Literature summary for 2.4.1.260 extracted from

Chantret, I.; Dupre, T.; Delenda, C.; Bucher, S.; Dancourt, J.; Barnier, A.; Charollais, A.; Heron, D.; Bader-Meunier, B.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E.H.
Congenital disorders of glycosylation type Ig is defined by a deficiency in dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase (2002), J. Biol. Chem., 277, 25815-25822.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
F142V	the F142V replacement in hALG12p is the cause of inefficient addition of the eighth mannose residue onto Man7GlcNAc2-PP-dolichol during glycoprotein biosynthesis in a patient with type I congenital disorders of glycosylation. The patient is homozygous for the point mutation that causes an amino acid substitution in a conserved region of dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl alpha6-mannosyltransferase. Skin biopsy fibroblasts from a CDG I patient have a reduced capacity to add the eighth mannose residue onto the lipid-linked oligosaccharide precursor. The fibroblasts of the patient are capable of the direct transfer of Man7GlcNAc2 from dolichol onto protein and that this N-linked structure can be glucosylated by UDP-glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9BV10	-	-

Synonyms

Synonyms	Comment	Organism
ALG12	-	Homo sapiens
dolichyl-P-Man:Man7GlcNAc2-PP-dolichyl alpha6-mannosyltransferase	-	Homo sapiens
dolichyl-P-mannose:Man7GlcNAc2-PP-dolichyl mannosyltransferase	-	Homo sapiens

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Release 2023.1 (January 2023)