O95433 · AHSA1_HUMAN
- ProteinActivator of 90 kDa heat shock protein ATPase homolog 1
- GeneAHSA1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids338 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Acts as a co-chaperone of HSP90AA1 (PubMed:29127155).
Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155).
Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360).
Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155).
Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360).
Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Molecular Function | ATPase activator activity | |
Molecular Function | cadherin binding | |
Molecular Function | Hsp90 protein binding | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | positive regulation of ATP-dependent activity | |
Biological Process | protein folding |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameActivator of 90 kDa heat shock protein ATPase homolog 1
- Short namesAHA1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95433
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: May transiently interact with the endoplasmic reticulum.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 223 | Phosphomimetic mutant. Increases the binding to HSP90AA1 resulting in TSC1 dissociation from HSP90AA1. | ||||
Sequence: Y → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 311 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000215820 | 1-338 | UniProt | Activator of 90 kDa heat shock protein ATPase homolog 1 | |||
Sequence: MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF | |||||||
Modified residue | 3 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 182 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 183 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 193 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 203 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 212 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 223 | UniProt | Phosphotyrosine; by ABL | ||||
Sequence: Y | |||||||
Modified residue | 258 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1.
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Expressed in numerous tissues, including brain, heart, skeletal muscle and kidney and, at lower levels, liver and placenta.
Induction
By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with HSPCA/HSP90 (PubMed:12504007, PubMed:12604615).
Interacts (phosphorylated on Tyr-223) with HSP90AA1; the interaction activates HSP90AA1 ATPase activity (PubMed:27353360, PubMed:29127155).
Interacts with HSP90AB1 (By similarity).
Interacts with GCH1 (PubMed:16696853).
Interacts with SRPK1 (PubMed:19240134).
Interacts with FLCN (PubMed:27353360).
Interacts (phosphorylated on Tyr-223) with HSP90AA1; the interaction activates HSP90AA1 ATPase activity (PubMed:27353360, PubMed:29127155).
Interacts with HSP90AB1 (By similarity).
Interacts with GCH1 (PubMed:16696853).
Interacts with SRPK1 (PubMed:19240134).
Interacts with FLCN (PubMed:27353360).
(Microbial infection) Interacts with vesicular stomatitis virus glycoprotein (VSV G) (via cytoplasmic tail).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95433 | GCH1 P30793 | 3 | EBI-448610, EBI-958183 | |
BINARY | O95433 | HSP90AA1 P07900 | 6 | EBI-448610, EBI-296047 | |
BINARY | O95433 | HSP90AB1 P08238 | 5 | EBI-448610, EBI-352572 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O95433-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length338
- Mass (Da)38,274
- Last updated1999-05-01 v1
- ChecksumE6B686DDD8D7D729
O95433-2
- Name2
- Differences from canonical
- 283-338: HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF → SHCHSG
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 67-68 | in Ref. 7; AAF29000 | ||||
Sequence: EA → CL | ||||||
Alternative sequence | VSP_055797 | 283-338 | in isoform 2 | |||
Sequence: HFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF → SHCHSG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ243310 EMBL· GenBank· DDBJ | CAB45684.1 EMBL· GenBank· DDBJ | mRNA | ||
AF164791 EMBL· GenBank· DDBJ | AAF80755.1 EMBL· GenBank· DDBJ | mRNA | ||
AK300766 EMBL· GenBank· DDBJ | BAG62431.1 EMBL· GenBank· DDBJ | mRNA | ||
AK313824 EMBL· GenBank· DDBJ | BAG36559.1 EMBL· GenBank· DDBJ | mRNA | ||
AF111168 EMBL· GenBank· DDBJ | AAD09623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471061 EMBL· GenBank· DDBJ | EAW81291.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000321 EMBL· GenBank· DDBJ | AAH00321.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007398 EMBL· GenBank· DDBJ | AAH07398.2 EMBL· GenBank· DDBJ | mRNA | ||
AF161440 EMBL· GenBank· DDBJ | AAF29000.1 EMBL· GenBank· DDBJ | mRNA |