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Protein

Histone H2B 1.1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B 1.1
Short name:
H2B1.1
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6493994. hist1h2bj.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 126125Histone H2B 1.1PRO_0000071854Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61N6-acetyllysineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei21 – 211N6-acetyllysineBy similarity
Glycosylationi113 – 1131O-linked (GlcNAc)By similarity
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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.1 Publication
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP02281.

PTM databases

iPTMnetiP02281.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi103448. 5 interactions.
DIPiDIP-38577N.
IntActiP02281. 3 interactions.

Structurei

Secondary structure

1
126
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Beta strandi18 – 203Combined sources
Helixi39 – 4911Combined sources
Helixi57 – 8428Combined sources
Beta strandi88 – 903Combined sources
Helixi92 – 10211Combined sources
Helixi105 – 12319Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80D/H28-126[»]
1F66X-ray2.60D/H1-126[»]
1KX3X-ray2.00D/H2-126[»]
1KX4X-ray2.60D/H2-126[»]
1KX5X-ray1.94D/H2-126[»]
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/H2-126[»]
2F8NX-ray2.90H5-126[»]
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[»]
3REHX-ray2.50D/H5-126[»]
3REIX-ray2.65D/H5-126[»]
3REJX-ray2.55D/H5-126[»]
3REKX-ray2.60D/H5-126[»]
3RELX-ray2.70D/H5-126[»]
3TU4X-ray3.00D/H5-126[»]
3UT9X-ray2.20D/H2-126[»]
3UTAX-ray2.07D/H2-126[»]
3UTBX-ray2.20D/H2-126[»]
4J8UX-ray2.38D/H2-126[»]
4J8VX-ray2.58D/H2-126[»]
4J8WX-ray2.41D/H2-126[»]
4J8XX-ray2.87D/H2-126[»]
4KGCX-ray2.69D/H1-126[»]
4KHAX-ray2.35A34-126[»]
4LD9X-ray3.31D/H1-126[»]
4R8PX-ray3.28D/H5-126[»]
4WU8X-ray2.45D/H2-126[»]
4WU9X-ray2.60D/H2-126[»]
4XUJX-ray3.18D/H2-126[»]
4XZQX-ray2.40D/H34-126[»]
4YS3X-ray3.00D/H34-126[»]
4Z66X-ray2.50D/H34-126[»]
4ZUXX-ray3.82D/H/N/R5-126[»]
5E5AX-ray2.81D/H5-126[»]
5F99X-ray2.63D/H5-126[»]
5HQ2X-ray4.50H5-126[»]
ProteinModelPortaliP02281.
SMRiP02281. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02281.

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

HOVERGENiHBG007774.
KOiK11252.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02281-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPAKSAPA PKKGSKKAVT KTQKKDGKKR RKSRKESYAI YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM SIMNSFVNDV FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSAK
Length:126
Mass (Da):13,934
Last modified:January 23, 2007 - v2
Checksum:iDA6C122EC8359FD9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA. Translation: CAA26816.1.
M21287 Genomic DNA. Translation: AAA49768.1.
BC077399 mRNA. Translation: AAH77399.1.
PIRiB92918. HSXLB1.
RefSeqiNP_001086753.1. NM_001093284.1.
UniGeneiXl.46757.

Genome annotation databases

GeneIDi446588.
KEGGixla:446588.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA. Translation: CAA26816.1.
M21287 Genomic DNA. Translation: AAA49768.1.
BC077399 mRNA. Translation: AAH77399.1.
PIRiB92918. HSXLB1.
RefSeqiNP_001086753.1. NM_001093284.1.
UniGeneiXl.46757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80D/H28-126[»]
1F66X-ray2.60D/H1-126[»]
1KX3X-ray2.00D/H2-126[»]
1KX4X-ray2.60D/H2-126[»]
1KX5X-ray1.94D/H2-126[»]
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/H2-126[»]
2F8NX-ray2.90H5-126[»]
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[»]
3REHX-ray2.50D/H5-126[»]
3REIX-ray2.65D/H5-126[»]
3REJX-ray2.55D/H5-126[»]
3REKX-ray2.60D/H5-126[»]
3RELX-ray2.70D/H5-126[»]
3TU4X-ray3.00D/H5-126[»]
3UT9X-ray2.20D/H2-126[»]
3UTAX-ray2.07D/H2-126[»]
3UTBX-ray2.20D/H2-126[»]
4J8UX-ray2.38D/H2-126[»]
4J8VX-ray2.58D/H2-126[»]
4J8WX-ray2.41D/H2-126[»]
4J8XX-ray2.87D/H2-126[»]
4KGCX-ray2.69D/H1-126[»]
4KHAX-ray2.35A34-126[»]
4LD9X-ray3.31D/H1-126[»]
4R8PX-ray3.28D/H5-126[»]
4WU8X-ray2.45D/H2-126[»]
4WU9X-ray2.60D/H2-126[»]
4XUJX-ray3.18D/H2-126[»]
4XZQX-ray2.40D/H34-126[»]
4YS3X-ray3.00D/H34-126[»]
4Z66X-ray2.50D/H34-126[»]
4ZUXX-ray3.82D/H/N/R5-126[»]
5E5AX-ray2.81D/H5-126[»]
5F99X-ray2.63D/H5-126[»]
5HQ2X-ray4.50H5-126[»]
ProteinModelPortaliP02281.
SMRiP02281. Positions 5-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi103448. 5 interactions.
DIPiDIP-38577N.
IntActiP02281. 3 interactions.

PTM databases

iPTMnetiP02281.

Proteomic databases

PRIDEiP02281.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi446588.
KEGGixla:446588.

Organism-specific databases

CTDi8970.
XenbaseiXB-GENE-6493994. hist1h2bj.

Phylogenomic databases

HOVERGENiHBG007774.
KOiK11252.

Miscellaneous databases

EvolutionaryTraceiP02281.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH2B11_XENLA
AccessioniPrimary (citable) accession number: P02281
Secondary accession number(s): Q6AZT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.