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H2B2_CANAL
ID   H2B2_CANAL              Reviewed;         130 AA.
AC   Q59VP1; A0A1D8PD85;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Histone H2B.2;
GN   Name=HTB2; OrderedLocusNames=CAALFM_C104180WA;
GN   ORFNames=CaO19.1052, CaO19.8654;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
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 by STE20 to form H2BS10ph during progression
CC       through meiotic prophase. May be correlated with chromosome
CC       condensation (By similarity). {ECO:0000250}.
CC   -!- PTM: Acetylated by GCN5 to form H2BK11ac and H2BK16ac. H2BK16ac can
CC       also be formed by ESA1. Acetylation of N-terminal lysines and
CC       particularly formation of H2BK11acK16ac has a positive effect on
CC       transcription (By similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su
CC       or H2BK17su, occurs preferentially near the telomeres and represses
CC       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-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-
CC       8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11;
CC       H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su =
CC       sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 =
CC       monoubiquitinated Lys-124. {ECO:0000305}.
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DR   EMBL; CP017623; AOW26093.1; -; Genomic_DNA.
DR   RefSeq; XP_713656.1; XM_708563.1.
DR   AlphaFoldDB; Q59VP1; -.
DR   SMR; Q59VP1; -.
DR   BioGRID; 1227729; 1.
DR   STRING; 237561.Q59VP1; -.
DR   GeneID; 3644716; -.
DR   KEGG; cal:CAALFM_C104180WA; -.
DR   CGD; CAL0000199081; orf19.8654.
DR   VEuPathDB; FungiDB:C1_04180W_A; -.
DR   eggNOG; KOG1744; Eukaryota.
DR   HOGENOM; CLU_075666_1_3_1; -.
DR   InParanoid; Q59VP1; -.
DR   OMA; PRMSIMN; -.
DR   OrthoDB; 1536672at2759; -.
DR   PRO; PR:Q59VP1; -.
DR   Proteomes; UP000000559; Chromosome 1.
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; IDA:CGD.
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..130
FT                   /note="Histone H2B.2"
FT                   /id="PRO_0000245456"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         7
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         17
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        7
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        17
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        124
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   130 AA;  14103 MW;  FF1E08AA9ADEF7CB CRC64;
     MAPKAEKKPA SKAPAEKKPA AKKTASTDGA KKRTKARKET YSSYIYKVLK QTHPDTGISQ
     KAMSIMNSFV NDIFERIASE ASKLAAYNKK STISAREIQT AVRLILPGEL AKHAVSEGTR
     AVTKYSSASN
 
 
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