2.4.1.142: chitobiosyldiphosphodolichol beta-mannosyltransferase
This is an abbreviated version!
For detailed information about chitobiosyldiphosphodolichol beta-mannosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.142
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2.4.1.142
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oligosaccharide
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n-glycosylation
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mannosylation
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dolichol-linked
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lipid-linked
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n-linked
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n-glycans
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asparagine-linked
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disease-causing
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glycosylphosphatidylinositol
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glycolipids
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rough
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pharmacology
- 2.4.1.142
- oligosaccharide
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n-glycosylation
-
mannosylation
-
dolichol-linked
-
lipid-linked
-
n-linked
- n-glycans
-
asparagine-linked
-
disease-causing
- glycosylphosphatidylinositol
- glycolipids
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rough
- pharmacology
Reaction
Synonyms
ALG1, ALG1 beta1,4 mannosyltransferase, Alg1 mannosyltransferase, Alg1 protein, Alg1p, beta-1,4 mannosyltransferase, beta1,4-MT, chitobiosyldiphosphodolichol beta-mannosyltransferase, GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase, GDP-mannose-dolichol diphosphochitobiose mannosyltransferase, guanosine diphosphate-mannose:GlcNAc2-PP-dolichol mannosyltransferase-1, guanosine diphosphomannose-dolichol diphosphochitobiose mannosyltransferase, mannosyltransferase I, MT-1, MT-I
ECTree
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Localization
Localization on EC 2.4.1.142 - chitobiosyldiphosphodolichol beta-mannosyltransferase
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ER, the predicted transmembrane domain localizes the N-terminus of Alg1 into the ER lumen. The N-terminal transmembrane domain including the following positively charged amino acids and an N-terminal amphiphilic-like alpha-helix domain exposed on the protein surface strictly coordinate the Alg1 orientation on the ER membrane. The N- and C-termini of Alg1 are located to luminal and cytosolic side of the ER, respectively. The conserved proline 20 residue has no effect on its membrane-spanning property. The positively charged amino acids (K35, K38, K39 and R40) downstream of the N-terminal transmembrane region are important for ER membrane attachment
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ER, the predicted transmembrane domain localizes the N-terminus of Alg1 into the ER lumen. The N-terminal transmembrane domain including the following positively charged amino acids and an N-terminal amphiphilic-like alpha-helix domain exposed on the protein surface strictly coordinate the Alg1 orientation on the ER membrane. The N- and C-termini of Alg1 are located to luminal and cytosolic side of the ER, respectively. The conserved proline 20 residue has no effect on its membrane-spanning property. The positively charged amino acids (K35, K38, K39 and R40) downstream of the N-terminal transmembrane region are important for ER membrane attachment
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membrane topology of Alg1, overview. A conserved alpha-helix domain, Alg1 Nalpha3 domain, contributes to the membrane association of Alg1 protein
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membrane topology of Alg1, overview. A conserved alpha-helix domain, Alg1 Nalpha3 domain, contributes to the membrane association of Alg1 protein
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