H2B1_CHICK
ID H2B1_CHICK Reviewed; 126 AA.
AC P0C1H3; P02279; Q92067;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Histone H2B 1/2/3/4/6;
DE AltName: Full=H2B I;
DE AltName: Full=H2B II;
DE AltName: Full=H2B III;
DE AltName: Full=H2B IV;
DE AltName: Full=H2B VI;
GN Name=H2B-I;
GN and
GN Name=H2B-II;
GN and
GN Name=H2B-III;
GN and
GN Name=H2B-IV;
GN and
GN Name=H2B-VI;
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].
RX PubMed=7096326; DOI=10.1016/s0021-9258(18)34160-7;
RA Grandy D.K., Engel J.D., Dodgson J.B.;
RT "Complete nucleotide sequence of a chicken H2B histone gene.";
RL J. Biol. Chem. 257:8577-8580(1982).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3267232; DOI=10.1093/nar/16.17.8571;
RA Sturm R.A., Dalton S., Wells J.R.E.;
RT "Conservation of histone H2A/H2B intergene regions: a role for the H2B
RT specific element in divergent transcription.";
RL Nucleic Acids Res. 16:8571-8586(1988).
RN [6]
RP PROTEIN SEQUENCE OF 2-126.
RX PubMed=7074112; DOI=10.1016/0167-4838(82)90004-8;
RA van Helden P., Strickland W.N., Strickland M., von Holt C.;
RT "The complete amino-acid sequence of histone H2B from erythrocytes of the
RT adult domestic fowl Gallus domesticus.";
RL Biochim. Biophys. Acta 703:17-20(1982).
RN [7]
RP PROTEIN SEQUENCE OF 2-30 AND 62-90.
RC TISSUE=Erythrocyte;
RX PubMed=638193; DOI=10.1016/0005-2795(78)90572-x;
RA van Helden P., Strickland W.N., Brandt W.F., von Holt C.;
RT "Histone H2B variants from the erythrocytes of an amphibian, a reptile and
RT a bird.";
RL Biochim. Biophys. Acta 533:278-281(1978).
RN [8]
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 [9]
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 [10]
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 [11]
RP FUNCTION AS AN ANTIBIOTIC, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16389069; DOI=10.1016/j.bbrc.2005.12.054;
RA Silphaduang U., Hincke M.T., Nys Y., Mine Y.;
RT "Antimicrobial proteins in chicken reproductive system.";
RL Biochem. Biophys. Res. Commun. 340:648-655(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
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).
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. {ECO:0000269|PubMed:16389069}.
CC -!- FUNCTION: Has broad-spectrum antibacterial activity. May be important
CC in the antimicrobial defenses of chick reproductive system during
CC follicle development in the ovary and egg formation in the oviduct.
CC {ECO:0000269|PubMed:16389069}.
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 -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; V00415; CAA23706.1; -; Genomic_DNA.
DR EMBL; X05094; CAA28745.1; -; Genomic_DNA.
DR EMBL; X05095; CAA28746.1; -; Genomic_DNA.
DR EMBL; X05096; CAA28747.1; -; Genomic_DNA.
DR EMBL; X05097; CAA28748.1; -; Genomic_DNA.
DR EMBL; X05098; CAA28749.1; -; Genomic_DNA.
DR EMBL; X05100; CAA28751.1; -; Genomic_DNA.
DR EMBL; X57263; CAA40537.1; -; Genomic_DNA.
DR EMBL; X07763; CAA30590.1; -; Genomic_DNA.
DR EMBL; X07766; CAA30596.1; -; Genomic_DNA.
DR PIR; B26399; B26399.
DR PIR; S14510; HSCH22.
DR RefSeq; NP_001073188.1; NM_001079720.1.
DR RefSeq; XP_001232985.1; XM_001232984.3.
DR RefSeq; XP_001233227.1; XM_001233226.4.
DR RefSeq; XP_001233337.1; XM_001233336.4.
DR RefSeq; XP_004937730.1; XM_004937673.2.
DR PDB; 2ARO; X-ray; 2.10 A; B/F=1-126.
DR PDBsum; 2ARO; -.
DR AlphaFoldDB; P0C1H3; -.
DR SMR; P0C1H3; -.
DR BioGRID; 679231; 3.
DR IntAct; P0C1H3; 1.
DR STRING; 9031.ENSGALP00000021742; -.
DR iPTMnet; P0C1H3; -.
DR PaxDb; P0C1H3; -.
DR PRIDE; P0C1H3; -.
DR Ensembl; ENSGALT00000042841; ENSGALP00000042437; ENSGALG00000050309.
DR Ensembl; ENSGALT00000043224; ENSGALP00000042501; ENSGALG00000027571.
DR Ensembl; ENSGALT00000090832; ENSGALP00000065924; ENSGALG00000051251.
DR Ensembl; ENSGALT00000104386; ENSGALP00000071137; ENSGALG00000050350.
DR Ensembl; ENSGALT00000105242; ENSGALP00000071464; ENSGALG00000049751.
DR GeneID; 100858607; -.
DR GeneID; 417956; -.
DR GeneID; 770267; -.
DR KEGG; gga:100858607; -.
DR KEGG; gga:417956; -.
DR KEGG; gga:769973; -.
DR KEGG; gga:770188; -.
DR KEGG; gga:770267; -.
DR CTD; 291157; -.
DR CTD; 417956; -.
DR CTD; 770267; -.
DR VEuPathDB; HostDB:geneid_100858607; -.
DR VEuPathDB; HostDB:geneid_417956; -.
DR VEuPathDB; HostDB:geneid_770267; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P0C1H3; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P0C1H3; -.
DR TreeFam; TF300212; -.
DR Reactome; R-GGA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-GGA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-GGA-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-GGA-3214815; HDACs deacetylate histones.
DR Reactome; R-GGA-3214847; HATs acetylate histones.
DR Reactome; R-GGA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-GGA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-GGA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-GGA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-GGA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-GGA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
DR EvolutionaryTrace; P0C1H3; -.
DR PRO; PR:P0C1H3; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000027571; Expressed in granulocyte and 10 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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
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; Antibiotic; Antimicrobial; Chromosome;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:638193,
FT ECO:0000269|PubMed:7074112"
FT CHAIN 2..126
FT /note="Histone H2B 1/2/3/4/6"
FT /id="PRO_0000071846"
FT REGION 1..36
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 CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:2713375"
FT CONFLICT 14
FT /note="G -> A (in Ref. 2; CAA28745)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="E -> A (in Ref. 2; CAA28747)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="I -> S (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="T -> I (in Ref. 2; CAA28751)"
FT /evidence="ECO:0000305"
FT HELIX 39..49
FT /evidence="ECO:0007829|PDB:2ARO"
FT HELIX 57..84
FT /evidence="ECO:0007829|PDB:2ARO"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2ARO"
FT HELIX 92..102
FT /evidence="ECO:0007829|PDB:2ARO"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:2ARO"
SQ SEQUENCE 126 AA; 13922 MW; 908F039A02A3400D CRC64;
MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR KKSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK
