H2B5_CHICK
ID H2B5_CHICK Reviewed; 126 AA.
AC P0C1H4; P02279;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Histone H2B 5;
DE AltName: Full=H2B V;
GN Name=H2B-V;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn;
RX PubMed=2016071; DOI=10.1016/0378-1119(91)90190-m;
RA Nakayama T., Setoguchi Y.;
RT "Nucleotide sequence of a member of the chicken H2B histone-encoding gene
RT family.";
RL Gene 98:299-300(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
RC STRAIN=White leghorn;
RX PubMed=8804862; DOI=10.1093/dnares/3.2.95;
RA Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.;
RT "Organization of the chicken histone genes in a major gene cluster and
RT generation of an almost complete set of the core histone protein
RT sequences.";
RL DNA Res. 3:95-99(1996).
RN [3]
RP UBIQUITINATION.
RX PubMed=2713375; DOI=10.1021/bi00429a006;
RA Nickel B.E., Allis C.D., Davie J.R.;
RT "Ubiquitinated histone H2B is preferentially located in transcriptionally
RT active chromatin.";
RL Biochemistry 28:958-963(1989).
RN [4]
RP PHOSPHORYLATION AT SER-15.
RX PubMed=12757711; DOI=10.1016/s0092-8674(03)00355-6;
RA Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
RA Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
RT "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile
RT twenty kinase.";
RL Cell 113:507-517(2003).
RN [5]
RP ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
RX PubMed=12865423; DOI=10.1074/jbc.m305822200;
RA Myers F.A., Chong W., Evans D.R., Thorne A.W., Crane-Robinson C.;
RT "Acetylation of histone H2B mirrors that of H4 and H3 at the chicken beta-
RT globin locus but not at housekeeping genes.";
RL J. Biol. Chem. 278:36315-36322(2003).
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: Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for
CC epigenetic transcriptional activation and is also prerequisite for
CC histone H3 'Lys-4' and 'Lys-79' methylation.
CC {ECO:0000250|UniProtKB:P33778}.
CC -!- PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates
CC apoptotic chromatin condensation. {ECO:0000269|PubMed:12757711}.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; M57901; AAA48792.1; -; Genomic_DNA.
DR PIR; JH0362; JH0362.
DR RefSeq; NP_001073189.1; NM_001079721.1.
DR PDB; 2XQL; EM; 19.50 A; B/D/F/H/J=37-126.
DR PDBsum; 2XQL; -.
DR AlphaFoldDB; P0C1H4; -.
DR SMR; P0C1H4; -.
DR STRING; 9031.ENSGALP00000037260; -.
DR iPTMnet; P0C1H4; -.
DR PaxDb; P0C1H4; -.
DR Ensembl; ENSGALT00000092743; ENSGALP00000069619; ENSGALG00000052649.
DR GeneID; 417957; -.
DR KEGG; gga:417957; -.
DR CTD; 417957; -.
DR VEuPathDB; HostDB:geneid_417957; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P0C1H4; -.
DR OMA; SKEMSIM; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P0C1H4; -.
DR TreeFam; TF300212; -.
DR EvolutionaryTrace; P0C1H4; -.
DR PRO; PR:P0C1H4; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000052649; Expressed in testis and 12 other tissues.
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 DisProt; DP01649; -.
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; Glycoprotein;
KW Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..126
FT /note="Histone H2B 5"
FT /id="PRO_0000244864"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12865423"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12865423"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12757711"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12865423"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:12865423"
FT CARBOHYD 113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:2713375"
SQ SEQUENCE 126 AA; 13950 MW; 44A941FE24F77015 CRC64;
MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR RKSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
