Q12449 (AHA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
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.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.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from mutant phenotype Ref.5. Source: SGD response to stress Inferred from mutant phenotype Ref.5. Source: SGD
Cellular_component	cytoplasm Inferred from physical interaction Ref.5. Source: SGD
Molecular_function	ATPase activator activity Inferred from direct assay Ref.6. Source: UniProtKB chaperone binding Inferred from direct assay Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSC82	P15108	3	EBI-37072,EBI-8666
HSP82	P02829	7	EBI-37072,EBI-8659

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.10

Modified residue

49

1

Phosphoserine Ref.10

Modified residue

159

1

Phosphoserine Ref.10

Modified residue

172

1

Phosphoserine Ref.9

Modified residue

173

1

Phosphoserine Ref.10

Experimental info

Mutagenesis

53

1

D → A: No effect on Hsp90 ATPase activity but reduces Hsp90 binding affinity. Ref.11

Mutagenesis

53

1

D → K: Decreases activation of Hsp90 ATPase activity and substantially reduces Hsp90 binding affinity. Ref.11

Mutagenesis

59

1

R → A: Decreases activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11

Mutagenesis

60

1

K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11

Mutagenesis

62

1

K → A: Decreased activation of Hsp90 ATPase activity with a small reduction in Hsp90 binding affinity. Ref.11

Sequence conflict

28

1

L → I Ref.11

Secondary structure

1

.

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350

Helix Strand Turn

Details...

Helix

17 – 28

12

Beta strand

32 – 34

3

Beta strand

41 – 44

4

Beta strand

49 – 53

5

Beta strand

55 – 57

3

Beta strand

68 – 78

11

Beta strand

82 – 85

4

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 [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] [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. , 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, MASS SPECTROMETRY.
[10]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-49; SER-159 AND SER-173, MASS SPECTROMETRY.
[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.

PIR

S61581.

RefSeq

NP_010500.3. NM_001180522.3.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q12449.

SMR

Q12449. Positions 9-153, 213-348.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1831N.

IntAct

Q12449. 49 interactions.

MINT

MINT-401882.

Proteomic databases

PaxDb

Q12449.

PeptideAtlas

Q12449.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YDR214W; YDR214W; YDR214W.

GeneID

851800.

KEGG

sce:YDR214W.
sce:YDR219C.

Organism-specific databases

CYGD

YDR214w.

SGD

S000002622. AHA1.

Phylogenomic databases

eggNOG

COG5580.

GeneTree

ENSGT00390000006429.

HOGENOM

HOG000191277.

OMA

IFFYEWE.

OrthoDB

EOG4DZ549.

Gene expression databases

Genevestigator

Q12449.

GermOnline

YDR214W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.530.20. 1 hit.

InterPro

IPR013538. Activator_of_Hsp90_ATPase.
IPR015310. AHSA1_N.
IPR023393. START-like_dom.
[Graphical view]

Pfam

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

SMART

SM01000. Aha1_N. 1 hit.
[Graphical view]

SUPFAM

SSF103111. AHSA1_N. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q12449.

NextBio

969638.

Entry information

Entry name

AHA1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program