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P15108

- HSC82_YEAST

UniProt

P15108 - HSC82_YEAST

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Protein
ATP-dependent molecular chaperone HSC82
Gene
HSC82, YMR186W, YM8010.16
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei37 – 371ATP By similarity
Binding sitei79 – 791ATP By similarity
Binding sitei98 – 981ATP By similarity
Binding sitei124 – 1241ATP; via amide nitrogen By similarity
Binding sitei376 – 3761ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: SGD
  3. ATPase activity, coupled Source: SGD
  4. protein binding Source: IntAct
  5. unfolded protein binding Source: SGD
Complete GO annotation...

GO - Biological processi

  1. 'de novo' protein folding Source: SGD
  2. ATP catabolic process Source: GOC
  3. box C/D snoRNP assembly Source: SGD
  4. cellular response to heat Source: SGD
  5. proteasome assembly Source: SGD
  6. protein folding Source: SGD
  7. protein refolding Source: SGD
  8. telomere maintenance Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32874-MONOMER.
ReactomeiREACT_189032. Signaling by constitutively active EGFR.
REACT_189238. The NLRP3 inflammasome.
REACT_219346. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent molecular chaperone HSC82
Alternative name(s):
82 kDa heat shock cognate protein
Heat shock protein Hsp90 constitutive isoform
Gene namesi
Name:HSC82
Ordered Locus Names:YMR186W
ORF Names:YM8010.16
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIII

Organism-specific databases

SGDiS000004798. HSC82.

Subcellular locationi

Cytoplasm. Mitochondrion 2 Publications

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi453 – 4531L → 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. 1 Publication
Mutagenesisi493 – 4931E → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 705704ATP-dependent molecular chaperone HSC82UniRule annotation
PRO_0000062958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei653 – 6531Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15108.
PaxDbiP15108.
PeptideAtlasiP15108.
PRIDEiP15108.

2D gel databases

SWISS-2DPAGEP15108.

Expressioni

Inductioni

Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1.2 Publications

Gene expression databases

GenevestigatoriP15108.

Interactioni

Subunit structurei

Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AHA1Q124493EBI-8666,EBI-37072
ARO1P085663EBI-8666,EBI-2883
CNS1P333132EBI-8666,EBI-4806
CPR7P471032EBI-8666,EBI-5436
PPT1P530433EBI-8666,EBI-13796
SSA1P105912EBI-8666,EBI-8591
STI1P157053EBI-8666,EBI-18418

Protein-protein interaction databases

BioGridi35364. 1042 interactions.
DIPiDIP-1524N.
IntActiP15108. 142 interactions.
MINTiMINT-393096.
STRINGi4932.YMR186W.

Structurei

3D structure databases

ProteinModelPortaliP15108.
SMRiP15108. Positions 2-673.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati221 – 22551UniRule annotation
Repeati226 – 23052UniRule annotation
Repeati232 – 23653UniRule annotation
Repeati246 – 25054UniRule annotation

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 259394 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionUniRule annotation
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi701 – 7055TPR repeat-bindingUniRule annotation

Domaini

The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins By similarity.UniRule annotation

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0326.
GeneTreeiENSGT00750000117672.
HOGENOMiHOG000031988.
KOiK04079.
OMAiSINSENM.
OrthoDBiEOG7BP8B5.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view]
PANTHERiPTHR11528. PTHR11528. 1 hit.
PfamiPF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view]
PIRSFiPIRSF002583. Hsp90. 1 hit.
PRINTSiPR00775. HEATSHOCK90.
SMARTiSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEiPS00298. HSP90. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15108-1 [UniParc]FASTAAdd to Basket

« Hide

MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL    50
SDPKQLETEP DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG 100
TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKN NEDEQYIWES 150
NAGGSFTVTL DEVNERIGRG TVLRLFLKDD QLEYLEEKRI KEVIKRHSEF 200
VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE EVDEEEEEKK 250
PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL 300
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA 350
EDLIPEWLSF VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF 400
NEIAEDSEQF DKFYSAFAKN IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL 450
TSLTDYVTRM PEHQKNIYYI TGESLKAVEK SPFLDALKAK NFEVLFLTDP 500
IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI KEYEPLTKAL 550
KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS 600
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS 650
GFSLEEPTSF ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE 700
MEEVD 705
Length:705
Mass (Da):80,900
Last modified:January 23, 2007 - v4
Checksum:iDBD41524091B1F9B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti619 – 6191K → I1 Publication
Sequence conflicti621 – 6211L → T1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26044 Unassigned DNA. Translation: AAA02813.1.
Z49808 Genomic DNA. Translation: CAA89919.1.
BK006946 Genomic DNA. Translation: DAA10084.1.
PIRiS55133.
RefSeqiNP_013911.1. NM_001182692.1.

Genome annotation databases

EnsemblFungiiYMR186W; YMR186W; YMR186W.
GeneIDi855224.
KEGGisce:YMR186W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26044 Unassigned DNA. Translation: AAA02813.1 .
Z49808 Genomic DNA. Translation: CAA89919.1 .
BK006946 Genomic DNA. Translation: DAA10084.1 .
PIRi S55133.
RefSeqi NP_013911.1. NM_001182692.1.

3D structure databases

ProteinModelPortali P15108.
SMRi P15108. Positions 2-673.
ModBasei Search...

Protein-protein interaction databases

BioGridi 35364. 1042 interactions.
DIPi DIP-1524N.
IntActi P15108. 142 interactions.
MINTi MINT-393096.
STRINGi 4932.YMR186W.

Chemistry

ChEMBLi CHEMBL4199.

2D gel databases

SWISS-2DPAGE P15108.

Proteomic databases

MaxQBi P15108.
PaxDbi P15108.
PeptideAtlasi P15108.
PRIDEi P15108.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YMR186W ; YMR186W ; YMR186W .
GeneIDi 855224.
KEGGi sce:YMR186W.

Organism-specific databases

SGDi S000004798. HSC82.

Phylogenomic databases

eggNOGi COG0326.
GeneTreei ENSGT00750000117672.
HOGENOMi HOG000031988.
KOi K04079.
OMAi SINSENM.
OrthoDBi EOG7BP8B5.

Enzyme and pathway databases

BioCyci YEAST:G3O-32874-MONOMER.
Reactomei REACT_189032. Signaling by constitutively active EGFR.
REACT_189238. The NLRP3 inflammasome.
REACT_219346. HSF1-dependent transactivation.

Miscellaneous databases

NextBioi 978750.

Gene expression databases

Genevestigatori P15108.

Family and domain databases

Gene3Di 3.30.565.10. 1 hit.
HAMAPi MF_00505. HSP90.
InterProi IPR003594. HATPase_ATP-bd.
IPR019805. Heat_shock_protein_90_CS.
IPR001404. Hsp90_fam.
IPR020575. Hsp90_N.
IPR020568. Ribosomal_S5_D2-typ_fold.
[Graphical view ]
PANTHERi PTHR11528. PTHR11528. 1 hit.
Pfami PF02518. HATPase_c. 1 hit.
PF00183. HSP90. 1 hit.
[Graphical view ]
PIRSFi PIRSF002583. Hsp90. 1 hit.
PRINTSi PR00775. HEATSHOCK90.
SMARTi SM00387. HATPase_c. 1 hit.
[Graphical view ]
SUPFAMi SSF54211. SSF54211. 1 hit.
SSF55874. SSF55874. 1 hit.
PROSITEi PS00298. HSP90. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. 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].

Entry informationi

Entry nameiHSC82_YEAST
AccessioniPrimary (citable) accession number: P15108
Secondary accession number(s): D6W010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 146 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

External Data

Dasty 3

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