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MNL1 protein (Saccharomyces cerevisiae) - STRING interaction network
"MNL1" - Alpha-1,2-specific exomannosidase of the endoplasmic reticulum in Saccharomyces cerevisiae
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Predicted Interactions
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MNL1Alpha-1,2-specific exomannosidase of the endoplasmic reticulum; in complex with Pdi1p, generates a Man7GlcNac2 oligosaccharide signal on glycoproteins destined for ubiquitin-proteasome degradation; Alpha-1,2-specific exomannosidase involved in endoplasmic reticulum-associated degradation (ERAD). Delivers misfolded glycoproteins to proteasomes. Forms a complex with PDI1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response (796 aa)    
Predicted Functional Partners:
PDI1
Protein disulfide isomerase; multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; forms a complex with Mnl /.../t has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2 which promotes degradation in the unfolded protein response; Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bon [...] (522 aa)
     
 
  0.972
YOS9
ER quality-control lectin; integral subunit of the HRD ligase; binds to glycans with terminal alpha-1,6 linked mannose on misfolded N-glycosylated proteins and participates in targeting proteins to ERAD; member of the OS-9 protein family; Lectin involved in the quality control of the secretory pathway. As a member of the endoplasmic reticulum-associated degradation lumenal (ERAD-L) surveillance system, targets misfolded endoplasmic reticulum lumenal glycoproteins for degradation. The recognition of targets is N-glycan specific (542 aa)
     
 
  0.970
HRD3
ER membrane protein that plays a central role in ERAD; forms HRD complex with Hrd1p and ER-associated protein degradation (ERAD) determinants that engages in lumen to cytosol communication and coordination of ERAD events; Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of missfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD [...] (833 aa)
     
 
  0.883
CNE1
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast; Interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (502 aa)
     
 
  0.871
HRD1
Ubiquitin-protein ligase required for endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins; genetically linked to the unfolded protein response (UPR); regulated through association with Hrd3p; contains an H2 ring finger; E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the HRD1 ubiquitin ligase complex, [...] (551 aa)
     
   
  0.866
DER1
Endoplasmic reticulum membrane protein, required for ER-associated protein degradation of misfolded or unassembled proteins; N- and C- termini protrude into the cytoplasm, has similarity to Dfm1p; Component of the endoplasmic reticulum-associated degradation (ERAD) pathway. Specifically required for the ERAD-L pathway which mediates the degradation of proteins with misfolded lumenal domains within the endoplasmic reticulum (211 aa)
       
 
  0.849
SSM4
Ubiquitin-protein ligase involved in ER-associated protein degradation; located in the ER/nuclear envelope; ssm4 mutation suppresses mRNA instability caused by an rna14 mutation; E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, inluding endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase co [...] (1319 aa)
     
   
  0.760
SEC61
Essential subunit of Sec61 complex (Sec61p, Sbh1p, and Sss1p); forms a channel for SRP-dependent protein import and retrograde transport of misfolded proteins out of the ER; with Sec63 complex allows SRP-independent protein import into ER; Part of the Sec61 complex, which is the major component of a channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). The functional states of the translocon complex include co- and post- translational ER import, cotranslational membrane protein integration and retrograde transport of misfolded pro [...] (480 aa)
     
   
  0.754
USA1
Scaffold subunit of the Hrd1p ubiquitin ligase; also promotes ligase oligomerization; involved in ER-associated protein degradation (ERAD); interacts with the U1 snRNP-specific protein, Snp1p; Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane [...] (838 aa)
           
  0.747
KAR2
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; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
     
 
  0.746
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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