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EUG1/YDR518W Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrIV: 1478601 to 1480154 CDS: 1478601 - 1480154 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
EUG1	YDR518W		ORF, Verified	S000002926
Description
Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By isomerase activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0413 Assigned on 2007-05-23 UniProtKB protein disulfide isomerase activity Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62        IGI : Inferred from Genetic Interaction with SGD:PDI1 IMP : Inferred from Mutant Phenotype ISS : Inferred from Sequence or structural Similarity with SGD:PDI1 Assigned on 2006-08-18 SGD Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41        IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD GOA curators and MGI curators (2001) Gene Ontology annotation based on Enzyme Commission mapping.      IEA : Inferred from Electronic Annotation with IUBMB:5.3.4.1 Assigned on 2007-05-23 UniProtKB protein disulfide oxidoreductase activity Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62        IGI : Inferred from Genetic Interaction with SGD:PDI1 ISS : Inferred from Sequence or structural Similarity with SGD:PDI1 Assigned on 2006-08-18 SGD Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41        IDA : Inferred from Direct Assay Assigned on 2006-08-18 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By cell redox homeostasis DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR017936 , EBI:IPR013766 Assigned on 2009-01-12 UniProtKB cellular response to heat Wu WS and Li WH (2008) Identifying gene regulatory modules of heat shock response in yeast. BMC Genomics 9:439        RCA : Reviewed Computational Analysis Assigned on 2009-03-03 SGD protein folding Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62        IGI : Inferred from Genetic Interaction with SGD:PDI1 Assigned on 2002-11-08 SGD
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum Kumar A, et al. (2002) Subcellular localization of the yeast proteome. Genes Dev 16(6):707-19              IDA : Inferred from Direct Assay Assigned on 2002-05-07 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2009-10-01 UniProtKB endoplasmic reticulum lumen GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0096 Assigned on 2008-02-13 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]
No summary paragraph available

Basic References [TOP]

BASIC INFORMATION REFERENCES forEUG1/YDR518W for EUG1 1) Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11      2) Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for EUG1/YDR518W

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for EUG1/YDR518W

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MQVTTRF C-term DTVHDEL Length(aa) 517 MW(Da) 58,982 pI 4.63 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.157   Codon Adaptation Index 0.200   Frequency of Optimal Codons 0.513   Hydropathicity of Protein -0.171   Aromaticity Score 0.103

10 20 30 40 50 | | | | | MQVTTRFISAIVSFCLFASFTLAENSARATPGSDLLVLTEKKFKSFIESH PLVLVEFFAPWCLHSQILRPHLEEAASILKEHNVPVVQIDCEANSMVCLQ QTINTYPTLKIFKNGRIFDGQVYRGVKITDEITQYMIQLYEASVIYLNSE DEIQPYLENATLPVVINRGLTGLNETYQEVALDLAEDYVFLSLLDSEDKS LSIHLPNTTEPILFDGNVDSLVGNSVALTQWLKVVILPYFTDIEPDLFPK YISSNLPLAYFFYTSEEELEDYTDLFTQLGKENRGQINFIALNSTMFPHH VRFLNMREQFPLFAIHNMINNLKYGLPQLPEEEYAKLEKPQPLDRDMIVQ LVKDYREGTAKPIVKSEEIPKEQKSNVYKIVGKTHDDIVHDDDKDVLVKY YATWCIHSKRFAPIYEEIANVLASDESVRDKILIAEVDSGANDILSFPVT GYPTIALYPAGNNSKPIIFNKIRNLEDVFEFIKESGTHHIDGQAIYDKLH QAKDSEVSTEDTVHDEL*

Protein Structures from PDB: proteins of known structure with sequence similarity to EUG1/YDR518W, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to EUG1 Homolog Source (per PDB) Protein Alignment: EUG1 vs. Homolog External Links P-Value %Identical %Similar Alignment 2b5e ( Chain: A) Crystal structure of yeast protein disulfide isomerase PDB_Info PDB_Structure Saccharomyces cerevisiae 2.6e-78 42 30 View alignment SCOP MMDB CATH 3boa ( Chain: A) Crystal structure of yeast protein disulfide isomerase. PDB_Info PDB_Structure Saccharomyces cerevisiae 2.6e-78 42 30 View alignment SCOP MMDB CATH 3f8u ( Chain: A, C) Tapasin/erp57 heterodimer PDB_Info PDB_Structure Homo sapiens Chain A = 2.0e-30 28 33 View alignment SCOP MMDB CATH Chain C = 2.0e-30 28 33 View alignment 2djj ( Chain: A) Solution structure of the a' domain of thermophilic fungal protein disulfide isomerase PDB_Info PDB_Structure Humicola insolens 2.6e-15 42 35 View alignment SCOP MMDB CATH 2dmm ( Chain: A) The solution structure of the second thioredoxin domain of human protein disulfide-isomerase a3 PDB_Info PDB_Structure Homo sapiens 8.9e-12 36 35 View alignment SCOP MMDB CATH 2alb ( Chain: A) Nmr structure of the n-terminal domain a of the glycoprotein chaperone erp57 PDB_Info PDB_Structure Synthetic: yes; other_details: this sequence occurs naturally in humans 1.7e-10 43 25 View alignment SCOP MMDB CATH 2dj3 ( Chain: A) The solution structure of the third thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 3.4e-10 41 29 View alignment SCOP MMDB CATH 2r2j ( Chain: A) Crystal structure of human erp44 PDB_Info PDB_Structure Homo sapiens 5.7e-10 24 32 View alignment SCOP MMDB CATH 1x5c ( Chain: A) The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase PDB_Info PDB_Structure Homo sapiens 5.8e-09 34 38 View alignment SCOP MMDB CATH 2djk ( Chain: A) Solution structure of the b' domain of thermophilic fungal protein disulfide isomerase PDB_Info PDB_Structure Humicola insolens 1.5e-08 30 31 View alignment SCOP MMDB CATH 2dj2 ( Chain: A) The solution structure of the second thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 4.5e-08 36 33 View alignment SCOP MMDB CATH 2dj1 ( Chain: A) The solution structure of the first thioredoxin domain of mouse protein disulfide-isomerase a4 PDB_Info PDB_Structure Mus musculus 8.8e-08 38 29 View alignment SCOP MMDB CATH 1mek ( Chain: A) Human protein disulfide isomerase, nmr, 40 structures PDB_Info PDB_Structure Homo sapiens 1.5e-06 32 33 View alignment SCOP MMDB CATH 1x5d ( Chain: A) The solution structure of the second thioredoxin-like domain of human protein disulfide-isomerase a6 PDB_Info PDB_Structure Homo sapiens 1.7e-05 32 35 View alignment SCOP MMDB CATH 2diz ( Chain: A) The solution structure of the third thioredoxin domain of human thioredoxin domain-containing protein 5 PDB_Info PDB_Structure Homo sapiens 2.6e-05 34 35 View alignment SCOP MMDB CATH 3ed3 ( Chain: A, B) Crystal structure of the yeast dithiol/disulfide oxidoreductase mpd1p PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 4.4e-05 26 29 View alignment SCOP MMDB CATH Chain B = 4.4e-05 26 29 View alignment 2dml ( Chain: A) The solution structure of the first thioredoxin domain of mouse protein disulfide-isomerase a6 PDB_Info PDB_Structure Mus musculus 0.000210 37 30 View alignment SCOP MMDB CATH 2i1u ( Chain: A) Mycobacterium tuberculosis thioredoxin c PDB_Info PDB_Structure Mycobacterium tuberculosis 0.000259 34 26 View alignment SCOP MMDB CATH 1syr ( Chain: B, H, A, F, L, K, D, G, I, J, C, E) Initial structural analysis of plasmodium falciparum thioredoxin PDB_Info PDB_Structure Plasmodium falciparum 3D7 Chain B = 0.000420 29 32 View alignment SCOP MMDB CATH Chain H = 0.000420 29 32 View alignment Chain A = 0.000420 29 32 View alignment Chain F = 0.000420 29 32 View alignment Chain L = 0.000420 29 32 View alignment Chain K = 0.000420 29 32 View alignment Chain D = 0.000420 29 32 View alignment Chain G = 0.000420 29 32 View alignment Chain I = 0.000420 29 32 View alignment Chain J = 0.000420 29 32 View alignment Chain C = 0.000420 29 32 View alignment Chain E = 0.000420 29 32 View alignment 2yzu ( Chain: A) Crystal structure of oxidized thioredoxin from thermus thermophilus hb8 PDB_Info PDB_Structure Thermus thermophilus HB8 0.000469 33 34 View alignment SCOP MMDB CATH 2cvk ( Chain: A) Crystal structure of thermus thermophilus thioredoxin PDB_Info PDB_Structure Thermus thermophilus 0.000479 33 34 View alignment SCOP MMDB CATH 2puk ( Chain: G, C) Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin m PDB_Info PDB_Structure Synechocystis sp. | Spinacia oleracea Chain G = 0.002299 31 34 View alignment SCOP MMDB CATH Chain C = 0.002299 31 34 View alignment 1v98 ( Chain: B, A) Crystal structure analysis of thioredoxin from thermus thermophilus PDB_Info PDB_Structure Thermus thermophilus HB8 Chain B = 0.002900 32 27 View alignment SCOP MMDB CATH Chain A = 0.002900 32 27 View alignment 2o89 ( Chain: A) S. aureus thioredoxin p31t/c32s mutant PDB_Info PDB_Structure Staphylococcus aureus 0.003701 32 29 View alignment SCOP MMDB CATH 1quw ( Chain: A) Solution structure of the thioredoxin from bacillus acidocaldarius PDB_Info PDB_Structure Alicyclobacillus acidocaldarius 0.004897 35 29 View alignment SCOP MMDB CATH 1gl8 ( Chain: A) Solution structure of thioredoxin m from spinach, oxidized form PDB_Info PDB_Structure Spinacia oleracea 0.005599 30 34 View alignment SCOP MMDB CATH 1nsw ( Chain: C, A, B, D) The crystal structure of the k18g mutant of the thioredoxin from alicyclobacillus acidocaldarius PDB_Info PDB_Structure Alicyclobacillus acidocaldarius Chain C = 0.005701 35 29 View alignment SCOP MMDB CATH Chain A = 0.005701 35 29 View alignment Chain B = 0.005701 35 29 View alignment Chain D = 0.005701 35 29 View alignment 1fb6 ( Chain: A, B) Crystal structure of thioredoxin m from spinach chloroplast (oxidized form) PDB_Info PDB_Structure Spinacia oleracea Chain A = 0.005701 30 34 View alignment SCOP MMDB CATH Chain B = 0.005701 30 34 View alignment 1fb0 ( Chain: B, A) Crystal structure of thioredoxin m from spinach chloroplast (reduced form) PDB_Info PDB_Structure Spinacia oleracea Chain B = 0.005701 30 34 View alignment SCOP MMDB CATH Chain A = 0.005701 30 34 View alignment 2o87 ( Chain: A) S. aureus thioredoxin p31s mutant PDB_Info PDB_Structure Staphylococcus aureus 0.005701 33 28 View alignment SCOP MMDB CATH 1w89 ( Chain: F, D, C, E, A, B) Structure of the reduced form of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain F = 0.005799 29 35 View alignment SCOP MMDB CATH Chain D = 0.005799 29 35 View alignment Chain C = 0.005799 29 35 View alignment Chain E = 0.005799 29 35 View alignment Chain A = 0.005799 29 35 View alignment Chain B = 0.005799 29 35 View alignment 1w4v ( Chain: A, B, C, E, F, D) Structure of the oxidised form of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain A = 0.005799 29 35 View alignment SCOP MMDB CATH Chain B = 0.005799 29 35 View alignment Chain C = 0.005799 29 35 View alignment Chain E = 0.005799 29 35 View alignment Chain F = 0.005799 29 35 View alignment Chain D = 0.005799 29 35 View alignment 1uvz ( Chain: C, A, D, F, B, E) Structure of human thioredoxin 2 PDB_Info PDB_Structure Homo sapiens Chain C = 0.005799 29 35 View alignment SCOP MMDB CATH Chain A = 0.005799 29 35 View alignment Chain D = 0.005799 29 35 View alignment Chain F = 0.005799 29 35 View alignment Chain B = 0.005799 29 35 View alignment Chain E = 0.005799 29 35 View alignment 2ipa ( Chain: A) Solution structure of trx-arsc complex PDB_Info PDB_Structure Bacillus subtilis 0.006499 30 34 View alignment SCOP MMDB CATH 2voc ( Chain: A, B) Thioredoxin a active site mutants form mixed disulfide dimers that resemble enzyme-substrate reaction intermediate PDB_Info PDB_Structure Bacillus subtilis Chain A = 0.007197 30 34 View alignment SCOP MMDB CATH Chain B = 0.007197 30 34 View alignment 2o85 ( Chain: A) S. aureus thioredoxin p31t mutant PDB_Info PDB_Structure Staphylococcus aureus 0.009104 31 29 View alignment SCOP MMDB CATH 2o7k ( Chain: A) S. aureus thioredoxin PDB_Info PDB_Structure Staphylococcus aureus 0.009104 31 29 View alignment SCOP MMDB CATH

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
EUG1	SGD (2007) Information without a citation in SGD

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YDR518W	SGD Systematic Sequence
852130	NCBI: Gene ID
NP_010806.1	NCBI: RefSeq protein version ID
NP_010806.1	NCBI: RefSeq protein version ID
6320726	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources Organelle DB (UMich) YGAC Triples YPL.db at Uni Graz YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
23 curated references; 0 references not yet curated
Reviews	Hatahet F, et al. (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. Antioxid Redox Signal 11(11):2807-50	|EPS1 |MPD1 |MPD2 |PDI1
Mutants/Phenotypes Regulation of	Kim JH, et al. (2009) The unfolded protein response is necessary but not sufficient to compensate for defects in disulfide isomerization. J Biol Chem 284(16):10400-8	|ALG8 |APM3 |APS3 |ARL1 |AVL9 |CCZ1 |CDC50 |COG8 |EPS1 |ERV41 |ERV46 |FLD1 |GCS1 |GEF1 |MORE
Fungal Related Genes/Proteins Non-Fungal Related Genes/Proteins Protein Sequence Features	Marino SM and Gladyshev VN (2009) A structure-based approach for detection of thiol oxidoreductases and their catalytic redox-active cysteine residues. PLoS Comput Biol 5(5):e1000383	|AHP1 |BET3 |CAP2 |DOT5 |EPS1 |ERO1 |ERV1 |ERV2 |GLR1 |GPX1 |GPX2 |GRX1 |GRX2 |GRX3 |MORE
Mutants/Phenotypes	Shima J, et al. (2008) Possible roles of vacuolar H(+)-ATPase and mitochondrial function in tolerance to air-drying stress revealed by genome-wide screening of Saccharomyces cerevisiae deletion strains. Yeast 25(3):179-90	|ADA2 |ADK1 |ADO1 |AEP2 |AFG3 |ANP1 |APQ13 |ARF1 |ARG82 |ARV1 |ATG17 |ATP17 |BDF1 |BEM1 |MORE
Regulation of	Wu WS and Li WH (2008) Identifying gene regulatory modules of heat shock response in yeast. BMC Genomics 9:439	|ADD37 |AFR1 |AGX1 |AHA1 |AIM17 |ALD4 |ALG13 |ARA1 |ASI1 |ATG12 |ATG8 |BAG7 |BDH1 |CAD1 |MORE
RNA Levels and Processing	Cullen PJ, et al. (2006) Genome-wide analysis of the response to protein glycosylation deficiency in yeast. FEMS Yeast Res 6(8):1264-73	|ACS1 |ADR1 |ALD6 |AMS1 |CHS1 |CHS3 |CHS7 |CLB1 |CLB2 |CLN1 |CLN2 |CLN3 |CTT1 |DER1 |MORE
Reviews	Gruber CW, et al. (2006) Protein disulfide isomerase: the structure of oxidative folding. Trends Biochem Sci 31(8):455-64	|EPS1 |ERO1 |ERV2 |MPD1 |MPD2 |PDI1
Protein-protein Interactions Protein/Nucleic Acid Structure	Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41	|CNE1 |EPS1 |KAR2 |MPD1 |MPD2 |PDI1
RNA Levels and Processing Regulation of	Lai LC, et al. (2005) Dynamical remodeling of the transcriptome during short-term anaerobiosis in Saccharomyces cerevisiae: differential response and role of Msn2 and/or Msn4 and other factors in galactose and glucose media. Mol Cell Biol 25(10):4075-91	|AAC1 |ADE1 |ADE12 |ADE17 |ADE4 |AFR1 |AIM17 |AIM3 |AKR1 |AKR2 |ALA1 |ALD5 |ARE1 |ARN1 |MORE
Function/Process Protein Physical Properties Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65	|MPD1 |MPD2 |PDI1
Function/Process Genetic Interactions Mutants/Phenotypes Strains/Constructs	Xiao R, et al. (2004) The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279(48):49780-6	|EPS1 |MPD1 |MPD2 |PDI1
Function/Process Mutants/Phenotypes	Dimmer KS, et al. (2002) Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae. Mol Biol Cell 13(3):847-53	|ABF2 |ACO1 |ADA2 |ADK1 |AEP1 |AEP2 |AEP3 |AFG3 |AFT1 |AIM10 |AIM22 |ALY1 |APQ13 |ARG82 |MORE
RNA Levels and Processing Regulation of	Alexandre H, et al. (2001) Global gene expression during short-term ethanol stress in Saccharomyces cerevisiae. FEBS Lett 498(1):98-103	|AHP1 |ALD2 |ALD4 |APJ1 |ATG8 |CCC2 |CDC19 |CIT1 |CIT2 |CPR6 |CTT1 |DAK1 |EMI2 |ERO1 |MORE
Function/Process Protein Sequence Features	Fetrow JS, et al. (2001) Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight? Protein Sci 10(5):1005-14	|CDD1 |EPS1 |ERF2 |GRX1 |GRX2 |GRX3 |GRX4 |GRX5 |GRX6 |GRX7 |GRX8 |LEU5 |MPD1 |MPD2 |MORE
Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Substrates/Ligands/Cofactors	Norgaard P and Winther JR (2001) Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J 358(Pt 1):269-74	|PDI1
Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Strains/Constructs	Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62	|EPS1 |MPD1 |MPD2 |PDI1
Fungal Related Genes/Proteins	Bao WG, et al. (2000) Protein disulphide isomerase genes of Kluyveromyces lactis. Yeast 16(4):329-41	|MPD1 |PDI1
Regulation of	Travers KJ, et al. (2000) Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101(3):249-58	|ERO1 |FPR2 |INO1 |IRE1 |KAR2 |LHS1 |OPI1 |PDI1
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Strains/Constructs	Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77	|ERO1 |MPD2 |PDI1
DNA/RNA Sequence Features Regulation of Transcription	Mori K, et al. (1998) Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae. J Biol Chem 273(16):9912-20	|FPR2 |HAC1 |KAR2 |LHS1 |PDI1 |SCJ1
Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Strains/Constructs	Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38	|PDI1
Cellular Location Function/Process	Webster PA, et al. (1995) Properties and cellular functions of related yeast ER proteins protein disulphide-isomerase and Eug1p. Biochem Soc Trans 23(1):66S
Cellular Location Function/Process Fungal Related Genes/Proteins Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins RNA Levels and Processing Strains/Constructs	Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11	|PDI1

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