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Protein

Zuotin

Gene

ZUO1

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

Component of the ribosome-associated complex (RAC), a heterodimeric chaperone complex involved in regulation of accurate translation termination and in folding or maintaining nascent polypeptides in a folding-competent state. RAC stimulates the ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain. ZUO1 can act as a J-protein for SSB1/SSB2 only when associated with SSZ1.2 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • ribosome binding Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • protein folding Source: SGD
  • regulation of translational fidelity Source: SGD
  • ribosomal subunit export from nucleus Source: SGD
  • rRNA processing Source: SGD
  • translational frameshifting Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30947-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.

Protein family/group databases

MoonProtiP32527.

Names & Taxonomyi

Protein namesi
Recommended name:
Zuotin
Alternative name(s):
DnaJ-related protein ZUO1
Short name:
J protein ZUO1
Heat shock protein 40 homolog ZUO1
Ribosome-associated complex subunit ZUO1
Gene namesi
Name:ZUO1
Ordered Locus Names:YGR285C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR285C.
SGDiS000003517. ZUO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleolus Source: SGD
  • polysome Source: SGD
  • ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi128 – 1281H → Q: Loss of function, but still forms a heterodimer with SSZ1 and associates with ribosomes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 433433ZuotinPRO_0000071122Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei50 – 501PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32527.
PeptideAtlasiP32527.

PTM databases

iPTMnetiP32527.

Interactioni

Subunit structurei

RAC is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. RAC associates with ribosomes via ZUO1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SSZ1P387887EBI-29684,EBI-24570

GO - Molecular functioni

  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi33535. 102 interactions.
DIPiDIP-4720N.
IntActiP32527. 31 interactions.
MINTiMINT-517556.

Structurei

Secondary structure

1
433
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi348 – 36417Combined sources
Helixi371 – 3733Combined sources
Helixi374 – 38714Combined sources
Helixi390 – 40213Combined sources
Helixi404 – 4074Combined sources
Helixi408 – 42013Combined sources
Helixi426 – 4294Combined sources
Turni430 – 4323Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWXNMR-A348-433[»]
ProteinModelPortaliP32527.
SMRiP32527. Positions 358-433.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 17073JPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi306 – 35752Ala/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063419.
HOGENOMiHOG000171054.
InParanoidiP32527.
KOiK09522.
OMAiRTFSEDD.
OrthoDBiEOG7K3TX9.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR032003. RAC_head.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF16717. RAC_head. 1 hit.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32527-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSLPTLTSD ITVEVNSSAT KTPFVRRPVE PVGKFFLQHA QRTLRNHTWS
60 70 80 90 100
EFERIEAEKN VKTVDESNVD PDELLFDTEL ADEDLLTHDA RDWKTADLYA
110 120 130 140 150
AMGLSKLRFR ATESQIIKAH RKQVVKYHPD KQSAAGGSLD QDGFFKIIQK
160 170 180 190 200
AFETLTDSNK RAQYDSCDFV ADVPPPKKGT DYDFYEAWGP VFEAEARFSK
210 220 230 240 250
KTPIPSLGNK DSSKKEVEQF YAFWHRFDSW RTFEFLDEDV PDDSSNRDHK
260 270 280 290 300
RYIERKNKAA RDKKKTADNA RLVKLVERAV SEDPRIKMFK EEEKKEKERR
310 320 330 340 350
KWEREAGARA EAEAKAKAEA EAKAKAESEA KANASAKADK KKAKEAAKAA
360 370 380 390 400
KKKNKRAIRN SAKEADYFGD ADKATTIDEQ VGLIVDSLND EELVSTADKI
410 420 430
KANAAGAKEV LKESAKTIVD SGKLPSSLLS YFV
Length:433
Mass (Da):49,020
Last modified:October 1, 1993 - v1
Checksum:i0AA76BC11D3C7DAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63612 Genomic DNA. Translation: CAA45156.1.
Z73070 Genomic DNA. Translation: CAA97317.1.
AY692823 Genomic DNA. Translation: AAT92842.1.
BK006941 Genomic DNA. Translation: DAA08373.1.
PIRiS25194.
RefSeqiNP_011801.1. NM_001181414.1.

Genome annotation databases

EnsemblFungiiYGR285C; YGR285C; YGR285C.
GeneIDi853202.
KEGGisce:YGR285C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63612 Genomic DNA. Translation: CAA45156.1.
Z73070 Genomic DNA. Translation: CAA97317.1.
AY692823 Genomic DNA. Translation: AAT92842.1.
BK006941 Genomic DNA. Translation: DAA08373.1.
PIRiS25194.
RefSeqiNP_011801.1. NM_001181414.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LWXNMR-A348-433[»]
ProteinModelPortaliP32527.
SMRiP32527. Positions 358-433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33535. 102 interactions.
DIPiDIP-4720N.
IntActiP32527. 31 interactions.
MINTiMINT-517556.

Protein family/group databases

MoonProtiP32527.

PTM databases

iPTMnetiP32527.

Proteomic databases

MaxQBiP32527.
PeptideAtlasiP32527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR285C; YGR285C; YGR285C.
GeneIDi853202.
KEGGisce:YGR285C.

Organism-specific databases

EuPathDBiFungiDB:YGR285C.
SGDiS000003517. ZUO1.

Phylogenomic databases

GeneTreeiENSGT00530000063419.
HOGENOMiHOG000171054.
InParanoidiP32527.
KOiK09522.
OMAiRTFSEDD.
OrthoDBiEOG7K3TX9.

Enzyme and pathway databases

BioCyciYEAST:G3O-30947-MONOMER.
ReactomeiR-SCE-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

NextBioi973377.
PROiP32527.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR032003. RAC_head.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF16717. RAC_head. 1 hit.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Zuotin, a putative Z-DNA binding protein in Saccharomyces cerevisiae."
    Zhang S., Lockshin C., Herbert A., Winter E., Rich A.
    EMBO J. 11:3787-3796(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: 20B-12.
  2. "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2 genes and an ABC transporter gene."
    Volckaert G., Voet M., Robben J.
    Yeast 13:251-259(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Yeast Pdr13p and Zuo1p molecular chaperones are new functional Hsp70 and Hsp40 partners."
    Michimoto T., Aoki T., Toh-e A., Kikuchi Y.
    Gene 257:131-137(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SSZ1.
  7. "RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin."
    Gautschi M., Lilie H., Fuenfschilling U., Mun A., Ross S., Lithgow T., Ruecknagel P., Rospert S.
    Proc. Natl. Acad. Sci. U.S.A. 98:3762-3767(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN RAC.
  8. Cited for: MUTAGENESIS OF HIS-128.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "The ribosome-bound chaperones RAC and Ssb1/2p are required for accurate translation in Saccharomyces cerevisiae."
    Rakwalska M., Rospert S.
    Mol. Cell. Biol. 24:9186-9197(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1."
    Huang P., Gautschi M., Walter W., Rospert S., Craig E.A.
    Nat. Struct. Mol. Biol. 12:497-504(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZUO1_YEAST
AccessioniPrimary (citable) accession number: P32527
Secondary accession number(s): D6VV62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 143 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 86400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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