A0A8D0GSZ9 · A0A8D0GSZ9_SPHPU
- ProteinEstablishment of sister chromatid cohesion N-acetyltransferase 2
- GeneESCO2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids537 (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 > Lepidosauria > Sphenodontia > Sphenodontidae > Sphenodon
Accessions
- Primary accessionA0A8D0GSZ9
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-89 | Disordered | ||||
Sequence: PVKTFPTQTKWASSSSDEDKENQDSPLKSSPSRKLDSSPVQTATVPMEAHREPPRKMSPKSGSPY | ||||||
Compositional bias | 52-68 | Polar residues | ||||
Sequence: KSSPSRKLDSSPVQTAT | ||||||
Region | 117-189 | Disordered | ||||
Sequence: IHPLGQRNSDGNLPSASRTDTPQVEVKPVGNTDSKAPKRRRDPRQTKTQPRNSKKAKMEMAPVAPALGKEHSS | ||||||
Compositional bias | 121-144 | Polar residues | ||||
Sequence: GQRNSDGNLPSASRTDTPQVEVKP | ||||||
Region | 230-262 | Disordered | ||||
Sequence: SKKELPSPVAPPPISRPAAKGDQPREAAAPGPP | ||||||
Domain | 304-339 | N-acetyltransferase ESCO zinc-finger | ||||
Sequence: DAGQKHFCPVMCKACGMIYSAANPEDEAQHIQHHQR | ||||||
Domain | 456-524 | N-acetyltransferase ESCO acetyl-transferase | ||||
Sequence: EPAICGVSRIWVLSLMRRKGIARRLVDVVRNTFIFGCYLSTEEIAFSDPTPDGKLFATKYCQTPNFLVY |
Sequence similarities
Belongs to the acetyltransferase family. ECO subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length537
- Mass (Da)60,197
- Last updated2022-01-19 v1
- Checksum82390E103F7C8F22
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-68 | Polar residues | ||||
Sequence: KSSPSRKLDSSPVQTAT | ||||||
Compositional bias | 121-144 | Polar residues | ||||
Sequence: GQRNSDGNLPSASRTDTPQVEVKP |
Keywords
- Technical term