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Protein

ATP-dependent molecular chaperone HSC82

Gene

HSC82

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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.By similarity1 Publication

Sites

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

GO - Molecular functioni

  • ATPase activity Source: SGD
  • ATPase activity, coupled Source: SGD
  • ATP binding Source: UniProtKB-KW
  • unfolded protein binding Source: SGD

GO - Biological processi

  • 'de novo' protein folding Source: SGD
  • box C/D snoRNP assembly Source: SGD
  • cellular response to heat Source: SGD
  • proteasome assembly Source: SGD
  • protein folding Source: SGD
  • protein refolding Source: SGD
  • 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.
ReactomeiR-SCE-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-SCE-203615. eNOS activation.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-844456. The NLRP3 inflammasome.

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
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR186W.
SGDiS000004798. HSC82.

Subcellular locationi

GO - Cellular componenti

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

Chemistry

ChEMBLiCHEMBL4199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 705704ATP-dependent molecular chaperone HSC82PRO_0000062958Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei653 – 6531PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15108.
PeptideAtlasiP15108.
PRIDEiP15108.
TopDownProteomicsiP15108.

2D gel databases

SWISS-2DPAGEP15108.

PTM databases

iPTMnetiP15108.

Expressioni

Inductioni

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

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
ACC1Q009552EBI-8666,EBI-4814
AEP2P221362EBI-8666,EBI-3318
AHA1Q124497EBI-8666,EBI-37072
APL4Q120282EBI-8666,EBI-33025
ARL3Q028042EBI-8666,EBI-30136
ARO1P085664EBI-8666,EBI-2883
ASR1Q068343EBI-8666,EBI-33224
ATP2P008302EBI-8666,EBI-3242
ATP3P380772EBI-8666,EBI-3271
BEM2P399602EBI-8666,EBI-3517
BET3P361493EBI-8666,EBI-3567
BLM10P435832EBI-8666,EBI-22761
BUD3P255583EBI-8666,EBI-3840
CDC37P061016EBI-8666,EBI-4266
CDC73Q066974EBI-8666,EBI-29913
CNS1P333134EBI-8666,EBI-4806
COA3Q3E7B22EBI-8666,EBI-3680840
COG6P539592EBI-8666,EBI-4829
CPR6P5369120EBI-8666,EBI-5429
CPR7P471035EBI-8666,EBI-5436
DIG2Q033732EBI-8666,EBI-34019
DPH1P404872EBI-8666,EBI-25162
ECM16Q042172EBI-8666,EBI-1820
ECM2P382412EBI-8666,EBI-780
GAT1P435742EBI-8666,EBI-7340
GYL1Q043222EBI-8666,EBI-27427
HAT1Q123412EBI-8666,EBI-8176
HCH1P538343EBI-8666,EBI-28288
HOM6P311162EBI-8666,EBI-5840
HRD1Q081093EBI-8666,EBI-37613
HSP31Q044322EBI-8666,EBI-35591
HSP82P0282944EBI-8666,EBI-8659
HTZ1Q126922EBI-8666,EBI-8080
IES1P435792EBI-8666,EBI-22775
ILV1P009274EBI-8666,EBI-19200
IML1P471702EBI-8666,EBI-25710
LAM4P388002EBI-8666,EBI-24597
LEU1P072642EBI-8666,EBI-10122
MEF1P250392EBI-8666,EBI-6353
MRP4P329023EBI-8666,EBI-16248
MRPL50P537243EBI-8666,EBI-28472
MYO4P324923EBI-8666,EBI-11681
NOP14Q992072EBI-8666,EBI-35157
NOP53Q120802EBI-8666,EBI-29395
NTH1P323562EBI-8666,EBI-19509
NUS1Q120632EBI-8666,EBI-34546
PAT1P256444EBI-8666,EBI-204
PBA1Q057782EBI-8666,EBI-33792
PDR11P405502EBI-8666,EBI-13058
PGK1P005602EBI-8666,EBI-13275
PPT1P530436EBI-8666,EBI-13796
RAD51P254543EBI-8666,EBI-14709
RAD52P067782EBI-8666,EBI-14719
RCO1Q047793EBI-8666,EBI-28153
RKM3P382222EBI-8666,EBI-21417
RMD8P436203EBI-8666,EBI-23040
RPA34P470062EBI-8666,EBI-26109
RPB3P163703EBI-8666,EBI-15773
RPG1P382495EBI-8666,EBI-8981
RPL22AP057492EBI-8666,EBI-14552
RTK1Q121002EBI-8666,EBI-36072
RVB1Q039402EBI-8666,EBI-30712
SEA4P381644EBI-8666,EBI-21365
SEC23P153035EBI-8666,EBI-16584
SGF73P531654EBI-8666,EBI-23812
SGT1Q084463EBI-8666,EBI-17070
SNU66Q124202EBI-8666,EBI-260
SPT15P133932EBI-8666,EBI-19129
SSA1P105913EBI-8666,EBI-8591
SSB1P114843EBI-8666,EBI-8627
SSK2P535994EBI-8666,EBI-18191
SSZ1P387885EBI-8666,EBI-24570
STB3Q124272EBI-8666,EBI-34028
STI1P1570522EBI-8666,EBI-18418
SUP35P054534EBI-8666,EBI-6540
SWD3P381232EBI-8666,EBI-20881
TDH2P003582EBI-8666,EBI-7212
TEF4P360084EBI-8666,EBI-6329
TOM1Q032804EBI-8666,EBI-36817
UBI4P0CG633EBI-8666,EBI-7000452
UBP10P538744EBI-8666,EBI-19873
UFD2P548602EBI-8666,EBI-20003
VMA4P222032EBI-8666,EBI-20268
YEF3P165215EBI-8666,EBI-6338
YIR007WP405663EBI-8666,EBI-3657860
YPR089WO135852EBI-8666,EBI-33008
YPT6Q992603EBI-8666,EBI-29503

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35364. 1047 interactions.
DIPiDIP-1524N.
IntActiP15108. 538 interactions.
MINTiMINT-393096.

Structurei

3D structure databases

ProteinModelPortaliP15108.
SMRiP15108. Positions 2-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

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

Domaini

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

Sequence similaritiesi

Belongs to the heat shock protein 90 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

GeneTreeiENSGT00800000124093.
HOGENOMiHOG000031988.
InParanoidiP15108.
KOiK04079.
OMAiVAPETAM.
OrthoDBiEOG7BP8B5.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
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

        10         20         30         40         50
MAGETFEFQA EITQLMSLII NTVYSNKEIF LRELISNASD ALDKIRYQAL
60 70 80 90 100
SDPKQLETEP DLFIRITPKP EEKVLEIRDS GIGMTKAELI NNLGTIAKSG
110 120 130 140 150
TKAFMEALSA GADVSMIGQF GVGFYSLFLV ADRVQVISKN NEDEQYIWES
160 170 180 190 200
NAGGSFTVTL DEVNERIGRG TVLRLFLKDD QLEYLEEKRI KEVIKRHSEF
210 220 230 240 250
VAYPIQLLVT KEVEKEVPIP EEEKKDEEKK DEDDKKPKLE EVDEEEEEKK
260 270 280 290 300
PKTKKVKEEV QELEELNKTK PLWTRNPSDI TQEEYNAFYK SISNDWEDPL
310 320 330 340 350
YVKHFSVEGQ LEFRAILFIP KRAPFDLFES KKKKNNIKLY VRRVFITDEA
360 370 380 390 400
EDLIPEWLSF VKGVVDSEDL PLNLSREMLQ QNKIMKVIRK NIVKKLIEAF
410 420 430 440 450
NEIAEDSEQF DKFYSAFAKN IKLGVHEDTQ NRAALAKLLR YNSTKSVDEL
460 470 480 490 500
TSLTDYVTRM PEHQKNIYYI TGESLKAVEK SPFLDALKAK NFEVLFLTDP
510 520 530 540 550
IDEYAFTQLK EFEGKTLVDI TKDFELEETD EEKAEREKEI KEYEPLTKAL
560 570 580 590 600
KDILGDQVEK VVVSYKLLDA PAAIRTGQFG WSANMERIMK AQALRDSSMS
610 620 630 640 650
SYMSSKKTFE ISPKSPIIKE LKKRVDEGGA QDKTVKDLTN LLFETALLTS
660 670 680 690 700
GFSLEEPTSF ASRINRLISL GLNIDEDEET ETAPEASTEA PVEEVPADTE

MEEVD
Length:705
Mass (Da):80,900
Last modified:January 23, 2007 - v4
Checksum:iDBD41524091B1F9B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti619 – 6191K → I (PubMed:2674684).Curated
Sequence conflicti621 – 6211L → T (PubMed:2674684).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP15108.
SMRiP15108. Positions 2-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35364. 1047 interactions.
DIPiDIP-1524N.
IntActiP15108. 538 interactions.
MINTiMINT-393096.

Chemistry

ChEMBLiCHEMBL4199.

PTM databases

iPTMnetiP15108.

2D gel databases

SWISS-2DPAGEP15108.

Proteomic databases

MaxQBiP15108.
PeptideAtlasiP15108.
PRIDEiP15108.
TopDownProteomicsiP15108.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YMR186W.
SGDiS000004798. HSC82.

Phylogenomic databases

GeneTreeiENSGT00800000124093.
HOGENOMiHOG000031988.
InParanoidiP15108.
KOiK04079.
OMAiVAPETAM.
OrthoDBiEOG7BP8B5.

Enzyme and pathway databases

BioCyciYEAST:G3O-32874-MONOMER.
ReactomeiR-SCE-1474151. Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
R-SCE-203615. eNOS activation.
R-SCE-3371511. HSF1 activation.
R-SCE-3371568. Attenuation phase.
R-SCE-3371571. HSF1-dependent transactivation.
R-SCE-5218920. VEGFR2 mediated vascular permeability.
R-SCE-844456. The NLRP3 inflammasome.

Miscellaneous databases

NextBioi978750.
PROiP15108.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90.
InterProiIPR003594. HATPase_C.
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]
ProtoNetiSearch...

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: April 13, 2016
This is version 165 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.