Skip Header

Contribute Send feedback
Read comments (?) or add your own

P02281 (H2B11_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 99. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H2B 1.1
Short name=H2B1.1
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Mesobatrachia › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length126 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. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus. Chromosome.

Post-translational modification

Monoubiquitination of Lys-121 by BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation By similarity.

Phosphorylated on Ser-15 during developmentally programmed apoptosis; which may facilitate apoptotic chromatin condensation. Ref.4

Sequence similarities

Belongs to the histone H2B family.

Ontologies

Keywords
   Cellular componentChromosome
Nucleosome core
Nucleus
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processnucleosome assembly

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleosome

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 126125Histone H2B 1.1
PRO_0000071854

Amino acid modifications

Modified residue61N6-acetyllysine By similarity
Modified residue131N6-acetyllysine By similarity
Modified residue151Phosphoserine Ref.4
Modified residue161N6-acetyllysine By similarity
Modified residue211N6-acetyllysine By similarity
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Secondary structure

1 ............... 126
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02281 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DA6C122EC8359FD9

FASTA12613,934
        10         20         30         40         50         60 
MPEPAKSAPA PKKGSKKAVT KTQKKDGKKR RKSRKESYAI YVYKVLKQVH PDTGISSKAM 

        70         80         90        100        110        120 
SIMNSFVNDV FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT 


KYTSAK

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization and nucleotide sequence of two distinct histone gene clusters from Xenopus laevis. Identification of novel conserved upstream sequence elements."
Perry M., Thomsen G.H., Roeder R.G.
J. Mol. Biol. 185:479-499(1985) [PubMed: 3863963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (GENE CLUSTER X1H3).
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Histone H2B variants from the erythrocytes of an amphibian, a reptile and a bird."
van Helden P., Strickland W.N., Brandt W.F., von Holt C.
Biochim. Biophys. Acta 533:278-281(1978) [PubMed: 638193] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-30 AND 63-85.
Tissue: Erythrocyte.
[4]"Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase."
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.
Cell 113:507-517(2003) [PubMed: 12757711] [Abstract]
Cited for: PHOSPHORYLATION AT SER-15.
[5]"Crystal structure of the nucleosome core particle at 2.8 A resolution."
Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J.
Nature 389:251-260(1997) [PubMed: 9305837] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, SUBUNIT.
[6]"Crystal structures of nucleosome core particles in complex with minor groove DNA-binding ligands."
Suto R.K., Edayathumangalam R.S., White C.L., Melander C., Gottesfeld J.M., Dervan P.B., Luger K.
J. Mol. Biol. 326:371-380(2003) [PubMed: 12559907] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, SUBUNIT.
[7]"Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions."
Muthurajan U.M., Bao Y., Forsberg L.J., Edayathumangalam R.S., Dyer P.N., White C.L., Luger K.
EMBO J. 23:260-271(2004) [PubMed: 14739929] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X03018 Genomic DNA. Translation: CAA26816.1.
M21287 Genomic DNA. Translation: AAA49768.1.
BC077399 mRNA. Translation: AAH77399.1.
PIRHSXLB1. B92918.
RefSeqNP_001086753.1. NM_001093284.1.
UniGeneXl.46757.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80D/H28-126[»]
1F66X-ray2.60D/H2-125[»]
1KX3X-ray2.00D/H2-125[»]
1KX4X-ray2.60D/H2-125[»]
1KX5X-ray1.94D/H2-125[»]
1M18X-ray2.45D/H2-126[»]
1M19X-ray2.30D/H2-126[»]
1M1AX-ray2.65D/H2-126[»]
1P34X-ray2.70D/H2-126[»]
1P3AX-ray3.00D/H2-126[»]
1P3BX-ray3.00D/H2-126[»]
1P3FX-ray2.90D/H2-126[»]
1P3GX-ray2.70D/H2-126[»]
1P3IX-ray2.30D/H2-126[»]
1P3KX-ray2.90D/H2-126[»]
1P3LX-ray2.40D/H2-126[»]
1P3MX-ray2.90D/H2-126[»]
1P3OX-ray2.75D/H2-126[»]
1P3PX-ray2.70D/H2-126[»]
1S32X-ray2.05D/H5-126[»]
1ZBBX-ray9.00D/H/d/h2-126[»]
1ZLAX-ray2.90D/H4-126[»]
2F8NX-ray2.90H5-125[»]
2FJ7X-ray3.20D/H2-126[»]
2NZDX-ray2.65D/H2-126[»]
3B6FX-ray3.45D/H2-126[»]
3B6GX-ray3.45D/H2-126[»]
3KUYX-ray2.90D/H2-126[»]
3KWQX-ray3.50D/H34-126[»]
3KXBX-ray3.20D/H5-126[»]
3LELX-ray2.95D/H/N/R2-126[»]
3LJAX-ray2.75D/H5-126[»]
3LZ0X-ray2.50D/H2-126[»]
3LZ1X-ray2.50D/H2-126[»]
3MGPX-ray2.44D/H2-126[»]
3MGQX-ray2.65D/H2-126[»]
3MGRX-ray2.30D/H2-126[»]
3MGSX-ray3.15D/H2-126[»]
3MNNX-ray2.50D/H2-126[»]
3MVDX-ray2.90D/H5-126[»]
3O62X-ray3.22D/H5-126[»]
3TU4X-ray3.00D/H5-126[»]
ProteinModelPortalP02281.
SMRP02281. Positions 5-126.
ModBaseSearch...

Protein-protein interaction databases

IntActP02281. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID446588.
KEGGxla:446588.

Organism-specific databases

CTD8970.
XenbaseXB-GENE-6493994. hist1h2bj.

Phylogenomic databases

HOVERGENHBG007774.

Family and domain databases

InterProIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000558. Histone_H2B.
[Graphical view]
Gene3DG3DSA:1.10.20.10. Histone-fold. 1 hit.
KOK11252.
PANTHERPTHR23428. Histone_H2B. 1 hit.
PfamPF00125. Histone. 1 hit.
[Graphical view]
PRINTSPR00621. HISTONEH2B.
SMARTSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMSSF47113. Histone-fold. 1 hit.
PROSITEPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameH2B11_XENLA
AccessionPrimary (citable) accession number: P02281
Secondary accession number(s): Q6AZT0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents