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H2B2F_HUMAN
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   03-AUG-2022, entry version 151.
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).
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. 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; 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   SMR; Q5QNW6; -.
DR   BioGRID; 136811; 166.
DR   IntAct; Q5QNW6; 80.
DR   MINT; Q5QNW6; -.
DR   STRING; 9606.ENSP00000445831; -.
DR   ChEMBL; CHEMBL4295850; -.
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; Q5QNW6; -.
DR   PeptideAtlas; Q5QNW6; -.
DR   PRIDE; Q5QNW6; -.
DR   ProteomicsDB; 63624; -. [Q5QNW6-1]
DR   ProteomicsDB; 63625; -. [Q5QNW6-2]
DR   TopDownProteomics; Q5QNW6-1; -. [Q5QNW6-1]
DR   TopDownProteomics; Q5QNW6-2; -. [Q5QNW6-2]
DR   Antibodypedia; 40729; 173 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   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; ENSGT01050000244943; -.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   InParanoid; Q5QNW6; -.
DR   OMA; PGVMAPK; -.
DR   OrthoDB; 866496at2759; -.
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; 209 hits in 1005 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 98 other 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; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
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; Alternative splicing; Chromosome; DNA-binding;
KW   Glycoprotein; Hydroxylation; Isopeptide bond; Methylation; Nucleosome core;
KW   Nucleus; Phosphoprotein; Reference proteome; 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         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         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
 
 
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