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P02829 (HSP82_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 167. 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:
ATP-dependent molecular chaperone HSP82
Alternative name(s):
82 kDa heat shock protein
Heat shock protein Hsp90 heat-inducible isoform
Gene names
Name:HSP82
Synonyms:HSP90
Ordered Locus Names:YPL240C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.33

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. HAMAP-Rule MF_00505

Subunit structure

Homodimer. Interacts with the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. Interacts directly with the substrates GCN2, HAP1 and STE11. Ref.7 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19 Ref.20 Ref.35

Subcellular location

Cytoplasm Ref.21.

Induction

Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to Ref.4, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure. Ref.4 Ref.10

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1. HAMAP-Rule MF_00505

Miscellaneous

Present with 444943 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Inferred from direct assay PubMed 10564510. Source: SGD

ATP catabolic process

Inferred from direct assay PubMed 12235160. Source: GOC

box C/D snoRNP assembly

Inferred from mutant phenotype PubMed 18268103. Source: SGD

positive regulation of telomere maintenance via telomerase

Inferred from direct assay PubMed 17954556. Source: SGD

proteasome assembly

Inferred from direct assay PubMed 12853471. Source: SGD

protein refolding

Inferred from mutant phenotype PubMed 9371781. Source: SGD

protein targeting to mitochondrion

Inferred from physical interaction PubMed 12526792. Source: SGD

response to osmotic stress

Inferred from mutant phenotype PubMed 16487343. Source: SGD

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Inferred from direct assay PubMed 12235160. Source: SGD

identical protein binding

Inferred from physical interaction PubMed 18268103Ref.31. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11805826PubMed 12604615PubMed 14729968PubMed 15102838PubMed 15766533PubMed 15879519PubMed 16407978PubMed 16429126PubMed 18268103PubMed 18719252PubMed 18818696PubMed 18833289PubMed 23217712Ref.11PubMed 9819422. Source: IntAct

unfolded protein binding

Inferred from direct assay PubMed 10564510. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 709708ATP-dependent molecular chaperone HSP82 HAMAP-Rule MF_00505
PRO_0000062957

Regions

Repeat221 – 22551 HAMAP-Rule MF_00505
Repeat226 – 23052 HAMAP-Rule MF_00505
Repeat231 – 23553 HAMAP-Rule MF_00505
Repeat237 – 24154 HAMAP-Rule MF_00505
Repeat250 – 25455 HAMAP-Rule MF_00505
Region221 – 263435 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged region HAMAP-Rule MF_00505
Motif705 – 7095TPR repeat-binding HAMAP-Rule MF_00505

Sites

Binding site371ATP
Binding site791ATP
Binding site981ATP
Binding site1241ATP; via amide nitrogen
Binding site3801ATP

Amino acid modifications

Modified residue6571Phosphoserine By similarity

Experimental info

Mutagenesis221T → I: Induces a 6-fold increase in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.8
Mutagenesis411A → V: Causes a 98% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.8
Mutagenesis811G → S: Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.8
Mutagenesis831G → D: Abolishes ATPase activity. Ref.23
Mutagenesis971A → I: Abolishes interaction with SBA1. Ref.12
Mutagenesis1011T → I: Causes a 90% reduction in ATPase activity and a reduced client protein activation activity, leading to growth defect at high temperatures. Ref.8
Mutagenesis1071A → N: Induces a 6-fold increase in ATPase activity. Ref.18
Mutagenesis1701G → D: Induces a total loss of function at 34 degrees Celsius. Abolishes interaction with SBA1. Ref.8
Mutagenesis3131G → N or S: Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.6 Ref.8
Mutagenesis3491F → A or Q: Induces a loss of ATPase activity. Can be reactivated by AHA1. Ref.27
Mutagenesis3801R → A: Induces a loss of ATPase activity. Ref.27
Mutagenesis3811E → K: Reduces client protein activation activity. Resistant to ATPase activation by AHA1. Ref.8
Mutagenesis3841Q → A: Induces a loss of ATPase activity. Ref.27
Mutagenesis3871K → A: Decreases AHA1 binding affinity, but has no effect on client protein activation activity. Ref.29
Mutagenesis3871K → D: Decreases AHA1 binding affinity and substantially reduces client protein activation activity. Ref.29
Mutagenesis4311E → K: Specifically reduces the activation of the exogenous ligand glucocorticoid receptor. Ref.6
Mutagenesis4851S → Y: Abolishes interaction with SBA1. Ref.12
Mutagenesis5251T → I: Abolishes interaction with SBA1. Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.6
Mutagenesis5761A → T: Reduces client protein activation activity; when associated with K-579. Ref.6
Mutagenesis5771A → C: Enhances ATPase activity and client protein activation. Ref.31
Mutagenesis5771A → D: Reduces ATPase activity and client protein activation. Ref.31
Mutagenesis5771A → I: Enhances homodimerization, ATPase activity and client protein activation. Ref.31
Mutagenesis5771A → N: Reduces homodimerization, ATPase activity and client protein activation. Ref.31
Mutagenesis5791R → K: Reduces client protein activation activity; when associated with T-576. Ref.6
Mutagenesis5871A → T: No effect on ATPase activity. Reduces client protein activation activity, leading to growth defect at high temperatures. Ref.8
Sequence conflict4811A → S Ref.27

Secondary structure

....................................................................................................................... 709
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02829 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: D7C35676D668FB63

FASTA70981,406
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[5]"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] [Europe PMC] [Abstract]
Cited for: ATPASE ACTIVITY.
[6]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-313; GLU-431; THR-525; ALA-576 AND ARG-579.
[7]"Conservation of Hsp90 macromolecular complexes in Saccharomyces cerevisiae."
Chang H.-C.J., Lindquist S.
J. Biol. Chem. 269:24983-24988(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STI1 AND CPR6.
[8]"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] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF THR-22; ALA-41; GLY-81; THR-101; GLY-170; GLY-313; GLU-381 AND ALA-587.
[9]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CPR6 AND CPR7.
[10]"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] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis."
Obermann W.M., Sondermann H., Russo A.A., Pavletich N.P., Hartl F.U.
J. Cell Biol. 143:901-910(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SBA1.
[12]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SBA1, MUTAGENESIS OF ALA-97 AND SER-485.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HAP1.
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CNS1.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SSE1.
[16]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GCN2.
[17]"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] [Europe PMC] [Abstract]
Cited for: BINDING TO TPR REPEATS.
[18]"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] [Europe PMC] [Abstract]
Cited for: ATPASE ACTIVITY, MUTAGENESIS OF ALA-107.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CDC37 AND STE11.
[20]"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: INTERACTION WITH AHA1 AND HCH1.
[21]"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].
[22]"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].
[23]"The ATPase-dependent chaperoning activity of Hsp90a regulates thick filament formation and integration during skeletal muscle myofibrillogenesis."
Hawkins T.A., Haramis A.P., Etard C., Prodromou C., Vaughan C.K., Ashworth R., Ray S., Behra M., Holder N., Talbot W.S., Pearl L.H., Strahle U., Wilson S.W.
Development 135:1147-1156(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLY-83.
[24]"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].
[25]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[26]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2-214 IN COMPLEX WITH ADP AND GELDANAMYCIN.
[27]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 273-560, MUTAGENESIS OF PHE-349; ARG-380 AND GLN-384.
[28]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-214 IN COMPLEX WITH HUMAN CDC37.
[29]"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 272-530 IN COMPLEX WITH AHA1, MUTAGENESIS OF LYS-387.
[30]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]
[31]"Hsp90 is regulated by a switch point in the C-terminal domain."
Retzlaff M., Stahl M., Eberl H.C., Lagleder S., Beck J., Kessler H., Buchner J.
EMBO Rep. 10:1147-1153(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ALA-577.
[32]"Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin."
Roe S.M., Prodromou C., O'Brien R., Ladbury J.E., Piper P.W., Pearl L.H.
J. Med. Chem. 42:260-266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH RADICICOL, ATPASE ACTIVITY.
[33]"Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol."
Proisy N., Sharp S.Y., Boxall K., Connelly S., Roe S.M., Prodromou C., Slawin A.M., Pearl L.H., Workman P., Moody C.J.
Chem. Biol. 13:1203-1215(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1-214 IN COMPLEX WITH INHIBITORS, FUNCTION.
[34]"Intrinsic inhibition of the Hsp90 ATPase activity."
Richter K., Moser S., Hagn F., Friedrich R., Hainzl O., Heller M., Schlee S., Kessler H., Reinstein J., Buchner J.
J. Biol. Chem. 281:11301-11311(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 25-210, ATPASE ACTIVITY.
[35]"Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex."
Ali M.M., Roe S.M., Vaughan C.K., Meyer P., Panaretou B., Piper P.W., Prodromou C., Pearl L.H.
Nature 440:1013-1017(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-677 IN COMPLEX WITH SBA1 AND ATP, SUBUNIT.
[36]"Molecular characterization of macbecin as an Hsp90 inhibitor."
Martin C.J., Gaisser S., Challis I.R., Carletti I., Wilkinson B., Gregory M., Prodromou C., Roe S.M., Pearl L.H., Boyd S.M., Zhang M.Q.
J. Med. Chem. 51:2853-2857(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-219 IN COMPLEX WITH INHIBITOR, ATPASE ACTIVITY.
[37]"Structural basis of the radicicol resistance displayed by a fungal hsp90."
Prodromou C., Nuttall J.M., Millson S.H., Roe S.M., Sim T.S., Tan D., Workman P., Pearl L.H., Piper P.W.
ACS Chem. Biol. 4:289-297(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-220 IN COMPLEX WITH ADP; GELDANAMYCIN AND RADICICOL.
+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.
BK006949 Genomic DNA. Translation: DAA11197.1.
PIRHHBY90. A03313.
RefSeqNP_015084.1. NM_001184054.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4HX-ray2.50A1-220[»]
1AH6X-ray1.80A1-220[»]
1AH8X-ray2.10A/B1-220[»]
1AM1X-ray2.00A2-214[»]
1AMWX-ray1.85A1-214[»]
1BGQX-ray2.50A1-214[»]
1HK7X-ray2.50A/B273-560[»]
1US7X-ray2.30A1-214[»]
1USUX-ray2.15A273-530[»]
1USVX-ray2.70A/C/E/G272-530[»]
1ZW9X-ray1.90A1-220[»]
1ZWHX-ray1.65A1-220[»]
2AKPX-ray1.94A/B25-210[»]
2BRCX-ray1.60A1-214[»]
2BREX-ray2.00A/B1-219[»]
2CG9X-ray3.10A/B1-677[»]
2CGEX-ray3.00A/B/D273-677[»]
2CGFX-ray2.20A1-214[»]
2FXSX-ray2.00A1-220[»]
2IWSX-ray2.70A1-214[»]
2IWUX-ray2.80A1-214[»]
2IWXX-ray1.50A1-214[»]
2LSVNMR-B701-709[»]
2VW5X-ray1.90A/B/C/D1-214[»]
2VWCX-ray2.40A1-219[»]
2WEPX-ray2.00A1-220[»]
2WEQX-ray2.20A1-220[»]
2WERX-ray1.60A/B1-220[»]
2XD6X-ray2.20A1-214[»]
2XX2X-ray1.85A/B/C/D1-214[»]
2XX4X-ray2.20A1-214[»]
2XX5X-ray2.00A1-214[»]
2YGAX-ray2.37A1-220[»]
2YGEX-ray1.96A1-220[»]
2YGFX-ray2.00A1-220[»]
3C0EX-ray1.90A1-220[»]
3C11X-ray1.60A1-220[»]
3FP2X-ray1.98Q698-709[»]
4AS9X-ray2.71A1-220[»]
4ASAX-ray2.25A1-220[»]
4ASBX-ray3.08A1-220[»]
4ASFX-ray2.60A1-220[»]
4ASGX-ray2.20A1-220[»]
4CE1X-ray2.01A1-214[»]
4CE2X-ray2.38A1-214[»]
4CE3X-ray2.31A1-214[»]
ProteinModelPortalP02829.
SMRP02829. Positions 1-677.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35923. 1388 interactions.
DIPDIP-2262N.
IntActP02829. 337 interactions.
MINTMINT-560200.
STRING4932.YPL240C.

Chemistry

BindingDBP02829.
ChEMBLCHEMBL3536.

2D gel databases

SWISS-2DPAGEP02829.

Proteomic databases

MaxQBP02829.
PeptideAtlasP02829.
PRIDEP02829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL240C; YPL240C; YPL240C.
GeneID855836.
KEGGsce:YPL240C.

Organism-specific databases

CYGDYPL240c.
SGDS000006161. HSP82.

Phylogenomic databases

GeneTreeENSGT00550000074382.
HOGENOMHOG000031988.
KOK04079.
OMAASADVHM.
OrthoDBEOG7BP8B5.

Enzyme and pathway databases

BioCycYEAST:G3O-34126-MONOMER.

Gene expression databases

GenevestigatorP02829.

Family and domain databases

Gene3D3.30.565.10. 1 hit.
HAMAPMF_00505. HSP90.
InterProIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERPTHR11528. PTHR11528. 1 hit.
PfamPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFPIRSF002583. Hsp90. 1 hit.
PRINTSPR00775. HEATSHOCK90.
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEPS00298. HSP90. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02829.
NextBio980407.

Entry information

Entry nameHSP82_YEAST
AccessionPrimary (citable) accession number: P02829
Secondary accession number(s): D6W3D1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 167 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 XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: 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