P32527
Gene name |
ZUO1 (YGR285C) |
Protein name |
Zuotin |
Names |
DnaJ-related protein ZUO1, J protein ZUO1, Heat shock protein 40 homolog ZUO1, Ribosome-associated complex subunit ZUO1 |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YGR285C |
EC number |
|
Protein Class |
DNAJ HOMOLOG SUBFAMILY C MEMBER 2 (PTHR43999) |

Descriptions
The eukaryote-specific J-protein Zuo1 is an Hsp70 co-chaperone that is primarily associated with ribosomes and widely accepted to play an important role in the folding of nascent polypeptides. However, evidence from several organisms indicates that Zuo1 also has a direct role in transcriptional regulation. Zuo1 activates directly the zinc cluster transcription factor Pdr1 via a four-helix bundle formed by the C-terminal domain (CTD), which is 86 residues of Zuo1 (348-433) in Saccharomyces cerevisiae. Among these, the first helix (348-364) plays a role as an autoinhibitory domain on the remaining helixes (365-433) and prevents activation of Pdr1. Both truncation of the helix I and unfolding of the CTD by variants (Zou1-L411R or Zuo1-K351/355P) lead to the release of autoinhibition resulting in the high activation of the Pdr1.
Autoinhibitory domains (AIDs)
Target domain |
365-433 (C-terminal domain helices) |
Relief mechanism |
Others |
Assay |
Deletion assay, Mutagenesis experiment, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure

Activated structure

5 structures for P32527
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
2LWX | NMR | - | A | 348-433 | PDB |
5DJE | X-ray | 185 A | A/B | 166-303 | PDB |
7X34 | EM | 310 A | C | 334-433 | PDB |
7X3K | EM | 600 A | A | 1-433 | PDB |
AF-P32527-F1 | Predicted | AlphaFoldDB |
4 variants for P32527
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
s07-1063144 | 6 | T>A | No | SGRP | |
s07-1063093 | 23 | P>A | No | SGRP | |
s07-1062054 | 369 | G>D | No | SGRP | |
s07-1062037 | 375 | T>A | No | SGRP |
No associated diseases with P32527
16 regional properties for P32527
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | C2 domain | 1571 - 1687 | IPR000008 |
domain | Dbl homology (DH) domain | 1229 - 1415 | IPR000219 |
domain | EH domain | 14 - 109 | IPR000261-1 |
domain | EH domain | 214 - 310 | IPR000261-2 |
conserved_site | Guanine-nucleotide dissociation stimulator, CDC24, conserved site | 1363 - 1388 | IPR001331 |
domain | SH3 domain | 737 - 798 | IPR001452-1 |
domain | SH3 domain | 905 - 963 | IPR001452-2 |
domain | SH3 domain | 994 - 1052 | IPR001452-3 |
domain | SH3 domain | 1066 - 1130 | IPR001452-4 |
domain | SH3 domain | 1147 - 1206 | IPR001452-5 |
domain | Pleckstrin homology domain | 1432 - 1585 | IPR001849 |
domain | EF-hand domain | 53 - 88 | IPR002048-1 |
domain | EF-hand domain | 254 - 289 | IPR002048-2 |
binding_site | EF-Hand 1, calcium-binding site | 66 - 78 | IPR018247-1 |
binding_site | EF-Hand 1, calcium-binding site | 267 - 279 | IPR018247-2 |
domain | Intersectin-1, AP2 binding region | 795 - 909 | IPR032140 |
Functions
Description | ||
---|---|---|
EC Number | ||
Subcellular Localization |
|
|
PANTHER Family | PTHR43999 | DNAJ HOMOLOG SUBFAMILY C MEMBER 2 |
PANTHER Subfamily | PTHR43999:SF1 | DNAJ HOMOLOG SUBFAMILY C MEMBER 2 |
PANTHER Protein Class | chaperone | |
PANTHER Pathway Category | No pathway information available |
6 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
polysome | A multiribosomal structure representing a linear array of ribosomes held together by messenger RNA. They represent the active complexes in cellular protein synthesis and are able to incorporate amino acids into polypeptides both in vivo and in vitro. |
ribosome | An intracellular organelle, about 200 A in diameter, consisting of RNA and protein. It is the site of protein biosynthesis resulting from translation of messenger RNA (mRNA). It consists of two subunits, one large and one small, each containing only protein and RNA. Both the ribosome and its subunits are characterized by their sedimentation coefficients, expressed in Svedberg units (symbol: S). Hence, the prokaryotic ribosome (70S) comprises a large (50S) subunit and a small (30S) subunit, while the eukaryotic ribosome (80S) comprises a large (60S) subunit and a small (40S) subunit. Two sites on the ribosomal large subunit are involved in translation, namely the aminoacyl site (A site) and peptidyl site (P site). Ribosomes from prokaryotes, eukaryotes, mitochondria, and chloroplasts have characteristically distinct ribosomal proteins. |
3 GO annotations of molecular function
Name | Definition |
---|---|
DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
Hsp70 protein binding | Binding to a Hsp70 protein, heat shock proteins around 70kDa in size. |
ribosome binding | Binding to a ribosome. |
8 GO annotations of biological process
Name | Definition |
---|---|
'de novo' cotranslational protein folding | The process of assisting in the correct noncovalent assembly of the ribosome-bound nascent chains of a multidomain protein whilst other parts of the protein are still being translated. |
cellular response to cycloheximide | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a cycloheximide stimulus. Cycloheximide (actidione) is an antibiotic produced by some Streptomyces species which interferes with protein synthesis in eukaryotes. |
negative regulation of cell death | Any process that decreases the rate or frequency of cell death. Cell death is the specific activation or halting of processes within a cell so that its vital functions markedly cease, rather than simply deteriorating gradually over time, which culminates in cell death. |
positive regulation of transcription from RNA polymerase II promoter in response to stress | Any process that increases the frequency, rate or extent of transcription from an RNA polymerase II promoter as a result of a stimulus indicating the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). |
regulation of translational fidelity | Any process that modulates the ability of the translational apparatus to interpret the genetic code. |
ribosomal subunit export from nucleus | The directed movement of a ribosomal subunit from the nucleus into the cytoplasm. |
rRNA processing | Any process involved in the conversion of a primary ribosomal RNA (rRNA) transcript into one or more mature rRNA molecules. |
translational frameshifting | A mechanism whereby different proteins may result from a single mRNA molecule, due to a change in the parsing of three nucleotides per codon relative to an initiating AUG codon. |
4 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q99543 | DNAJC2 | DnaJ homolog subfamily C member 2 | Homo sapiens (Human) | PR |
P54103 | Dnajc2 | DnaJ homolog subfamily C member 2 | Mus musculus (Mouse) | PR |
Q7TQ20 | Dnajc2 | DnaJ homolog subfamily C member 2 | Rattus norvegicus (Rat) | PR |
Q6NWJ4 | dnajc2 | DnaJ homolog subfamily C member 2 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MFSLPTLTSD | ITVEVNSSAT | KTPFVRRPVE | PVGKFFLQHA | QRTLRNHTWS | EFERIEAEKN |
70 | 80 | 90 | 100 | 110 | 120 |
VKTVDESNVD | PDELLFDTEL | ADEDLLTHDA | RDWKTADLYA | AMGLSKLRFR | ATESQIIKAH |
130 | 140 | 150 | 160 | 170 | 180 |
RKQVVKYHPD | KQSAAGGSLD | QDGFFKIIQK | AFETLTDSNK | RAQYDSCDFV | ADVPPPKKGT |
190 | 200 | 210 | 220 | 230 | 240 |
DYDFYEAWGP | VFEAEARFSK | KTPIPSLGNK | DSSKKEVEQF | YAFWHRFDSW | RTFEFLDEDV |
250 | 260 | 270 | 280 | 290 | 300 |
PDDSSNRDHK | RYIERKNKAA | RDKKKTADNA | RLVKLVERAV | SEDPRIKMFK | EEEKKEKERR |
310 | 320 | 330 | 340 | 350 | 360 |
KWEREAGARA | EAEAKAKAEA | EAKAKAESEA | KANASAKADK | KKAKEAAKAA | KKKNKRAIRN |
370 | 380 | 390 | 400 | 410 | 420 |
SAKEADYFGD | ADKATTIDEQ | VGLIVDSLND | EELVSTADKI | KANAAGAKEV | LKESAKTIVD |
430 | |||||
SGKLPSSLLS | YFV |