Q99877 · H2B1N_HUMAN
- ProteinHistone H2B type 1-N
- GeneH2BC15
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids126 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | nucleosome assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H2B type 1-N
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99877
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 108 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data), glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylproline | ||||
Sequence: P | |||||||
Chain | PRO_0000071830 | 2-126 | UniProt | Histone H2B type 1-N | |||
Sequence: PEPSKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | |||||||
Modified residue | 3 | UniProt | ADP-ribosyl glutamic acid | ||||
Sequence: E | |||||||
Modified residue | 6 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-butyryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 6 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 6 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 7 | UniProt | ADP-ribosylserine | ||||
Sequence: S | |||||||
Modified residue | 12 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 12 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 12 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 12 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 13 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 13 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 13 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 15 | UniProt | Phosphoserine; by STK4/MST1 | ||||
Sequence: S | |||||||
Modified residue | 16 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 16 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 16 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 17 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 17 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 17 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 17 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 17 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-butyryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 21 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 21 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Modified residue | 24 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 24 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 24 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 24 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 25 | UniProt | N6-(2-hydroxyisobutyryl)lysine | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-crotonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 35 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 35 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue | 36 | UniProt | PolyADP-ribosyl glutamic acid | ||||
Sequence: E | |||||||
Modified residue | 37 | UniProt | Phosphoserine; by AMPK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 38 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 44 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 44 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 44 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 47 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 47 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 47 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 58 | UniProt | N6,N6-dimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 58 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 80 | UniProt | Dimethylated arginine | ||||
Sequence: R | |||||||
Modified residue | 86 | UniProt | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 86 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 86 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 86 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 86 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 87 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 93 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 109 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 109 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 109 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 109 | UniProt | N6-methyllysine; alternate | ||||
Sequence: K | |||||||
Glycosylation | 113 | UniProt | O-linked (GlcNAc) serine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 116 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 117 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-malonyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-methylated lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 117 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | N6-(2-hydroxyisobutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | N6-(beta-hydroxybutyryl)lysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | N6-glutaryllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | N6-lactoyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 121 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Cross-link | 121 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K |
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.
Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity).
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation (PubMed:12757711).
Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination
Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation (PubMed:12757711).
Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination
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 (PubMed:34874266).
H2BS6ADPr promotes recruitment of CHD1L (PubMed:34874266).
Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in response to single-strand breaks (PubMed:27530147).
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).
H2BS6ADPr promotes recruitment of CHD1L (PubMed:34874266).
Mono-ADP-ribosylated on Glu-3 (H2BE2ADPr) by PARP3 in response to single-strand breaks (PubMed:27530147).
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.
Lactylated in macrophages by EP300/P300 by using lactoyl-CoA directly derived from endogenous or exogenous lactate, leading to stimulates gene transcription.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MPEPSKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKE | ||||||
Compositional bias | 17-35 | Basic residues | ||||
Sequence: KAVTKAQKKDGKKRKRSRK |
Sequence similarities
Belongs to the histone H2B family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length126
- Mass (Da)13,922
- Last updated2007-01-23 v3
- ChecksumFAEB278D44BE702F
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
U3KQK0 | U3KQK0_HUMAN | H2BC15 | 166 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 17-35 | Basic residues | ||||
Sequence: KAVTKAQKKDGKKRKRSRK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z83336 EMBL· GenBank· DDBJ | CAB05938.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF531297 EMBL· GenBank· DDBJ | AAN06697.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK312228 EMBL· GenBank· DDBJ | BAG35161.1 EMBL· GenBank· DDBJ | mRNA | ||
Z98744 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX03114.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011372 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC101411 EMBL· GenBank· DDBJ | AAI01412.1 EMBL· GenBank· DDBJ | mRNA | ||
BC101412 EMBL· GenBank· DDBJ | AAI01413.1 EMBL· GenBank· DDBJ | mRNA | ||
BC101413 EMBL· GenBank· DDBJ | AAI01414.1 EMBL· GenBank· DDBJ | mRNA |