ATP-dependent molecular chaperone HSC82 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P15108 (HSC82_YEAST)

Last modified November 24, 2009. Version 100. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    ATP-dependent molecular chaperone HSC82
Alternative name(s):
    Heat shock protein Hsp90 constitutive isoform
    82 kDa heat shock cognate protein

Gene names

Name:	HSC82
Ordered Locus Names:	YMR186W
ORF Names:	YM8010.16

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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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.
Subunit structure	Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1. Ref.5 Ref.7 Ref.14
Subcellular location	Cytoplasm. Mitochondrion.
Induction	Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1. Ref.1 Ref.4
Miscellaneous	Present with 132053 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the heat shock protein 90 family.

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Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm Mitochondrion
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	proteasome assembly Inferred from mutant phenotype. Source: SGD protein folding Inferred from mutant phenotype. Source: SGD response to stress Ref.1 Inferred from mutant phenotype. Source: SGD telomere maintenance Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrion Ref.10 Inferred from direct assay. Source: SGD plasma membrane enriched fraction Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
CNS1	P33313	1	EBI-8666,EBI-4806
CPR7	P47103	1	EBI-8666,EBI-5436

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 705

704

ATP-dependent molecular chaperone HSC82

PRO_0000062958

Regions

Repeat

Repeat

Repeat

Repeat

Region

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

Region

701 – 705

Interaction surface for TPR repeats

Sites

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

ATP By similarity

Binding site

124

ATP By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.15

Modified residue

Phosphoserine Ref.15

Modified residue

278

Phosphoserine Ref.15

Modified residue

281

Phosphothreonine Ref.15

Modified residue

293

Phosphoserine Ref.15

Modified residue

330

Phosphoserine Ref.15 Ref.13

Modified residue

375

Phosphoserine Ref.15

Modified residue

446

Phosphoserine Ref.15

Modified residue

452

Phosphoserine Ref.15

Modified residue

471

Phosphothreonine Ref.15

Modified residue

474

Phosphoserine Ref.15

Modified residue

529

Phosphothreonine Ref.15

Modified residue

597

Phosphoserine Ref.15 Ref.12

Modified residue

598

Phosphoserine Ref.15 Ref.12

Modified residue

600

Phosphoserine Ref.12

Modified residue

602

Phosphotyrosine Ref.15

Modified residue

615

Phosphoserine Ref.15 Ref.13 Ref.11

Modified residue

653

Phosphoserine Ref.15

Experimental info

Mutagenesis

453

L → 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.6

Mutagenesis

493

E → 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.6

Sequence conflict

619

K → I Ref.1

Sequence conflict

621

L → T Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P15108-1 [UniParc].

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

705

80,900

        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

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References

	« Hide 'large scale' referencesShow '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: 2674684] [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. Barrell B.G. Nature 387:90-93(1997) [PubMed: 9169872] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	"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: 7483834] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8. Strain: ATCC 204508 / S288c.
[4]	"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.
[5]	"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: 11094077] [Abstract] Cited for: FUNCTION, INTERACTION WITH CNA2.
[6]	"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: 12121981] [Abstract] Cited for: MUTAGENESIS OF LEU-453 AND GLU-493.
[7]	"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: 15340069] [Abstract] Cited for: INTERACTION WITH SGT1.
[8]	"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].
[9]	"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].
[10]	"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: 14576278] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, MASS SPECTROMETRY.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597; SER-598 AND SER-600, MASS SPECTROMETRY.
[13]	"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-330 AND SER-615, MASS SPECTROMETRY.
[14]	"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: 18086883] [Abstract] Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[15]	"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-36; SER-51; SER-278; THR-281; SER-293; SER-330; SER-375; SER-446; SER-452; THR-471; SER-474; THR-529; SER-597; SER-598; TYR-602; SER-615 AND SER-653, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M26044 Unassigned DNA. Translation: AAA02813.1. Z49808 Genomic DNA. Translation: CAA89919.1.
PIR	S55133.
RefSeq	NP_013911.1.
3D structure databases
SMR	P15108. Positions 2-673.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1524N.
IntAct	P15108. 132 interactions.
STRING	P15108.
2-D gel databases
SWISS-2DPAGE	P15108.
Proteomic databases
PeptideAtlas	P15108.
PRIDE	P15108.
Genome annotation databases
Ensembl	YMR186W; YMR186W; YMR186W; Saccharomyces cerevisiae. [Genome view]
GeneID	855224.
KEGG	sce:YMR186W.
NMPDR	fig\|4932.3.peg.4963.
Organism-specific databases
CYGD	YMR186w.
SGD	S000004798. HSC82.
Phylogenomic databases
HOGENOM	P15108.
OMA	FYSAFAK
OrthoDB	EOG9BRZ2V
Gene expression databases
ArrayExpress	P15108.
Genevestigator	P15108.
GermOnline	YMR186W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR003594. ATP_bd_ATPase. 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	978750.

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Entry information

Entry name

HSC82_YEAST

Accession

Primary (citable) accession number: P15108

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 24, 2009
This is version 100 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents