Q00729 · H2B1A_RAT
- ProteinHistone H2B type 1-A
- GeneH2bc1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids127 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Variant histone specifically required to direct the transformation of dissociating nucleosomes to protamine in male germ cells. Entirely replaces classical histone H2B prior nucleosome to protamine transition and probably acts as a nucleosome dissociating factor that creates a more dynamic chromatin, facilitating the large-scale exchange of histones. 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 | cell surface | |
Cellular Component | female germ cell nucleus | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | DNA binding | |
Molecular Function | histone binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | chromatin organization | |
Biological Process | chromosome organization | |
Biological Process | inflammatory response | |
Biological Process | mononuclear cell migration | |
Biological Process | nucleosome assembly | |
Biological Process | nucleosome disassembly | |
Biological Process | plasminogen activation | |
Biological Process | sperm DNA condensation |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H2B type 1-A
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ00729
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylproline | ||||
Sequence: P | ||||||
Chain | PRO_0000071844 | 2-127 | Histone H2B type 1-A | |||
Sequence: PEVSAKGTTISKKGFKKAVTKTQKKEGRKRKRCRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | ||||||
Modified residue | 7 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 7 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 7 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 7 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 13 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 13 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 13 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 14 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 14 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 17 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 17 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 17 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 18 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 18 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 18 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 22 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 22 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 22 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 25 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 25 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 25 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 36 | N6-crotonyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 36 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 36 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | ||||||
Modified residue | 38 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 45 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 48 | N6-methyllysine | ||||
Sequence: K | ||||||
Modified residue | 59 | N6,N6-dimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 81 | Dimethylated arginine | ||||
Sequence: R | ||||||
Modified residue | 87 | N6,N6,N6-trimethyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 87 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 87 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 88 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 94 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 110 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 110 | N6-methyllysine | ||||
Sequence: K | ||||||
Modified residue | 117 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 118 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 118 | N6-methylated lysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 118 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-lactoyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 122 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 122 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K |
Post-translational modification
Monoubiquitination at Lys-36 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 of Lys-122 (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).
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).
Acetylated during spermatogenesis. Acetylated form is most abundant in spermatogonia compared to spermatocytes and round spermatids.
Phosphorylated at Thr-117 in spermatogonia, spermatocytes and round spermatids.
Methylated at Lys-118 in spermatogonia, spermatocytes and round spermatids.
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
Tissue specificity
Testis. Expressed in pachytene spermatocytes during meiotic prophase I in the absence of any significant DNA synthesis.
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.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-32 | Disordered | ||||
Sequence: MPEVSAKGTTISKKGFKKAVTKTQKKEGRKRK | ||||||
Compositional bias | 18-32 | Basic residues | ||||
Sequence: KAVTKTQKKEGRKRK |
Sequence similarities
Belongs to the histone H2B family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length127
- Mass (Da)14,225
- Last updated2007-01-23 v2
- Checksum14CE190F91769548
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2QBI8 | A0A8L2QBI8_RAT | H2bc1 | 139 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 18-32 | Basic residues | ||||
Sequence: KAVTKTQKKEGRKRK | ||||||
Sequence conflict | 36 | in Ref. 1; AAA74755/AAA74756 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M18045 EMBL· GenBank· DDBJ | AAA74755.1 EMBL· GenBank· DDBJ | mRNA | ||
M18046 EMBL· GenBank· DDBJ | AAA74756.1 EMBL· GenBank· DDBJ | mRNA | ||
X59962 EMBL· GenBank· DDBJ | CAA42587.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M25771 EMBL· GenBank· DDBJ | AAA74754.1 EMBL· GenBank· DDBJ | Genomic DNA |