• Version:
  • 11.0 [archived version]
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RER1 RER1 MANEA MANEA MAN1B1 MAN1B1 MGAT1 MGAT1 ERLEC1 ERLEC1 MOGS MOGS OS9 OS9 MAN2A1 MAN2A1 UGGT1 UGGT1 GANAB GANAB MAN2C1 MAN2C1
"MAN1B1" - Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase in Homo sapiens
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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MAN1B1Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase; Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trims the carbohydrates to Man(5-6)GlcNAc(2) (699 aa)    
Predicted Functional Partners:
MGAT1
Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase; Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans; Mannosyl-glycoprotein N-acetylglucosaminyltransferases (445 aa)
     
 
  0.953
GANAB
Neutral alpha-glucosidase AB; Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Required for PKD1/Polycystin-1 and PKD2/Polycystin-2 maturation and localization to the cell surface and cilia; Belongs to the glycosyl hydrolase 31 family (966 aa)
     
 
  0.946
MANEA
Glycoprotein endo-alpha-1,2-mannosidase; Mannosidases endo-alpha (462 aa)
           
  0.927
MOGS
Mannosyl-oligosaccharide glucosidase; Cleaves the distal alpha 1,2-linked glucose residue from the Glc(3)Man(9)GlcNAc(2) oligosaccharide precursor in a highly specific manner; Belongs to the glycosyl hydrolase 63 family (837 aa)
     
   
  0.830
MAN2A1
Alpha-mannosidase 2; Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway; Belongs to the glycosyl hydrolase 38 family (1144 aa)
     
   
  0.813
OS9
Protein OS-9; Lectin which functions in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD). May bind terminally misfolded non-glycosylated proteins as well as improperly folded glycoproteins, retain them in the ER, and possibly transfer them to the ubiquitination machinery and promote their degradation. Possible targets include TRPV4; MRH domain containing (667 aa)
     
   
  0.805
RER1
Protein RER1; Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment (196 aa)
       
 
  0.780
ERLEC1
Endoplasmic reticulum lectin 1; Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins; MRH domain containing (483 aa)
           
  0.778
MAN2C1
Alpha-mannosidase 2C1; Cleaves alpha 1,2-, alpha 1,3-, and alpha 1,6-linked mannose residues from glycoproteins. Involved in the degradation of free oligosaccharides in the cytoplasm; Belongs to the glycosyl hydrolase 38 family (1057 aa)
     
   
  0.734
UGGT1
UDP-glucose-glycoprotein glucosyltransferase 1; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation; UDP-glucose glycoprotein glucosyltransferases (1555 aa)
     
   
  0.693
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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