A0A7R7VEP2 · A0A7R7VEP2_ASPCH
- ProteinSerine/threonine-protein kinase ATG1
- GeneATG1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids953 (go to sequence)
- Protein existencePredicted
- Annotation score4/5
Function
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 52 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | autophagosome | |
Cellular Component | cytosol | |
Cellular Component | phagophore assembly site membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | autophagosome assembly | |
Biological Process | autophagy of mitochondrion | |
Biological Process | peptidyl-serine phosphorylation | |
Biological Process | piecemeal microautophagy of the nucleus | |
Biological Process | protein autophosphorylation | |
Biological Process | protein transport | |
Biological Process | regulation of autophagy | |
Biological Process | response to starvation | |
Biological Process | reticulophagy |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase ATG1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Aspergillus
Accessions
- Primary accessionA0A7R7VEP2
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Preautophagosomal structure membrane ; Peripheral membrane protein
Interaction
Subunit
Homodimer. Forms a ternary complex with ATG13 and ATG17.
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-20 | Disordered | |||
Domain | 23-328 | Protein kinase | |||
Region | 338-485 | Disordered | |||
Compositional bias | 360-374 | Polar residues | |||
Compositional bias | 385-400 | Polar residues | |||
Compositional bias | 428-446 | Pro residues | |||
Region | 517-581 | Disordered | |||
Compositional bias | 524-546 | Polar residues | |||
Region | 930-953 | Disordered | |||
Family and domain databases
Sequence
- Sequence statusComplete
- Length953
- Mass (Da)103,831
- Last updated2021-06-02 v1
- MD5 Checksum018661CC8AE348B7C719681509AA1DC6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 360-374 | Polar residues | |||
Compositional bias | 385-400 | Polar residues | |||
Compositional bias | 428-446 | Pro residues | |||
Compositional bias | 524-546 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP024416 EMBL· GenBank· DDBJ | BCR83231.1 EMBL· GenBank· DDBJ | Genomic DNA |