P62808 · H2B1_BOVIN

  • Protein
    Histone H2B type 1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleosome
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular Functionprotein heterodimerization activity
Molecular Functionstructural constituent of chromatin

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Histone H2B type 1

Organism names

  • Taxonomic identifier
  • Strains
    • Crossbred X Angus
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P62808
  • Secondary accessions
    • A1L599
    • A5PJG5
    • P02278
    • Q32PE8

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, cross-link, glycosylation.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylproline
ChainPRO_00000718252-126Histone H2B type 1
Modified residue3ADP-ribosyl glutamic acid
Modified residue6N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue6N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue6N6-acetyllysine; alternate
Modified residue6N6-butyryllysine; alternate
Modified residue6N6-crotonyllysine; alternate
Modified residue6N6-lactoyllysine; alternate
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue7ADP-ribosylserine
Modified residue12N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue12N6-acetyllysine; alternate
Modified residue12N6-crotonyllysine; alternate
Modified residue12N6-lactoyllysine; alternate
Modified residue13N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue13N6-acetyllysine; alternate
Modified residue13N6-crotonyllysine; alternate
Modified residue15Phosphoserine; by STK4/MST1
Modified residue16N6-acetyllysine; alternate
Modified residue16N6-crotonyllysine; alternate
Modified residue16N6-lactoyllysine; alternate
Modified residue17N6-acetyllysine; alternate
Modified residue17N6-crotonyllysine; alternate
Modified residue17N6-glutaryllysine; alternate
Modified residue17N6-lactoyllysine; alternate
Modified residue21N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue21N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue21N6-acetyllysine; alternate
Modified residue21N6-butyryllysine; alternate
Modified residue21N6-crotonyllysine; alternate
Modified residue21N6-lactoyllysine; alternate
Cross-link21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Modified residue24N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue24N6-acetyllysine; alternate
Modified residue24N6-crotonyllysine; alternate
Modified residue24N6-lactoyllysine; alternate
Modified residue25N6-(2-hydroxyisobutyryl)lysine
Modified residue35N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue35N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue35N6-crotonyllysine; alternate
Modified residue35N6-glutaryllysine; alternate
Modified residue35N6-succinyllysine; alternate
Cross-link35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residue36PolyADP-ribosyl glutamic acid
Modified residue37Phosphoserine; by AMPK
Modified residue44N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue44N6-glutaryllysine; alternate
Modified residue44N6-lactoyllysine; alternate
Modified residue47N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue47N6-glutaryllysine; alternate
Modified residue47N6-methyllysine; alternate
Modified residue58N6,N6-dimethyllysine; alternate
Modified residue58N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue80Dimethylated arginine
Modified residue86N6,N6,N6-trimethyllysine; alternate
Modified residue86N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue86N6-acetyllysine; alternate
Modified residue86N6-lactoyllysine; alternate
Modified residue87Omega-N-methylarginine
Modified residue93Omega-N-methylarginine
Modified residue109N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue109N6-glutaryllysine; alternate
Modified residue109N6-lactoyllysine; alternate
Modified residue109N6-methyllysine; alternate
Glycosylation113O-linked (GlcNAc) serine
Modified residue116Phosphothreonine
Modified residue117N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue117N6-(beta-hydroxybutyryl)lysine; alternate
Modified residue117N6-glutaryllysine; alternate
Modified residue117N6-lactoyllysine; alternate
Modified residue117N6-methylated lysine; alternate
Modified residue117N6-succinyllysine; alternate
Modified residue121N6-(2-hydroxyisobutyryl)lysine; alternate
Modified residue121N6-glutaryllysine; alternate
Modified residue121N6-lactoyllysine; alternate
Modified residue121N6-succinyllysine; alternate
Cross-link121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate

Post-translational modification

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).
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 (By similarity).
GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).
ADP-ribosylated by PARP1 or PARP2 on Ser-7 (H2BS6ADPr) in response to DNA damage (By similarity).
H2BS6ADPr promotes recruitment of CHD1L (By similarity).
Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in response to single-strand breaks (By similarity).
Poly ADP-ribosylation on Glu-36 (H2BE35ADPr) by PARP1 regulates adipogenesis: it inhibits phosphorylation at Ser-37 (H2BS36ph), thereby blocking expression of pro-adipogenetic genes (By similarity).
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 (By similarity).
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

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

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-36Disordered
Compositional bias17-35Basic residues

Sequence similarities

Belongs to the histone H2B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    126
  • Mass (Da)
    13,906
  • Last updated
    2007-01-23 v2
  • Checksum
    FAE1479F44BE703D
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAA9T057A0AAA9T057_BOVINH2BC7131

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias17-35Basic residues
Sequence conflict21in Ref. 4; AA sequence

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BT029886
EMBL· GenBank· DDBJ
ABM06136.1
EMBL· GenBank· DDBJ
mRNA
BC108143
EMBL· GenBank· DDBJ
AAI08144.1
EMBL· GenBank· DDBJ
mRNA
BC142102
EMBL· GenBank· DDBJ
AAI42103.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp