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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)DescriptionActionsGraphical viewLength
Mutagenesisi128H → Q: Loss of function, but still forms a heterodimer with SSZ1 and associates with ribosomes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000711221 – 433ZuotinAdd BLAST433

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32527.
PRIDEiP32527.

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 interactors.
DIPiDIP-4720N.
IntActiP32527. 31 interactors.
MINTiMINT-517556.

Structurei

Secondary structure

1433
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi348 – 364Combined sources17
Helixi371 – 373Combined sources3
Helixi374 – 387Combined sources14
Helixi390 – 402Combined sources13
Helixi404 – 407Combined sources4
Helixi408 – 420Combined sources13
Helixi426 – 429Combined sources4
Turni430 – 432Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LWXNMR-A348-433[»]
5DJEX-ray1.85A/B166-303[»]
ProteinModelPortaliP32527.
SMRiP32527.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 170JPROSITE-ProRule annotationAdd BLAST73

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi306 – 357Ala/Lys-richAdd BLAST52

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063419.
HOGENOMiHOG000171054.
InParanoidiP32527.
KOiK09522.
OMAiRTFSEDD.
OrthoDBiEOG092C36RH.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LWXNMR-A348-433[»]
5DJEX-ray1.85A/B166-303[»]
ProteinModelPortaliP32527.
SMRiP32527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Protein family/group databases

MoonProtiP32527.

PTM databases

iPTMnetiP32527.

Proteomic databases

MaxQBiP32527.
PRIDEiP32527.

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.
OrthoDBiEOG092C36RH.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP32527.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
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...

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: November 30, 2016
This is version 149 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.