ID   H2B_CRYNB               Reviewed;         139 AA.
AC   P0CO03; Q55X48; Q5KMT4;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Histone H2B;
GN   Name=HTB1; OrderedLocusNames=CNBB5140;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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   -!- PTM: Monoubiquitinated by the UBC2-BRE1 complex to form H2BK123ub1.
CC       H2BK123ub1 gives a specific tag for epigenetic transcriptional
CC       activation and is also prerequisite for H3K4me and H3K79me formation.
CC       H2BK123ub1 also modulates the formation of double-strand breaks during
CC       meiosis and is a prerequisite for DNA-damage checkpoint activation (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated to form H2BS10ph during progression through meiotic
CC       prophase. May be correlated with chromosome condensation (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Acetylation of N-terminal lysines and particularly formation of
CC       H2BK11ac has a positive effect on transcription. {ECO:0000250}.
CC   -!- PTM: Sumoylation to form H2BK6su occurs preferentially near the
CC       telomeres and represses gene transcription. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC   -!- CAUTION: To ensure consistency between histone entries, we follow the
CC       'Brno' nomenclature for histone modifications, with positions referring
CC       to those used in the literature for the 'closest' model organism. Due
CC       to slight variations in histone sequences between organisms and to the
CC       presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC       actual positions of modified amino acids in the sequence generally
CC       differ. In this entry the following conventions are used: H2BK6ac =
CC       acetylated Lys-9; H2BK6su = sumoylated Lys-9; H2BS10ph = phosphorylated
CC       Ser-13; H2BK11ac = acetylated Lys-17; H2BK123ub1 = monoubiquitinated
CC       Lys-134. {ECO:0000305}.
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DR   EMBL; AAEY01000011; EAL22339.1; -; Genomic_DNA.
DR   RefSeq; XP_776986.1; XM_771893.1.
DR   AlphaFoldDB; P0CO03; -.
DR   SMR; P0CO03; -.
DR   EnsemblFungi; AAW41759; AAW41759; CNB00560.
DR   EnsemblFungi; EAL22339; EAL22339; CNBB5140.
DR   GeneID; 4934609; -.
DR   KEGG; cnb:CNBB5140; -.
DR   VEuPathDB; FungiDB:CNBB5140; -.
DR   HOGENOM; CLU_075666_2_1_1; -.
DR   Proteomes; UP000001435; Chromosome 2.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; -; 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   3: Inferred from homology;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..139
FT                   /note="Histone H2B"
FT                   /id="PRO_0000410106"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         9
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        9
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        134
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  14753 MW;  A2BCA4CDE22C7C6D CRC64;
     MAPKSVASKA PASQASKAPA AASKAPAKAA KTSAAPKDGA KKRSKKRVES YSSYIYKVLK
     QVHPDTGISN KAMAILNSFV SDIFERIATE ASKLASYNHR STISSREIQT SVRLILPGEL
     SKHAISEGTK AVTKYSSSK