ALG13
entrez
79868
canonical
uniprot
Q9NP73
canonical
ensembl
ENSG00000101901
resolver
ensp
ENSP00000361047
resolver
ensp
ENSP00000378260
resolver
ensp
ENSP00000392990
resolver
ensp
ENSP00000477513
resolver
ensp
ENSP00000480711
resolver
ensp
ENSP00000485333
resolver
ensp
ENSP00000485392
resolver
ensp
ENSP00000485624
resolver
ensp
ENSP00000597424
resolver
ensp
ENSP00000676972
resolver
ensp
ENSP00000736189
resolver
enst
ENST00000473389
resolver
enst
ENST00000482742
resolver
enst
ENST00000623189
resolver
genesymbol
ALG13
resolver
genesymbol_syn
CXorf45
resolver
genesymbol_syn
GLT28D1
resolver
hgnc
HGNC:30881
resolver
uniprot
A0A087WT15
resolver
uniprot
A0A087WX43
resolver
uniprot
B1AKD6
resolver
uniprot
B1AKM1
resolver
uniprot
B2R5L5
resolver
uniprot
B7Z6J0
resolver
uniprot
B7Z804
resolver
uniprot
B7Z847
resolver
uniprot
B7Z9A8
resolver
uniprot
B7ZAJ1
resolver
uniprot
B7ZB57
resolver
uniprot
Q17RC3
resolver
uniprot
Q5JXY9
resolver
uniprot
Q9H5U8
resolver
uniprot_entry
A0A087WT15_HUMAN
resolver
uniprot_entry
A0A087WX43_HUMAN
resolver
uniprot_entry
ALG13_HUMAN
resolver
uniprot_sec
B1AKD6
resolver
uniprot_sec
B1AKM1
resolver
uniprot_sec
B2R5L5
resolver
uniprot_sec
B7Z6J0
resolver
uniprot_sec
B7Z804
resolver
uniprot_sec
B7Z847
resolver
uniprot_sec
B7Z9A8
resolver
uniprot_sec
B7ZAJ1
resolver
uniprot_sec
B7ZB57
resolver
uniprot_sec
Q17RC3
resolver
uniprot_sec
Q5JXY9
resolver
uniprot_sec
Q9H5U8
resolver
amino_acid_sequence
MKCVFVTVGTTSFDDLIACVSAPDSLQKIESLGYNRLILQIGRGTVVPEPFSTESFTLDVYRYKDSLKEDIQKADLVISHAGAGSCLETLEKGKPLVVVINEKLMNNHQLELAKQLHKEGHLFYCTCRVLTCPGQAKSIASAPGKCQDSAALTSTAFSGLDFGLLSGYLHKQALVTATHPTCTLLFPSCHAFFPLPLTPTLYKMHKGWKNYCSQKSLNEASMDEYLGSLGLFRKLTAKDASCLFRAISEQLFCSQVHHLEIRKACVSYMRENQQTFESYVEGSFEKYLERLGDPKESAGQLEIRALSLIYNRDFILYRFPGKPPTYVTDNGYEDKILLCYSSSGHYDSVYSKQFQSSAAVCQAVLYEILYKDVFVVDEEELKTAIKLFRSGSKKNRNNAVTGSEDAHTDYKSSNQNRMEEWGACYNAENIPEGYNKGTEETKSPENPSKMPFPYKVLKALDPEIYRNVEFDVWLDSRKELQKSDYMEYAGRQYYLGDKCQVCLESEGRYYNAHIQEVGNENNSVTVFIEELAEKHVVPLANLKPVTQVMSVPAWNAMPSRKGRGYQKMPGGYVPEIVISEMDIKQQKKMFKKIRGKEVYMTMAYGKGDPLLPPRLQHSMHYGHDPPMHYSQTAGNVMSNEHFHPQHPSPRQGRGYGMPRNSSRFINRHNMPGPKVDFYPGPGKRCCQSYDNFSYRSRSFRRSHRQMSCVNKESQYGFTPGNGQMPRGLEETITFYEVEEGDETAYPTLPNHGGPSTMVPATSGYCVGRRGHSSGKQTLNLEEGNGQSENGRYHEEYLYRAEPDYETSGVYSTTASTANLSLQDRKSCSMSPQDTVTSYNYPQKMMGNIAAVAASCANNVPAPVLSNGAAANQAISTTSVSSQNAIQPLFVSPPTHGRPVIASPSYPCHSAIPHAGASLPPPPPPPPPPPPPPPPPPPPPPPPPPPALDVGETSNLQPPPPLPPPPYSCDPSGSDLPQDTKVLQYYFNLGLQCYYHSYWHSMVYVPQMQQQLHVENYPVYTEPPLVDQTVPQCYSEVRREDGIQAEASANDTFPNADSSSVPHGAVYYPVMSDPYGQPPLPGFDSCLPVVPDYSCVPPWHPVGTAYGGSSQIHGAINPGPIGCIAPSPPASHYVPQGM
uniprot
proteins
disease_involvement
DISEASE: Developmental and epileptic encephalopathy 36 (DEE36) [MIM:300884]: A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. Some DEE36 patients may present with an abnormal isoelectric focusing of serum transferrin, consistent with a diagnostic classification of congenital disorder of glycosylation type I. 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:22492991, ECO:0000269|PubMed:23033978, ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:26138355, ECO:0000269|PubMed:27476654, ECO:0000269|PubMed:36200043}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.4.1.141
uniprot
proteins
function
FUNCTION: Catalytic subunit of the UDP-N-acetylglucosamine transferase complex 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. On the cytoplasmic face of the endoplasmic reticulum, the dimeric ALG13/ALG14 complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway. {ECO:0000269|PubMed:22492991}.; FUNCTION: [Isoform 2]: Catalytic subunit of the UDP-N-acetylglucosamine transferase complex 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. On the cytoplasmic face of the endoplasmic reticulum, the dimeric ALG13/ALG14 complex catalyzes the second step of dolichol pyrophosphate biosynthesis, transferring a beta1,4-linked N-acetylglucosamine (GlcNAc) from UDP-GlcNAc to GlcNAc-pyrophosphatedolichol (Gn-PDol) to produce N,N'-diacetylchitobiosyl diphosphodolichol. N,N'-diacetylchitobiosyl diphosphodolichol is a substrate for ALG1, the following enzyme in the biosynthetic pathway. {ECO:0000269|PubMed:16100110, ECO:0000269|PubMed:36200043}.; FUNCTION: [Isoform 1]: No glycosyltransferase or deubiquitinase activity is detected for this potential multifunctional enzyme. {ECO:0000269|PubMed:23827681, ECO:0000269|PubMed:36200043}.
uniprot
proteins
mass_dalton
126056
uniprot
proteins
mutagenesis
MUTAGEN 17; /note="I->N: Decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36200043"; MUTAGEN 81; /note="A->T: Decreased N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase activity."; /evidence="ECO:0000269|PubMed:36200043
uniprot
proteins
pathway_participation
PATHWAY: [Isoform 2]: Protein modification; protein glycosylation. {ECO:0000269|PubMed:22492991, ECO:0000269|PubMed:36200043}.
uniprot
proteins
protein_family
Glycosyltransferase 28 family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16100110
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22492991
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
23827681
uniprot
proteins
pubmed
23934111
uniprot
proteins
pubmed
26138355
uniprot
proteins
pubmed
27476654
uniprot
proteins
pubmed
32816001
uniprot
proteins
pubmed
36200043
uniprot
proteins
sequence_length
1137
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16100110}; Peripheral membrane protein {ECO:0000269|PubMed:16100110, ECO:0000269|PubMed:36200043}. Note=Recruited to the cytosolic face of the endoplasmic reticulum membrane through its interaction with ALG14. {ECO:0000269|PubMed:16100110}.
uniprot
proteins