ALG11
entrez
440138
canonical
uniprot
Q2TAA5
canonical
ensembl
ENSG00000253710
resolver
ensp
ENSP00000430236
resolver
enst
ENST00000521508
resolver
genesymbol
ALG11
resolver
genesymbol_syn
GT8
resolver
hgnc
HGNC:32456
resolver
uniprot
A5PLP3
resolver
uniprot
B4DKW9
resolver
uniprot
Q5TAN9
resolver
uniprot
Q6DKI6
resolver
uniprot
Q96FI7
resolver
uniprot_entry
ALG11_HUMAN
resolver
uniprot_sec
A5PLP3
resolver
uniprot_sec
B4DKW9
resolver
uniprot_sec
Q5TAN9
resolver
uniprot_sec
Q6DKI6
resolver
uniprot_sec
Q96FI7
resolver
amino_acid_sequence
MAAGERSWCLCKLLRFFYSLFFPGLIVCGTLCVCLVIVLWGIRLLLQRKKKLVSTSKNGKNQMVIAFFHPYCNAGGGGERVLWCALRALQKKYPEAVYVVYTGDVNVNGQQILEGAFRRFNIRLIHPVQFVFLRKRYLVEDSLYPHFTLLGQSLGSIFLGWEALMQCVPDVYIDSMGYAFTLPLFKYIGGCQVGSYVHYPTISTDMLSVVKNQNIGFNNAAFITRNPFLSKVKLIYYYLFAFIYGLVGSCSDVVMVNSSWTLNHILSLWKVGNCTNIVYPPCDVQTFLDIPLHEKKMTPGHLLVSVGQFRPEKNHPLQIRAFAKLLNKKMVESPPSLKLVLIGGCRNKDDELRVNQLRRLSEDLGVQEYVEFKINIPFDELKNYLSEATIGLHTMWNEHFGIGVVECMAAGTIILAHNSGGPKLDIVVPHEGDITGFLAESEEDYAETIAHILSMSAEKRLQIRKSARASVSRFSDQEFEVTFLSSVEKLFK
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of glycosylation 1P (CDG1P) [MIM:613661]: 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. {ECO:0000269|PubMed:20080937, ECO:0000269|PubMed:22213132}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.1.131
uniprot
proteins
function
FUNCTION: GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. Catalyzes, on the cytoplasmic face of the endoplasmic reticulum, the addition of the fourth and fifth mannose residues to the dolichol-linked oligosaccharide chain, to produce Man(5)GlcNAc(2)-PP-dolichol core oligosaccharide (PubMed:20080937). Man(5)GlcNAc(2)-PP-dolichol is a substrate for ALG3, the following enzyme in the biosynthetic pathway (PubMed:10581255). {ECO:0000269|PubMed:10581255, ECO:0000269|PubMed:20080937}.
uniprot
proteins
mass_dalton
55651
uniprot
proteins
mutagenesis
MUTAGEN 86; /note="L->A: No effect on GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity."; /evidence="ECO:0000269|PubMed:20080937"; MUTAGEN 86; /note="L->P: Decreased GDP-Man:Man3GlcNAc2-PP-Dol alpha-1,2-mannosyltransferase activity."; /evidence="ECO:0000269|PubMed:20080937
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:20080937}.
uniprot
proteins
protein_family
Glycosyltransferase 4 subfamily
uniprot
proteins
protein_family
Glycosyltransferase group 1 family
uniprot
proteins
pubmed
10581255
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
20080937
uniprot
proteins
pubmed
22213132
uniprot
proteins
sequence_length
492
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20080937}; Single-pass membrane protein {ECO:0000250|UniProtKB:P53954}.
uniprot
proteins
transmembrane_region
TRANSMEM 20..40; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins