Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Binding sitei37ATPBy similarity1
Binding sitei79ATPBy similarity1
Binding sitei98ATPBy similarity1
Binding sitei124ATP; via amide nitrogenBy similarity1
Binding sitei376ATPBy similarity1

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-6798695. Neutrophil degranulation.
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)DescriptionActionsGraphical viewLength
Mutagenesisi453L → 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 Publication1
Mutagenesisi493E → 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 Publication1

Chemistry databases

ChEMBLiCHEMBL4199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000629582 – 705ATP-dependent molecular chaperone HSC82Add BLAST704

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei653PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15108.
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
AHA1Q124493EBI-8666,EBI-37072
ARO1P085663EBI-8666,EBI-2883
CNS1P333132EBI-8666,EBI-4806
CPR7P471032EBI-8666,EBI-5436
PPT1P530433EBI-8666,EBI-13796
SEA4P381642EBI-8666,EBI-21365
SSA1P105912EBI-8666,EBI-8591
STI1P157053EBI-8666,EBI-18418

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi35364. 1051 interactors.
DIPiDIP-1524N.
IntActiP15108. 143 interactors.
MINTiMINT-393096.

Structurei

3D structure databases

ProteinModelPortaliP15108.
SMRiP15108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati221 – 22515
Repeati226 – 23025
Repeati232 – 23635
Repeati246 – 25045

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni221 – 2594 X 5 AA repeats of [DE]-[DE]-[DE]-K-K; highly charged regionAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi701 – 705TPR repeat-binding5

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

GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
InParanoidiP15108.
KOiK04079.
OMAiNNEDEQY.
OrthoDBiEOG092C1GW3.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti619K → I (PubMed:2674684).Curated1
Sequence conflicti621L → T (PubMed:2674684).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35364. 1051 interactors.
DIPiDIP-1524N.
IntActiP15108. 143 interactors.
MINTiMINT-393096.

Chemistry databases

ChEMBLiCHEMBL4199.

PTM databases

iPTMnetiP15108.

2D gel databases

SWISS-2DPAGEP15108.

Proteomic databases

MaxQBiP15108.
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

GeneTreeiENSGT00840000129758.
HOGENOMiHOG000031988.
InParanoidiP15108.
KOiK04079.
OMAiNNEDEQY.
OrthoDBiEOG092C1GW3.

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-6798695. Neutrophil degranulation.
R-SCE-844456. The NLRP3 inflammasome.

Miscellaneous databases

PROiP15108.

Family and domain databases

Gene3Di3.30.565.10. 1 hit.
HAMAPiMF_00505. HSP90. 1 hit.
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...

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: November 30, 2016
This is version 172 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.