Entity Details

Primary name ALG8_HUMAN
Entity type UniProt
Source Source Link

Details

AccessionQ9BVK2
EntryNameALG8_HUMAN
FullNameProbable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
TaxID9606
Evidenceevidence at protein level
Length526
SequenceStatuscomplete
DateCreated2002-05-27
DateModified2021-06-02

Ontological Relatives

GenesALG8

GO terms

Show/Hide Table
GOName
GO:0000033 alpha-1,3-mannosyltransferase activity
GO:0005789 endoplasmic reticulum membrane
GO:0006487 protein N-linked glycosylation
GO:0006488 dolichol-linked oligosaccharide biosynthetic process
GO:0006490 oligosaccharide-lipid intermediate biosynthetic process
GO:0016021 integral component of membrane
GO:0018279 protein N-linked glycosylation via asparagine
GO:0042283 dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase activity

Subcellular Location

Show/Hide Table
Subcellular Location
Endoplasmic reticulum membrane

Domains

Show/Hide Table
DomainNameCategoryType
IPR004856 Glycosyl transferase, ALG6/ALG8FamilyFamily
IPR039487 Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferaseFamilyFamily

Diseases

Show/Hide Table
Disease IDSourceNameDescription
617874 OMIMPolycystic liver disease 3 with or without kidney cysts (PCLD3)A form of polycystic liver disease, an autosomal dominant hepatobiliary disease characterized by overgrowth of biliary epithelium and supportive connective tissue, resulting in multiple liver cysts. PCLD3 patients may also develop kidney cysts that usually do not result in clinically significant renal disease. The disease is caused by variants affecting the gene represented in this entry.
608104 OMIMCongenital disorder of glycosylation 1H (CDG1H)A form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions. The disease is caused by variants affecting the gene represented in this entry.