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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

  • '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

Keywordsi

Molecular functionChaperone
Biological processStress response
LigandATP-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-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
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-6785807 Interleukin-4 and 13 signaling
R-SCE-6798695 Neutrophil degranulation
R-SCE-844456 The NLRP3 inflammasome
R-SCE-8939211 ESR-mediated signaling

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

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
MRPL50P537243EBI-8666,EBI-28472
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
PPT1P530435EBI-8666,EBI-13796
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
SRP1Q028212EBI-8666,EBI-1797
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, 1191 interactors
ComplexPortaliCPX-1276 HMC complex
DIPiDIP-1524N
IntActiP15108, 567 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

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: July 18, 2018
This is version 190 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. 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

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