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Histone H2B 1/2/3/4/6 (H2B I) (H2B II) (H2B III) (H2B IV) (H2B VI)

 H2B1_CHICK              Reviewed;         126 AA.
P0C1H3; P02279; Q92067;
11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 107.
RecName: Full=Histone H2B 1/2/3/4/6;
AltName: Full=H2B I;
AltName: Full=H2B II;
AltName: Full=H2B III;
AltName: Full=H2B IV;
AltName: Full=H2B VI;
Name=H2B-I;
and
Name=H2B-II;
and
Name=H2B-III;
and
Name=H2B-IV;
and
Name=H2B-VI;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7096326;
Grandy D.K., Engel J.D., Dodgson J.B.;
"Complete nucleotide sequence of a chicken H2B histone gene.";
J. Biol. Chem. 257:8577-8580(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=White leghorn; TISSUE=Blood;
PubMed=3822819; DOI=10.1093/nar/15.3.1063;
Grandy D.K., Dodgson J.B.;
"Structure and organization of the chicken H2B histone gene family.";
Nucleic Acids Res. 15:1063-1080(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2016071; DOI=10.1016/0378-1119(91)90190-M;
Nakayama T., Setoguchi Y.;
"Nucleotide sequence of a member of the chicken H2B histone-encoding
gene family.";
Gene 98:299-300(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND NOMENCLATURE.
STRAIN=White leghorn;
PubMed=8804862; DOI=10.1093/dnares/3.2.95;
Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.;
"Organization of the chicken histone genes in a major gene cluster and
generation of an almost complete set of the core histone protein
sequences.";
DNA Res. 3:95-99(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3267232; DOI=10.1093/nar/16.17.8571;
Sturm R.A., Dalton S., Wells J.R.E.;
"Conservation of histone H2A/H2B intergene regions: a role for the H2B
specific element in divergent transcription.";
Nucleic Acids Res. 16:8571-8586(1988).
[6]
PROTEIN SEQUENCE OF 2-126.
PubMed=7074112; DOI=10.1016/0167-4838(82)90004-8;
van Helden P., Strickland W.N., Strickland M., von Holt C.;
"The complete amino-acid sequence of histone H2B from erythrocytes of
the adult domestic fowl Gallus domesticus.";
Biochim. Biophys. Acta 703:17-20(1982).
[7]
PROTEIN SEQUENCE OF 2-30 AND 62-90.
TISSUE=Erythrocyte;
PubMed=638193; DOI=10.1016/0005-2795(78)90572-X;
van Helden P., Strickland W.N., Brandt W.F., von Holt C.;
"Histone H2B variants from the erythrocytes of an amphibian, a reptile
and a bird.";
Biochim. Biophys. Acta 533:278-281(1978).
[8]
UBIQUITINATION.
PubMed=2713375; DOI=10.1021/bi00429a006;
Nickel B.E., Allis C.D., Davie J.R.;
"Ubiquitinated histone H2B is preferentially located in
transcriptionally active chromatin.";
Biochemistry 28:958-963(1989).
[9]
PHOSPHORYLATION AT SER-15.
PubMed=12757711; DOI=10.1016/S0092-8674(03)00355-6;
Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
"Apoptotic phosphorylation of histone H2B is mediated by mammalian
sterile twenty kinase.";
Cell 113:507-517(2003).
[10]
ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
PubMed=12865423; DOI=10.1074/jbc.M305822200;
Myers F.A., Chong W., Evans D.R., Thorne A.W., Crane-Robinson C.;
"Acetylation of histone H2B mirrors that of H4 and H3 at the chicken
beta-globin locus but not at housekeeping genes.";
J. Biol. Chem. 278:36315-36322(2003).
[11]
FUNCTION AS AN ANTIBIOTIC, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16389069; DOI=10.1016/j.bbrc.2005.12.054;
Silphaduang U., Hincke M.T., Nys Y., Mine Y.;
"Antimicrobial proteins in chicken reproductive system.";
Biochem. Biophys. Res. Commun. 340:648-655(2006).
[12]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=1946434; DOI=10.1073/pnas.88.22.10148;
Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.;
"The nucleosomal core histone octamer at 3.1 A resolution: a
tripartite protein assembly and a left-handed superhelix.";
Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. {ECO:0000269|PubMed:16389069}.
-!- FUNCTION: Has broad-spectrum antibacterial activity. May be
important in the antimicrobial defenses of chick reproductive
system during follicle development in the ovary and egg formation
in the oviduct. {ECO:0000269|PubMed:16389069}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Monoubiquitination of Lys-121 by the BRE1 gives a specific
tag for epigenetic transcriptional activation and is also
prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
{ECO:0000250|UniProtKB:P33778}.
-!- PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates
apoptotic chromatin condensation. {ECO:0000269|PubMed:12757711}.
-!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; V00415; CAA23706.1; -; Genomic_DNA.
EMBL; X05094; CAA28745.1; -; Genomic_DNA.
EMBL; X05095; CAA28746.1; -; Genomic_DNA.
EMBL; X05096; CAA28747.1; -; Genomic_DNA.
EMBL; X05097; CAA28748.1; -; Genomic_DNA.
EMBL; X05098; CAA28749.1; -; Genomic_DNA.
EMBL; X05100; CAA28751.1; -; Genomic_DNA.
EMBL; X57263; CAA40537.1; -; Genomic_DNA.
EMBL; X07763; CAA30590.1; -; Genomic_DNA.
EMBL; X07766; CAA30596.1; -; Genomic_DNA.
PIR; B26399; B26399.
PIR; S14510; HSCH22.
RefSeq; NP_001073188.1; NM_001079720.1.
RefSeq; XP_001232985.1; XM_001232984.3.
RefSeq; XP_001233227.1; XM_001233226.4.
RefSeq; XP_001233337.1; XM_001233336.4.
RefSeq; XP_004937730.1; XM_004937673.2.
UniGene; Gga.39843; -.
UniGene; Gga.40038; -.
PDB; 2ARO; X-ray; 2.10 A; B/F=1-126.
PDBsum; 2ARO; -.
ProteinModelPortal; P0C1H3; -.
SMR; P0C1H3; -.
BioGrid; 679231; 3.
IntAct; P0C1H3; 1.
STRING; 9031.ENSGALP00000037300; -.
iPTMnet; P0C1H3; -.
PaxDb; P0C1H3; -.
PRIDE; P0C1H3; -.
Ensembl; ENSGALT00000021778; ENSGALP00000021742; ENSGALG00000042263.
Ensembl; ENSGALT00000042841; ENSGALP00000042437; ENSGALG00000027594.
Ensembl; ENSGALT00000043224; ENSGALP00000042501; ENSGALG00000027571.
Ensembl; ENSGALT00000052037; ENSGALP00000053434; ENSGALG00000039722.
Ensembl; ENSGALT00000054609; ENSGALP00000054120; ENSGALG00000037934.
GeneID; 100858607; -.
GeneID; 417956; -.
GeneID; 769973; -.
GeneID; 770188; -.
GeneID; 770267; -.
KEGG; gga:100858607; -.
KEGG; gga:417956; -.
KEGG; gga:769973; -.
KEGG; gga:770188; -.
KEGG; gga:770267; -.
CTD; 417956; -.
CTD; 770188; -.
CTD; 770267; -.
CTD; 8343; -.
CTD; 8348; -.
eggNOG; KOG1744; Eukaryota.
eggNOG; ENOG4111NV5; LUCA.
GeneTree; ENSGT00940000153443; -.
HOGENOM; HOG000231213; -.
HOVERGEN; HBG007774; -.
InParanoid; P0C1H3; -.
KO; K11252; -.
OMA; DIFDRMA; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P0C1H3; -.
TreeFam; TF300212; -.
Reactome; R-GGA-212300; PRC2 methylates histones and DNA.
Reactome; R-GGA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-GGA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-GGA-3214847; HATs acetylate histones.
Reactome; R-GGA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-GGA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-GGA-5689880; Ub-specific processing proteases.
Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-GGA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-GGA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-GGA-69473; G2/M DNA damage checkpoint.
Reactome; R-GGA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-GGA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-GGA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-GGA-9018519; Estrogen-dependent gene expression.
EvolutionaryTrace; P0C1H3; -.
PRO; PR:P0C1H3; -.
Proteomes; UP000000539; Chromosome 1.
Bgee; ENSGALG00000027174; Expressed in 10 organ(s), highest expression level in testis.
GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000558; Histone_H2B.
PANTHER; PTHR23428; PTHR23428; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00621; HISTONEH2B.
SMART; SM00427; H2B; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00357; HISTONE_H2B; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Antibiotic; Antimicrobial; Chromosome;
Complete proteome; Direct protein sequencing; DNA-binding;
Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:638193,
ECO:0000269|PubMed:7074112}.
CHAIN 2 126 Histone H2B 1/2/3/4/6.
/FTId=PRO_0000071846.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000269|PubMed:12865423}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000269|PubMed:12865423}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000269|PubMed:12757711}.
MOD_RES 16 16 N6-acetyllysine.
{ECO:0000269|PubMed:12865423}.
MOD_RES 21 21 N6-acetyllysine.
{ECO:0000269|PubMed:12865423}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:2713375}.
CONFLICT 14 14 G -> A (in Ref. 2; CAA28745).
{ECO:0000305}.
CONFLICT 36 36 E -> A (in Ref. 2; CAA28747).
{ECO:0000305}.
CONFLICT 62 62 I -> S (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 123 123 T -> I (in Ref. 2; CAA28751).
{ECO:0000305}.
HELIX 39 49 {ECO:0000244|PDB:2ARO}.
HELIX 57 84 {ECO:0000244|PDB:2ARO}.
STRAND 88 90 {ECO:0000244|PDB:2ARO}.
HELIX 92 102 {ECO:0000244|PDB:2ARO}.
HELIX 105 124 {ECO:0000244|PDB:2ARO}.
SEQUENCE 126 AA; 13922 MW; 908F039A02A3400D CRC64;
MPEPAKSAPA PKKGSKKAVT KTQKKGDKKR KKSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSSK


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