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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: -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

Miscellaneous

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

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

Keywordsi

Molecular functionChaperone
Biological processStress 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

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
PaxDbiQ12449
PRIDEiQ12449

PTM databases

CarbonylDBiQ12449
iPTMnetiQ12449

Expressioni

Inductioni

By heat shock.1 Publication

Interactioni

Subunit structurei

Monomer. Interacts with HSP82.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • chaperone binding Source: SGD

Protein-protein interaction databases

BioGridi32268112 interactors.
DIPiDIP-1831N
IntActiQ12449 64 interactors.
MINTiQ12449
STRINGi4932.YDR214W

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
OMAiEYYVRSI
OrthoDBiEOG092C4FB3

Family and domain databases

Gene3Di3.15.10.201 hit
3.30.530.201 hit
InterProiView protein in InterPro
IPR013538 Activator_of_Hsp90_ATPase
IPR036338 Aha1
IPR015310 AHSA1_N
IPR023393 START-like_dom_sf
PfamiView protein in Pfam
PF09229 Aha1_N, 1 hit
PF08327 AHSA1, 1 hit
SMARTiView protein in SMART
SM01000 Aha1_N, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiAHA1_YEAST
AccessioniPrimary (citable) accession number: Q12449
Secondary accession number(s): D6VSJ8, Q02565, Q7LIE3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: March 28, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome