Reviewed, UniProtKB/Swiss-Prot Q12449 (AHA1_YEAST)

Names and origin

Protein names

Recommended 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

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.4 Ref.5
Subunit structure	Monomer. Interacts with HSP82. Ref.4 Ref.5
Subcellular location	Cytoplasm. Ref.6
Induction	By heat shock. Ref.4
Miscellaneous	Present with 13939 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the AHA1 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein folding Ref.4 Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Ref.4 Inferred from physical interaction. Source: SGD
Molecular function	ATPase activator activity Ref.4 Ref.5 Inferred from direct assay. Source: UniProtKB chaperone binding Ref.4 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSP82	P02829	2	EBI-37072,EBI-8659
SPE2	P21182	1	EBI-37072,EBI-5655

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 350

350

Hsp90 co-chaperone AHA1

PRO_0000215822

Amino acid modifications

Modified residue

35

1

Phosphoserine Ref.9

Modified residue

49

1

Phosphoserine Ref.9

Modified residue

159

1

Phosphoserine Ref.9

Modified residue

172

1

Phosphoserine Ref.8

Modified residue

173

1

Phosphoserine Ref.9

Experimental info

Mutagenesis

53

1

D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. Ref.10

Mutagenesis

53

1

D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. Ref.10

Mutagenesis

59

1

R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10

Mutagenesis

60

1

K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10

Mutagenesis

62

1

K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.10

Sequence conflict

28

1

L → I Ref.10

Secondary structure

1

.

.

.

.

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.

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.

.

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350

Helix Strand Turn

Details...

Helix

17 – 28

12

Beta strand

41 – 44

4

Beta strand

49 – 53

5

Beta strand

68 – 78

11

Beta strand

88 – 99

12

Helix

104 – 106

3

Beta strand

110 – 113

4

Helix

123 – 130

8

Helix

132 – 150

19

Sequences

	Sequence		Length	Mass (Da)
	Q12449-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 06DF6B40EB5050BE	FASTA	350	39,436
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"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. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"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: 3515197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 129-350.
[4]	"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: 12504007] [Abstract] Cited for: FUNCTION, INDUCTION, INTERACTION WITH HSP82.
[5]	"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: 12604615] [Abstract] Cited for: FUNCTION, INTERACTION WITH HSP82.
[6]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[7]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-159 AND SER-173, MASS SPECTROMETRY.
[10]	"Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery." Meyer P. EMBO J. 23:511-519(2004) [PubMed: 14739935] [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.
[11]	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: 15039704] [Abstract]
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z68194 Genomic DNA. Translation: CAA92357.1.
Z68195 Genomic DNA. Translation: CAA92365.1.
AY557694 Genomic DNA. Translation: AAS56020.1.
U28414 Genomic DNA. Translation: AAA73862.1.

PIR

S61581.

RefSeq

NP_010500.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1831N.

IntAct

Q12449. 90 interactions.

Proteomic databases

PeptideAtlas

Q12449.

PRIDE

Q12449.

Genome annotation databases

Ensembl

YDR214W. Saccharomyces cerevisiae. [Contig view]

GeneID

851800.

GenomeReviews

Gene locus YDR214W in contig Z71256_GR.

KEGG

sce:YDR214W.

NMPDR

fig|4932.3.peg.1257.

Organism-specific databases

CYGD

YDR214w.

SGD

S000002622. AHA1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

Q12449.

Gene expression databases

GermOnline

YDR214W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
[Graphical view]

Pfam

PF09229. Aha1_N. 1 hit.
PF08327. AHSA1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

969638.

Entry information

Entry name

AHA1_YEAST

Accession

Primary (citable) accession number: Q12449
Secondary accession number(s): Q02565, Q7LIE3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)