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P02283 (H2B_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2B
Gene names
Name:His2B
AND
Name:His2B:CG17949
ORF Names:CG17949
AND
Name:His2B:CG33868
ORF Names:CG33868
AND
Name:His2B:CG33870
ORF Names:CG33870
AND
Name:His2B:CG33872
ORF Names:CG33872
AND
Name:His2B:CG33874
ORF Names:CG33874
AND
Name:His2B:CG33876
ORF Names:CG33876
AND
Name:His2B:CG33878
ORF Names:CG33878
AND
Name:His2B:CG33880
ORF Names:CG33880
AND
Name:His2B:CG33882
ORF Names:CG33882
AND
Name:His2B:CG33884
ORF Names:CG33884
AND
Name:His2B:CG33886
ORF Names:CG33886
AND
Name:His2B:CG33888
ORF Names:CG33888
AND
Name:His2B:CG33890
ORF Names:CG33890
AND
Name:His2B:CG33892
ORF Names:CG33892
AND
Name:His2B:CG33894
ORF Names:CG33894
AND
Name:His2B:CG33896
ORF Names:CG33896
AND
Name:His2B:CG33898
ORF Names:CG33898
AND
Name:His2B:CG33900
ORF Names:CG33900
AND
Name:His2B:CG33902
ORF Names:CG33902
AND
Name:His2B:CG33904
ORF Names:CG33904
AND
Name:His2B:CG33906
ORF Names:CG33906
AND
Name:His2B:CG33908
ORF Names:CG33908
AND
Name:His2B:CG33910
ORF Names:CG33910
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length123 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 structure

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.

Post-translational modification

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 Probable.

Phosphorylation on Ser-34 by Taf-1 potentiates transcriptional activation.

Methylation at Pro-2 increases upon heat shock. Ref.6

GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-118. It fluctuates in response to extracellular glucose, and associates with transcribed genes Probable.

Sequence similarities

Belongs to the histone H2B family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN7O152652EBI-188137,EBI-708350From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 123122Histone H2B
PRO_0000071861

Amino acid modifications

Modified residue21N-methylproline; partial Ref.6
Modified residue341Phosphoserine; by TAF1 Ref.7
Glycosylation1101O-linked (GlcNAc) By similarity
Cross-link118Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable

Experimental info

Sequence conflict771R → C AA sequence Ref.1

Secondary structure

........... 123
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02283 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0774D25F34003062

FASTA12313,696
        10         20         30         40         50         60 
MPPKTSGKAA KKAGKAQKNI TKTDKKKKRK RKESYAIYIY KVLKQVHPDT GISSKAMSIM 

        70         80         90        100        110        120 
NSFVNDIFER IAAEASRLAH YNKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT 


SSK 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of histone 2B of Drosophila melanogaster."
Elgin S.C.R., Schilling J., Hood L.E.
Biochemistry 18:5679-5685(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE (HIS2B).
[2]"tRNA derived insertion element in histone gene repeating unit of Drosophila melanogaster."
Matsuo Y., Yamazaki T.
Nucleic Acids Res. 17:225-238(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2B).
Strain: AK-194.
[3]"The genome sequence of Drosophila melanogaster."
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. expand/collapse author list , 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.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS2B:CG17949).
Strain: Berkeley.
[4]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[5]Goldberg M.L.
Thesis (1979), University of Stanford, United States
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-118 (HIS2B).
[6]"Methylation of Drosophila histones at proline, lysine, and arginine residues during heat shock."
Desrosiers R., Tanguay R.M.
J. Biol. Chem. 263:4686-4692(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT PRO-2.
[7]"TAF1 activates transcription by phosphorylation of serine 33 in histone H2B."
Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.
Science 304:1010-1014(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-34.
[8]"Bre1 is required for Notch signaling and histone modification."
Bray S., Musisi H., Bienz M.
Dev. Cell 8:279-286(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE UBIQUITINATION.
[9]"GlcNAcylation of histone H2B facilitates its monoubiquitination."
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.
Nature 480:557-560(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14215 Genomic DNA. Translation: CAA32432.1.
AE014134 Genomic DNA. Translation: AAN11124.1.
AE014134 Genomic DNA. Translation: AAZ66483.1.
AE014134 Genomic DNA. Translation: AAZ66487.1.
AE014134 Genomic DNA. Translation: AAZ66492.1.
AE014134 Genomic DNA. Translation: AAZ66496.1.
AE014134 Genomic DNA. Translation: AAZ66501.1.
AE014134 Genomic DNA. Translation: AAZ66506.1.
AE014134 Genomic DNA. Translation: AAZ66511.1.
AE014134 Genomic DNA. Translation: AAZ66521.1.
AE014134 Genomic DNA. Translation: AAZ66531.1.
AE014134 Genomic DNA. Translation: AAZ66576.1.
AE014134 Genomic DNA. Translation: AAZ66571.1.
AE014134 Genomic DNA. Translation: AAZ66566.1.
AE014134 Genomic DNA. Translation: AAZ66561.1.
AE014134 Genomic DNA. Translation: AAZ66556.1.
AE014134 Genomic DNA. Translation: AAZ66551.1.
AE014134 Genomic DNA. Translation: AAZ66546.1.
AE014134 Genomic DNA. Translation: AAZ66541.1.
AE014134 Genomic DNA. Translation: AAZ66536.1.
AE014134 Genomic DNA. Translation: AAZ66479.1.
AE014134 Genomic DNA. Translation: AAZ66581.1.
AE014134 Genomic DNA. Translation: AAZ66526.1.
AE014134 Genomic DNA. Translation: AAZ66516.1.
PIRHSFF22. S10095.
RefSeqNP_001027283.1. NM_001032112.1.
NP_001027287.1. NM_001032116.1.
NP_001027291.1. NM_001032120.1.
NP_001027296.1. NM_001032125.1.
NP_001027300.1. NM_001032129.1.
NP_001027305.1. NM_001032134.1.
NP_001027310.1. NM_001032139.1.
NP_001027315.1. NM_001032144.1.
NP_001027320.1. NM_001032149.1.
NP_001027325.1. NM_001032154.1.
NP_001027330.1. NM_001032159.1.
NP_001027335.1. NM_001032164.1.
NP_001027340.1. NM_001032169.1.
NP_001027345.1. NM_001032174.1.
NP_001027350.1. NM_001032179.1.
NP_001027355.1. NM_001032184.1.
NP_001027360.1. NM_001032189.1.
NP_001027365.1. NM_001032194.1.
NP_001027370.1. NM_001032199.1.
NP_001027375.1. NM_001032204.1.
NP_001027380.1. NM_001032209.1.
NP_001027385.1. NM_001032214.1.
NP_724342.1. NM_165381.3.
UniGeneDm.29523.
Dm.30218.
Dm.30222.
Dm.30875.
Dm.30877.
Dm.30878.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2NQBX-ray2.30D/H2-123[»]
2PYOX-ray2.43D/H2-123[»]
4INMX-ray3.50D/H/N/R33-122[»]
ProteinModelPortalP02283.
SMRP02283. Positions 4-123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid533862. 1 interaction.
77520. 6 interactions.
DIPDIP-22804N.
IntActP02283. 7 interactions.
MINTMINT-1560639.

Proteomic databases

PaxDbP02283.
PRIDEP02283.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0085927; FBpp0085281; FBgn0061209.
FBtr0091872; FBpp0091113; FBgn0053868.
FBtr0091874; FBpp0091115; FBgn0053870.
FBtr0091876; FBpp0091117; FBgn0053872.
FBtr0091878; FBpp0091119; FBgn0053874.
FBtr0091880; FBpp0091121; FBgn0053876.
FBtr0091882; FBpp0091123; FBgn0053878.
FBtr0091884; FBpp0091125; FBgn0053880.
FBtr0091886; FBpp0091127; FBgn0053882.
FBtr0091888; FBpp0091129; FBgn0053884.
FBtr0091890; FBpp0091131; FBgn0053886.
FBtr0091892; FBpp0091133; FBgn0053888.
FBtr0091894; FBpp0091135; FBgn0053890.
FBtr0091896; FBpp0091137; FBgn0053892.
FBtr0091898; FBpp0091139; FBgn0053894.
FBtr0091900; FBpp0091141; FBgn0053896.
FBtr0091902; FBpp0091143; FBgn0053898.
FBtr0091904; FBpp0091145; FBgn0053900.
FBtr0091906; FBpp0091147; FBgn0053902.
FBtr0091908; FBpp0091149; FBgn0053904.
FBtr0091910; FBpp0091151; FBgn0053906.
FBtr0091912; FBpp0091153; FBgn0053908.
FBtr0091914; FBpp0091155; FBgn0053910.
GeneID326273.
3771809.
3771891.
3771957.
3772013.
3772058.
3772081.
3772083.
3772094.
3772099.
3772104.
3772166.
3772203.
3772248.
3772264.
3772265.
3772271.
3772276.
3772299.
3772336.
3772496.
3772502.
3772575.
KEGGdme:Dmel_CG17949.
dme:Dmel_CG33868.
dme:Dmel_CG33870.
dme:Dmel_CG33872.
dme:Dmel_CG33874.
dme:Dmel_CG33876.
dme:Dmel_CG33878.
dme:Dmel_CG33880.
dme:Dmel_CG33882.
dme:Dmel_CG33884.
dme:Dmel_CG33886.
dme:Dmel_CG33888.
dme:Dmel_CG33890.
dme:Dmel_CG33892.
dme:Dmel_CG33894.
dme:Dmel_CG33896.
dme:Dmel_CG33898.
dme:Dmel_CG33900.
dme:Dmel_CG33902.
dme:Dmel_CG33904.
dme:Dmel_CG33906.
dme:Dmel_CG33908.
dme:Dmel_CG33910.
UCSCCG17949-RA. d. melanogaster.

Organism-specific databases

CTD326273.
3771809.
3771891.
3771957.
3772013.
3772058.
3772081.
3772083.
3772094.
3772099.
3772104.
3772166.
3772203.
3772248.
3772264.
3772265.
3772271.
3772276.
3772299.
3772336.
3772496.
3772502.
3772575.
FlyBaseFBgn0001198. His2B.
FBgn0061209. His2B:CG17949.
FBgn0053868. His2B:CG33868.
FBgn0053870. His2B:CG33870.
FBgn0053872. His2B:CG33872.
FBgn0053874. His2B:CG33874.
FBgn0053876. His2B:CG33876.
FBgn0053878. His2B:CG33878.
FBgn0053880. His2B:CG33880.
FBgn0053882. His2B:CG33882.
FBgn0053884. His2B:CG33884.
FBgn0053886. His2B:CG33886.
FBgn0053888. His2B:CG33888.
FBgn0053890. His2B:CG33890.
FBgn0053892. His2B:CG33892.
FBgn0053894. His2B:CG33894.
FBgn0053896. His2B:CG33896.
FBgn0053898. His2B:CG33898.
FBgn0053900. His2B:CG33900.
FBgn0053902. His2B:CG33902.
FBgn0053904. His2B:CG33904.
FBgn0053906. His2B:CG33906.
FBgn0053908. His2B:CG33908.
FBgn0053910. His2B:CG33910.

Phylogenomic databases

eggNOGNOG289161.
GeneTreeENSGT00730000110319.
InParanoidP02283.
KOK11252.
OMADCIVEPE.
OrthoDBEOG72VH8J.
PhylomeDBP02283.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERPTHR23428. PTHR23428. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMSSF47113. SSF47113. 1 hit.
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02283.
NextBio847933.
PROP02283.

Entry information

Entry nameH2B_DROME
AccessionPrimary (citable) accession number: P02283
Secondary accession number(s): Q4ABE1, Q9W5U7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase