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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: -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

Miscellaneous

Present with 132053 molecules/cell in log phase SD medium.1 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

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32874-MONOMER

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP15108
PRIDEiP15108
TopDownProteomicsiP15108

2D gel databases

SWISS-2DPAGEiP15108

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi35364, 1192 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-1524N
IntActiP15108, 177 interactors
MINTiP15108
STRINGi4932.YMR186W

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

GeneTreeiENSGT00920000149061
HOGENOMiHOG000031988
InParanoidiP15108
KOiK04079
OMAiVKRHSEF
OrthoDBiEOG092C1GW3

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit

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

Similar proteinsi

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, 1192 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-1524N
IntActiP15108, 177 interactors
MINTiP15108
STRINGi4932.YMR186W

Chemistry databases

ChEMBLiCHEMBL4199

PTM databases

iPTMnetiP15108

2D gel databases

SWISS-2DPAGEiP15108

Proteomic databases

MaxQBiP15108
PaxDbiP15108
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

GeneTreeiENSGT00920000149061
HOGENOMiHOG000031988
InParanoidiP15108
KOiK04079
OMAiVKRHSEF
OrthoDBiEOG092C1GW3

Enzyme and pathway databases

BioCyciYEAST:G3O-32874-MONOMER

Miscellaneous databases

PROiPR:P15108

Family and domain databases

CDDicd00075 HATPase_c, 1 hit
Gene3Di1.20.120.790, 1 hit
3.30.565.10, 1 hit
HAMAPiMF_00505 HSP90, 1 hit
InterProiView protein in InterPro
IPR003594 HATPase_C
IPR036890 HATPase_C_sf
IPR019805 Heat_shock_protein_90_CS
IPR037196 HSP90_C
IPR001404 Hsp90_fam
IPR020575 Hsp90_N
IPR020568 Ribosomal_S5_D2-typ_fold
PANTHERiPTHR11528 PTHR11528, 1 hit
PfamiView protein in Pfam
PF02518 HATPase_c, 1 hit
PF00183 HSP90, 1 hit
PIRSFiPIRSF002583 Hsp90, 1 hit
PRINTSiPR00775 HEATSHOCK90
SMARTiView protein in SMART
SM00387 HATPase_c, 1 hit
SUPFAMiSSF110942 SSF110942, 1 hit
SSF54211 SSF54211, 1 hit
SSF55874 SSF55874, 1 hit
PROSITEiView protein in PROSITE
PS00298 HSP90, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHSC82_YEAST
AccessioniPrimary (citable) accession number: P15108
Secondary accession number(s): D6W010
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: October 10, 2018
This is version 192 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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