ROT2/YBR229C Single Page Format

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SGD Locus Page

Names and Identifiers [TOP] [NEXT] Help
Standard Name Systematic Name Alias Feature Type SGDID
ROT2 YBR229C GLS2 ORF, Verified S000000433
Description
Glucosidase II catalytic subunit required for normal cell wall synthesis; mutations in rot2 suppress tor2 mutations, and are synthetically lethal with rot1 mutations

GO Annotations [TOP] [NEXT] Help
Molecular Function
Annotation(s)Reference(s)EvidenceAssigned By
alpha-glucosidase activitySimons JF, et al. (1998) Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p. EMBO J 17(2):396-405
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
IDA : Inferred from Direct Assay
Assigned on 2006-01-19
SGD
glucan 1,3-alpha-glucosidase activityGOA curators and MGI curators (2001) Gene Ontology annotation based on Enzyme Commission mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with IUBMB:3.2.1.84
Assigned on 2008-02-13
UniProtKB
hydrolase activityGOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:KW-0378
Assigned on 2007-05-23
UniProtKB
hydrolase activity, acting on glycosyl bondsGOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:KW-0326
Assigned on 2007-05-23
UniProtKB
hydrolase activity, hydrolyzing O-glycosyl compoundsDDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:IPR000322
Assigned on 2007-05-23
UniProtKB
Biological Process
Annotation(s)Reference(s)EvidenceAssigned By
carbohydrate metabolic processDDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:IPR000322
Assigned on 2009-10-01
UniProtKB
fungal-type cell wall biogenesisSimons JF, et al. (1998) Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p. EMBO J 17(2):396-405
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
IMP : Inferred from Mutant Phenotype
Assigned on 2002-07-08
SGD
metabolic processGOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:KW-0326
Assigned on 2007-05-23
UniProtKB
Cellular Component
Annotation(s)Reference(s)EvidenceAssigned By
alpha-glucosidase II complexWilkinson BM, et al. (2006) Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J Biol Chem 281(10):6325-33
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
IPI : Inferred from Physical Interaction with SGD:GTB1
Assigned on 2008-01-03
SGD
endoplasmic reticulumTrombetta ES, et al. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem 271(44):27509-16
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
ISS : Inferred from Sequence or structural Similarity
Assigned on 2002-07-08
SGD
GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:KW-0256
Assigned on 2007-05-23
UniProtKB
GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.
SGD Papers Entry  Reference full text  
IEA : Inferred from Electronic Annotation with EBI:SL-0095
Assigned on 2008-02-13
UniProtKB
endoplasmic reticulum lumenWilkinson BM, et al. (2006) Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J Biol Chem 281(10):6325-33
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
IDA : Inferred from Direct Assay
Assigned on 2006-01-19
SGD
mitochondrionSickmann A, et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
SGD Papers Entry  Pubmed Entry  Web Supplement  yfgdb  
IDA : Inferred from Direct Assay
Assigned on 2004-09-28
SGD
Reinders J, et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Web Supplement  yfgdb  
IDA : Inferred from Direct Assay
Assigned on 2006-12-12
SGD

Pathways [TOP] [NEXT] Help
No pathways available

Summary Paragraph [TOP] [NEXT] Help
SUMMARY PARAGRAPH for ROT2/YBR229C for ROT2
During N-linked glycosylation of proteins, oligosaccharide chains are assembled on the carrier molecule dolichyl pyrophosphate in the following order: 2 molecules of N-acetylglucosamine (GlcNAc), 9 molecules of mannose, and 3 molecules of glucose. These 14-residue oligosaccharide cores are then transferred to asparagine residues on nascent polypeptide chains in the endoplasmic reticulum (ER). As proteins progress through the Golgi apparatus, the oligosaccharide cores are modified by trimming and extension to generate a diverse array of glycosylated proteins (reviewed in 1, 2).

ROT2, also known as GLS2, encodes glucosidase II, a lumenal enzyme of the ER. After Cwh41p (glucosidase I) removes the most distal glucose from N-linked oligosaccharides (3), Rot2p trims the two remaining glucose moieties previously added by Alg8p and Alg6p. Human (OMIM) and rat glucosidase II each consist of two subunits: a catalytic alpha subunit, which is the homolog of ROT2, and a beta subunit whose putative role is to target the enzyme to the ER (3, 4). While no beta subunit has been identified in yeast, Rot2p lacks an obvious transmembrane domain or ER retention signal (3). (Note: humans have a second, unrelated glucosidase II (OMIM) involved in glycogen metabolism.)

Mutants lacking Rot2p have no detectable growth defect (3) but have reduced levels of beta-1,6-glucan (5) and elevated levels of chitin (6) in the cell walls. In mutants lacking Rot2p, removal of the outermost glucose from N-linked oligosaccharides proceeds at normal rates, and one mannose moiety is removed at greatly reduced rates (7). Also drastically slowed is the degradation of misfolded glycosylated proteins (7).

Last Updated: 2005-07-12

Basic References [TOP]   Help
BASIC INFORMATION REFERENCES forROT2/YBR229C for ROT2
1)Herscovics A and Orlean P (1993) Glycoprotein biosynthesis in yeast. FASEB J 7(6):540-50
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
2)Burda P and Aebi M (1999) The dolichol pathway of N-linked glycosylation. Biochim Biophys Acta 1426(2):239-57
SGD Papers Entry  Pubmed Entry  
3)Trombetta ES, et al. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem 271(44):27509-16
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
4)Pelletier MF, et al. (2000) The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology 10(8):815-27
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
5)Simons JF, et al. (1998) Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p. EMBO J 17(2):396-405
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
6)Bickle M, et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J 17(8):2235-45
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
7)Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33
SGD Papers Entry  Pubmed Entry  Reference LINKOUT  

Mutant Phenotypes [TOP] [NEXT] Help
Phenotype page for ROT2/YBR229C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT] Help
Interaction page for ROT2/YBR229C

Homologs [TOP] [NEXT] Help
  • Comparison Resources
  • Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT] Help
    Protein Sequence Calculations
    from Predicted Full length Translation
    N-term MVLLKWL
    C-term EDWEVIF
    Length(aa) 954
    MW(Da) 110,265
    pI 6.11
    Amino Acid Composition (full length)
    GCG tools: PepPlot, Helical Wheel, PepStruct

    Transcript Translation Calculations
    Codon Bias 0.107  
    Codon Adaptation Index 0.167  
    Frequency of Optimal Codons 0.485  
    Hydropathicity of Protein -0.336  
    Aromaticity Score 0.129  

                              10        20        30        40        50
                               |         |         |         |         |
                      MVLLKWLVCQLVFFTAFSHAFTDYLLKKCAQSGFCHRNRVYAENIAKSHH
                      CYYKVDAESIAHDPLENVLHATIIKTIPRLEGDDIAVQFPFSLSFLQDHS
                      VRFTINEKERMPTNSSGLLISSQRFNETWKYAFDKKFQEEANRTSIPQFH
                      FLKQKQTVNSFWSKISSFLSLSNSTADTFHLRNGDVSVEIFAEPFQLKVY
                      WQNALKLIVNEQNFLNIEHHRTKQENFAHVLPEETTFNMFKDNFLYSKHD
                      SMPLGPESVALDFSFMGSTNVYGIPEHATSLRLMDTSGGKEPYRLFNVDV
                      FEYNIGTSQPMYGSIPFMFSSSSTSIFWVNAADTWVDIKYDTSKNKTMTH
                      WISENGVIDVVMSLGPDIPTIIDKFTDLTGRPFLPPISSIGYHQCRWNYN
                      DEMDVLTVDSQMDAHMIPYDFIWLDLEYTNDKKYFTWKQHSFPNPKRLLS
                      KLKKLGRNLVVLIDPHLKKDYEISDRVINENVAVKDHNGNDYVGHCWPGN
                      SIWIDTISKYGQKIWKSFFERFMDLPADLTNLFIWNDMNEPSIFDGPETT
                      APKDLIHDNYIEERSVHNIYGLSVHEATYDAIKSIYSPSDKRPFLLTRAF
                      FAGSQRTAATWTGDNVANWDYLKISIPMVLSNNIAGMPFIGADIAGFAED
                      PTPELIARWYQAGLWYPFFRAHAHIDTKRREPYLFNEPLKSIVRDIIQLR
                      YFLLPTLYTMFHKSSVTGFPIMNPMFIEHPEFAELYHIDNQFYWSNSGLL
                      VKPVTEPGQSETEMVFPPGIFYEFASLHSFINNGTDLIEKNISAPLDKIP
                      LFIEGGHIITMKDKYRRSSMLMKNDPYVIVIAPDTEGRAVGDLYVDDGET
                      FGYQRGEYVETQFIFENNTLKNVRSHIPENLTGIHHNTLRNTNIEKIIIA
                      KNNLQHNITLKDSIKVKKNGEESSLPTRSSYENDNKITILNLSLDITEDW
                      EVIF*
    

    Protein Structures from PDB: proteins of known structure with sequence similarity to ROT2/YBR229C, based on Smith-Waterman analysis. [TOP] [NEXT] Help
    PDB protein structure(s) homologous to ROT2Homolog Source (per PDB)Protein Alignment: ROT2 vs. HomologExternal Links
    P-Value%Identical%SimilarAlignment
    2qly ( Chain: A)
    Crystral structure of the n-terminal subunit of human maltase-glucoamylase
  • PDB_Info
  • PDB_Structure
  • Homo sapiens3.9e-572927View alignmentSCOP
    MMDB
    CATH
    2qmj ( Chain: A)
    Crystral structure of the n-terminal subunit of human maltase-glucoamylase in complex with acarbose
  • PDB_Info
  • PDB_Structure
  • Homo sapiens3.9e-572927View alignmentSCOP
    MMDB
    CATH
    3ctt ( Chain: A)
    Crystal complex of n-terminal human maltase-glucoamylase with casuarine
  • PDB_Info
  • PDB_Structure
  • Homo sapiens3.9e-572927View alignmentSCOP
    MMDB
    CATH
    2g3m ( Chain: C, A, B, F, E, D)
    Crystal structure of the sulfolobus solfataricus alpha- glucosidase mala
  • PDB_Info
  • PDB_Structure
  • Sulfolobus solfataricusChain C = 3.0e-502933View alignmentSCOP
    MMDB
    CATH
    Chain A = 3.0e-502933View alignment
    Chain B = 3.0e-502933View alignment
    Chain F = 3.0e-502933View alignment
    Chain E = 3.0e-502933View alignment
    Chain D = 3.0e-502933View alignment
    2g3n ( Chain: A, B, C, E, F, D)
    Crystal structure of the sulfolobus solfataricus alpha- glucosidase mala in complex with beta-octyl-glucopyranoside
  • PDB_Info
  • PDB_Structure
  • Sulfolobus solfataricusChain A = 3.0e-502933View alignmentSCOP
    MMDB
    CATH
    Chain B = 3.0e-502933View alignment
    Chain C = 3.0e-502933View alignment
    Chain E = 3.0e-502933View alignment
    Chain F = 3.0e-502933View alignment
    Chain D = 3.0e-502933View alignment
    3ffj ( Chain: A, B)
    The crystal structure of the glycosyl hydrolase (family 31) from ruminococcus obeum atcc 29174
  • PDB_Info
  • PDB_Structure
  • Ruminococcus obeum ATCC 29174Chain A = 2.1e-402733View alignmentSCOP
    MMDB
    CATH
    Chain B = 2.1e-402733View alignment
    1we5 ( Chain: B, E, A, C, D, F)
    Crystal structure of alpha-xylosidase from escherichia coli
  • PDB_Info
  • PDB_Structure
  • Escherichia coliChain B = 8.4e-252433View alignmentSCOP
    MMDB
    CATH
    Chain E = 8.4e-252433View alignment
    Chain A = 8.4e-252433View alignment
    Chain C = 8.4e-252433View alignment
    Chain D = 8.4e-252433View alignment
    Chain F = 8.4e-252433View alignment
    2f2h ( Chain: A, F, E, C, B, D)
    Structure of the yici thiosugar michaelis complex
  • PDB_Info
  • PDB_Structure
  • Escherichia coliChain A = 8.4e-252433View alignmentSCOP
    MMDB
    CATH
    Chain F = 8.4e-252433View alignment
    Chain E = 8.4e-252433View alignment
    Chain C = 8.4e-252433View alignment
    Chain B = 8.4e-252433View alignment
    Chain D = 8.4e-252433View alignment
    1xsi ( Chain: D, E, B, C, F, A)
    Structure of a family 31 alpha glycosidase
  • PDB_Info
  • PDB_Structure
  • Escherichia coliChain D = 8.5e-252433View alignmentSCOP
    MMDB
    CATH
    Chain E = 8.5e-252433View alignment
    Chain B = 8.5e-252433View alignment
    Chain C = 8.5e-252433View alignment
    Chain F = 8.5e-252433View alignment
    Chain A = 8.5e-252433View alignment
    1xsj ( Chain: A, F, B, C, D, E)
    Structure of a family 31 alpha glycosidase
  • PDB_Info
  • PDB_Structure
  • Escherichia coliChain A = 8.5e-252433View alignmentSCOP
    MMDB
    CATH
    Chain F = 8.5e-252433View alignment
    Chain B = 8.5e-252433View alignment
    Chain C = 8.5e-252433View alignment
    Chain D = 8.5e-252433View alignment
    Chain E = 8.5e-252433View alignment
    1xsk ( Chain: E, C, F, D, B, A)
    Structure of a family 31 alpha glycosidase glycosyl-enzyme intermediate
  • PDB_Info
  • PDB_Structure
  • Escherichia coliChain E = 8.5e-252433View alignmentSCOP
    MMDB
    CATH
    Chain C = 8.5e-252433View alignment
    Chain F = 8.5e-252433View alignment
    Chain D = 8.5e-252433View alignment
    Chain B = 8.5e-252433View alignment
    Chain A = 8.5e-252433View alignment

    Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT] Help
  • Functional Analysis
  • 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] Help
    Nomenclature History
    Standard NameReference
    ROT2SGD (2007) Information without a citation in SGD
    SGD Papers Entry  

    Sequence Retrieval [TOP] [NEXT] Help
    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
  • Sequence from other databases
    Sequence IDSource
    YBR229CSGD Systematic Sequence
    852530NCBI: Gene ID
    NP_009788.1NCBI: RefSeq protein version ID
    NP_009788.1NCBI: RefSeq protein version ID
    6319706NCBI: NCBI protein GI

    Map and Displays [TOP] [NEXT] Help
    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] Help
  • Localization Resources
  • Community Annotation [TOP] [NEXT] Help
    No community annotation available.

    Literature Guide: papers categorized by topic. [TOP]   Help
    TopicsReferenceOther Genes Addressed
    35 curated references; 0 references not yet curated
    Alias
    Genetic Interactions
    Mutants/Phenotypes
    Strains/Constructs
    Clerc S, et al. (2009) Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum. J Cell Biol 184(1):159-72
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
    |ALG12 |ALG3 |ALG8 |ALG9 |MNL1 |MNS1 |PDI1 |PRC1 |YOS9
    Mutants/Phenotypes
    Regulation of
    Strains/Constructs
    Quinn RP, et al. (2009) A novel role for Gtb1p in glucose trimming of N-linked glycans. Glycobiology 19(12):1408-16
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG8 |CWH41 |GTB1 |MNS1
    Large-scale phenotype analysis
    Tan SX, et al. (2009) Cu, Zn superoxide dismutase and NADP(H) homeostasis are required for tolerance of endoplasmic reticulum stress in Saccharomyces cerevisiae. Mol Biol Cell 20(5):1493-508
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |AAT2 |ADO1 |AIM26 |ALG7 |ARO2 |BCK1 |BUR2 |CCS1 |CNB1 |CNM67 |CRZ1 |CSG2 |ELP2 |ERG2 |MORE
    Alias
    Fungal Related Genes/Proteins
    Deshpande N, et al. (2008) Protein glycosylation pathways in filamentous fungi. Glycobiology 18(8):626-37
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG1 |ALG11 |ALG12 |ALG13 |ALG14 |ALG2 |ALG3 |ALG6 |ALG7 |ALG8 |ALG9 |ANP1 |CWH41 |DIE2 |MORE
    Mutants/Phenotypes
    Herrero AB, et al. (2008) Levels of SCS7/FA2H-Mediated Fatty Acid 2-Hydroxylation Determine the Sensitivity of Cells to Antitumor PM02734. Cancer Res 68(23):9779-87
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |AIM44 |ALD6 |ALG6 |API2 |APL1 |APL5 |APM3 |ATP15 |ATP4 |ATP5 |ATP7 |BRE5 |BST1 |CAT5 |MORE
    Reviews
    Jigami Y (2008) Yeast glycobiology and its application. Biosci Biotechnol Biochem 72(3):637-48
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG1 |ALG11 |ALG12 |ALG13 |ALG14 |ALG2 |ALG3 |ALG5 |ALG6 |ALG7 |ALG8 |ALG9 |ANP1 |CWH41 |MORE
    Mutants/Phenotypes
    Loukin S, et al. (2008) A genome-wide survey suggests an osmoprotective role for vacuolar Ca2+ release in cell wall-compromised yeast. FASEB J 22(7):2405-15
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG5 |ALG6 |ALG8 |BST1 |CSF1 |DIE2 |GAS1 |GDA1 |GUP1 |HHY1 |HUR1 |KRE1 |KRE6 |LAS21 |MORE
    Mutants/Phenotypes
    Non-Fungal Related Genes/Proteins
    McCue PP and Phang JM (2008) Identification of Human Intracellular Targets of the Medicinal Herb St. John's Wort by Chemical-Genetic Profiling in Yeast. J Agric Food Chem 56(22):11011-11017
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ABD1 |ACS1 |ADP1 |AHC1 |APN2 |ASR1 |ATP5 |BCK2 |BFR1 |CBP6 |CHK1 |CIN8 |CRR1 |CTF19 |MORE
    Fungal Related Genes/Proteins
    Mora-Montes HM, et al. (2007) Endoplasmic Reticulum {alpha}-Glycosidases of Candida albicans Are Required for N Glycosylation, Cell Wall Integrity, and Normal Host-Fungus Interaction. Eukaryot Cell 6(12):2184-93
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |CWH41 |MNS1
    Regulatory Role
    Transcription
    Wu D, et al. (2007) Covert genetic selections to optimize phenotypes. PLoS ONE 2(11):e1200
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
    |BET2 |EGD2 |FUN12 |LSM3 |MLC2 |RPL5 |RPS9A |RPS9B |SFB2 |SLM1 |UTP10
    Reviews
    Lesage G and Bussey H (2006) Cell wall assembly in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70(2):317-43
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ANP1 |BGL2 |BIG1 |CDA1 |CDA2 |CHS1 |CHS2 |CHS3 |CHS6 |CHS7 |CNE1 |CRH1 |CRR1 |CTS1 |MORE
    Cellular Location
    Reinders J, et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Web Supplement  yfgdb  
    |AAC1 |AAC3 |AAT1 |ABC1 |ABF2 |ACC1 |ACH1 |ACK1 |ACN9 |ACO1 |ACO2 |ACP1 |ACS1 |ADH3 |MORE
    Protein-protein Interactions
    Welsh LM, et al. (2006) Genetic and molecular interactions of the Erv41p-Erv46p complex involved in transport between the endoplasmic reticulum and Golgi complex. J Cell Sci 119(Pt 22):4730-40
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  yfgdb  
    |ERV41 |ERV46 |VMA21 |VMA22 |VPH2 |VPS1
    Cellular Location
    Function/Process
    Mutants/Phenotypes
    Protein-protein Interactions
    Strains/Constructs
    Wilkinson BM, et al. (2006) Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum. J Biol Chem 281(10):6325-33
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |GTB1
    Regulatory Role
    Gardocki ME, et al. (2005) Genomic analysis of PIS1 gene expression. Eukaryot Cell 4(3):604-14
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  yfgdb  
    |AAD4 |ACB1 |ACE2 |ADH2 |APT1 |ATG17 |ATG19 |ATG27 |ATG29 |BAS1 |CIK1 |COQ4 |CPD1 |CPS1 |MORE
    Cross-species Expression
    Schirawski J, et al. (2005) Endoplasmic reticulum glucosidase II is required for pathogenicity of Ustilago maydis. Plant Cell 17(12):3532-43
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ROT1
    Function/Process
    Genetic Interactions
    Schuldiner M, et al. (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Web Supplement  yfgdb  SGD Curated Comments & Errata
    |ALG12 |ALG3 |ALG5 |ALG6 |ALG8 |ALG9 |API2 |APL5 |APL6 |APM3 |APS3 |ARL1 |ARL3 |ARV1 |MORE
    Non-Fungal Related Genes/Proteins
    Other Features
    Tomich CH, et al. (2005) Homology modeling and molecular interaction field studies of alpha-glucosidases as a guide to structure-based design of novel proposed anti-HIV inhibitors. J Comput Aided Mol Des 19(2):83-92
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
    |CWH41
    Function/Process
    Genetic Interactions
    Mutants/Phenotypes
    Strains/Constructs
    Hitt R and Wolf DH (2004) DER7, encoding alpha-glucosidase I is essential for degradation of malfolded glycoproteins of the endoplasmic reticulum. FEMS Yeast Res 4(8):815-20
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
    |CWH41
    Genetic Interactions
    Strains/Constructs
    Tong AH, et al. (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Web Supplement  yfgdb  
    |AAD4 |AAH1 |ABF2 |ACE2 |ADH6 |AEP2 |AFG1 |AGP1 |AHC1 |AHC2 |AIM21 |AIM22 |AIM26 |AIM29 |MORE
    Cellular Location
    Sickmann A, et al. (2003) The proteome of Saccharomyces cerevisiae mitochondria. Proc Natl Acad Sci U S A 100(23):13207-12
    SGD Papers Entry  Pubmed Entry  Web Supplement  yfgdb  
    |AAC1 |AAC3 |AAT1 |ABC1 |ABF2 |ACC1 |ACH1 |ACK1 |ACO1 |ACO2 |ACP1 |ACS1 |ADH3 |ADK2 |MORE
    Function/Process
    Mutants/Phenotypes
    Strains/Constructs
    Avaro S, et al. (2002) Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants. Yeast 19(4):351-71
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  
    |ALG12 |ALG9 |APM3 |ERV29 |GAS1 |MON2 |OST2 |OST4 |RCY1 |SYS1 |TLG2 |VAC7 |VAM6 |VPS53 |MORE
    Function/Process
    Mutants/Phenotypes
    Strains/Constructs
    de Groot PW, et al. (2001) A genomic approach for the identification and classification of genes involved in cell wall formation and its regulation in Saccharomyces cerevisiae. Comp Funct Genomics 2(3):124-42
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  Reference LINKOUT  
    |AAD4 |AIM22 |ALG12 |ALK2 |ARE2 |ARG2 |ARP5 |ASI2 |ATG4 |ATG9 |AVL9 |AVT1 |AVT4 |BFA1 |MORE
    Alias
    Function/Process
    Cipollo JF and Trimble RB (2000) The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Deltaalg9 mutant reveals a regulatory role for the Alg3p alpha1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. J Biol Chem 275(6):4267-77
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG3 |ALG6 |ALG8 |ALG9 |CWH41 |DIE2 |OCH1 |SEC18
    Reviews
    Herscovics A (1999) Processing glycosidases of Saccharomyces cerevisiae. Biochim Biophys Acta 1426(2):275-85
    SGD Papers Entry  Pubmed Entry  
    |CWH41 |MNS1
    Function/Process
    Genetic Interactions
    Mutants/Phenotypes
    Strains/Constructs
    Bickle M, et al. (1998) Cell wall integrity modulates RHO1 activity via the exchange factor ROM2. EMBO J 17(8):2235-45
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |BIG1 |CWH41 |FKS1 |GAS1 |RHO1 |ROM2 |ROT1 |SAC7 |TOR2
    Substrates/Ligands/Cofactors
    Jakob CA, et al. (1998) Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J Cell Biol 142(5):1223-33
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG12 |ALG9 |MNS1 |PRC1
    Mutants/Phenotypes
    Other Features
    Strains/Constructs
    Jakob CA, et al. (1998) Genetic tailoring of N-linked oligosaccharides: the role of glucose residues in glycoprotein processing of Saccharomyces cerevisiae in vivo. Glycobiology 8(2):155-64
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ALG6 |ALG8 |DIE2 |SEC18
    Alias
    Function/Process
    Simons JF, et al. (1998) Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p. EMBO J 17(2):396-405
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |CWH41 |KAR2
    Non-Fungal Related Genes/Proteins
    Freeze HH, et al. (1997) Consequences of disrupting the gene that encodes alpha-glucosidase II in the N-linked oligosaccharide biosynthesis pathway of Dictyostelium discoideum. Dev Genet 21(3):177-86
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  

    Genetic Interactions
    Mutants/Phenotypes
    Strains/Constructs
    Schmidt A, et al. (1997) The yeast phosphatidylinositol kinase homolog TOR2 activates RHO1 and RHO2 via the exchange factor ROM2. Cell 88(4):531-42
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  
    |ACT1 |BAG7 |BEM2 |BEM3 |RHO1 |RHO2 |ROM2 |ROT1 |SAC7 |TOR2
    Alias
    Cellular Location
    Function/Process
    Mutants/Phenotypes
    Non-Fungal Related Genes/Proteins
    Protein Sequence Features
    Strains/Constructs
    Trombetta ES, et al. (1996) Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem 271(44):27509-16
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  

    Function/Process
    Other Features
    Substrates/Ligands/Cofactors
    Braun C, et al. (1995) Mechanism-based inhibition of yeast alpha-glucosidase and human pancreatic alpha-amylase by a new class of inhibitors. 2-Deoxy-2,2-difluoro-alpha-glycosides. J Biol Chem 270(45):26778-81
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  

    Function/Process
    Protein Physical Properties
    Substrates/Ligands/Cofactors
    Techniques and Reagents
    Saunier B, et al. (1982) Inhibition of N-linked complex oligosaccharide formation by 1-deoxynojirimycin, an inhibitor of processing glucosidases. J Biol Chem 257(23):14155-61
    SGD Papers Entry  Pubmed Entry  Reference LINKOUT  Reference LINKOUT  
    |CWH41 |MNS1
    Fungal Related Genes/Proteins
    Regulation of
    Bhanot P and Brown RG (1980) Effect of 3-O-methyl-D-glucose on the production of glycosidases by Cryptococcus laurentii and Saccharomyces cerevisiae. Can J Microbiol 26(11):1289-95
    SGD Papers Entry  Pubmed Entry  
    |FSP2 |GTB1 |MAL12 |MAL22 |MAL32 |MAL42 |MAL62 |SUC1 |SUC2 |SUC3 |SUC4 |SUC5 |SUC7 |YIL172C |MORE


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    SGDtm pages Database Copyright © 1997-2010 The Board of Trustees of Leland Stanford Junior University. Permission to use the information contained in this database was given by the researchers/institutes who contributed or published the information. Users of the database are solely responsible for compliance with any copyright restrictions, including those applying to the author abstracts. Documents from this server are provided "AS-IS" without any warranty, expressed or implied. The SGD project at Stanford University is supported by a Genome Research Resource Grant from the US National Human Genome Research Institute, part of the US National Institutes of Health.