P0C5Y9 · H2AB1_HUMAN
- ProteinHistone H2A-Bbd type 1
- GeneH2AB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids115 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing (PubMed:22795134).
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 (PubMed:15257289, PubMed:16287874, PubMed:16957777, PubMed:17591702, PubMed:17726088, PubMed:18329190, PubMed:22795134).
Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo (PubMed:15257289, PubMed:16957777, PubMed:17591702, PubMed:24336483).
They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase (PubMed:17591702, PubMed:24753410).
They associate with spliceosome components and are required for mRNA splicing (PubMed:22795134).
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 (PubMed:15257289, PubMed:16287874, PubMed:16957777, PubMed:17591702, PubMed:17726088, PubMed:18329190, PubMed:22795134).
Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo (PubMed:15257289, PubMed:16957777, PubMed:17591702, PubMed:24336483).
They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase (PubMed:17591702, PubMed:24753410).
They associate with spliceosome components and are required for mRNA splicing (PubMed:22795134).
Miscellaneous
In contrast to other H2A histones, it does not contain the conserved residues that are the target of post-translational modifications.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | euchromatin | |
Cellular Component | nucleosome | |
Cellular Component | nucleus | |
Molecular Function | nucleosomal DNA binding | |
Molecular Function | protein heterodimerization activity | |
Molecular Function | structural constituent of chromatin | |
Biological Process | heterochromatin formation | |
Biological Process | mRNA processing | |
Biological Process | nucleosome assembly |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone H2A-Bbd type 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP0C5Y9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associated with the active X chromosome and with autosomes, while it is absent from the inactive X chromosome and excluded from Barr bodies.
Keywords
- Cellular component
Disease & Variants
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000312805 | 1-115 | Histone H2A-Bbd type 1 | |||
Sequence: MPRRRRRRGSSGAGGRGRTCSRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVPELAGNEAQNSGERNITPLLLDMVVHNDRLLSTLFNTTTISQVAPGED |
Proteomic databases
PTM 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. May be incorporated into a proportion of nucleosomes, replacing one or more H2A molecules.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-21 | Disordered | ||||
Sequence: MPRRRRRRGSSGAGGRGRTCS | ||||||
Region | 87-115 | Docking domain | ||||
Sequence: LLDMVVHNDRLLSTLFNTTTISQVAPGED |
Domain
The docking domain is responsible for the weaker heterodimerization with H2B.
Sequence similarities
Belongs to the histone H2A family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length115
- Mass (Da)12,697
- Last updated2007-12-04 v1
- Checksum57CA60C8C2F5744B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 109 | in Ref. 4; AAI28035 | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X86012 EMBL· GenBank· DDBJ | CAA59998.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR542230 EMBL· GenBank· DDBJ | CAG47026.1 EMBL· GenBank· DDBJ | mRNA | ||
BX842559 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC128034 EMBL· GenBank· DDBJ | AAI28035.1 EMBL· GenBank· DDBJ | mRNA |