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Histone H2B

 H2B_DROME               Reviewed;         123 AA.
P02283; Q4ABE1; Q9W5U7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
12-SEP-2018, entry version 186.
RecName: Full=Histone H2B;
Name=His2B;
and
Name=His2B:CG17949; ORFNames=CG17949;
and
Name=His2B:CG33868; ORFNames=CG33868;
and
Name=His2B:CG33870; ORFNames=CG33870;
and
Name=His2B:CG33872; ORFNames=CG33872;
and
Name=His2B:CG33874; ORFNames=CG33874;
and
Name=His2B:CG33876; ORFNames=CG33876;
and
Name=His2B:CG33878; ORFNames=CG33878;
and
Name=His2B:CG33880; ORFNames=CG33880;
and
Name=His2B:CG33882; ORFNames=CG33882;
and
Name=His2B:CG33884; ORFNames=CG33884;
and
Name=His2B:CG33886; ORFNames=CG33886;
and
Name=His2B:CG33888; ORFNames=CG33888;
and
Name=His2B:CG33890; ORFNames=CG33890;
and
Name=His2B:CG33892; ORFNames=CG33892;
and
Name=His2B:CG33894; ORFNames=CG33894;
and
Name=His2B:CG33896; ORFNames=CG33896;
and
Name=His2B:CG33898; ORFNames=CG33898;
and
Name=His2B:CG33900; ORFNames=CG33900;
and
Name=His2B:CG33902; ORFNames=CG33902;
and
Name=His2B:CG33904; ORFNames=CG33904;
and
Name=His2B:CG33906; ORFNames=CG33906;
and
Name=His2B:CG33908; ORFNames=CG33908;
and
Name=His2B:CG33910; ORFNames=CG33910;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
PROTEIN SEQUENCE (HIS2B).
PubMed=117830; DOI=10.1021/bi00592a025;
Elgin S.C.R., Schilling J., Hood L.E.;
"Sequence of histone 2B of Drosophila melanogaster.";
Biochemistry 18:5679-5685(1979).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2B).
STRAIN=AK-194;
PubMed=2536150; DOI=10.1093/nar/17.1.225;
Matsuo Y., Yamazaki T.;
"tRNA derived insertion element in histone gene repeating unit of
Drosophila melanogaster.";
Nucleic Acids Res. 17:225-238(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS2B:CG17949).
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118 (HIS2B).
Goldberg M.L.;
Thesis (1979), University of Stanford, United States.
[6]
METHYLATION AT PRO-2.
PubMed=3127388;
Desrosiers R., Tanguay R.M.;
"Methylation of Drosophila histones at proline, lysine, and arginine
residues during heat shock.";
J. Biol. Chem. 263:4686-4692(1988).
[7]
CAUTION.
PubMed=15143281; DOI=10.1126/science.1095001;
Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.;
"TAF1 activates transcription by phosphorylation of serine 33 in
histone H2B.";
Science 304:1010-1014(2004).
[8]
PROBABLE UBIQUITINATION.
PubMed=15691768; DOI=10.1016/j.devcel.2004.11.020;
Bray S., Musisi H., Bienz M.;
"Bre1 is required for Notch signaling and histone modification.";
Dev. Cell 8:279-286(2005).
[9]
GLYCOSYLATION.
PubMed=22121020; DOI=10.1038/nature10656;
Fujiki R., Hashiba W., Sekine H., Yokoyama A., Chikanishi T., Ito S.,
Imai Y., Kim J., He H.H., Igarashi K., Kanno J., Ohtake F.,
Kitagawa H., Roeder R.G., Brown M., Kato S.;
"GlcNAcylation of histone H2B facilitates its monoubiquitination.";
Nature 480:557-560(2011).
[10]
SUCCINYLATION AT LYS-44; LYS-114 AND LYS-118.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
-!- 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.
-!- 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.
-!- INTERACTION:
O15265:ATXN7 (xeno); NbExp=2; IntAct=EBI-188137, EBI-708350;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Monoubiquitination of Lys-118 by Bre1 gives a specific tag
for epigenetic transcriptional activation and is also prerequisite
for histone H3 'Lys-4' and 'Lys-79' methylation.
{ECO:0000305|PubMed:3127388}.
-!- PTM: Methylation at Pro-2 increases upon heat shock.
{ECO:0000269|PubMed:3127388}.
-!- PTM: GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-
118. It fluctuates in response to extracellular glucose, and
associates with transcribed genes (Probable). {ECO:0000305}.
-!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
-!- CAUTION: Was reported to be phosphorylated at Ser-34
(PubMed:15143281). However, the paper was retracted because some
data, results and conclusions in the paper are not reliable.
{ECO:0000305|PubMed:15143281}.
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EMBL; X14215; CAA32432.1; -; Genomic_DNA.
EMBL; AE014134; AAN11124.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66483.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66487.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66492.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66496.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66501.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66506.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66511.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66521.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66531.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66576.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66571.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66566.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66561.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66556.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66551.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66546.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66541.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66536.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66479.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66581.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66526.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66516.1; -; Genomic_DNA.
PIR; S10095; HSFF22.
RefSeq; NP_001027283.1; NM_001032112.2.
RefSeq; NP_001027287.1; NM_001032116.2.
RefSeq; NP_001027291.1; NM_001032120.2.
RefSeq; NP_001027296.1; NM_001032125.2.
RefSeq; NP_001027300.1; NM_001032129.2.
RefSeq; NP_001027305.1; NM_001032134.2.
RefSeq; NP_001027310.1; NM_001032139.2.
RefSeq; NP_001027315.1; NM_001032144.2.
RefSeq; NP_001027320.1; NM_001032149.2.
RefSeq; NP_001027325.1; NM_001032154.2.
RefSeq; NP_001027330.1; NM_001032159.2.
RefSeq; NP_001027335.1; NM_001032164.2.
RefSeq; NP_001027340.1; NM_001032169.2.
RefSeq; NP_001027345.1; NM_001032174.2.
RefSeq; NP_001027350.1; NM_001032179.2.
RefSeq; NP_001027355.1; NM_001032184.2.
RefSeq; NP_001027360.1; NM_001032189.2.
RefSeq; NP_001027365.1; NM_001032194.2.
RefSeq; NP_001027370.1; NM_001032199.2.
RefSeq; NP_001027375.1; NM_001032204.2.
RefSeq; NP_001027380.1; NM_001032209.2.
RefSeq; NP_001027385.1; NM_001032214.2.
RefSeq; NP_724342.1; NM_165381.4.
PDB; 2NQB; X-ray; 2.30 A; D/H=2-123.
PDB; 2PYO; X-ray; 2.43 A; D/H=2-123.
PDB; 4QLC; X-ray; 3.50 A; D/H=2-123.
PDB; 4X23; X-ray; 3.50 A; D/H/N/R=33-122.
PDB; 5CVE; X-ray; 1.50 A; D/E=3-10.
PDBsum; 2NQB; -.
PDBsum; 2PYO; -.
PDBsum; 4QLC; -.
PDBsum; 4X23; -.
PDBsum; 5CVE; -.
ProteinModelPortal; P02283; -.
SMR; P02283; -.
BioGrid; 533862; 1.
BioGrid; 77520; 19.
DIP; DIP-22804N; -.
IntAct; P02283; 8.
MINT; P02283; -.
STRING; 7227.FBpp0091155; -.
iPTMnet; P02283; -.
PaxDb; P02283; -.
PRIDE; P02283; -.
EnsemblMetazoa; FBtr0085927; FBpp0085281; FBgn0061209.
EnsemblMetazoa; FBtr0091872; FBpp0091113; FBgn0053868.
EnsemblMetazoa; FBtr0091874; FBpp0091115; FBgn0053870.
EnsemblMetazoa; FBtr0091876; FBpp0091117; FBgn0053872.
EnsemblMetazoa; FBtr0091878; FBpp0091119; FBgn0053874.
EnsemblMetazoa; FBtr0091880; FBpp0091121; FBgn0053876.
EnsemblMetazoa; FBtr0091882; FBpp0091123; FBgn0053878.
EnsemblMetazoa; FBtr0091884; FBpp0091125; FBgn0053880.
EnsemblMetazoa; FBtr0091886; FBpp0091127; FBgn0053882.
EnsemblMetazoa; FBtr0091888; FBpp0091129; FBgn0053884.
EnsemblMetazoa; FBtr0091890; FBpp0091131; FBgn0053886.
EnsemblMetazoa; FBtr0091892; FBpp0091133; FBgn0053888.
EnsemblMetazoa; FBtr0091894; FBpp0091135; FBgn0053890.
EnsemblMetazoa; FBtr0091896; FBpp0091137; FBgn0053892.
EnsemblMetazoa; FBtr0091898; FBpp0091139; FBgn0053894.
EnsemblMetazoa; FBtr0091900; FBpp0091141; FBgn0053896.
EnsemblMetazoa; FBtr0091902; FBpp0091143; FBgn0053898.
EnsemblMetazoa; FBtr0091904; FBpp0091145; FBgn0053900.
EnsemblMetazoa; FBtr0091906; FBpp0091147; FBgn0053902.
EnsemblMetazoa; FBtr0091908; FBpp0091149; FBgn0053904.
EnsemblMetazoa; FBtr0091910; FBpp0091151; FBgn0053906.
EnsemblMetazoa; FBtr0091912; FBpp0091153; FBgn0053908.
EnsemblMetazoa; FBtr0091914; FBpp0091155; FBgn0053910.
GeneID; 326273; -.
GeneID; 3771809; -.
GeneID; 3771891; -.
GeneID; 3771957; -.
GeneID; 3772013; -.
GeneID; 3772058; -.
GeneID; 3772081; -.
GeneID; 3772083; -.
GeneID; 3772094; -.
GeneID; 3772099; -.
GeneID; 3772104; -.
GeneID; 3772166; -.
GeneID; 3772203; -.
GeneID; 3772248; -.
GeneID; 3772264; -.
GeneID; 3772265; -.
GeneID; 3772271; -.
GeneID; 3772276; -.
GeneID; 3772299; -.
GeneID; 3772336; -.
GeneID; 3772496; -.
GeneID; 3772502; -.
GeneID; 3772575; -.
KEGG; dme:Dmel_CG17949; -.
KEGG; dme:Dmel_CG33868; -.
KEGG; dme:Dmel_CG33870; -.
KEGG; dme:Dmel_CG33872; -.
KEGG; dme:Dmel_CG33874; -.
KEGG; dme:Dmel_CG33876; -.
KEGG; dme:Dmel_CG33878; -.
KEGG; dme:Dmel_CG33880; -.
KEGG; dme:Dmel_CG33882; -.
KEGG; dme:Dmel_CG33884; -.
KEGG; dme:Dmel_CG33886; -.
KEGG; dme:Dmel_CG33888; -.
KEGG; dme:Dmel_CG33890; -.
KEGG; dme:Dmel_CG33892; -.
KEGG; dme:Dmel_CG33894; -.
KEGG; dme:Dmel_CG33896; -.
KEGG; dme:Dmel_CG33898; -.
KEGG; dme:Dmel_CG33900; -.
KEGG; dme:Dmel_CG33902; -.
KEGG; dme:Dmel_CG33904; -.
KEGG; dme:Dmel_CG33906; -.
KEGG; dme:Dmel_CG33908; -.
KEGG; dme:Dmel_CG33910; -.
UCSC; CG17949-RA; d. melanogaster.
CTD; 326273; -.
CTD; 3771809; -.
CTD; 3771891; -.
CTD; 3771957; -.
CTD; 3772013; -.
CTD; 3772058; -.
CTD; 3772081; -.
CTD; 3772083; -.
CTD; 3772094; -.
CTD; 3772099; -.
CTD; 3772104; -.
CTD; 3772166; -.
CTD; 3772203; -.
CTD; 3772248; -.
CTD; 3772264; -.
CTD; 3772265; -.
CTD; 3772271; -.
CTD; 3772276; -.
CTD; 3772299; -.
CTD; 3772336; -.
CTD; 3772496; -.
CTD; 3772502; -.
CTD; 3772575; -.
FlyBase; FBgn0001198; His2B.
FlyBase; FBgn0061209; His2B:CG17949.
FlyBase; FBgn0053868; His2B:CG33868.
FlyBase; FBgn0053870; His2B:CG33870.
FlyBase; FBgn0053872; His2B:CG33872.
FlyBase; FBgn0053874; His2B:CG33874.
FlyBase; FBgn0053876; His2B:CG33876.
FlyBase; FBgn0053878; His2B:CG33878.
FlyBase; FBgn0053880; His2B:CG33880.
FlyBase; FBgn0053882; His2B:CG33882.
FlyBase; FBgn0053884; His2B:CG33884.
FlyBase; FBgn0053886; His2B:CG33886.
FlyBase; FBgn0053888; His2B:CG33888.
FlyBase; FBgn0053890; His2B:CG33890.
FlyBase; FBgn0053892; His2B:CG33892.
FlyBase; FBgn0053894; His2B:CG33894.
FlyBase; FBgn0053896; His2B:CG33896.
FlyBase; FBgn0053898; His2B:CG33898.
FlyBase; FBgn0053900; His2B:CG33900.
FlyBase; FBgn0053902; His2B:CG33902.
FlyBase; FBgn0053904; His2B:CG33904.
FlyBase; FBgn0053906; His2B:CG33906.
FlyBase; FBgn0053908; His2B:CG33908.
FlyBase; FBgn0053910; His2B:CG33910.
eggNOG; KOG1744; Eukaryota.
eggNOG; ENOG4111NV5; LUCA.
GeneTree; ENSGT00760000118976; -.
InParanoid; P02283; -.
KO; K11252; -.
OMA; SKEMSIM; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P02283; -.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-212300; PRC2 methylates histones and DNA.
Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-DME-3214815; HDACs deacetylate histones.
Reactome; R-DME-3214847; HATs acetylate histones.
Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-DME-427413; NoRC negatively regulates rRNA expression.
Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
EvolutionaryTrace; P02283; -.
PRO; PR:P02283; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0053868; Expressed in 3 organ(s), highest expression level in larva.
Genevisible; P02283; DM.
GO; GO:0000788; C:nuclear nucleosome; ISS:FlyBase.
GO; GO:0000786; C:nucleosome; TAS:FlyBase.
GO; GO:0003677; F:DNA binding; ISS:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006333; P:chromatin assembly or disassembly; ISS:FlyBase.
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; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Glycoprotein; Isopeptide bond;
Methylation; Nucleosome core; Nucleus; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed.
CHAIN 2 123 Histone H2B.
/FTId=PRO_0000071861.
MOD_RES 2 2 N-methylproline; partial.
{ECO:0000269|PubMed:3127388}.
MOD_RES 44 44 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 114 114 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 118 118 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
CARBOHYD 110 110 O-linked (GlcNAc) serine. {ECO:0000250}.
CROSSLNK 118 118 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305}.
CONFLICT 77 77 R -> C (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 36 46 {ECO:0000244|PDB:2NQB}.
HELIX 54 81 {ECO:0000244|PDB:2NQB}.
HELIX 89 99 {ECO:0000244|PDB:2NQB}.
HELIX 102 121 {ECO:0000244|PDB:2NQB}.
SEQUENCE 123 AA; 13696 MW; 0774D25F34003062 CRC64;
MPPKTSGKAA KKAGKAQKNI TKTDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM
NSFVNDIFER IAAEASRLAH YNKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT
SSK


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