. [Q5QNW6-1] DR RefSeq; NP_001154806.1; NM_001161334.1. [Q5QNW6-2] DR PDB; 6MUO; EM; 3.60 A; D/H=34-125. DR PDB; 6MUP; EM; 3.50 A; D/H=34-125. DR PDBsum; 6MUO; -. DR PDBsum; 6MUP; -. DR AlphaFoldDB; Q5QNW6; -. DR EMDB; EMD-9250; -. DR EMDB; EMD-9251; -. DR SMR; Q5QNW6; -. DR BioGRID; 136811; 179. DR IntAct; Q5QNW6; 80. DR MINT; Q5QNW6; -. DR STRING; 9606.ENSP00000445831; -. DR ChEMBL; CHEMBL4295850; -. DR GlyCosmos; Q5QNW6; 1 site, No reported glycans. DR GlyGen; Q5QNW6; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q5QNW6; -. DR MetOSite; Q5QNW6; -. DR PhosphoSitePlus; Q5QNW6; -. DR SwissPalm; Q5QNW6; -. DR BioMuta; HIST2H2BF; -. DR DMDM; 74743113; -. DR EPD; Q5QNW6; -. DR jPOST; Q5QNW6; -. DR MassIVE; Q5QNW6; -. DR MaxQB; Q5QNW6; -. DR PaxDb; 9606-ENSP00000445831; -. DR PeptideAtlas; Q5QNW6; -. DR PRIDE; Q5QNW6; -. DR ProteomicsDB; 63624; -. [Q5QNW6-1] DR ProteomicsDB; 63625; -. [Q5QNW6-2] DR Pumba; Q5QNW6; -. DR TopDownProteomics; Q5QNW6-1; -. [Q5QNW6-1] DR TopDownProteomics; Q5QNW6-2; -. [Q5QNW6-2] DR Antibodypedia; 40729; 185 antibodies from 15 providers. DR DNASU; 440689; -. DR Ensembl; ENST00000369167.3; ENSP00000358164.1; ENSG00000203814.7. [Q5QNW6-1] DR Ensembl; ENST00000545683.1; ENSP00000445831.1; ENSG00000203814.7. [Q5QNW6-2] DR GeneID; 440689; -. DR KEGG; hsa:440689; -. DR MANE-Select; ENST00000369167.3; ENSP00000358164.1; NM_001024599.5; NP_001019770.1. DR UCSC; uc001esr.5; human. [Q5QNW6-1] DR AGR; HGNC:24700; -. DR CTD; 440689; -. DR DisGeNET; 440689; -. DR GeneCards; H2BC18; -. DR HGNC; HGNC:24700; H2BC18. DR HPA; ENSG00000203814; Low tissue specificity. DR neXtProt; NX_Q5QNW6; -. DR OpenTargets; ENSG00000203814; -. DR VEuPathDB; HostDB:ENSG00000203814; -. DR eggNOG; KOG1744; Eukaryota. DR GeneTree; ENSGT01100000263506; -. DR HOGENOM; CLU_075666_2_1_1; -. DR InParanoid; Q5QNW6; -. DR OMA; QRWDLYI; -. DR PhylomeDB; Q5QNW6; -. DR TreeFam; TF300212; -. DR PathwayCommons; Q5QNW6; -. DR Reactome; R-HSA-3214815; HDACs deacetylate histones. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR Reactome; R-HSA-9609690; HCMV Early Events. DR Reactome; R-HSA-9610379; HCMV Late Events. DR SignaLink; Q5QNW6; -. DR SIGNOR; Q5QNW6; -. DR BioGRID-ORCS; 440689; 212 hits in 1078 CRISPR screens. DR ChiTaRS; HIST2H2BF; human. DR GeneWiki; HIST2H2BF; -. DR GenomeRNAi; 440689; -. DR Pharos; Q5QNW6; Tdark. DR PRO; PR:Q5QNW6; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q5QNW6; Protein. DR Bgee; ENSG00000203814; Expressed in bone marrow cell and 99 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. 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:SF384; HISTONE H2B TYPE 2-F; 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; KW Chromosome; DNA-binding; Glycoprotein; Hydroxylation; 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..126 FT /note="Histone H2B type 2-F" FT /id="PRO_0000244826" FT REGION 1..36 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 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 7 FT /note="ADP-ribosylserine" FT /evidence="ECO:0000269|PubMed:34874266" 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:0000250|UniProtKB:P62807" 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 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:0007744|PubMed:19608861" 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:0007744|PubMed:19608861" 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:0007744|PubMed:19608861" 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 36 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000250|UniProtKB:Q64475" 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:0000250|UniProtKB:P62807" FT MOD_RES 58 FT /note="N6,N6-dimethyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P62807" 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:0000250|UniProtKB:P62807" 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:0007744|PubMed:28112733" 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:16713563" FT VAR_SEQ 126 FT /note="K -> KLIGPILWK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043431" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:6MUP" FT TURN 57..59 FT /evidence="ECO:0007829|PDB:6MUP" FT HELIX 60..67 FT /evidence="ECO:0007829|PDB:6MUP" FT HELIX 70..75 FT /evidence="ECO:0007829|PDB:6MUP" FT HELIX 78..84 FT /evidence="ECO:0007829|PDB:6MUP" FT HELIX 93..102 FT /evidence="ECO:0007829|PDB:6MUP" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:6MUP" FT TURN 117..122 FT /evidence="ECO:0007829|PDB:6MUP" SQ SEQUENCE 126 AA; 13920 MW; E951DF3D7E97C106 CRC64; MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT KYTSSK //