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Protein

Histone H2B 1.1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionDNA-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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000718542 – 126Histone H2B 1.1Add BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei15Phosphoserine1 Publication1
Modified residuei16N6-acetyllysineBy similarity1
Modified residuei21N6-acetyllysineBy similarity1
Glycosylationi113O-linked (GlcNAc) serineBy similarity1
Cross-linki121Glycyl 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

Binary interactionsi

WithEntry#Exp.IntActNotes
RCC1P187542EBI-1251201,EBI-992720From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi103448, 7 interactors
DIPiDIP-38577N
IntActiP02281, 7 interactors

Structurei

Secondary structure

1126
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP02281
SMRiP02281
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
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR007125 Histone_H2A/H2B/H3
IPR000558 Histone_H2B
PANTHERiPTHR23428 PTHR23428, 1 hit
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PRINTSiPR00621 HISTONEH2B
SMARTiView protein in SMART
SM00427 H2B, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00357 HISTONE_H2B, 1 hit

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

Similar proteinsi

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
PDB 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[»]
5CP6X-ray2.60D/H2-126[»]
5DNMX-ray2.81D/H2-126[»]
5DNNX-ray2.80D/H2-126[»]
5E5AX-ray2.81D/H5-126[»]
5F99X-ray2.63D/H5-126[»]
5G2EX-ray6.70D/H/L/P/T/X28-126[»]
5HQ2X-ray4.50H5-126[»]
5NL0X-ray5.40D/H/N5-126[»]
5O9Gelectron microscopy4.80D5-126[»]
H5-125[»]
5OMXX-ray2.32D/H5-126[»]
5ONGX-ray2.80D/H5-126[»]
5ONWX-ray2.80D/H5-126[»]
5OXVX-ray6.72D/H/N/R1-126[»]
5OY7X-ray5.77D/H/L/P/T/X/b/f1-126[»]
5X0Xelectron microscopy3.97D/H2-126[»]
5X0Yelectron microscopy3.97D/H5-126[»]
5XF6X-ray2.63D/H2-126[»]
6ESFelectron microscopy3.70D/H5-126[»]
6ESGelectron microscopy5.40D/H5-126[»]
6ESHelectron microscopy5.10D/H5-126[»]
6ESIelectron microscopy6.30D/H5-126[»]
ProteinModelPortaliP02281
SMRiP02281
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi103448, 7 interactors
DIPiDIP-38577N
IntActiP02281, 7 interactors

PTM databases

iPTMnetiP02281

Proteomic databases

PRIDEiP02281

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi446588
KEGGixla:446588

Organism-specific databases

CTDi446588
XenbaseiXB-GENE-6493994 hist1h2bj

Phylogenomic databases

HOVERGENiHBG007774
KOiK11252

Miscellaneous databases

EvolutionaryTraceiP02281

Family and domain databases

Gene3Di1.10.20.10, 1 hit
InterProiView protein in InterPro
IPR009072 Histone-fold
IPR007125 Histone_H2A/H2B/H3
IPR000558 Histone_H2B
PANTHERiPTHR23428 PTHR23428, 1 hit
PfamiView protein in Pfam
PF00125 Histone, 1 hit
PRINTSiPR00621 HISTONEH2B
SMARTiView protein in SMART
SM00427 H2B, 1 hit
SUPFAMiSSF47113 SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00357 HISTONE_H2B, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiH2B11_XENLA
AccessioniPrimary (citable) accession number: P02281
Secondary accession number(s): Q6AZT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 141 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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