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Protein

Hsp70/Hsp90 co-chaperone CNS1

Gene

CNS1

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

Co-chaperone that binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). Stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions.2 Publications

GO - Molecular functioni

  • Hsp70 protein binding Source: SGD
  • Hsp90 protein binding Source: SGD
  • ribosome binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-29105-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp70/Hsp90 co-chaperone CNS1
Alternative name(s):
Cyclophilin seven suppressor 1
STI1 stress-inducible protein homolog
Gene namesi
Name:CNS1
Ordered Locus Names:YBR155W
ORF Names:YBR1205
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR155W.
SGDiS000000359. CNS1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901G → D in CNS1-1; disrupts interaction with Hsp90, temperature-sensitive defect impairing Hsp90-dependent function. 1 Publication
Mutagenesisi140 – 1401C → R in CNS1-2; disrupts interaction with Hsp90, temperature-sensitive defect impairing Hsp90-dependent function. 1 Publication
Mutagenesisi260 – 2601D → G in CNS1-3; temperature-sensitive defect impairing Hsp90-dependent function; when associated with G-324 and S-330. 1 Publication
Mutagenesisi324 – 3241E → G in CNS1-3; temperature-sensitive defect impairing Hsp90-dependent function; when associated with G-260 and S-330. 1 Publication
Mutagenesisi330 – 3301L → S in CNS1-3; temperature-sensitive defect impairing Hsp90-dependent function; when associated with G-260 and G-324. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 385385Hsp70/Hsp90 co-chaperone CNS1PRO_0000106279Add
BLAST

Proteomic databases

MaxQBiP33313.
PeptideAtlasiP33313.

Expressioni

Inductioni

Not induced by heat shock.1 Publication

Interactioni

Subunit structurei

Monomer. Component of Hsp70 and Hsp90 chaperone complexes. Interacts (via TPR repeats) with HSC82 and HSP82 (via C-terminal MEEVD pentapeptide). Interacts with CPR7, SSA1 and SPI1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CPR7P471032EBI-4806,EBI-5436
HGH1P483623EBI-4806,EBI-8304
HSC82P151082EBI-4806,EBI-8666
HSP82P028295EBI-4806,EBI-8659

GO - Molecular functioni

  • Hsp70 protein binding Source: SGD
  • Hsp90 protein binding Source: SGD

Protein-protein interaction databases

BioGridi32854. 32 interactions.
DIPiDIP-1271N.
IntActiP33313. 9 interactions.
MINTiMINT-411470.

Structurei

3D structure databases

ProteinModelPortaliP33313.
SMRiP33313. Positions 86-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati83 – 11634TPR 1Add
BLAST
Repeati121 – 15434TPR 2Add
BLAST
Repeati155 – 18935TPR 3Add
BLAST

Sequence similaritiesi

Belongs to the TTC4 family.Curated
Contains 3 TPR repeats.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00510000049371.
HOGENOMiHOG000216688.
InParanoidiP33313.
OMAiRRCINDC.
OrthoDBiEOG7FR7S9.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P33313-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVNANGGY TKPQKYVPGP GDPELPPQLS EFKDKTSDEI LKEMNRMPFF
60 70 80 90 100
MTKLDETDGA GGENVELEAL KALAYEGEPH EIAENFKKQG NELYKAKRFK
110 120 130 140 150
DARELYSKGL AVECEDKSIN ESLYANRAAC ELELKNYRRC IEDCSKALTI
160 170 180 190 200
NPKNVKCYYR TSKAFFQLNK LEEAKSAATF ANQRIDPENK SILNMLSVID
210 220 230 240 250
RKEQELKAKE EKQQREAQER ENKKIMLESA MTLRNITNIK THSPVELLNE
260 270 280 290 300
GKIRLEDPMD FESQLIYPAL IMYPTQDEFD FVGEVSELTT VQELVDLVLE
310 320 330 340 350
GPQERFKKEG KENFTPKKVL VFMETKAGGL IKAGKKLTFH DILKKESPDV
360 370 380
PLFDNALKIY IVPKVESEGW ISKWDKQKAL ERRSV
Length:385
Mass (Da):44,112
Last modified:February 1, 1994 - v1
Checksum:i742F8254DFDB02A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 138ANGGYTKP → RQMEDIPNQ in AAC60555 (PubMed:8488729).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71329 Genomic DNA. Translation: CAA50473.1.
Z36024 Genomic DNA. Translation: CAA85114.1.
S59774 Genomic DNA. Translation: AAC60555.2.
AY557873 Genomic DNA. Translation: AAS56199.1.
BK006936 Genomic DNA. Translation: DAA07270.1.
PIRiS40699.
RefSeqiNP_009713.1. NM_001178503.1.

Genome annotation databases

EnsemblFungiiYBR155W; YBR155W; YBR155W.
GeneIDi852452.
KEGGisce:YBR155W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71329 Genomic DNA. Translation: CAA50473.1.
Z36024 Genomic DNA. Translation: CAA85114.1.
S59774 Genomic DNA. Translation: AAC60555.2.
AY557873 Genomic DNA. Translation: AAS56199.1.
BK006936 Genomic DNA. Translation: DAA07270.1.
PIRiS40699.
RefSeqiNP_009713.1. NM_001178503.1.

3D structure databases

ProteinModelPortaliP33313.
SMRiP33313. Positions 86-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32854. 32 interactions.
DIPiDIP-1271N.
IntActiP33313. 9 interactions.
MINTiMINT-411470.

Proteomic databases

MaxQBiP33313.
PeptideAtlasiP33313.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR155W; YBR155W; YBR155W.
GeneIDi852452.
KEGGisce:YBR155W.

Organism-specific databases

EuPathDBiFungiDB:YBR155W.
SGDiS000000359. CNS1.

Phylogenomic databases

GeneTreeiENSGT00510000049371.
HOGENOMiHOG000216688.
InParanoidiP33313.
OMAiRRCINDC.
OrthoDBiEOG7FR7S9.

Enzyme and pathway databases

BioCyciYEAST:G3O-29105-MONOMER.

Miscellaneous databases

NextBioi971372.
PROiP33313.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF00515. TPR_1. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 2 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 1 hit.
PROSITEiPS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II including three essential open reading frames."
    Baur A., Schaaff-Gerstenschlaeger I., Boles E., Miosga T., Rose M., Zimmermann F.K.
    Yeast 9:289-293(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "CNS1 encodes an essential p60/Sti1 homolog in Saccharomyces cerevisiae that suppresses cyclophilin 40 mutations and interacts with Hsp90."
    Dolinski K.J., Cardenas M.E., Heitman J.
    Mol. Cell. Biol. 18:7344-7352(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH CPR7 AND HSC82, INDUCTION.
  6. "Cns1 is an essential protein associated with the hsp90 chaperone complex in Saccharomyces cerevisiae that can restore cyclophilin 40-dependent functions in cpr7Delta cells."
    Marsh J.A., Kalton H.M., Gaber R.F.
    Mol. Cell. Biol. 18:7353-7359(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH HSP82.
  7. "Functional interactions between Hsp90 and the co-chaperones Cns1 and Cpr7 in Saccharomyces cerevisiae."
    Tesic M., Marsh J.A., Cullinan S.B., Gaber R.F.
    J. Biol. Chem. 278:32692-32701(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH HSP82, MUTAGENESIS OF GLY-90; CYS-140; ASP-260; GLU-324 AND LEU-330.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "Cns1 is an activator of the Ssa1 ATPase activity."
    Hainzl O., Wegele H., Richter K., Buchner J.
    J. Biol. Chem. 279:23267-23273(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH HSP82 AND SSA1.

Entry informationi

Entry nameiCNS1_YEAST
AccessioniPrimary (citable) accession number: P33313
Secondary accession number(s): D6VQF0, Q02125
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 672 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.