H2B1_KLULA
ID H2B1_KLULA Reviewed; 132 AA.
AC Q6CK60;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Histone H2B.1;
GN Name=HTB1; OrderedLocusNames=KLLA0F13310g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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 and probably also H2BK16su or
CC H2BK17su, occurs preferentially near the telomeres and represses gene
CC 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; H2BS10ph = phosphorylated
CC Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17;
CC H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1
CC = monoubiquitinated Lys-125. {ECO:0000305}.
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DR EMBL; CR382126; CAG98387.1; -; Genomic_DNA.
DR RefSeq; XP_455679.1; XM_455679.1.
DR PDB; 6UPH; EM; 2.70 A; D/H=1-132.
DR PDBsum; 6UPH; -.
DR AlphaFoldDB; Q6CK60; -.
DR SMR; Q6CK60; -.
DR STRING; 28985.XP_455679.1; -.
DR EnsemblFungi; CAG98387; CAG98387; KLLA0_F13310g.
DR GeneID; 2895972; -.
DR KEGG; kla:KLLA0_F13310g; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_3_1; -.
DR InParanoid; Q6CK60; -.
DR OMA; PGVMAPK; -.
DR Proteomes; UP000000598; Chromosome F.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA-binding; Isopeptide bond;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..132
FT /note="Histone H2B.1"
FT /id="PRO_0000245296"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
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 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 125
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:6UPH"
FT HELIX 61..87
FT /evidence="ECO:0007829|PDB:6UPH"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:6UPH"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:6UPH"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:6UPH"
SQ SEQUENCE 132 AA; 14296 MW; CE8932DDB5B6AFE4 CRC64;
MSAKASKAPA SKAPAEKKPA AKKTSSSTDP SKKRTKARKE TYSSYIYKVL KQTHPDTGIS
QKSMSILNSF VNDIFERIAT ESSKLAAYNK KSTISAREIQ TAVRLILPGE LAKHAVSEGT
RAVTKYSSST QA
