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Protein

Hsp90 co-chaperone AHA1

Gene

AHA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.2 Publications

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • chaperone binding Source: SGD

GO - Biological processi

  • cellular response to heat Source: SGD
  • protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciYEAST:G3O-29796-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp90 co-chaperone AHA1
Alternative name(s):
Activator of Hsp90 ATPase protein 1
Gene namesi
Name:AHA1
Ordered Locus Names:YDR214W
ORF Names:YD8142.16, YD8142B.06
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR214W.
SGDiS000002622. AHA1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. 1 Publication1
Mutagenesisi53D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. 1 Publication1
Mutagenesisi59R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication1
Mutagenesisi60K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication1
Mutagenesisi62K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002158221 – 350Hsp90 co-chaperone AHA1Add BLAST350

Proteomic databases

MaxQBiQ12449.
PRIDEiQ12449.

PTM databases

iPTMnetiQ12449.

Expressioni

Inductioni

By heat shock.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with HSP82.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSC82P151083EBI-37072,EBI-8666
HSP82P028297EBI-37072,EBI-8659

GO - Molecular functioni

  • chaperone binding Source: SGD

Protein-protein interaction databases

BioGridi32268. 88 interactors.
DIPiDIP-1831N.
IntActiQ12449. 38 interactors.
MINTiMINT-401882.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 28Combined sources12
Beta strandi32 – 34Combined sources3
Beta strandi41 – 44Combined sources4
Beta strandi49 – 53Combined sources5
Beta strandi55 – 57Combined sources3
Beta strandi68 – 78Combined sources11
Beta strandi82 – 85Combined sources4
Beta strandi88 – 99Combined sources12
Helixi104 – 106Combined sources3
Beta strandi110 – 113Combined sources4
Helixi123 – 130Combined sources8
Helixi132 – 150Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1USUX-ray2.15B1-156[»]
1USVX-ray2.70B/D/F/H1-156[»]
ProteinModelPortaliQ12449.
SMRiQ12449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12449.

Family & Domainsi

Sequence similaritiesi

Belongs to the AHA1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000006429.
HOGENOMiHOG000191277.
OMAiVMKWRYN.
OrthoDBiEOG092C4FB3.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTiSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMiSSF103111. SSF103111. 1 hit.

Sequencei

Sequence statusi: Complete.

Q12449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI
60 70 80 90 100
EGDCEVNQRK GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF
110 120 130 140 150
DSEASSYQFD ISIFKETSEL SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH
160 170 180 190 200
GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS ASKPKKNALP SSTSTSAPVS
210 220 230 240 250
STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL AWTRSAQFFN
260 270 280 290 300
SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM
310 320 330 340 350
TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL
Length:350
Mass (Da):39,436
Last modified:November 1, 1996 - v1
Checksum:i06DF6B40EB5050BE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti28L → I (PubMed:14739935).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68194 Genomic DNA. Translation: CAA92357.1.
Z68195 Genomic DNA. Translation: CAA92365.1.
AY557694 Genomic DNA. Translation: AAS56020.1.
U28414 Genomic DNA. Translation: AAA73862.1.
BK006938 Genomic DNA. Translation: DAA12058.1.
PIRiS61581.
RefSeqiNP_010500.3. NM_001180522.3.

Genome annotation databases

EnsemblFungiiYDR214W; YDR214W; YDR214W.
GeneIDi851800.
KEGGisce:YDR214W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68194 Genomic DNA. Translation: CAA92357.1.
Z68195 Genomic DNA. Translation: CAA92365.1.
AY557694 Genomic DNA. Translation: AAS56020.1.
U28414 Genomic DNA. Translation: AAA73862.1.
BK006938 Genomic DNA. Translation: DAA12058.1.
PIRiS61581.
RefSeqiNP_010500.3. NM_001180522.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1USUX-ray2.15B1-156[»]
1USVX-ray2.70B/D/F/H1-156[»]
ProteinModelPortaliQ12449.
SMRiQ12449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32268. 88 interactors.
DIPiDIP-1831N.
IntActiQ12449. 38 interactors.
MINTiMINT-401882.

PTM databases

iPTMnetiQ12449.

Proteomic databases

MaxQBiQ12449.
PRIDEiQ12449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR214W; YDR214W; YDR214W.
GeneIDi851800.
KEGGisce:YDR214W.

Organism-specific databases

EuPathDBiFungiDB:YDR214W.
SGDiS000002622. AHA1.

Phylogenomic databases

GeneTreeiENSGT00390000006429.
HOGENOMiHOG000191277.
OMAiVMKWRYN.
OrthoDBiEOG092C4FB3.

Enzyme and pathway databases

BioCyciYEAST:G3O-29796-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ12449.
PROiQ12449.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamiPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTiSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMiSSF103111. SSF103111. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAHA1_YEAST
AccessioniPrimary (citable) accession number: Q12449
Secondary accession number(s): D6VSJ8, Q02565, Q7LIE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13939 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.