A0A0U1Z3U1 · A0A0U1Z3U1_SINCH
- ProteinHeat shock protein 90beta
- GeneHSP90beta
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids725 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 41 | ATP (UniProtKB | ChEBI) | |||
Binding site | 45 | ATP (UniProtKB | ChEBI) | |||
Binding site | 87 | ATP (UniProtKB | ChEBI) | |||
Binding site | 92 | ATP (UniProtKB | ChEBI) | |||
Binding site | 100 | ATP (UniProtKB | ChEBI) | |||
Binding site | 106 | ATP (UniProtKB | ChEBI) | |||
Binding site | 107-108 | ATP (UniProtKB | ChEBI) | |||
Binding site | 127-132 | ATP (UniProtKB | ChEBI) | |||
Binding site | 178 | ATP (UniProtKB | ChEBI) | |||
Binding site | 390 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | dynein axonemal particle | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Cellular Component | protein-containing complex | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | disordered domain specific binding | |
Molecular Function | unfolded protein binding | |
Biological Process | cellular response to heat | |
Biological Process | protein stabilization |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Neoteleostei > Acanthomorphata > Eupercaria > Centrarchiformes > Centrarchoidei > Sinipercidae > Siniperca
Accessions
- Primary accessionA0A0U1Z3U1
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 34-188 | Histidine kinase/HSP90-like ATPase | |||
Region | 221-268 | Disordered | |||
Compositional bias | 238-268 | Basic and acidic residues | |||
Region | 695-725 | Disordered | |||
Compositional bias | 709-725 | Acidic residues | |||
Sequence similarities
Belongs to the heat shock protein 90 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length725
- Mass (Da)83,298
- Last updated2016-03-16 v1
- Checksum3144DF872499FFD2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 238-268 | Basic and acidic residues | |||
Compositional bias | 709-725 | Acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KM189831 EMBL· GenBank· DDBJ | AJP74821.1 EMBL· GenBank· DDBJ | mRNA | ||
KP218256 EMBL· GenBank· DDBJ | AJP74823.1 EMBL· GenBank· DDBJ | Genomic DNA |