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Protein

Histone H2B type 2-B

Gene

Hist2h2bb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type 2-B
Alternative name(s):
H2b 616
Gene namesi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2448413. Hist2h2bb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002448352 – 126Histone H2B type 2-BAdd BLAST125

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylprolineCombined sources1
Modified residuei6N6-acetyllysine; alternateCombined sources1
Modified residuei6N6-crotonyllysine; alternate1 Publication1
Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei12N6-acetyllysine; alternateCombined sources1
Modified residuei12N6-crotonyllysine; alternate1 Publication1
Modified residuei13N6-acetyllysine; alternateBy similarity1
Modified residuei13N6-crotonyllysine; alternate1 Publication1
Modified residuei15Phosphoserine; by STK4/MST12 Publications1
Modified residuei16N6-acetyllysine; alternateBy similarity1
Modified residuei16N6-crotonyllysine; alternate1 Publication1
Modified residuei17N6-acetyllysine; alternateCombined sources1
Modified residuei17N6-crotonyllysine; alternate1 Publication1
Modified residuei21N6-acetyllysine; alternateCombined sources1
Modified residuei21N6-crotonyllysine; alternate1 Publication1
Modified residuei24N6-acetyllysine; alternateBy similarity1
Modified residuei24N6-crotonyllysine; alternate1 Publication1
Modified residuei35N6-crotonyllysine; alternate1 Publication1
Cross-linki35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei37Phosphoserine; by AMPK1 Publication1
Modified residuei47N6-methyllysineBy similarity1
Modified residuei58N6,N6-dimethyllysineBy similarity1
Modified residuei80Dimethylated arginineBy similarity1
Modified residuei86N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei86N6-acetyllysine; alternateBy similarity1
Modified residuei87Omega-N-methylarginineBy similarity1
Modified residuei93Omega-N-methylarginineBy similarity1
Modified residuei109N6-methyllysineBy similarity1
Modified residuei116PhosphothreonineBy similarity1
Modified residuei117N6-methylated lysineBy similarity1
Cross-linki121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity).By similarity
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination. Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription.3 Publications
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ64525.
PaxDbiQ64525.
PeptideAtlasiQ64525.
PRIDEiQ64525.
TopDownProteomicsiQ64525.

PTM databases

iPTMnetiQ64525.
PhosphoSitePlusiQ64525.

Expressioni

Gene expression databases

BgeeiENSMUSG00000050936.

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.

Protein-protein interaction databases

BioGridi235108. 8 interactors.
IntActiQ64525. 1 interactor.
STRINGi10090.ENSMUSP00000135427.

Structurei

3D structure databases

ProteinModelPortaliQ64525.
SMRiQ64525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00860000133714.
HOVERGENiHBG007774.
InParanoidiQ64525.
KOiK11252.
OMAiNSERWAV.
OrthoDBiEOG091G0XGD.
TreeFamiTF300212.

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.

Q64525-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDPAKSAPA PKKGSKKAVT KVQKKDGKKR KRSRKESYSV YVYKVLKQVH
60 70 80 90 100
PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR
110 120
LLLPGELAKH AVSEGTKAVT KYTSSK
Length:126
Mass (Da):13,920
Last modified:January 23, 2007 - v3
Checksum:iE951DF3D7E97C106
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62675 Genomic DNA. Translation: AAB04773.1.
AK134918 mRNA. No translation available.
CCDSiCCDS57243.1.
RefSeqiNP_783597.2. NM_175666.2.
UniGeneiMm.297655.
Mm.451071.

Genome annotation databases

EnsembliENSMUST00000177113; ENSMUSP00000135427; ENSMUSG00000105827.
GeneIDi319189.
KEGGimmu:319189.
UCSCiuc008qmp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62675 Genomic DNA. Translation: AAB04773.1.
AK134918 mRNA. No translation available.
CCDSiCCDS57243.1.
RefSeqiNP_783597.2. NM_175666.2.
UniGeneiMm.297655.
Mm.451071.

3D structure databases

ProteinModelPortaliQ64525.
SMRiQ64525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi235108. 8 interactors.
IntActiQ64525. 1 interactor.
STRINGi10090.ENSMUSP00000135427.

PTM databases

iPTMnetiQ64525.
PhosphoSitePlusiQ64525.

Proteomic databases

MaxQBiQ64525.
PaxDbiQ64525.
PeptideAtlasiQ64525.
PRIDEiQ64525.
TopDownProteomicsiQ64525.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000177113; ENSMUSP00000135427; ENSMUSG00000105827.
GeneIDi319189.
KEGGimmu:319189.
UCSCiuc008qmp.1. mouse.

Organism-specific databases

CTDi338391.
MGIiMGI:2448413. Hist2h2bb.

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
GeneTreeiENSGT00860000133714.
HOVERGENiHBG007774.
InParanoidiQ64525.
KOiK11252.
OMAiNSERWAV.
OrthoDBiEOG091G0XGD.
TreeFamiTF300212.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.
R-MMU-3214847. HATs acetylate histones.
R-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
R-MMU-427413. NoRC negatively regulates rRNA expression.
R-MMU-5334118. DNA methylation.
R-MMU-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-MMU-573389. NoRC negatively regulates rRNA expression.
R-MMU-912497. Meiotic Recombination.

Miscellaneous databases

PROiQ64525.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000050936.

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 nameiH2B2B_MOUSE
AccessioniPrimary (citable) accession number: Q64525
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.