A0A2K5CF62 · A0A2K5CF62_AOTNA
- ProteinEstablishment of sister chromatid cohesion N-acetyltransferase 2
- GeneESCO2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids692 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- L-lysyl-[protein] + acetyl-CoA = N6-acetyl-L-lysyl-[protein] + CoA + H+
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell junction | |
Cellular Component | chromocenter | |
Cellular Component | Golgi apparatus | |
Cellular Component | nucleoplasm | |
Cellular Component | pericentric heterochromatin | |
Cellular Component | site of double-strand break | |
Cellular Component | XY body | |
Molecular Function | lysine N-acetyltransferase activity, acting on acetyl phosphate as donor | |
Molecular Function | metal ion binding | |
Molecular Function | peptide-lysine-N-acetyltransferase activity | |
Biological Process | chromosome segregation | |
Biological Process | double-strand break repair | |
Biological Process | hematopoietic progenitor cell differentiation | |
Biological Process | mitotic sister chromatid cohesion | |
Biological Process | post-translational protein acetylation | |
Biological Process | protein localization to chromatin | |
Biological Process | regulation of DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Platyrrhini > Aotidae > Aotus
Accessions
- Primary accessionA0A2K5CF62
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 230-249 | Disordered | |||
Region | 388-420 | Disordered | |||
Compositional bias | 390-415 | Basic and acidic residues | |||
Domain | 478-517 | N-acetyltransferase ESCO zinc-finger | |||
Domain | 633-691 | N-acetyltransferase ESCO acetyl-transferase | |||
Sequence similarities
Belongs to the acetyltransferase family. ECO subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length692
- Mass (Da)78,123
- Last updated2018-03-28 v1
- MD5 ChecksumDC2EFE8FE7EE5DFE53A2ED20A4441781
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2K5CF58 | A0A2K5CF58_AOTNA | ESCO2 | 644 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 390-415 | Basic and acidic residues | |||
Keywords
- Technical term