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Q12449 (AHA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hsp90 co-chaperone AHA1
Alternative name(s):
Activator of Hsp90 ATPase protein 1
Gene names
Name:AHA1
Ordered Locus Names:YDR214W
ORF Names:YD8142.16, YD8142B.06
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6

Subunit structure

Monomer. Interacts with HSP82. Ref.5 Ref.6

Subcellular location

Cytoplasm Ref.7.

Induction

By heat shock. Ref.5

Miscellaneous

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

Sequence similarities

Belongs to the AHA1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSC82P151083EBI-37072,EBI-8666
HSP82P028297EBI-37072,EBI-8659

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Hsp90 co-chaperone AHA1
PRO_0000215822

Experimental info

Mutagenesis531D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. Ref.11
Mutagenesis531D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. Ref.11
Mutagenesis591R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11
Mutagenesis601K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11
Mutagenesis621K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11
Sequence conflict281L → I Ref.11

Secondary structure

......................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12449 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 06DF6B40EB5050BE

FASTA35039,436
        10         20         30         40         50         60 
MVVNNPNNWH WVDKNCIGWA KEYFKQKLVG VEAGSVKDKK YAKIKSVSSI EGDCEVNQRK 

        70         80         90        100        110        120 
GKVISLFDLK ITVLIEGHVD SKDGSALPFE GSINVPEVAF DSEASSYQFD ISIFKETSEL 

       130        140        150        160        170        180 
SEAKPLIRSE LLPKLRQIFQ QFGKDLLATH GNDIQVPESQ VKSNYTRGNQ KSSFTEIKDS 

       190        200        210        220        230        240 
ASKPKKNALP SSTSTSAPVS STNKVPQNGS GNSTSIYLEP TFNVPSSELY ETFLDKQRIL 

       250        260        270        280        290        300 
AWTRSAQFFN SGPKLETKEK FELFGGNVIS ELVSCEKDKK LVFHWKLKDW SAPFNSTIEM 

       310        320        330        340        350 
TFHESQEFHE TKLQVKWTGI PVGEEDRVRA NFEEYYVRSI KLTFGFGAVL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
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]"Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1."
Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., Cramer R., Mollapour M., Workman P., Piper P.W., Pearl L.H., Prodromou C.
Mol. Cell 10:1307-1318(2002) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
[12]Erratum
Meyer P., Prodromou C., Liao C., Hu B., Mark Roe S., Vaughan C.K., Vlasic I., Panaretou B., Piper P.W., Pearl L.H.
EMBO J. 23:1402-1410(2004) [PubMed] [Europe PMC] [Abstract]
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS61581.
RefSeqNP_010500.3. NM_001180522.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1USUX-ray2.15B1-156[»]
1USVX-ray2.70B/D/F/H1-156[»]
ProteinModelPortalQ12449.
SMRQ12449. Positions 9-153, 213-348.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32268. 83 interactions.
DIPDIP-1831N.
IntActQ12449. 37 interactions.
MINTMINT-401882.

Proteomic databases

PaxDbQ12449.
PeptideAtlasQ12449.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR214W; YDR214W; YDR214W.
GeneID851800.
KEGGsce:YDR214W.

Organism-specific databases

CYGDYDR214w.
SGDS000002622. AHA1.

Phylogenomic databases

eggNOGCOG5580.
GeneTreeENSGT00390000006429.
HOGENOMHOG000191277.
OMAEAHEPER.
OrthoDBEOG7Q5HQC.

Enzyme and pathway databases

BioCycYEAST:G3O-29796-MONOMER.

Gene expression databases

GenevestigatorQ12449.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]
PfamPF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]
SMARTSM01000. Aha1_N. 1 hit.
[Graphical view]
SUPFAMSSF103111. SSF103111. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ12449.
NextBio969638.
PROQ12449.

Entry information

Entry nameAHA1_YEAST
AccessionPrimary (citable) accession number: Q12449
Secondary accession number(s): D6VSJ8, Q02565, Q7LIE3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references