H2B_CRYNJ
ID H2B_CRYNJ Reviewed; 139 AA.
AC P0CO02; Q55X48; Q5KMT4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Histone H2B;
GN Name=HTB1; OrderedLocusNames=CNB00560;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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; AE017342; AAW41759.1; -; Genomic_DNA.
DR RefSeq; XP_569066.1; XM_569066.1.
DR AlphaFoldDB; P0CO02; -.
DR SMR; P0CO02; -.
DR STRING; 5207.AAW41759; -.
DR PaxDb; P0CO02; -.
DR PRIDE; P0CO02; -.
DR EnsemblFungi; AAW41759; AAW41759; CNB00560.
DR GeneID; 3255623; -.
DR KEGG; cne:CNB00560; -.
DR VEuPathDB; FungiDB:CNB00560; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P0CO02; -.
DR OMA; AQLCQTT; -.
DR OrthoDB; 1536672at2759; -.
DR Proteomes; UP000002149; 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; 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 3: Inferred from homology;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..139
FT /note="Histone H2B"
FT /id="PRO_0000245294"
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
