Reviewed, UniProtKB/Swiss-Prot P02829 (HSP82_YEAST)

Names and origin

Protein names

Recommended name:
    ATP-dependent molecular chaperone HSP82
Alternative name(s):
    Heat shock protein Hsp90 heat-inducible isoform
    82 kDa heat shock protein

Gene names

Name:	HSP82
Synonyms:	HSP90
Ordered Locus Names:	YPL240C

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	709 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. The nucleotide-free form of the dimer is found in an open conformation in which the N-termini are not dimerized and the complex is ready for client protein binding. Binding of ATP induces large conformational changes, resulting in the formation of a ring-like closed structure in which the N-terminal domains associate intramolecularly with the middle domain and also dimerize with each other, stimulating their intrinsic ATPase activity and acting as a clamp on the substrate. Finally, ATP hydrolysis results in the release of the substrate. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.
Enzyme regulation	Inhibited by geldanamycin, macbecin I and radicicol, which bind to the ATP-binding pocket. Co-chaperones CDC37, SBA1 and STI1 reduce ATPase activity. Co-chaperones AHA1 and HCH1 increase ATPase activity.
Subunit structure	Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1 bind with their TPR repeats to the N-terminal pentapeptide MEEVD. Interacts directly with the substrates GCN2, HAP1 and STE11. Ref.6 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.17 Ref.18
Subcellular location	Cytoplasm Ref.19.
Induction	Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to Ref.3, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure. Ref.3 Ref.9
Miscellaneous	Present with 444943 molecules/cell in log phase SD medium. Ref.20
Sequence similarities	Belongs to the heat shock protein 90 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	'de novo' protein folding Inferred from direct assay. Source: SGD positive regulation of telomere maintenance via telomerase Inferred from direct assay. Source: SGD proteasome assembly Inferred from direct assay. Source: SGD protein refolding Inferred from mutant phenotype. Source: SGD protein targeting to mitochondrion Inferred from physical interaction. Source: SGD response to osmotic stress Inferred from mutant phenotype. Source: SGD
Cellular component	cytoplasm Ref.19 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Inferred from direct assay. Source: SGD unfolded protein binding Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P25607	1	EBI-8659,EBI-22033
	P38272	1	EBI-8659,EBI-21600
	Q12407	1	EBI-8659,EBI-33162
ACF4	P47129	1	EBI-8659,EBI-25556
ACR3	Q06598	1	EBI-8659,EBI-2122
AHA1	Q12449	4	EBI-8659,EBI-37072
AVT6	P40074	1	EBI-8659,EBI-22666
BAP3	P41815	1	EBI-8659,EBI-3419
BSD2	P38356	1	EBI-8659,EBI-3783
CDC37	Q16543	1	EBI-8659,EBI-295634	From a different organism.
CFD1	P40558	1	EBI-8659,EBI-24924
CNS1	P33313	3	EBI-8659,EBI-4806
COG5	P53951	1	EBI-8659,EBI-4841
COG7	P53195	1	EBI-8659,EBI-4847
COG8	Q04632	1	EBI-8659,EBI-6035
CPR7	P47103	1	EBI-8659,EBI-5436
FUN26	P31381	1	EBI-8659,EBI-7145
GMH1	P36125	1	EBI-8659,EBI-26378
GND1	P38720	1	EBI-8659,EBI-1965
GVP36	P40531	1	EBI-8659,EBI-25006
NMD5	P46970	1	EBI-8659,EBI-12084
OLE1	P21147	1	EBI-8659,EBI-2098
PHO86	P46956	1	EBI-8659,EBI-13337
SBA1	P28707	2	EBI-8659,EBI-26838
SHE4	P51534	1	EBI-8659,EBI-17086
SLT2	Q00772	1	EBI-8659,EBI-17372
SOR2	Q07786	1	EBI-8659,EBI-33572
SSU81	P40073	1	EBI-8659,EBI-18140
TAH1	P25638	1	EBI-8659,EBI-21956
YPR089W	O13585	1	EBI-8659,EBI-33008

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 709

709

ATP-dependent molecular chaperone HSP82

PRO_0000062957

Regions

Repeat

221 – 225

5

1

Repeat

226 – 230

5

2

Repeat

231 – 235

5

3

Repeat

237 – 241

5

4

Repeat

250 – 254

5

5

Region

221 – 263

43

5 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged region

Region

705 – 709

5

Interaction surface for TPR repeats

Sites

Binding site

37

1

ATP

Binding site

79

1

ATP

Binding site

92

1

ATP

Binding site

124

1

ATP

Amino acid modifications

Modified residue

657

1

Phosphoserine Ref.21

Modified residue

663

1

Phosphoserine Ref.21

Experimental info

Mutagenesis

22

1

T → I: Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.7

Mutagenesis

41

1

A → V: Causes a 98% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.7

Mutagenesis

81

1

G → S: Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.7

Mutagenesis

97

1

A → I: Abolishes interaction with SBA1. Ref.10

Mutagenesis

101

1

T → I: Causes a 90% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.7

Mutagenesis

107

1

A → N: Induces a 6-fold increase in ATPase activity. Ref.16

Mutagenesis

170

1

G → D: Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. Ref.7

Mutagenesis

313

1

G → N or S: Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.7 Ref.5

Mutagenesis

349

1

F → A or Q: Induces a loss of ATPase activity. Can be reactivated by AHA1. Ref.24

Mutagenesis

380

1

R → A: Induces a loss of ATPase activity. Ref.24

Mutagenesis

381

1

E → K: Reduces client protein activation activity. Resistant to ATPase activation by AHA1. Ref.7

Mutagenesis

384

1

Q → A: Induces a loss of ATPase activity. Ref.24

Mutagenesis

387

1

K → A: Decreases AHA1 binding affinity, but has no effect on client protein activation activity. Ref.26

Mutagenesis

387

1

K → D: Decreases AHA1 binding affinity and substantially reduces client protein activation activity. Ref.26

Mutagenesis

431

1

E → K: Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. Ref.5

Mutagenesis

485

1

S → Y: Abolishes interaction with SBA1. Ref.10

Mutagenesis

525

1

T → I: Abolishes interaction with SBA1. Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.5

Mutagenesis

576

1

A → T: Reduces client protein activation activity; when associated with K-579. Ref.5

Mutagenesis

579

1

R → K: Reduces client protein activation activity; when associated with T-576. Ref.5

Mutagenesis

587

1

A → T: No effect on ATPase activity. Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.7

Sequence conflict

481

1

A → S Ref.24

Secondary structure

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709

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

10 – 21

12

Helix

29 – 48

20

Helix

53 – 56

4

Beta strand

64 – 69

6

Helix

70 – 72

3

Beta strand

74 – 79

6

Helix

86 – 92

7

Turn

93 – 95

3

Helix

101 – 110

10

Helix

114 – 120

7

Helix

123 – 129

7

Beta strand

131 – 139

9

Beta strand

145 – 150

6

Beta strand

152 – 160

9

Beta strand

162 – 164

3

Beta strand

168 – 177

10

Helix

182 – 185

4

Helix

187 – 197

11

Beta strand

205 – 212

8

Helix

276 – 278

3

Helix

281 – 283

3

Helix

286 – 297

12

Beta strand

304 – 311

8

Beta strand

313 – 315

3

Beta strand

317 – 323

7

Turn

329 – 332

4

Beta strand

341 – 345

5

Beta strand

348 – 352

5

Helix

360 – 362

3

Beta strand

366 – 373

8

Helix

387 – 408

22

Helix

411 – 431

21

Turn

433 – 435

3

Helix

436 – 440

5

Beta strand

444 – 447

4

Beta strand

450 – 456

7

Helix

457 – 462

6

Beta strand

470 – 475

6

Helix

479 – 483

5

Helix

488 – 493

6

Beta strand

498 – 501

4

Helix

504 – 513

10

Beta strand

519 – 523

5

Helix

540 – 544

5

Helix

545 – 547

3

Helix

548 – 556

9

Beta strand

572 – 574

3

Beta strand

576 – 579

4

Helix

587 – 593

7

Beta strand

612 – 615

4

Helix

620 – 630

11

Beta strand

637 – 640

4

Helix

643 – 653

11

Helix

663 – 670

8

Beta strand

672 – 675

4

Sequences

	Sequence		Length	Mass (Da)
	P02829-1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: D7C35676D668FB63	FASTA	709	81,406
	10 20 30 40 50 60 MASETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYKSL SDPKQLETEP 70 80 90 100 110 120 DLFIRITPKP EQKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF 130 140 150 160 170 180 GVGFYSLFLV ADRVQVISKS NDDEQYIWES NAGGSFTVTL DEVNERIGRG TILRLFLKDD 190 200 210 220 230 240 QLEYLEEKRI KEVIKRHSEF VAYPIQLVVT KEVEKEVPIP EEEKKDEEKK DEEKKDEDDK 250 260 270 280 290 300 KPKLEEVDEE EEKKPKTKKV KEEVQEIEEL NKTKPLWTRN PSDITQEEYN AFYKSISNDW 310 320 330 340 350 360 EDPLYVKHFS VEGQLEFRAI LFIPKRAPFD LFESKKKKNN IKLYVRRVFI TDEAEDLIPE 370 380 390 400 410 420 WLSFVKGVVD SEDLPLNLSR EMLQQNKIMK VIRKNIVKKL IEAFNEIAED SEQFEKFYSA 430 440 450 460 470 480 FSKNIKLGVH EDTQNRAALA KLLRYNSTKS VDELTSLTDY VTRMPEHQKN IYYITGESLK 490 500 510 520 530 540 AVEKSPFLDA LKAKNFEVLF LTDPIDEYAF TQLKEFEGKT LVDITKDFEL EETDEEKAER 550 560 570 580 590 600 EKEIKEYEPL TKALKEILGD QVEKVVVSYK LLDAPAAIRT GQFGWSANME RIMKAQALRD 610 620 630 640 650 660 SSMSSYMSSK KTFEISPKSP IIKELKKRVD EGGAQDKTVK DLTKLLYETA LLTSGFSLDE 670 680 690 700 PTSFASRINR LISLGLNIDE DEETETAPEA STAAPVEEVP ADTEMEEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae." Farrelly F.W., Finkelstein D.B. J. Biol. Chem. 259:5745-5751(1984) [PubMed: 6325446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J. Nature 387:103-105(1997) [PubMed: 9169875] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures." Borkovich K.A., Farrelly F.W., Finkelstein D.B., Taulien J., Lindquist S. Mol. Cell. Biol. 9:3919-3930(1989) [PubMed: 2674684] [Abstract] Cited for: INDUCTION.
[4]	"Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases." Nadeau K., Das A., Walsh C.T. J. Biol. Chem. 268:1479-1487(1993) [PubMed: 8419347] [Abstract] Cited for: ATPASE ACTIVITY.
[5]	"Isolation of Hsp90 mutants by screening for decreased steroid receptor function." Bohen S.P., Yamamoto K.R. Proc. Natl. Acad. Sci. U.S.A. 90:11424-11428(1993) [PubMed: 8248264] [Abstract] Cited for: MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
[6]	"Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae." Chang H.-C.J., Lindquist S. J. Biol. Chem. 269:24983-24988(1994) [PubMed: 7929182] [Abstract] Cited for: INTERACTION WITH STI1 AND CPR6.
[7]	"Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase." Nathan D.F., Lindquist S. Mol. Cell. Biol. 15:3917-3925(1995) [PubMed: 7791797] [Abstract] Cited for: MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313; GLU-381 AND ALA-587.
[8]	"A cyclophilin function in Hsp90-dependent signal transduction." Duina A.A., Chang H.-C.J., Marsh J.A., Lindquist S., Gaber R.F. Science 274:1713-1715(1996) [PubMed: 8939862] [Abstract] Cited for: INTERACTION WITH CPR6 AND CPR7.
[9]	"A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication." Zarzov P., Boucherie H., Mann C. J. Cell Sci. 110:1879-1891(1997) [PubMed: 9296388] [Abstract] Cited for: INDUCTION.
[10]	"SBA1 encodes a yeast hsp90 cochaperone that is homologous to vertebrate p23 proteins." Fang Y., Fliss A.E., Rao J., Caplan A.J. Mol. Cell. Biol. 18:3727-3734(1998) [PubMed: 9632755] [Abstract] Cited for: INTERACTION WITH SBA1, MUTAGENESIS OF ALA-97 AND SER-485.
[11]	"Molecular mechanism governing heme signaling in yeast: a higher-order complex mediates heme regulation of the transcriptional activator HAP1." Zhang L., Hach A., Wang C. Mol. Cell. Biol. 18:3819-3828(1998) [PubMed: 9632766] [Abstract] Cited for: INTERACTION WITH HAP1.
[12]	"CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90." Dolinski K.J., Cardenas M.E., Heitman J. Mol. Cell. Biol. 18:7344-7352(1998) [PubMed: 9819421] [Abstract] Cited for: INTERACTION WITH CNS1.
[13]	"The yeast Hsp110 family member, Sse1, is an Hsp90 cochaperone." Liu X.-D., Morano K.A., Thiele D.J. J. Biol. Chem. 274:26654-26660(1999) [PubMed: 10480867] [Abstract] Cited for: INTERACTION WITH SSE1.
[14]	"Hsp90 binds and regulates Gcn2, the ligand-inducible kinase of the alpha subunit of eukaryotic translation initiation factor 2." Donze O., Picard D. Mol. Cell. Biol. 19:8422-8432(1999) [PubMed: 10567567] [Abstract] Cited for: INTERACTION WITH GCN2.
[15]	"Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine." Scheufler C., Brinker A., Bourenkov G., Pegoraro S., Moroder L., Bartunik H., Hartl F.U., Moarefi I. Cell 101:199-210(2000) [PubMed: 10786835] [Abstract] Cited for: BINDING TO TPR REPEATS.
[16]	"The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains." Prodromou C., Panaretou B., Chohan S., Siligardi G., O'Brien R., Ladbury J.E., Roe S.M., Piper P.W., Pearl L.H. EMBO J. 19:4383-4392(2000) [PubMed: 10944121] [Abstract] Cited for: ATPASE ACTIVITY, MUTAGENESIS OF ALA-107.
[17]	"The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest." Abbas-Terki T., Donze O., Picard D. FEBS Lett. 467:111-116(2000) [PubMed: 10664467] [Abstract] Cited for: INTERACTION WITH CDC37 AND STE11.
[18]	"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: INTERACTION WITH AHA1 AND HCH1.
[19]	"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].
[20]	"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].
[21]	"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-657 AND SER-663, MASS SPECTROMETRY.
[22]	"A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone." Prodromou C., Roe S.M., Piper P.W., Pearl L.H. Nat. Struct. Biol. 4:477-482(1997) [PubMed: 9187656] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[23]	"Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone." Prodromou C., Roe S.M., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H. Cell 90:65-75(1997) [PubMed: 9230303] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214.
[24]	"Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions." Meyer P., Prodromou C., Hu B., Vaughan C.K., Roe S.M., Panaretou B., Piper P.W., Pearl L.H. Mol. Cell 11:647-658(2003) [PubMed: 12667448] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, MUTAGENESIS OF PHE-349; ARG-380 AND GLN-384.
[25]	"The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)." Roe S.M., Ali M.M., Meyer P., Vaughan C.K., Panaretou B., Piper P.W., Prodromou C., Pearl L.H. Cell 116:87-98(2004) [PubMed: 14718169] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN CDC37.
[26]	"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 272-530 IN COMPLEX WITH AHA1, MUTAGENESIS OF LYS-387.
[27]	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

EMBL
GenBank
DDBJ

K01387 Unassigned RNA. Translation: AAA02743.1.
Z67751 Genomic DNA. Translation: CAA91604.1.
Z73596 Genomic DNA. Translation: CAA97961.1.

PIR

HHBY90. A03313.

RefSeq

NP_015084.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A4H	X-ray	2.50	A	1-220	[»]
1AH6	X-ray	1.80	A	1-220	[»]
1AH8	X-ray	2.10	A/B	1-220	[»]
1AM1	X-ray	2.00	A	2-214	[»]
1AMW	X-ray	1.85	A	1-214	[»]
1BGQ	X-ray	2.50	A	1-214	[»]
1HK7	X-ray	2.50	A/B	273-560	[»]
1US7	X-ray	2.30	A	1-214	[»]
1USU	X-ray	2.15	A	273-530	[»]
1USV	X-ray	2.70	A/C/E/G	272-530	[»]
1ZW9	X-ray	1.90	A	1-220	[»]
1ZWH	X-ray	1.65	A	1-220	[»]
2AKP	X-ray	1.94	A/B	25-210	[»]
2BRC	X-ray	1.60	A	1-214	[»]
2BRE	X-ray	2.00	A/B	1-219	[»]
2CG9	X-ray	3.10	A/B	1-677	[»]
2CGE	X-ray	3.00	A/B/D	273-677	[»]
2CGF	X-ray	2.20	A	1-214	[»]
2FXS	X-ray	2.00	A	1-220	[»]
2IWS	X-ray	2.70	A	1-214	[»]
2IWU	X-ray	2.80	A	1-214	[»]
2IWX	X-ray	1.50	A	1-214	[»]
2VW5	X-ray	1.90	A/B/C/D	1-214	[»]
2VWC	X-ray	2.40	A	1-219	[»]
2WEP	X-ray	2.00	A	1-220	[»]
2WEQ	X-ray	2.20	A	1-220	[»]
2WER	X-ray	1.60	A/B	1-220	[»]
3C0E	X-ray	1.90	A	1-220	[»]
3C11	X-ray	1.60	A	1-220	[»]
3FP2	X-ray	1.98	Q	698-709	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2262N.

IntAct

P02829. 330 interactions.

STRING

P02829.

2-D gel databases

SWISS-2DPAGE

P02829.

Proteomic databases

PeptideAtlas

P02829.

PRIDE

P02829.

Genome annotation databases

Ensembl

YPL240C; YPL240C; YPL240C; Saccharomyces cerevisiae. [Genome view]

GeneID

855836.

KEGG

sce:YPL240C.

NMPDR

fig|4932.3.peg.6211.

Organism-specific databases

CYGD

YPL240c.

SGD

S000006161. HSP82.

Phylogenomic databases

eggNOG

fuNOG05217.

HOGENOM

HBG631012.

OMA

CEEKRVK.

OrthoDB

EOG9BRZ2V.

PhylomeDB

P02829.

Gene expression databases

ArrayExpress

P02829.

Genevestigator

P02829.

GermOnline

YPL240C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR003594. ATPase-like_ATP-bd.
IPR001404. Chaperone_htpG.
IPR019805. Heat_shock_protein_90_CS.
IPR020576. Hsp90_C.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]

Gene3D

G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.

PANTHER

PTHR11528. Hsp90. 1 hit.

Pfam

PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]

PIRSF

PIRSF002583. Hsp90. 1 hit.

PRINTS

PR00775. HEATSHOCK90.

SMART

SM00387. HATPase_c. 1 hit.
[Graphical view]

PROSITE

PS00298. HSP90. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

980407.

Entry information

Entry name

HSP82_YEAST

Accession

Primary (citable) accession number: P02829

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 19, 2010
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)