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KAR2/YJL034W 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   ChrX: 381321 to 383369 CDS: 381321 - 383369 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
KAR2	YJL034W	GRP78	ORF, Verified	S000003571
Description
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

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By ATP binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001023 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0067 Assigned on 2007-05-23 UniProtKB ATPase activity Tokunaga M, et al. (1992) Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae. J Biol Chem 267(25):17553-9      IDA : Inferred from Direct Assay Assigned on 2002-11-26 SGD nucleotide binding GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0547 Assigned on 2007-05-23 UniProtKB unfolded protein binding Kimata Y, et al. (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14(6):2559-69        IMP : Inferred from Mutant Phenotype Assigned on 2006-02-01 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By ER-associated protein catabolic process Nishikawa SI, et al. (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153(5):1061-70        IMP : Inferred from Mutant Phenotype Assigned on 2006-02-01 SGD ER-nuclear signaling pathway Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT SRP-dependent cotranslational protein targeting to membrane, translocation Brodsky JL, et al. (1995) BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci U S A 92(21):9643-6        IMP : Inferred from Mutant Phenotype Assigned on 2006-06-13 SGD karyogamy during conjugation with cellular fusion Brizzio V, et al. (1999) Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae. Mol Biol Cell 10(3):609-26        IMP : Inferred from Mutant Phenotype IGI : Inferred from Genetic Interaction Assigned on 2002-12-06 SGD posttranslational protein targeting to membrane, translocation Matlack KE, et al. (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97(5):553-64        IDA : Inferred from Direct Assay Assigned on 2006-06-13 SGD Brodsky JL, et al. (1995) BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum. Proc Natl Acad Sci U S A 92(21):9643-6        IMP : Inferred from Mutant Phenotype Assigned on 2006-06-13 SGD protein folding Tian W, et al. (2008) Combining guilt-by-association and guilt-by-profiling to predict Saccharomyces cerevisiae gene function. Genome Biol 9 Suppl 1:S7              RCA : Reviewed Computational Analysis Assigned on 2009-09-03 YeastFunc response to stress GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0346 Assigned on 2008-02-14 UniProtKB response to unfolded protein Kimata Y, et al. (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14(6):2559-69        IMP : Inferred from Mutant Phenotype Assigned on 2006-02-01 SGD Huttenhower C and Troyanskaya OG (2009) Prediction of Gene Ontology annotations by integrating high-throughput datasets    RCA : Reviewed Computational Analysis Assigned on 2009-08-06 bioPIXIE_MEFIT
Cellular Component Annotation(s) Reference(s) Evidence Assigned By endoplasmic reticulum Rose MD, et al. (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57(7):1211-21        IDA : Inferred from Direct Assay Assigned on 2006-02-01 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 luminal surveillance complex Denic V, et al. (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126(2):349-59        IDA : Inferred from Direct Assay Assigned on 2008-02-06 SGD

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for KAR2/YJL034W for KAR2 KAR2 encodes an essential protein that is a member of the HSP70 family of molecular chaperones (1, 2). In the lumen of the endoplasmic reticulum (ER), Kar2p binds to secretory and transmembrane precursor proteins to prevent their misfolding (2, 1). Kar2p also facilitates protein translocation into the ER (3), membrane fusion during karyogamy (1), and ER-associated degradation (4). Kar2p is a homolog of bacterial DnaK (5) and the mammalian protein BiP/GRP78/HSPA5 (OMIM) and has 67% identity to mouse BiP (1). KAR2 has a high basal expression level which is further induced under conditions that lead to the accumulation of unfolded proteins and triggering of the Unfolded Protein Response (UPR) (1, 2). Not only is KAR2 expression induced by UPR, but Kar2p is also involved in regulating UPR through its interaction with the kinase/nuclease Ire1p (6). In the absence of unfolded peptides, Kar2p binds to Ire1p, maintaining Ire1p in an inactive state. During UPR, binding of an increased number of unfolded proteins to Kar2p causes the displacement of Kar2p from Ire1p (6, 7). Ire1p then adopts an active conformation, initiating a signal cascade that subsequently increases levels of the transcriptional activator Hac1p (reviewed in 8). Hac1p recognizes a 22 base pair UPR element, containing the consensus sequence 5'-CANCNTG-3', that is present in the promoters of UPR-regulated genes including KAR2 (9, 10). KAR2 expression is also induced by heat shock, a response separate from its response to unfolded protein stress and mediated by a heat shock element in the KAR2 promoter (2, 11). Studies in homologous HSP70 proteins suggest that Kar2p substrate binding and release may be regulated by ATP (reviewed in 12). In S. cerevisiae, it has been shown that maximal Kar2p activity requires interaction with other proteins that stimulate ATP turnover. The intrinsically weak ATPase activity of Kar2p is enhanced by interaction with the DnaJ/HSP40 protein chaperone family members Sec63p, Scj1p, and Jem1p (5, 13, 14). Subsequent ADP-ATP exchange is promoted by the nucleotide exchange factor Sil1p and the protein chaperone Lhs1p (15, 16). It was also shown that the ATPase activity of Lhs1p is reciprocally activated by Kar2p (16). Last Updated: 2006-02-01

Basic References [TOP]

BASIC INFORMATION REFERENCES forKAR2/YJL034W for KAR2 1) Normington K, et al. (1989) S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57(7):1223-36        2) Rose MD, et al. (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene. Cell 57(7):1211-21        3) Matlack KE, et al. (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97(5):553-64        4) Nishikawa SI, et al. (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153(5):1061-70        5) Scidmore MA, et al. (1993) Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologues of DnaK and DnaJ in the endoplasmic reticulum. Mol Biol Cell 4(11):1145-59      6) Kimata Y, et al. (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14(6):2559-69        7) Okamura K, et al. (2000) Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem Biophys Res Commun 279(2):445-50        8) Kaufman RJ (1999) Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev 13(10):1211-33        9) Mori K, et al. (1992) A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J 11(7):2583-93      10) 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        11) Kohno K, et al. (1993) The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol 13(2):877-90      12) Bukau B and Horwich AL (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92(3):351-66        13) Schlenstedt G, et al. (1995) A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J Cell Biol 129(4):979-88      14) Brizzio V, et al. (1999) Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiae. Mol Biol Cell 10(3):609-26        15) Kabani M, et al. (2000) Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol Cell Biol 20(18):6923-34        16) Steel GJ, et al. (2004) Coordinated activation of Hsp70 chaperones. Science 303(5654):98-101        17) Romisch K (1999) Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci 112 ( Pt 23)():4185-91        18) Tokunaga M, et al. (1992) Purification and characterization of BiP/Kar2 protein from Saccharomyces cerevisiae. J Biol Chem 267(25):17553-9

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for KAR2/YJL034W

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for KAR2/YJL034W

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) 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 MFFNRLS C-term YFEHDEL Length(aa) 682 MW(Da) 74,467 pI 4.62 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.481   Codon Adaptation Index 0.440   Frequency of Optimal Codons 0.695   Hydropathicity of Protein -0.318   Aromaticity Score 0.065

10 20 30 40 50 | | | | | MFFNRLSAGKLLVPLSVVLYALFVVILPLQNSFHSSNVLVRGADDVENYG TVIGIDLGTTYSCVAVMKNGKTEILANEQGNRITPSYVAFTDDERLIGDA AKNQVAANPQNTIFDIKRLIGLKYNDRSVQKDIKHLPFNVVNKDGKPAVE VSVKGEKKVFTPEEISGMILGKMKQIAEDYLGTKVTHAVVTVPAYFNDAQ RQATKDAGTIAGLNVLRIVNEPTAAAIAYGLDKSDKEHQIIVYDLGGGTF DVSLLSIENGVFEVQATSGDTHLGGEDFDYKIVRQLIKAFKKKHGIDVSD NNKALAKLKREAEKAKRALSSQMSTRIEIDSFVDGIDLSETLTRAKFEEL NLDLFKKTLKPVEKVLQDSGLEKKDVDDIVLVGGSTRIPKVQQLLESYFD GKKASKGINPDEAVAYGAAVQAGVLSGEEGVEDIVLLDVNALTLGIETTG GVMTPLIKRNTAIPTKKSQIFSTAVDNQPTVMIKVYEGERAMSKDNNLLG KFELTGIPPAPRGVPQIEVTFALDANGILKVSATDKGTGKSESITITNDK GRLTQEEIDRMVEEAEKFASEDASIKAKVESRNKLENYAHSLKNQVNGDL GEKLEEEDKETLLDAANDVLEWLDDNFETAIAEDFDEKFESLSKVAYPIT SKLYGGADGSGAADYDDEDEDDDGDYFEHDEL*

Protein Structures from PDB: proteins of known structure with sequence similarity to KAR2/YJL034W, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to KAR2 Homolog Source (per PDB) Protein Alignment: KAR2 vs. Homolog External Links P-Value %Identical %Similar Alignment 3c7n ( Chain: B, A) Structure of the hsp110:hsc70 nucleotide exchange complex PDB_Info PDB_Structure Saccharomyces cerevisiae | Bos taurus Chain B = 1.8e-141 67 21 View alignment SCOP MMDB CATH Chain A = 4.3e-46 28 34 View alignment 1yuw ( Chain: A) Crystal structure of bovine hsc70(aa1-554)e213a/d214a mutant PDB_Info PDB_Structure Bos taurus 7.8e-141 67 21 View alignment SCOP MMDB CATH 2v7z ( Chain: B, A) Crystal structure of the 70-kda heat shock cognate protein from rattus norvegicus in post-atp hydrolysis state PDB_Info PDB_Structure Rattus norvegicus Chain B = 2.9e-139 67 22 View alignment SCOP MMDB CATH Chain A = 2.9e-139 67 22 View alignment 2kho ( Chain: A) Heat shock protein 70 PDB_Info PDB_Structure Unknown 2.1e-106 51 26 View alignment SCOP MMDB CATH 3iuc ( Chain: C, A) Heat shock 70kDa protei PDB_Info PDB_Structure Unknown Chain C = 2.5e-103 70 20 View alignment SCOP MMDB CATH Chain A = 2.5e-103 70 20 View alignment 2v7y ( Chain: A) Crystal structure of the molecular chaperone dnak from geobacillus kaustophilus hta426 in post-atp hydrolysis state PDB_Info PDB_Structure Geobacillus kaustophilus HTA426 1.4e-102 56 22 View alignment SCOP MMDB CATH 2qw9 ( Chain: A, B) Crystal structure of bovine hsc70 (1-394aa)in the apo state PDB_Info PDB_Structure Bos taurus Chain A = 9.6e-97 66 22 View alignment SCOP MMDB CATH Chain B = 9.6e-97 66 22 View alignment 2qwm ( Chain: A, B) Crystal structure of bovine hsc70 (1-394aa)in the adp*vi state PDB_Info PDB_Structure Bos taurus Chain A = 9.6e-97 66 22 View alignment SCOP MMDB CATH Chain B = 9.6e-97 66 22 View alignment 2qwl ( Chain: B, A) Crystal structure of bovine hsc70 (1-394aa)in the adp state PDB_Info PDB_Structure Bos taurus Chain B = 9.6e-97 66 22 View alignment SCOP MMDB CATH Chain A = 9.6e-97 66 22 View alignment 2qwp ( Chain: A) Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)r171c and bovine auxilin (810-910aa) d876c in the adp*pi form #2 PDB_Info PDB_Structure Bos taurus 4.6e-96 66 21 View alignment SCOP MMDB CATH 2qwr ( Chain: A) Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)r171c and bovine auxilin (810-910aa) d876c in the amppnp intact form PDB_Info PDB_Structure Bos taurus 4.6e-96 66 21 View alignment SCOP MMDB CATH 2qwn ( Chain: A) Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-386aa)r171c and bovine auxilin (810-910aa) d876c in the adp*pi state PDB_Info PDB_Structure Bos taurus 4.6e-96 66 21 View alignment SCOP MMDB CATH 2qwq ( Chain: A) Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)r171c and bovine auxilin (810-910aa) d876c in the amppnp hydrolyzed form PDB_Info PDB_Structure Bos taurus 4.6e-96 66 21 View alignment SCOP MMDB CATH 2qwo ( Chain: A) Crystal structure of disulfide-bond-crosslinked complex of bovine hsc70 (1-394aa)r171c and bovine auxilin (810-910aa) d876c in the adp*pi form #1 PDB_Info PDB_Structure Bos taurus 4.6e-96 66 21 View alignment SCOP MMDB CATH 1ngi ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 1.4e-95 66 22 View alignment SCOP MMDB CATH 1hpm ( Chain: A) How potassium affects the activity of the molecular chaperone hsc70. ii. potassium binds specifically in the atpase active site PDB_Info PDB_Structure Bos taurus 1.4e-95 66 22 View alignment SCOP MMDB CATH 1ngj ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 1.4e-95 66 22 View alignment SCOP MMDB CATH 3hsc ( Chain: A) Three-dimensional structure of the atpase fragment of a 70k heat-shock cognate protein PDB_Info PDB_Structure Bos taurus 1.4e-95 66 22 View alignment SCOP MMDB CATH 1bup ( Chain: A) T13s mutant of bovine 70 kilodalton heat shock protein PDB_Info PDB_Structure Bos taurus 2.0e-95 66 22 View alignment SCOP MMDB CATH 1ngb ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 2.4e-95 66 22 View alignment SCOP MMDB CATH 1atr ( Chain: A) Threonine 204 of the chaperone protein hsc70 influences the structure of the active site but is not essential for atp hydrolysis PDB_Info PDB_Structure Bos taurus 2.7e-95 66 22 View alignment SCOP MMDB CATH 1ats ( Chain: A) Threonine 204 of the chaperone protein hsc70 influences the structure of the active site but is not essential for atp hydrolysis PDB_Info PDB_Structure Bos taurus 3.2e-95 66 21 View alignment SCOP MMDB CATH 1ngh ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 3.2e-95 66 22 View alignment SCOP MMDB CATH 1ngf ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 3.2e-95 66 22 View alignment SCOP MMDB CATH 1ngd ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 3.2e-95 66 22 View alignment SCOP MMDB CATH 1nga ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 3.7e-95 66 21 View alignment SCOP MMDB CATH 1ngg ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 4.2e-95 66 22 View alignment SCOP MMDB CATH 1ngc ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 4.2e-95 66 22 View alignment SCOP MMDB CATH 1nge ( Chain: A) Structural basis of the 70-kilodalton heat shock cognate protein atp hydrolytic activity, ii. structure of the active site with adp or atp bound to wild type and mutant atpase fragment PDB_Info PDB_Structure Bos taurus 4.2e-95 66 22 View alignment SCOP MMDB CATH 3cqx ( Chain: B, A) Chaperone complex PDB_Info PDB_Structure Mus musculus Chain B = 4.2e-95 66 21 View alignment SCOP MMDB CATH Chain A = 4.2e-95 66 21 View alignment 1ba0 ( Chain: A) Heat-shock cognate 70kd protein 44kd atpase n-terminal 1nge 3 PDB_Info PDB_Structure Bos taurus 4.7e-95 66 21 View alignment SCOP MMDB CATH 3fzl ( Chain: A) Crystal structures of hsc70/bag1 in complex with small molecule inhibitors PDB_Info PDB_Structure Homo sapiens 6.3e-95 66 22 View alignment SCOP MMDB CATH 3fzm ( Chain: A) Crystal structures of hsc70/bag1 in complex with small molecule inhibitors PDB_Info PDB_Structure Homo sapiens 6.3e-95 66 22 View alignment SCOP MMDB CATH 3fzh ( Chain: A) Crystal structures of hsc70/bag1 in complex with small molecule inhibitors PDB_Info PDB_Structure Homo sapiens 6.3e-95 66 22 View alignment SCOP MMDB CATH 3fzk ( Chain: A) Crystal structures of hsc70/bag1 in complex with small molecule inhibitors PDB_Info PDB_Structure Homo sapiens 6.3e-95 66 22 View alignment SCOP MMDB CATH 3fzf ( Chain: A) Crystal structure of hsc70/bag1 in complex with atp PDB_Info PDB_Structure Homo sapiens 6.3e-95 66 22 View alignment SCOP MMDB CATH 1hx1 ( Chain: A) Crystal structure of a bag domain in complex with the hsc70 atpase domain PDB_Info PDB_Structure Bos taurus | Homo sapiens 6.7e-95 66 22 View alignment SCOP MMDB CATH 1kaz ( Chain: A) Kd heat shock cognate protein atpase domain, k71e mutant PDB_Info PDB_Structure Bos taurus 1.2e-94 66 22 View alignment SCOP MMDB CATH 1ba1 ( Chain: A) Heat-shock cognate 70kd protein 44kd atpase n-terminal mutant with cys 17 replaced by lys PDB_Info PDB_Structure Bos taurus 1.2e-94 66 21 View alignment SCOP MMDB CATH 1qqo ( Chain: A) E175s mutant of bovine 70 kilodalton heat shock protein PDB_Info PDB_Structure Bos taurus 1.2e-94 66 22 View alignment SCOP MMDB CATH 1kay ( Chain: A) Kd heat shock cognate protein atpase domain, k71a mutant PDB_Info PDB_Structure Bos taurus 1.7e-94 66 21 View alignment SCOP MMDB CATH 2bup ( Chain: A) T13g mutant of the atpase fragment of bovine hsc70 PDB_Info PDB_Structure Bos taurus 1.7e-94 66 21 View alignment SCOP MMDB CATH 1kax ( Chain: A) Kd heat shock cognate protein atpase domain, k71m mutant PDB_Info PDB_Structure Bos taurus 1.9e-94 66 21 View alignment SCOP MMDB CATH 2e88 ( Chain: A) Crystal structure of the human hsp70 atpase domain in the apo form PDB_Info PDB_Structure Homo sapiens 2.3e-94 66 23 View alignment SCOP MMDB CATH 2e8a ( Chain: A) Crystal structure of the human hsp70 atpase domain in complex with amp-pnp PDB_Info PDB_Structure Homo sapiens 2.3e-94 66 23 View alignment SCOP MMDB CATH 3d2f ( Chain: B, D, C, A) Crystal structure of a complex of sse1p and hsp70 PDB_Info PDB_Structure Saccharomyces cerevisiae | Homo sapiens Chain B = 3.4e-94 66 23 View alignment SCOP MMDB CATH Chain D = 3.4e-94 66 23 View alignment Chain C = 5.8e-49 28 36 View alignment Chain A = 5.8e-49 28 36 View alignment 3d2e ( Chain: B, D, C, A) Crystal structure of a complex of sse1p and hsp70, selenomethionine-labeled crystals PDB_Info PDB_Structure Saccharomyces cerevisiae | Homo sapiens Chain B = 3.4e-94 66 23 View alignment SCOP MMDB CATH Chain D = 3.4e-94 66 23 View alignment Chain C = 5.8e-49 28 36 View alignment Chain A = 5.8e-49 28 36 View alignment 1hjo ( Chain: A) Heat-shock 70kd protein 42kd atpase n-terminal domain PDB_Info PDB_Structure Homo sapiens 3.4e-94 66 23 View alignment SCOP MMDB CATH 1s3x ( Chain: A) The crystal structure of the human hsp70 atpase domain PDB_Info PDB_Structure Homo sapiens 3.9e-94 66 23 View alignment SCOP MMDB CATH 1qqm ( Chain: A) D199s mutant of bovine 70 kilodalton heat shock protein PDB_Info PDB_Structure Bos taurus 5.0e-94 66 22 View alignment SCOP MMDB CATH 3gdq ( Chain: A) Atp-ase domain of the human heat shock 70 kda protein 1- like in complex with adp PDB_Info PDB_Structure Homo sapiens 5.6e-94 65 23 View alignment SCOP MMDB CATH 3i33 ( Chain: A) Heat shock-related 70 k PDB_Info PDB_Structure Unknown 7.5e-94 64 22 View alignment SCOP MMDB CATH 3fe1 ( Chain: C, A, B) Crystal structure of the human heat shock 70kda protein 6 (hsp70b') atp-ase domain in complex with adp PDB_Info PDB_Structure Homo sapiens Chain C = 1.3e-93 63 24 View alignment SCOP MMDB CATH Chain A = 1.3e-93 63 24 View alignment Chain B = 1.3e-93 63 24 View alignment 1qqn ( Chain: A) D206s mutant of bovine 70 kilodalton heat shock protein PDB_Info PDB_Structure Bos taurus 1.6e-93 66 21 View alignment SCOP MMDB CATH 3gl1 ( Chain: A, B) Crystal structure of atpase domain of ssb1 chaperone, a member of the hsp70 family, from saccharomyces cerevisiae PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 3.0e-89 61 26 View alignment SCOP MMDB CATH Chain B = 3.0e-89 61 26 View alignment 1dkg ( Chain: D) Crystal structure of the nucleotide exchange factor grpe bound to the atpase domain of the molecular chaperone dnak PDB_Info PDB_Structure Escherichia coli 2.5e-69 53 25 View alignment SCOP MMDB CATH 3h0x ( Chain: A) Crystal structure of peptide-binding domain of kar2 protein from saccharomyces cerevisiae PDB_Info PDB_Structure Saccharomyces cerevisiae 2.8e-49 100 0 View alignment SCOP MMDB CATH 2qxl ( Chain: A, B) Crystal structure analysis of sse1, a yeast hsp110 PDB_Info PDB_Structure Saccharomyces cerevisiae Chain A = 4.3e-46 28 34 View alignment SCOP MMDB CATH Chain B = 4.3e-46 28 34 View alignment 1xqs ( Chain: C, D) Crystal structure of the hspbp1 core domain complexed with the fragment of hsp70 atpase domain PDB_Info PDB_Structure Homo sapiens Chain C = 1.6e-38 56 32 View alignment SCOP MMDB CATH Chain D = 1.6e-38 56 32 View alignment 7hsc ( Chain: A) High resolution solution structure of the heat shock cognate-70 kd substrate binding domain obtained by multidimensional nmr techniques PDB_Info PDB_Structure Rattus norvegicus 3.4e-38 72 20 View alignment SCOP MMDB CATH 1ckr ( Chain: A) High resolution solution structure of the heat shock cognate-70 kd substrate binding domain obtained by multidimensional nmr techniques PDB_Info PDB_Structure Rattus norvegicus 3.4e-38 72 20 View alignment SCOP MMDB CATH 2op6 ( Chain: A) Peptide-binding domain of heat shock 70 kda protein d precursor from c.elegans PDB_Info PDB_Structure Caenorhabditis elegans 7.6e-33 68 21 View alignment SCOP MMDB CATH 3dob ( Chain: B, A) Peptide-binding domain of heat shock 70 kda protein f44e5.5 from c.elegans. PDB_Info PDB_Structure Caenorhabditis elegans Chain B = 8.6e-33 68 17 View alignment SCOP MMDB CATH Chain A = 8.6e-33 68 17 View alignment 2bpr ( Chain: A) Nmr structure of the substrate binding domain of dnak, 25 structures PDB_Info PDB_Structure Escherichia coli 9.6e-29 54 26 View alignment SCOP MMDB CATH 1bpr ( Chain: A) Nmr structure of the substrate binding domain of dnak, minimized average structure PDB_Info PDB_Structure Escherichia coli 9.6e-29 54 26 View alignment SCOP MMDB CATH 3dpp ( Chain: B, A) Crystal structure of the substrate binding domain of e. coli dnak in complex with a long pyrrhocoricin-derived inhibitor peptide (form a) PDB_Info PDB_Structure Escherichia coli Chain B = 1.3e-28 48 27 View alignment SCOP MMDB CATH Chain A = 1.3e-28 48 27 View alignment 3dpq ( Chain: A, B, E, F) Crystal structure of the substrate binding domain of e. coli dnak in complex with a long pyrrhocoricin-derived inhibitor peptide (form b) PDB_Info PDB_Structure Escherichia coli Chain A = 1.3e-28 48 27 View alignment SCOP MMDB CATH Chain B = 1.3e-28 48 27 View alignment Chain E = 1.3e-28 48 27 View alignment Chain F = 1.3e-28 48 27 View alignment 3dpo ( Chain: A, B) Crystal structure of the substrate binding domain of e. coli dnak in complex with a short pyrrhocoricin-derived inhibitor peptide PDB_Info PDB_Structure Escherichia coli Chain A = 1.3e-28 48 27 View alignment SCOP MMDB CATH Chain B = 1.3e-28 48 27 View alignment 1dky ( Chain: B, A) The substrate binding domain of dnak in complex with a substrate peptide, determined from type 2 native crystals PDB_Info PDB_Structure Escherichia coli Chain B = 1.4e-28 48 27 View alignment SCOP MMDB CATH Chain A = 1.4e-28 48 27 View alignment 1dkz ( Chain: A) The substrate binding domain of dnak in complex with a substrate peptide, determined from type 1 native crystals PDB_Info PDB_Structure Escherichia coli 1.4e-28 48 27 View alignment SCOP MMDB CATH 1dkx ( Chain: A) The substrate binding domain of dnak in complex with a substrate peptide, determined from type 1 selenomethionyl crystals PDB_Info PDB_Structure Escherichia coli 1.7e-28 48 26 View alignment SCOP MMDB CATH 3dqg ( Chain: C, B, A, D) Peptide-binding domain of heat shock 70 kda protein f, mitochondrial precursor, from caenorhabditis elegans. PDB_Info PDB_Structure Caenorhabditis elegans Chain C = 3.8e-28 61 24 View alignment SCOP MMDB CATH Chain B = 3.8e-28 61 24 View alignment Chain A = 3.8e-28 61 24 View alignment Chain D = 3.8e-28 61 24 View alignment 1q5l ( Chain: A) Nmr structure of the substrate binding domain of dnak bound to the peptide nrllltg PDB_Info PDB_Structure Escherichia coli 6.0e-21 62 22 View alignment SCOP MMDB CATH 1dg4 ( Chain: A) Nmr structure of the substrate binding domain of dnak in the apo form PDB_Info PDB_Structure Escherichia coli 8.5e-21 63 20 View alignment SCOP MMDB CATH 1u00 ( Chain: A) Hsca substrate binding domain complexed with the iscu recognition peptide elppvkihc PDB_Info PDB_Structure Escherichia coli 1.3e-15 35 33 View alignment SCOP MMDB CATH 1jce ( Chain: A) Mreb from thermotoga maritima PDB_Info PDB_Structure Thermotoga maritima 4.2e-06 27 26 View alignment SCOP MMDB CATH 1jcf ( Chain: A) Mreb from thermotoga maritima, trigonal PDB_Info PDB_Structure Thermotoga maritima 4.2e-06 27 26 View alignment SCOP MMDB CATH 1jcg ( Chain: A) Mreb from thermotoga maritima, amppnp PDB_Info PDB_Structure Thermotoga maritima 4.2e-06 27 26 View alignment SCOP MMDB CATH 1ud0 ( Chain: B, C, A, D) Crystal structure of the c-terminal 10-kda subdomain of hsc70 PDB_Info PDB_Structure Rattus norvegicus Chain B = 0.000230 42 28 View alignment SCOP MMDB CATH Chain C = 0.000230 42 28 View alignment Chain A = 0.000230 42 28 View alignment Chain D = 0.000230 42 28 View alignment 2p32 ( Chain: F, A, E, B, C, D) Crystal structure of the c-terminal 10 kda subdomain from c. elegans hsp70 PDB_Info PDB_Structure Caenorhabditis elegans Chain F = 0.000279 41 30 View alignment SCOP MMDB CATH Chain A = 0.000279 41 30 View alignment Chain E = 0.000279 41 30 View alignment Chain B = 0.000279 41 30 View alignment Chain C = 0.000279 41 30 View alignment Chain D = 0.000279 41 30 View alignment

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
KAR2	SGD (2007) Information without a citation in SGD

Mapping Notes

Date	Note
1997-10-20	Edition 14: SSD1 has also been used to refer to KAR2/YJL034W; should not be confused with SSD1, the putative phosphatase, on chromosome IV. Cherry JM, et al. (1997) Genetic and physical maps of Saccharomyces cerevisiae. Nature 387(6632 Suppl):67-73

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
YJL034W	SGD Systematic Sequence
853418	NCBI: Gene ID
NP_012500.1	NCBI: RefSeq protein version ID
NP_012500.1	NCBI: RefSeq protein version ID
6322426	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 YeastRC Localization (Seattle) YGAC Triples 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
297 curated references; 0 references not yet curated
Reviews	Hoseki J, et al. (2010) Mechanism and components of endoplasmic reticulum-associated degradation. J Biochem 147(1):19-25	|CDC48 |DER1 |HRD1 |HRD3 |SSM4 |UBX2 |USA1 |YOS9
Non-Fungal Related Genes/Proteins Reviews	Kohno K (2010) Stress-sensing mechanisms in the unfolded protein response: similarities and differences between yeast and mammals. J Biochem 147(1):27-33	|HAC1 |IRE1
Protein-protein Interactions	Puts CF, et al. (2010) A P(4)-ATPase Protein Interaction Network Reveals a Link between Aminophospholipid Transport and Phosphoinositide Metabolism. J Proteome Res 9(2):833-42	|ACC1 |ARC1 |CDC50 |DRS2 |INO1 |ITR1 |MHP1 |PYC1 |PYC2 |SAC1 |SEC26 |SSD1 |TCB3 |VNX1
Cellular Location	Copic A, et al. (2009) Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics 182(3):757-69	|ALG3 |CSF1 |EOS1 |HAC1 |HTZ1 |LHS1 |MNN11 |MRPL16 |PHO88 |UBX2 |YLR065C
Protein-protein Interactions	Gong Y, et al. (2009) An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell. Mol Syst Biol 5:275	|APJ1 |CAJ1 |CWC23 |DJP1 |ECM10 |ERJ5 |GIM3 |GIM4 |GIM5 |HLJ1 |HSC82 |HSP104 |HSP12 |HSP26 |MORE
Cellular Location	Griffith J and Reggiori F (2009) Ultrastructural Analysis of Nanogold-labeled Endocytic Compartments of Yeast Saccharomyces cerevisiae Using a Cryosectioning Procedure. J Histochem Cytochem 57(8):801-9	|PMA1 |VAM3 |VPS4
Protein Processing/Modification/Regulation Transcription	Lin FM, et al. (2009) Comparative proteomic analysis of tolerance and adaptation of ethanologenic Saccharomyces cerevisiae to furfural, a lignocellulosic inhibitory compound. Appl Environ Microbiol 75(11):3765-76	|ACO1 |ACO2 |ACT1 |ADH1 |ADH2 |ADH5 |ADH6 |AHP1 |ALD2 |ALD3 |ALD4 |ALD5 |CDC19 |CIT1 |MORE
Protein Processing/Modification/Regulation	Lin FM, et al. (2009) Temporal quantitative proteomics of Saccharomyces cerevisiae in response to a nonlethal concentration of furfural. Proteomics 9(24):5471-83	|ACO1 |ACT1 |AHP1 |CYS3 |EGD2 |ENO1 |GLK1 |GPD1 |GRE2 |GRX4 |HOM6 |HSC82 |HSP31 |MET14 |MORE
RNA Levels and Processing Regulation of	Lu C, et al. (2009) Slow growth induces heat-shock resistance in normal and respiratory-deficient yeast. Mol Biol Cell 20(3):891-903	|MDJ1 |MPD1 |SOD1 |SOD2 |SSA1 |SSA4
Protein-protein Interactions	Markov DA, et al. (2009) Identification of proteins associated with the yeast mitochondrial RNA polymerase by tandem affinity purification. Yeast 26(8):423-40	|HSP60 |MGM101 |MSS116 |MTF1 |MTF2 |PET127 |PET309 |RPO41 |SIS1 |SSC1 |YML6
Mutants/Phenotypes Strains/Constructs	Melloy P, et al. (2009) Distinct roles for key karyogamy proteins during yeast nuclear fusion. Mol Biol Cell 20(17):3773-82	|JEM1 |KAR5 |PRM3
RNA Levels and Processing	Metzger MB and Michaelis S (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19	|ADE17 |ALF1 |CCT3 |CIK1 |DGK1 |ECM29 |GET3 |HAC1 |HRD1 |IDH1 |ITR1 |MAG1 |MIA40 |OTU1 |MORE
Mutants/Phenotypes Strains/Constructs	Pineau L, et al. (2009) Lipid-induced ER stress: synergistic effects of sterols and saturated fatty acids. Traffic 10(6):673-90	|HAC1 |HEM1 |IRE1 |OLE1 |PMA1
Reviews	Rasheva VI and Domingos PM (2009) Cellular responses to endoplasmic reticulum stress and apoptosis. Apoptosis 14(8):996-1007	|IRE1
Function/Process Protein Processing/Modification/Regulation	Rossignol T, et al. (2009) The proteome of a wine yeast strain during fermentation, correlation with the transcriptome. J Appl Microbiol 107(1):47-55	|ACT1 |ADE5,7 |ADH1 |AHP1 |ARO9 |ASC1 |ASN1 |CDC48 |CYS3 |EFT1 |ENO1 |ENO2 |ERG6 |FBA1 |MORE
Large-scale protein detection Regulation of	Santos PM, et al. (2009) Insights into yeast adaptive response to the agricultural fungicide mancozeb: a toxicoproteomics approach. Proteomics 9(3):657-70	|ACO1 |ADE3 |AFT1 |AHP1 |ALD3 |ALD4 |APA1 |ARG1 |CDC19 |CLC1 |CPA2 |CYS3 |CYS4 |EFT1 |MORE
Mutants/Phenotypes	Tartakoff AM and Jaiswal P (2009) Nuclear fusion and genome encounter during yeast zygote formation. Mol Biol Cell 20(12):2932-42	|CBF2 |GAR1 |HMG1 |HTB2 |IRE1 |KAR1 |NOP56 |NUP49 |PRM3 |SEC18 |SPC42
Fungal Related Genes/Proteins	Yi M, et al. (2009) The ER Chaperone LHS1 Is Involved in Asexual Development and Rice Infection by the Blast Fungus Magnaporthe oryzae. Plant Cell 21(2):681-95	|LHS1
Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	de Keyzer J, et al. (2009) Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo. J Biol Chem 284(46):31564-71	|IRE1 |LHS1
Cellular Location Regulation of Strains/Constructs	Aguilera-Romero A, et al. (2008) The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus. J Cell Biol 180(4):713-20	|EMP24 |ERV25 |GCS1 |GLO3 |IRE1 |RER1 |SEC21 |SEC23 |SEC27
Mutants/Phenotypes Strains/Constructs	Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8	|AAR2 |ABD1 |ABF1 |ACC1 |ACP1 |ADE13 |AFG2 |ALA1 |ALG1 |ALG13 |ALG14 |ALG2 |ALG7 |ALR1 |MORE
Strains/Constructs Techniques and Reagents	Devenish RJ, et al. (2008) Monitoring organelle turnover in yeast using fluorescent protein tags. Methods Enzymol 451:109-31	|COX9 |NAB2 |NVJ1 |PEX14 |SEC63
Cellular Location	Federovitch CM, et al. (2008) Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum remodeling in Saccharomyces cerevisiae. Mol Biol Cell 19(10):4506-20	|BNI1 |BNR1 |CHO2 |ERG28 |ERV25 |HER1 |HER2 |HMG1 |HMG2 |HOF1 |HRD1 |NEM1 |OPI3 |PSD1 |MORE
Protein-protein Interactions	Goder V, et al. (2008) The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p. FEBS Lett 582(11):1575-80	|CDC48 |DER1 |DFM1 |HRD1 |HRD3 |NPL4 |SHP1 |UBX2 |UBX7 |UFD1 |USA1 |YOS9
Techniques and Reagents	Kamena F, et al. (2008) Ypt1p is essential for retrograde Golgi-ER transport and for Golgi maintenance in S. cerevisiae. J Cell Sci 121(Pt 8):1293-302	|ANP1 |ARF1 |BOS1 |EMP47 |MNN1 |SEC22 |SED5 |SLY1 |UFE1 |YPT1 |YPT31 |YPT32
Genetic Interactions Mutants/Phenotypes Protein Processing/Modification/Regulation RNA Levels and Processing Strains/Constructs	Liu Y and Chang A (2008) Heat shock response relieves ER stress. EMBO J 27(7):1049-59	|EMP24 |ERV29 |GAS1 |HRD1 |HSF1 |HSP150 |IRE1 |PEP4 |PHO8 |PRC1 |SVP26
Protein-protein Interactions	Makio T, et al. (2008) Identification and characterization of a Jem1p ortholog of Candida albicans: dissection of Jem1p functions in karyogamy and protein quality control in Saccharomyces cerevisiae. Genes Cells 13(10):1015-26	|JEM1 |MPS3 |SCJ1
Protein Sequence Features Techniques and Reagents	Merksamer PI, et al. (2008) Real-time redox measurements during endoplasmic reticulum stress reveal interlinked protein folding functions. Cell 135(5):933-47	|CYC1 |ERO1 |HAC1 |HRD1 |IRE1 |PDI1 |PRC1 |SEC61
RNA Levels and Processing Regulation of Transcription	Parikh BA, et al. (2008) Ricin Inhibits Activation of the Unfolded Protein Response by Preventing Splicing of the HAC1 mRNA. J Biol Chem 283(10):6145-53	|DER1 |HAC1
Cellular Location Genetic Interactions Regulation of Strains/Constructs	Schuldiner M, et al. (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134(4):634-45	|BOS1 |GET1 |GET2 |GET3 |GOS1 |PEP12 |PEX15 |SBH1 |SBH2 |SCS2 |SEC22 |SED5 |TLG2 |UBC6 |MORE
Protein Processing/Modification/Regulation	Seo HY, et al. (2008) Proteomic Analysis of Recombinant Saccharomyces cerevisiae Upon Iron Deficiency Induced via Human H-Ferritin Production. J Microbiol Biotechnol 18(8):1368-76	|ADK1 |ALD4 |ARA1 |ATP3 |CDC48 |GAL7 |GCD3 |GRE3 |HBN1 |HSP104 |HSP26 |HSP78 |IDH1 |IGO2 |MORE
Protein Processing/Modification/Regulation	Shen Y, et al. (2008) Mass spectrometry analysis of proteome-wide proteolytic post-translational degradation of proteins. Anal Chem 80(15):5819-28	|ACT1 |BFR1 |COF1 |FBA1 |HSP10 |NSP1 |NUP2 |OM45 |PGK1 |PRE2 |PRE3 |PUP1 |RPL3 |SRV2 |MORE
DNA/RNA Sequence Features Protein-Nucleic Acid Interactions	Shivaswamy S and Iyer VR (2008) Stress-dependent dynamics of global chromatin remodeling in yeast: dual role for SWI/SNF in the heat shock stress response. Mol Cell Biol 28(7):2221-34	|CHD1 |DDR2 |GLK1 |HSF1 |HSP82 |ISW1 |ISW2 |SNF2 |SPL2 |SSA1
Genetic Interactions Protein-protein Interactions Strains/Constructs	Takeuchi M, et al. (2008) Saccharomyces cerevisiae Rot1 Is an Essential Molecular Chaperone in the Endoplasmic Reticulum. Mol Biol Cell 19(8):3514-25	|DRS2 |GUP1 |KRE5 |KRE6 |ROT1 |UBC7
Reviews	Ydenberg CA and Rose MD (2008) Yeast mating: a model system for studying cell and nuclear fusion. Methods Mol Biol 475:3-20	|AGA1 |ASG7 |BEM1 |BIK1 |BIM1 |BNI1 |CDC24 |CDC42 |CHS3 |CHS5 |CIK1 |FAR1 |FIG1 |FIG2 |MORE
Alias Protein Processing/Modification/Regulation RNA Levels and Processing Regulation of	Zhang H, et al. (2008) The effect of calnexin deletion on the expression level of binding protein (BiP) under heat stress conditions in Saccharomyces cerevisiae. Cell Mol Biol Lett 13(4):621-31	|CNE1
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Carla Fama M, et al. (2007) The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum. Biochim Biophys Acta 1773(2):232-42	|ERJ5 |IRE1 |JEM1 |SCJ1
Reviews	Chen EH, et al. (2007) Cell-cell fusion. FEBS Lett 581(11):2181-93	|AGA1 |AGA2 |ASG7 |BIK1 |CDC42 |CDC48 |FAR1 |FIG1 |FUS1 |FUS2 |FUS3 |GPA1 |KAR3 |PRM1 |MORE
Evolution Fungal Related Genes/Proteins	Coronado JE, et al. (2007) Conserved processes and lineage-specific proteins in fungal cell wall evolution. Eukaryot Cell 6(12):2269-77	|ACF2 |AGA1 |AGA2 |ANS1 |BAR1 |BGL2 |BSC1 |CCW12 |CCW14 |CDA1 |CDA2 |CHS1 |CHS2 |CHS3 |MORE
Cross-species Expression Fungal Related Genes/Proteins Industrial Applications Strains/Constructs	Gasser B, et al. (2007) Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl Environ Microbiol 73(20):6499-507	|BFR2 |BMH2 |COG6 |COY1 |CUP5 |ERO1 |HAC1 |IMH1 |KIN2 |PDI1 |SEC31 |SSA4 |SSE1 |SSO2
Fungal Related Genes/Proteins	Georg Rde C and Gomes SL (2007) Comparative expression analysis of members of the Hsp70 family in the chytridiomycete Blastocladiella emersonii. Gene 386(1-2):24-34	|ECM10 |LHS1 |SSA1 |SSA2 |SSA3 |SSA4 |SSB1 |SSB2 |SSC1 |SSE1 |SSE2 |SSZ1
Cellular Location Function/Process	Han S, et al. (2007) Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1. J Biol Chem 282(36):26140-9	|HLJ1 |HSF1 |PMA1 |SSA1 |SSA2 |SSA3 |SSA4 |STE6 |YDJ1
Alias Protein-protein Interactions	Kimata Y, et al. (2007) Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J Cell Biol 179(1):75-86	|HAC1 |IRE1
RNA Levels and Processing Regulation of	Nakamura T, et al. (2007) EOS1, whose deletion confers sensitivity to oxidative stress, is involved in N-glycosylation in Saccharomyces cerevisiae. Biochem Biophys Res Commun 353(2):293-8	|EOS1
Protein-protein Interactions	Ng W, et al. (2007) Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120(Pt 4):682-91	|CDC48 |CUE1 |HRD1 |RPT1 |RPT3 |RPT5 |RPT6 |SBH1 |SEC61 |SEC62 |SEC63 |SEC72 |SSH1 |SSM4 |MORE
Protein-protein Interactions	Oikawa D, et al. (2007) Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1. J Cell Sci 120(Pt 9):1681-8	|HAC1 |IRE1
Mutants/Phenotypes Protein Sequence Features Protein-protein Interactions Protein/Nucleic Acid Structure Strains/Constructs Substrates/Ligands/Cofactors	Todd-Corlett A, et al. (2007) Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein response in Saccharomyces cerevisiae. J Mol Biol 367(3):770-87	|IRE1
Protein Physical Properties	White MA, et al. (2007) Characteristics affecting expression and solubilization of yeast membrane proteins. J Mol Biol 365(3):621-36	|ALG1 |ALG7 |APQ12 |AQY1 |ARE2 |ATG9 |ATP4 |BET1 |BIG1 |BOS1 |BRR6 |CAX4 |CHO1 |COS7 |MORE
Regulation of	de Groot MJ, et al. (2007) Quantitative proteomics and transcriptomics of anaerobic and aerobic yeast cultures reveals post-transcriptional regulation of key cellular processes. Microbiology 153(Pt 11):3864-3878	|ACO1 |ACO2 |ACS1 |ACS2 |ADE13 |ADE17 |ADE2 |ADE3 |ADE4 |ADE5,7 |ADE6 |ADH1 |ADH2 |ADH5 |MORE
Mutants/Phenotypes Strains/Constructs	Apodaca J, et al. (2006) Cellular tolerance of prion protein PrP in yeast involves proteolysis and the unfolded protein response. Biochem Biophys Res Commun 347(1):319-26	|CUE1 |DER1 |HRD1 |HRD3 |IRE1 |SSM4
Reviews	Boyce M and Yuan J (2006) Cellular response to endoplasmic reticulum stress: a matter of life or death. Cell Death Differ 13(3):363-73	|CDC48 |CUE1 |DER1 |GCN2 |GCN4 |HAC1 |HRD1 |HRD3 |IRE1 |PDI1 |SEC61 |UBC1 |UBC6 |UBC7
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
Evolution Fungal Related Genes/Proteins	De Hertogh B, et al. (2006) Emergence of species-specific transporters during evolution of the hemiascomycete phylum. Genetics 172(2):771-81	|AAC1 |AAC3 |ACS2 |ADP1 |ADY2 |AGC1 |AGP1 |AGP2 |AGP3 |ALP1 |ALR1 |ALR2 |ANT1 |AQR1 |MORE
Function/Process Protein-protein Interactions	Denic V, et al. (2006) A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation. Cell 126(2):349-59	|CDC48 |EMP47 |HRD1 |HRD3 |UBX2 |YOS9
Protein-protein Interactions	Fujita M, et al. (2006) Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins. Mol Biol Cell 17(2):834-50	|BST1 |GAS1
Function/Process Mutants/Phenotypes	Heiligenstein S, et al. (2006) Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD. EMBO J 25(20):4717-27	|CDC48 |DSK2 |HRD1 |JEM1 |NPL4 |PDI1 |PMR1 |RAD23 |RSP5 |SCJ1 |SPF1 |UBC1 |UBC4 |UBC6 |MORE
Regulation of Transcription	Jesch SA, et al. (2006) Multiple endoplasmic reticulum-to-nucleus signaling pathways coordinate phospholipid metabolism with gene expression by distinct mechanisms. J Biol Chem 281(33):24070-83	|ACC1 |CDS1 |CHO1 |CKI1 |CPT1 |FAA4 |FAS1 |FAS2 |HAC1 |INO1 |INO2 |ITR1 |MGA2 |OLE1 |MORE
Regulation of Transcription	Kumar A, et al. (2006) Homocysteine- and cysteine-mediated growth defect is not associated with induction of oxidative stress response genes in yeast. Biochem J 396(1):61-9	|CYS4 |FBA1 |HAC1 |MET13 |MET6 |STR2 |TDH2
Regulation of	Matsumoto R, et al. (2006) Search for novel stress-responsive protein components using a yeast mutant lacking two cytosolic Hsp70 genes, SSA1 and SSA2. Mol Cells 21(3):381-8	|ENO1 |ENO2 |FBA1 |HSC82 |HSP104 |HYP2 |SOD1 |SSA1 |SSA2 |SSA4 |STI1 |TDH3
Strains/Constructs Techniques and Reagents	Rakestraw A and Wittrup KD (2006) Contrasting secretory processing of simultaneously expressed heterologous proteins in Saccharomyces cerevisiae. Biotechnol Bioeng 93(5):896-905	|AGA2 |HAC1 |PDI1
Protein-protein Interactions Techniques and Reagents	Tagwerker C, et al. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48	|AAC1 |AAC3 |ACB1 |ACC1 |ACS2 |ADE3 |ADE5,7 |ADE6 |ADH4 |ADO1 |AGP1 |AHA1 |AHP1 |ALA1 |MORE
Function/Process Genetic Interactions Mutants/Phenotypes Protein-protein Interactions	Takeuchi M, et al. (2006) Causal links between protein folding in the ER and events along the secretory pathway. Autophagy 2(4):323-4	|ROT1
Genetic Interactions Protein-protein Interactions RNA Levels and Processing Regulation of	Takeuchi M, et al. (2006) Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding. J Biochem 139(3):597-605	|CNE1 |LHS1 |ROT1 |SCJ1
Cross-species Expression	Zhang W, et al. (2006) Enhanced Secretion of Heterologous Proteins in Pichia pastoris Following Overexpression of Saccharomyces cerevisiae Chaperone Proteins. Biotechnol Prog 22(4):1090-5	|PDI1 |SEC63 |SSA1 |YDJ1
Reviews	Anken E and Braakman I (2005) Endoplasmic reticulum stress and the making of a professional secretory cell. Crit Rev Biochem Mol Biol 40(5):269-83	|GCN4 |HAC1 |IRE1
Protein-protein Interactions	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 |EUG1 |MPD1 |MPD2 |PDI1
DNA/RNA Sequence Features Fungal Related Genes/Proteins	Liu YY, et al. (2005) Overexpression of an Anti-CD3 Immunotoxin Increases Expression and Secretion of Molecular Chaperone BiP/Kar2p by Pichia pastoris. Appl Environ Microbiol 71(9):5332-40
Regulation of Transcription	Matsumoto R, et al. (2005) The stress response against denatured proteins in the deletion of cytosolic chaperones SSA1/2 is different from heat-shock response in Saccharomyces cerevisiae. BMC Genomics 6():141	|CTT1 |DER1 |ERO1 |HSP104 |HSP26 |HSP78 |MRP8 |MRPL10 |PDI1 |PRE1 |RPL25 |RPL37A |RPL8B |RPN12 |MORE
RNA Levels and Processing Regulation of	Mendelsohn RD, et al. (2005) A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast. Biochim Biophys Acta 1723(1-3):33-44	|ALG3 |ALG5 |ALG6 |ALG7 |CHS1 |CNE1 |GPX2 |GSC2 |URA3 |YBR241C |YBR242W
Reviews	Nishikawa S, et al. (2005) Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). J Biochem 137(5):551-5
Reviews	Osborne AR, et al. (2005) Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol 21():529-50	|SBH1 |SBH2 |SEC61 |SSH1 |SSS1
DNA/RNA Sequence Features Function/Process Regulation of Transcription	Seppa L and Makarow M (2005) Regulation and recovery of functions of Saccharomyces cerevisiae chaperone BiP/Kar2p after thermal insult. Eukaryot Cell 4(12):2008-16	|HSP78 |LHS1
Fungal Related Genes/Proteins	Sims AH, et al. (2005) Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo. Appl Environ Microbiol 71(5):2737-47	|BCH2 |EPT1 |INO1 |NCE102 |RPT3 |SEC27 |SEC63 |SEC65 |SEC72 |SHR3 |SLC1 |SRP54 |UBA1
Other Features	Smith JD, et al. (2005) Elevated expression temperature in a mesophilic host results in increased secretion of a hyperthermophilic enzyme and decreased cell stress. Biochim Biophys Acta 1752(1):18-25
Function/Process Mutants/Phenotypes Strains/Constructs	Uchimura S, et al. (2005) Effects of N-glycosylation and inositol on the ER stress response in yeast Saccharomyces cerevisiae. Biosci Biotechnol Biochem 69(7):1274-80	|ALG6 |ALG8 |DIE2 |HAC1 |INO1
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Xu P, et al. (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab Eng 7(4):269-79	|IRE1 |PDI1
Techniques and Reagents	Bonza MC, et al. (2004) Functional expression in yeast of an N-deleted form of At-ACA8, a plasma membrane Ca(2+)-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant. Planta 218(5):814-23
Non-Fungal Related Genes/Proteins	Elkabetz Y, et al. (2004) Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: roles of endoplamic reticulum-bound p97/Cdc48p and proteasome. J Biol Chem 279(6):3980-9	|CDC48
Genetic Interactions	Huyer G, et al. (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J Biol Chem 279(37):38369-78	|CDC48 |HLJ1 |HRD1 |SEC61 |SSA1 |SSH1 |SSM4 |STE6 |YDJ1
Regulation of Transcription	Ichimura T, et al. (2004) Transcriptomic and proteomic analysis of a 14-3-3 gene-deficient yeast. Biochemistry 43(20):6149-58	|ACO1 |ADE4 |ALD4 |ARG3 |ARG8 |ASN1 |ASN2 |BMH1 |BMH2 |CAR2 |CIT1 |CIT2 |FAS2 |GCV3 |MORE
Reviews	Kimata Y and Kohno K (2004) [How is ER stress sensed?] Tanpakushitsu Kakusan Koso 49(7 Suppl):998-1001	|IRE1
Function/Process Genetic Interactions Mutants/Phenotypes Protein-protein Interactions Strains/Constructs Techniques and Reagents	Kimata Y, et al. (2004) A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J Cell Biol 167(3):445-56	|IRE1
Fungal Related Genes/Proteins	Lahav R, et al. (2004) Alterations in protein synthesis and levels of heat shock 70 proteins in response to salt stress of the halotolerant yeast Rhodotorula mucilaginosa. Antonie Van Leeuwenhoek 85(4):259-69	|PDI1 |SSB1 |SSB2
Non-Fungal Related Genes/Proteins	Nikolaidis N and Nei M (2004) Concerted and nonconcerted evolution of the Hsp70 gene superfamily in two sibling species of nematodes. Mol Biol Evol 21(3):498-505	|LHS1 |SSA1 |SSA2 |SSA3 |SSA4 |SSC1 |SSE1 |SSE2 |SSQ1 |SSZ1
Regulation of Transcription	Ogawa N and Mori K (2004) Autoregulation of the HAC1 gene is required for sustained activation of the yeast unfolded protein response. Genes Cells 9(2):95-104	|HAC1
Cellular Location Strains/Constructs	Otte S and Barlowe C (2004) Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles. Nat Cell Biol 6(12):1189-94	|ERV29
Function/Process Techniques and Reagents	Plath K, et al. (2004) Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum. Mol Biol Cell 15(1):1-10	|SEC61 |SEC62 |SEC66 |SEC72
Function/Process Mutants/Phenotypes Strains/Constructs	Smith JD, et al. (2004) Protein disulfide isomerase, but not binding protein, overexpression enhances secretion of a non-disulfide-bonded protein in yeast. Biotechnol Bioeng 85(3):340-50
Function/Process Protein Physical Properties Protein-protein Interactions Regulation of Regulatory Role Strains/Constructs	Steel GJ, et al. (2004) Coordinated activation of Hsp70 chaperones. Science 303(5654):98-101	|IRE1 |LHS1 |SEC63 |SIL1
DNA/RNA Sequence Features RNA Levels and Processing Regulation of	Aburatani S, et al. (2003) Discovery of novel transcription control relationships with gene regulatory networks generated from multiple-disruption full genome expression libraries. DNA Res 10(1):1-8	|ACO1 |ACS1 |AGA1 |ARG3 |ARG4 |CAR1 |CAR2 |CPA2 |CRC1 |DAL1 |DMC1 |FRE1 |HEM3 |HOP1 |MORE
Strains/Constructs	Butz JA, et al. (2003) Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast. Biotechnol Bioeng 84(3):292-304
Cellular Location	Fu L and Sztul E (2003) Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator. J Cell Biol 160(2):157-63	|SAR1 |SEC12 |SEC13 |SEC23
RNA Levels and Processing Regulation of	Heikkinen HL, et al. (2003) Initiation-mediated mRNA decay in yeast affects heat-shock mRNAs, and works through decapping and 5'-to-3' hydrolysis. Nucleic Acids Res 31(14):4006-16	|DCP1 |HSC82 |HSP82 |KEM1 |NAM7 |NMD2 |PRT1 |SSA1 |SSA3 |SSC1
Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Protein-protein Interactions Protein/Nucleic Acid Structure Strains/Constructs Substrates/Ligands/Cofactors	Kabani M, et al. (2003) Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. Mol Biol Cell 14(8):3437-48	|JEM1 |SEC63
Function/Process Protein Sequence Features Protein-protein Interactions Regulatory Role Strains/Constructs	Kimata Y, et al. (2003) Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins. Mol Biol Cell 14(6):2559-69	|IRE1
Reviews	Kostova Z and Wolf DH (2003) For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J 22(10):2309-17	|CDC48 |HRD3 |IRE1 |MNL1 |MNS1 |SEC61 |UBC7
Function/Process Mutants/Phenotypes Strains/Constructs	Lee K, et al. (2003) The unfolded protein response is required for haploid tolerance in yeast. J Biol Chem 278(14):11818-27	|HAC1 |IRE1
DNA/RNA Sequence Features Regulation of Transcription	Norgaard P, et al. (2003) Gene regulation in response to protein disulphide isomerase deficiency. Yeast 20(7):645-52	|ERO1 |MPD1 |MPD2 |PDI1
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Palmer EA, et al. (2003) Differential requirements of novel A1PiZ degradation deficient (ADD) genes in ER-associated protein degradation. J Cell Sci 116(Pt 11):2361-73	|ADD37 |ADD66 |CSR1 |DOG2 |ERV29 |SWP82 |URH1
Function/Process Mutants/Phenotypes Strains/Constructs Substrates/Ligands/Cofactors	Taxis C, et al. (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J Biol Chem 278(38):35903-13	|CDC48 |CWC23 |DER1 |HLJ1 |HRD1 |HRD3 |HSP104 |JID1 |NPL4 |SSA1 |SSA2 |SSA3 |SSA4 |UBC1 |MORE
Regulation of Transcription	Valkonen M, et al. (2003) Effects of inactivation and constitutive expression of the unfolded- protein response pathway on protein production in the yeast Saccharomyces cerevisiae. Appl Environ Microbiol 69(4):2065-72	|HAC1
Function/Process Mutants/Phenotypes Strains/Constructs Techniques and Reagents	Yabal M, et al. (2003) Translocation of the C terminus of a tail-anchored protein across the endoplasmic reticulum membrane in yeast mutants defective in signal peptide-driven translocation. J Biol Chem 278(5):3489-96	|LHS1 |SBH1 |SBH2 |SEC61 |SEC62 |SEC63
Cellular Location	Ferreira T, et al. (2002) Quality control in the yeast secretory pathway: a misfolded PMA1 H+-ATPase reveals two checkpoints. J Biol Chem 277(23):21027-40	|PEP4 |PMA1 |SLA2
RNA Levels and Processing Regulation of	Hyde M, et al. (2002) Induction of secretory pathway components in yeast is associated with increased stability of their mRNA. J Cell Biol 156(6):993-1001	|INO1 |IRE1 |SEC61
Function/Process Regulation of	Kabani M, et al. (2002) Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol Cell Biol 22(13):4677-89	|FES1 |SIL1 |SSA1 |YDJ1
Regulation of Transcription	Song Y, et al. (2002) Different effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of two glycosylated amyloidogenic lysozymes. FEBS Lett 512(1-3):213-7	|CNE1 |PDI1
Function/Process	Steel GJ, et al. (2002) Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery. Biochemistry 41(39):11914-20	|SEC61 |SSH1
Cellular Location	Taxis C, et al. (2002) ER-golgi traffic is a prerequisite for efficient ER degradation. Mol Biol Cell 13(6):1806-18	|DER1 |HRD1 |HRD3 |SEC12 |SEC18 |SEC23 |SED5 |UFE1
Cellular Location Protein-protein Interactions	Wittke S, et al. (2002) Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae. Mol Biol Cell 13(7):2223-32	|MF(ALPHA)1 |PRC1 |SEC61 |SSH1 |SUC2
Fungal Related Genes/Proteins	van der Heide M, et al. (2002) Overproduction of BiP negatively affects the secretion of Aspergillus niger glucose oxidase by the yeast Hansenula polymorpha. Appl Microbiol Biotechnol 58(4):487-94
Cellular Location Protein-protein Interactions	Andag U, et al. (2001) The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem 276(42):39150-60	|COP1 |DSL1 |ERD2 |SEC20 |SEC22 |TIP20
Cellular Location Regulation of	Belden WJ and Barlowe C (2001) Deletion of yeast p24 genes activates the unfolded protein response. Mol Biol Cell 12(4):957-69	|EMP24 |ERD2 |ERV25 |IRE1
Reviews	Imaizumi K, et al. (2001) The unfolded protein response and Alzheimer's disease. Biochim Biophys Acta 1536(2-3):85-96	|IRE1
Function/Process Protein-protein Interactions Techniques and Reagents	Morrow MW and Brodsky JL (2001) Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180. Traffic 2(10):705-16	|SBH1 |SEC61 |SEC62 |SEC63 |SEC66 |SEC72 |SSS1 |TEF2
Protein Processing/Modification/Regulation	Mutka SC and Walter P (2001) Multifaceted physiological response allows yeast to adapt to the loss of the signal recognition particle-dependent protein-targeting pathway. Mol Biol Cell 12(3):577-88
Function/Process Mutants/Phenotypes Strains/Constructs	Nishikawa SI, et al. (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J Cell Biol 153(5):1061-70	|JEM1 |SCJ1 |SEC61 |SEC63
Cellular Location	Paunola E, et al. (2001) Inhibition of translocation of beta -lactamase into the yeast endoplasmic reticulum by covalently bound benzylpenicillin. J Biol Chem 276(37):34553-9
Function/Process Techniques and Reagents	Reilly BA, et al. (2001) Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol Biol Cell 12(12):3783-96	|DSL1 |RET2 |SEC20 |SLY1 |TIP20 |UFE1
Function/Process RNA Levels and Processing Regulation of	Song Y, et al. (2001) Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J Biochem 130(6):757-64	|CNE1 |PDI1
Regulation of	Suzuki C (2001) Immunochemical and mutational analyses of P-type ATPase Spf1p involved in the yeast secretory pathway. Biosci Biotechnol Biochem 65(11):2405-11	|OCH1 |SEC12 |SPF1
Cellular Location Function/Process Protein-protein Interactions	Young BP, et al. (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20(1-2):262-71	|SEC62 |SEC63 |SEC65 |SEC66 |SEC72
Function/Process	Zhang Y, et al. (2001) Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol Biol Cell 12(5):1303-14	|SSA1 |SSA2 |SSA3 |SSA4 |UBC6 |UBC7
Reviews	van Laar T, et al. (2001) Mif1: a missing link between the unfolded protein response pathway and ER-associated protein degradation? Curr Protein Pept Sci 2(2):169-90	|HAC1 |HRD1 |HRD3 |IRE1 |MAS1 |UBC6
Function/Process Strains/Constructs	Bannister SJ and Wittrup KD (2000) Glutathione excretion in response to heterologous protein secretion in Saccharomyces cerevisiae. Biotechnol Bioeng 68(4):389-95
Function/Process Genetic Interactions RNA Levels and Processing Regulation of Strains/Constructs	Casagrande R, et al. (2000) Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol Cell 5(4):729-35	|ERO1 |HAC1 |IRE1 |LHS1 |PDI1
Cellular Location	Chen J and Ahlquist P (2000) Brome mosaic virus polymerase-like protein 2a is directed to the endoplasmic reticulum by helicase-like viral protein 1a. J Virol 74(9):4310-8
Protein Sequence Features Protein-protein Interactions	Chevalier M, et al. (2000) Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1. J Biol Chem 275(26):19620-7	|SEC63 |YDJ1
Function/Process Other Features	Eisfeld K, et al. (2000) Endocytotic uptake and retrograde transport of a virally encoded killer toxin in yeast. Mol Microbiol 37(4):926-40	|CNE1 |END3 |ERD1 |ERD2 |KEX1 |SEC61 |SLA2
Non-Fungal Related Genes/Proteins	Kabani M, et al. (2000) A highly representative two-hybrid genomic library for the yeast Yarrowia lipolytica. Gene 241(2):309-15	|SIL1
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Protein-protein Interactions Strains/Constructs	Kabani M, et al. (2000) Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum. Mol Cell Biol 20(18):6923-34	|MGE1 |SEC63 |SIL1
Fungal Related Genes/Proteins	Kim K and Ogrydziak DM (2000) Yarrowia lipolytica SRP receptor alpha-subunit. Yeast 16(13):1243-52	|SRP101
Cellular Location	Muniz M, et al. (2000) The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 148(5):925-30	|EMP24 |ERV25 |GAP1 |GAS1
Function/Process Genetic Interactions Strains/Constructs	Ng DT, et al. (2000) The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control. J Cell Biol 150(1):77-88	|GAS1 |GPI10 |HAC1 |IRE1 |LHS1 |MCD4 |PER1 |PRC1 |RFT1 |RPN4 |SEC61 |