H2B1_CANGA
ID H2B1_CANGA Reviewed; 129 AA.
AC Q6FWM8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone H2B.1;
GN Name=HTB1; OrderedLocusNames=CAGL0C04389g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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-5; H2BK6su = sumoylated Lys-5; H2BK7ac = acetylated Lys-
CC 6; H2BK7su = sumoylated Lys-6; H2BS10ph = phosphorylated Ser-9;
CC H2BK11ac = acetylated Lys-10; H2BK16ac = acetylated Lys-15; H2BK16su =
CC sumoylated Lys-15; H2BK17su = sumoylated Lys-16; H2BK123ub1 =
CC monoubiquitinated Lys-122. {ECO:0000305}.
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DR EMBL; CR380949; CAG58272.1; -; Genomic_DNA.
DR RefSeq; XP_445366.1; XM_445366.1.
DR AlphaFoldDB; Q6FWM8; -.
DR SMR; Q6FWM8; -.
DR STRING; 5478.XP_445366.1; -.
DR EnsemblFungi; CAG58272; CAG58272; CAGL0C04389g.
DR GeneID; 2886743; -.
DR KEGG; cgr:CAGL0C04389g; -.
DR CGD; CAL0127264; CAGL0C04389g.
DR VEuPathDB; FungiDB:CAGL0C04389g; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_3_1; -.
DR InParanoid; Q6FWM8; -.
DR OMA; AQLCQTT; -.
DR Proteomes; UP000002428; Chromosome C.
DR GO; GO:0005576; C:extracellular region; IDA:CGD.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..129
FT /note="Histone H2B.1"
FT /id="PRO_0000071931"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 16
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 129 AA; 14003 MW; A000C3E3FE5DB7C2 CRC64;
MSAEKKPASK APAEKKPAAK KTAPSADGKK RTKARKETYS SYIYKVLKQT HPDTGISQKS
MSILNSFVND IFERIASEAS KLAAYNKKST ISAREIQTAV RLILPGELAK HAVSEGTRAV
TKYSSSTQA
