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SCJ1 SCJ1 HIS3 HIS3 PEP4 PEP4 ERD2 ERD2 LEU2 LEU2 PDI1 PDI1 TRP1 TRP1 EUG1 EUG1 FPR2 FPR2 URA3 URA3 PRB1 PRB1 CAN1 CAN1 ACT1 ACT1 KAR2 KAR2 LHS1 LHS1 SEC61 SEC61 ERO1 ERO1 ADE2 ADE2
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Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SCJ1DnaJ-related protein SCJ1; One of several homologs of bacterial chaperone DnaJ; located in the ER lumen where it cooperates with Kar2p to mediate maturation of proteins. (377 aa)
HIS3Imidazoleglycerol-phosphate dehydratase; catalyzes the sixth step in histidine biosynthesis; mutations cause histidine auxotrophy and sensitivity to Cu, Co, and Ni salts; transcription is regulated by general amino acid control via Gcn4p. (220 aa)
PEP4Saccharopepsin; Vacuolar aspartyl protease (proteinase A); required for posttranslational precursor maturation of vacuolar proteinases; important for protein turnover after oxidative damage; plays a protective role in acetic acid induced apoptosis; synthesized as a zymogen, self-activates. (405 aa)
ERD2ER lumen protein-retaining receptor; HDEL receptor; an integral membrane protein that binds to the HDEL motif in proteins destined for retention in the endoplasmic reticulum; has a role in maintenance of normal levels of ER-resident proteins; Belongs to the ERD2 family. (219 aa)
LEU2Beta-isopropylmalate dehydrogenase (IMDH); catalyzes the third step in the leucine biosynthesis pathway; can additionally catalyze the conversion of beta-ethylmalate into alpha-ketovalerate; Belongs to the isocitrate and isopropylmalate dehydrogenases family. (364 aa)
PDI1Protein disulfide isomerase; multifunctional oxidoreductase of the ER lumen, essential for disulfide bond formation in secretory and cell-surface proteins, processing of non-native disulfide bonds; Ero1p activator; complexes with exomannosidase, Mnl1p to facilitate the recognition of misfolded glycoproteins and the trimming of glycan Man8GlcNAc2 to Man7GlcNAc2 on substrates, thereby accelerating ERAD; PDI1 has a paralog, EUG1, that arose from the whole genome duplication. (522 aa)
TRP1Phosphoribosylanthranilate isomerase; catalyzes the third step in tryptophan biosynthesis; in 2004, the sequence of TRP1 from strain S228C was updated by changing the previously annotated internal STOP (TAA) to serine (TCA); enhances vegetative growth at low and high temperatures when used as an auxotrophic marker in strains such as W303. (224 aa)
EUG1Protein disulfide-isomerase EUG1; Protein disulfide isomerase of the endoplasmic reticulum lumen; EUG1 has a paralog, PDI1, that arose from the whole genome duplication; function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER. (517 aa)
FPR2Membrane-bound peptidyl-prolyl cis-trans isomerase (PPIase); binds to the drugs FK506 and rapamycin; expression pattern suggests possible involvement in ER protein trafficking; relocalizes from nucleus to vacuole upon DNA replication stress; mutation is functionally complemented by human FKBP2. (135 aa)
URA3Orotidine-5'-phosphate (OMP) decarboxylase; catalyzes the sixth enzymatic step in the de novo biosynthesis of pyrimidines, converting OMP into uridine monophosphate (UMP); converts 5-FOA into 5-fluorouracil, a toxic compound. (267 aa)
PRB1Cerevisin; Vacuolar proteinase B (yscB) with H3 N-terminal endopeptidase activity; serine protease of the subtilisin family; involved in protein degradation in the vacuole and required for full protein degradation during sporulation; activity inhibited by Pbi2p; protein abundance increases in response to DNA replication stress; PRB1 has a paralog, YSP3, that arose from the whole genome duplication. (635 aa)
CAN1Plasma membrane arginine permease; requires phosphatidyl ethanolamine (PE) for localization, exclusively associated with lipid rafts; mutation confers canavanine resistance; CAN1 has a paralog, ALP1, that arose from the whole genome duplication. (590 aa)
ACT1Actin; structural protein involved in cell polarization, endocytosis, and other cytoskeletal functions. (375 aa)
KAR2Endoplasmic reticulum chaperone BiP; ATPase involved in protein import into the ER; also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p. (682 aa)
LHS1Heat shock protein 70 homolog LHS1; Molecular chaperone of the endoplasmic reticulum lumen; involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway. (881 aa)
SEC61Conserved ER protein translocation channel; essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms channel for SRP-dependent protein import; with Sec63 complex allows SRP-independent protein import into ER; involved in posttranslational soluble protein import into the ER, ERAD of soluble substrates, and misfolded soluble protein export from the ER. (480 aa)
ERO1Endoplasmic oxidoreductin-1; Thiol oxidase required for oxidative protein folding in the ER; essential for maintaining ER redox balance; feedback regulated via reduction and oxidation of regulatory bonds; reduced Pdi1p activates Ero1p by direct reduction of Ero1p regulatory bonds; depletion of thiol substrates and accumulation of oxidized Pdi1p results in inactivation of Ero1p by both Pdi1p-mediated oxidation and autonomous oxidation of Ero1p regulatory bonds; ero1-1 mutation complemented by human ERO1L. (563 aa)
ADE2Phosphoribosylaminoimidazole carboxylase; catalyzes a step in the 'de novo' purine nucleotide biosynthetic pathway; red pigment accumulates in mutant cells deprived of adenine. (571 aa)
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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