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P15108 (HSC82_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 HSC82
Alternative name(s):
82 kDa heat shock cognate protein
Heat shock protein Hsp90 constitutive isoform
Gene names
Name:HSC82
Ordered Locus Names:YMR186W
ORF Names:YM8010.16
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length705 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 such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity By similarity. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures. Ref.6

Subunit structure

Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1. Ref.6 Ref.8 Ref.12

Subcellular location

Cytoplasm. Mitochondrion Ref.9 Ref.11.

Induction

Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1. Ref.1 Ref.5

Domain

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins By similarity. HAMAP-Rule MF_00505

Miscellaneous

Present with 132053 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the heat shock protein 90 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Mitochondrion
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' protein folding

Inferred from sequence or structural similarity Ref.1. Source: SGD

ATP catabolic process

Inferred from direct assay PubMed 18492664. Source: GOC

box C/D snoRNP assembly

Inferred from mutant phenotype PubMed 18268103. Source: SGD

cellular response to heat

Inferred from mutant phenotype Ref.1. Source: SGD

proteasome assembly

Inferred from mutant phenotype PubMed 12853471. Source: SGD

protein folding

Inferred from mutant phenotype PubMed 7791797. Source: SGD

protein refolding

Inferred from sequence or structural similarity Ref.1. Source: SGD

telomere maintenance

Inferred from mutant phenotype PubMed 17954556. Source: SGD

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay PubMed 18492664. Source: SGD

ATPase activity, coupled

Inferred from sequence or structural similarity Ref.1. Source: SGD

protein binding

Inferred from physical interaction PubMed 11805826PubMed 15766533PubMed 16429126PubMed 18719252PubMed 23217712PubMed 9819421. Source: IntAct

unfolded protein binding

Inferred from direct assay PubMed 9465043. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 705704ATP-dependent molecular chaperone HSC82 HAMAP-Rule MF_00505
PRO_0000062958

Regions

Repeat221 – 22551 HAMAP-Rule MF_00505
Repeat226 – 23052 HAMAP-Rule MF_00505
Repeat232 – 23653 HAMAP-Rule MF_00505
Repeat246 – 25054 HAMAP-Rule MF_00505
Region221 – 259394 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged region HAMAP-Rule MF_00505
Motif701 – 7055TPR repeat-binding HAMAP-Rule MF_00505

Sites

Binding site371ATP By similarity
Binding site791ATP By similarity
Binding site981ATP By similarity
Binding site1241ATP; via amide nitrogen By similarity
Binding site3761ATP By similarity

Amino acid modifications

Modified residue6531Phosphoserine Ref.13

Experimental info

Mutagenesis4531L → A: Leads to growth defect at 37 degrees Celsius, probably by disrupting the intramolecular interaction of the N-termini with the middle domains; when associated with A-493. Ref.7
Mutagenesis4931E → A: Leads to growth defect at 37 degrees Celsius, probably by disrupting the intramolecular interaction of the N-termini with the middle domains; when associated with A-453. Ref.7
Sequence conflict6191K → I Ref.1
Sequence conflict6211L → T Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15108 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: DBD41524091B1F9B

FASTA70580,900
        10         20         30         40         50         60 
MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL SDPKQLETEP 

        70         80         90        100        110        120 
DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG TKAFMEALSA GADVSMIGQF 

       130        140        150        160        170        180 
GVGFYSLFLV ADRVQVISKN NEDEQYIWES NAGGSFTVTL DEVNERIGRG TVLRLFLKDD 

       190        200        210        220        230        240 
QLEYLEEKRI KEVIKRHSEF VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE 

       250        260        270        280        290        300 
EVDEEEEEKK PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL 

       310        320        330        340        350        360 
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA EDLIPEWLSF 

       370        380        390        400        410        420 
VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF NEIAEDSEQF DKFYSAFAKN 

       430        440        450        460        470        480 
IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL TSLTDYVTRM PEHQKNIYYI TGESLKAVEK 

       490        500        510        520        530        540 
SPFLDALKAK NFEVLFLTDP IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI 

       550        560        570        580        590        600 
KEYEPLTKAL KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS 

       610        620        630        640        650        660 
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS GFSLEEPTSF 

       670        680        690        700 
ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE MEEVD 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE, INDUCTION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(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]"Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index."
Boucherie H., Dujardin G., Kermorgant M., Monribot C., Slonimski P.P., Perrot M.
Yeast 11:601-613(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8.
Strain: ATCC 204508 / S288c.
[5]"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.
[6]"Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin."
Imai J., Yahara I.
Mol. Cell. Biol. 20:9262-9270(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CNA2.
[7]"Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone."
Matsumoto S., Tanaka E., Nemoto T.K., Ono T., Takagi T., Imai J., Kimura Y., Yahara I., Kobayakawa T., Ayuse T., Oi K., Mizuno A.
J. Biol. Chem. 277:34959-34966(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LEU-453 AND GLU-493.
[8]"Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex."
Bansal P.K., Abdulle R., Kitagawa K.
Mol. Cell. Biol. 24:8069-8079(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SGT1.
[9]"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].
[10]"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].
[11]"The proteome of Saccharomyces cerevisiae mitochondria."
Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., Pfanner N., Meisinger C.
Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[12]"Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NAP1, IDENTIFICATION BY MASS SPECTROMETRY.
[13]"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-653, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M26044 Unassigned DNA. Translation: AAA02813.1.
Z49808 Genomic DNA. Translation: CAA89919.1.
BK006946 Genomic DNA. Translation: DAA10084.1.
PIRS55133.
RefSeqNP_013911.1. NM_001182692.1.

3D structure databases

ProteinModelPortalP15108.
SMRP15108. Positions 2-673.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35364. 1042 interactions.
DIPDIP-1524N.
IntActP15108. 142 interactions.
MINTMINT-393096.
STRING4932.YMR186W.

Chemistry

ChEMBLCHEMBL4199.

2D gel databases

SWISS-2DPAGEP15108.

Proteomic databases

MaxQBP15108.
PaxDbP15108.
PeptideAtlasP15108.
PRIDEP15108.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR186W; YMR186W; YMR186W.
GeneID855224.
KEGGsce:YMR186W.

Organism-specific databases

SGDS000004798. HSC82.

Phylogenomic databases

eggNOGCOG0326.
GeneTreeENSGT00750000117672.
HOGENOMHOG000031988.
KOK04079.
OMASINSENM.
OrthoDBEOG7BP8B5.

Enzyme and pathway databases

BioCycYEAST:G3O-32874-MONOMER.

Gene expression databases

GenevestigatorP15108.

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

NextBio978750.

Entry information

Entry nameHSC82_YEAST
AccessionPrimary (citable) accession number: P15108
Secondary accession number(s): D6W010
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families