H2B7_CHICK
ID H2B7_CHICK Reviewed; 126 AA.
AC P0C1H5; P02279;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone H2B 7;
DE AltName: Full=H2B VII;
GN Name=H2B-VII;
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; TISSUE=Blood;
RX PubMed=3822819; DOI=10.1093/nar/15.3.1063;
RA Grandy D.K., Dodgson J.B.;
RT "Structure and organization of the chicken H2B histone gene family.";
RL Nucleic Acids Res. 15:1063-1080(1987).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=1946434; DOI=10.1073/pnas.88.22.10148;
RA Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.;
RT "The nucleosomal core histone octamer at 3.1 A resolution: a tripartite
RT protein assembly and a left-handed superhelix.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, AND
RP SUBUNIT.
RX PubMed=15299701; DOI=10.1107/s0907444995009139;
RA Harp J.M., Uberbacher E.C., Roberson A.E., Palmer E.L., Gewiess A.,
RA Bunick G.J.;
RT "X-ray diffraction analysis of crystals containing twofold symmetric
RT nucleosome core particles.";
RL Acta Crystallogr. D 52:283-288(1996).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), AND SUBUNIT.
RX PubMed=12876341; DOI=10.1107/s0907444903011880;
RA Chantalat L., Nicholson J.M., Lambert S.J., Reid A.J., Donovan M.J.,
RA Reynolds C.D., Wood C.M., Baldwin J.P.;
RT "Structure of the histone-core octamer in KCl/phosphate crystals at 2.15 A
RT resolution.";
RL Acta Crystallogr. D 59:1395-1407(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. {ECO:0000269|PubMed:12876341, ECO:0000269|PubMed:15299701,
CC ECO:0000269|PubMed:1946434}.
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; X05099; CAA28750.1; -; Genomic_DNA.
DR EMBL; U37575; AAC60000.1; -; Genomic_DNA.
DR RefSeq; XP_015144978.1; XM_015289492.1.
DR PDB; 1EQZ; X-ray; 2.50 A; B/F=1-126.
DR PDB; 1HIO; X-ray; 3.10 A; B=37-126.
DR PDB; 1HQ3; X-ray; 2.15 A; B/F=1-126.
DR PDB; 1TZY; X-ray; 1.90 A; B/F=1-126.
DR PDB; 2HIO; X-ray; 3.10 A; B=2-126.
DR PDB; 3C9K; EM; 20.00 A; B/F=2-126.
DR PDBsum; 1EQZ; -.
DR PDBsum; 1HIO; -.
DR PDBsum; 1HQ3; -.
DR PDBsum; 1TZY; -.
DR PDBsum; 2HIO; -.
DR PDBsum; 3C9K; -.
DR AlphaFoldDB; P0C1H5; -.
DR SMR; P0C1H5; -.
DR IntAct; P0C1H5; 1.
DR iPTMnet; P0C1H5; -.
DR Ensembl; ENSGALT00000073535; ENSGALP00000055900; ENSGALG00000036908.
DR KEGG; gga:107053803; -.
DR VEuPathDB; HostDB:geneid_429558; -.
DR GeneTree; ENSGT01050000244921; -.
DR InParanoid; P0C1H5; -.
DR OMA; DIFDRMA; -.
DR OrthoDB; 1536672at2759; -.
DR EvolutionaryTrace; P0C1H5; -.
DR PRO; PR:P0C1H5; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000036908; Expressed in granulocyte and 7 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:0044877; F:protein-containing complex binding; ISS:UniProtKB.
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 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 7"
FT /id="PRO_0000244865"
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"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:1TZY"
FT HELIX 57..84
FT /evidence="ECO:0007829|PDB:1TZY"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:1TZY"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:1TZY"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:1TZY"
SQ SEQUENCE 126 AA; 13964 MW; B14EC3822B5DAA97 CRC64;
MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR KRARKESYSI YVYKVLKQVH PDTGISSKAM
SIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
