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Q12449

- AHA1_YEAST

UniProt

Q12449 - AHA1_YEAST

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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: 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

  1. ATPase activator activity Source: UniProtKB
  2. chaperone binding Source: SGD

GO - Biological processi

  1. cellular response to heat Source: SGD
  2. positive regulation of ATPase activity Source: GOC
  3. 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
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR214w.
SGDiS000002622. AHA1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. 1 Publication
Mutagenesisi53 – 531D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. 1 Publication
Mutagenesisi59 – 591R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication
Mutagenesisi60 – 601K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication
Mutagenesisi62 – 621K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350Hsp90 co-chaperone AHA1PRO_0000215822Add
BLAST

Proteomic databases

MaxQBiQ12449.
PaxDbiQ12449.
PeptideAtlasiQ12449.

Expressioni

Inductioni

By heat shock.1 Publication

Gene expression databases

GenevestigatoriQ12449.

Interactioni

Subunit structurei

Monomer. Interacts with HSP82.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi32268. 86 interactions.
DIPiDIP-1831N.
IntActiQ12449. 37 interactions.
MINTiMINT-401882.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 2812Combined sources
Beta strandi32 – 343Combined sources
Beta strandi41 – 444Combined sources
Beta strandi49 – 535Combined sources
Beta strandi55 – 573Combined sources
Beta strandi68 – 7811Combined sources
Beta strandi82 – 854Combined sources
Beta strandi88 – 9912Combined sources
Helixi104 – 1063Combined sources
Beta strandi110 – 1134Combined sources
Helixi123 – 1308Combined sources
Helixi132 – 15019Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1USUX-ray2.15B1-156[»]
1USVX-ray2.70B/D/F/H1-156[»]
ProteinModelPortaliQ12449.
SMRiQ12449. Positions 9-153, 213-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ12449.

Family & Domainsi

Sequence similaritiesi

Belongs to the AHA1 family.Curated

Phylogenomic databases

eggNOGiCOG5580.
GeneTreeiENSGT00390000006429.
HOGENOMiHOG000191277.
OMAiPEVSHEN.
OrthoDBiEOG7Q5HQC.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281L → I(PubMed:14739935)Curated

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 .
PIRi S61581.
RefSeqi NP_010500.3. NM_001180522.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1USU X-ray 2.15 B 1-156 [» ]
1USV X-ray 2.70 B/D/F/H 1-156 [» ]
ProteinModelPortali Q12449.
SMRi Q12449. Positions 9-153, 213-348.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32268. 86 interactions.
DIPi DIP-1831N.
IntActi Q12449. 37 interactions.
MINTi MINT-401882.

Proteomic databases

MaxQBi Q12449.
PaxDbi Q12449.
PeptideAtlasi Q12449.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR214W ; YDR214W ; YDR214W .
GeneIDi 851800.
KEGGi sce:YDR214W.

Organism-specific databases

CYGDi YDR214w.
SGDi S000002622. AHA1.

Phylogenomic databases

eggNOGi COG5580.
GeneTreei ENSGT00390000006429.
HOGENOMi HOG000191277.
OMAi PEVSHEN.
OrthoDBi EOG7Q5HQC.

Enzyme and pathway databases

BioCyci YEAST:G3O-29796-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q12449.
NextBioi 969638.
PROi Q12449.

Gene expression databases

Genevestigatori Q12449.

Family and domain databases

Gene3Di 3.30.530.20. 1 hit.
InterProi IPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view ]
Pfami PF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view ]
SMARTi SM01000. Aha1_N. 1 hit.
[Graphical view ]
SUPFAMi SSF103111. SSF103111. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Sequence homology of the yeast regulatory protein ADR1 with Xenopus transcription factor TFIIIA."
    Hartshorne T.A., Blumberg H., Young E.T.
    Nature 320:283-287(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350.
  5. Cited for: FUNCTION, INDUCTION, INTERACTION WITH HSP82.
  6. "Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone."
    Lotz G.P., Lin H., Harst A., Obermann W.M.J.
    J. Biol. Chem. 278:17228-17235(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP82.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery."
    Meyer P.
    EMBO J. 23:511-519(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-156 IN COMPLEX WITH HSP82, MUTAGENESIS OF ASP-53; ARG-59; LYS-60 AND LYS-62.

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 26, 2014
This is version 112 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

External Data

Dasty 3