DPAGT1
entrez
1798
canonical
uniprot
Q9H3H5
canonical
ensembl
ENSG00000172269
resolver
ensp
ENSP00000346142
resolver
ensp
ENSP00000506856
resolver
ensp
ENSP00000508129
resolver
ensp
ENSP00000685008
resolver
enst
ENST00000682326
resolver
enst
ENST00000682946
resolver
genesymbol
DPAGT1
resolver
genesymbol_syn
DPAGT2
resolver
hgnc
HGNC:2995
resolver
uniprot
A0A804HI18
resolver
uniprot
A0A804HKZ3
resolver
uniprot
O15216
resolver
uniprot
Q86WV9
resolver
uniprot
Q9BWE6
resolver
uniprot_entry
A0A804HI18_HUMAN
resolver
uniprot_entry
A0A804HKZ3_HUMAN
resolver
uniprot_entry
GPT_HUMAN
resolver
uniprot_sec
O15216
resolver
uniprot_sec
Q86WV9
resolver
uniprot_sec
Q9BWE6
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by natural nucleoside antibiotic tunicamycin, which acts as a structural analog and competitor of UDP-GlcNAc (PubMed:29459785, PubMed:30388443, PubMed:9451016). Activated by mannosylphosphoryldolichol and phospholipids such as phosphatidylglycerol and phosphatidylcholine (Probable). {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443, ECO:0000269|PubMed:9451016, ECO:0000305|PubMed:29459785}.
uniprot
proteins
amino_acid_sequence
MWAFSELPMPLLINLIVSLLGFVATVTLIPAFRGHFIAARLCGQDLNKTSRQQIPESQGVISGAVFLIILFCFIPFPFLNCFVKEQCKAFPHHEFVALIGALLAICCMIFLGFADDVLNLRWRHKLLLPTAASLPLLMVYFTNFGNTTIVVPKPFRPILGLHLDLGILYYVYMGLLAVFCTNAINILAGINGLEAGQSLVISASIIVFNLVELEGDCRDDHVFSLYFMIPFFFTTLGLLYHNWYPSRVFVGDTFCYFAGMTFAVVGILGHFSKTMLLFFMPQVFNFLYSLPQLLHIIPCPRHRIPRLNIKTGKLEMSYSKFKTKSLSFLGTFILKVAESLQLVTVHQSETEDGEFTECNNMTLINLLLKVLGPIHERNLTLLLLLLQILGSAITFSIRYQLVRLFYDV
uniprot
proteins
disease_involvement
DISEASE: Congenital disorder of glycosylation 1J (CDG1J) [MIM:608093]: 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:12872255, ECO:0000269|PubMed:30388443}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Myasthenic syndrome, congenital, 13 (CMS13) [MIM:614750]: A form of congenital myasthenic syndrome, a group of disorders characterized by failure of neuromuscular transmission, including pre-synaptic, synaptic, and post-synaptic disorders that are not of autoimmune origin. Clinical features are easy fatigability and muscle weakness. CMS13 is characterized by muscle weakness mostly affecting proximal limb muscles, minimal involvement of facial, ocular and bulbar muscles, and tubular aggregates present on muscle biopsy. Symptoms include difficulty walking and frequent falls. Younger patients show hypotonia and poor head control. Neurophysiological features indicate a disorder of neuromuscular transmission on electromyography. {ECO:0000269|PubMed:22742743, ECO:0000269|PubMed:30388443}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.8.15
uniprot
proteins
function
FUNCTION: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase 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 the initial step of dolichol-linked oligosaccharide biosynthesis, transferring GlcNAc-1-P from cytosolic UDP-GlcNAc onto the carrier lipid dolichyl phosphate (P-dolichol), yielding GlcNAc-P-P-dolichol embedded in the cytoplasmic leaflet of the endoplasmic reticulum membrane. {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443, ECO:0000269|PubMed:9451016}.
uniprot
proteins
mass_dalton
46090
uniprot
proteins
mutagenesis
MUTAGEN 30; /note="P->S: Mildly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 69; /note="I->N: No significant effect on UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 103; /note="L->F: Impairs protein stability."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 114; /note="A->G: No significant effect on UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 115; /note="D->A,N: Strongly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 115; /note="D->E: Mildly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 116; /note="D->A,N: Strongly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 122; /note="W->A: Strongly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 125; /note="K->A,E,N: Loss of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 168; /note="L->P: Strongly reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 182; /note="N->A: Loss of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 185; /note="N->A,D: Loss of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 252; /note="D->A: Reduces binding to inhibitor. Nearly abolishes UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443"; MUTAGEN 264; /note="V->M: No significant effect on UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 301; /note="R->C,H: Loss of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 302; /note="H->A: Loss of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 303; /note="R->A: Reduced UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443"; MUTAGEN 385; /note="L->R: No significant effect on UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity."; /evidence="ECO:0000269|PubMed:30388443
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443, ECO:0000269|PubMed:9451016}.
uniprot
proteins
protein_family
Glycosyltransferase 4 family
uniprot
proteins
pubmed
12872255
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
22742743
uniprot
proteins
pubmed
29459785
uniprot
proteins
pubmed
30388443
uniprot
proteins
pubmed
9451016
uniprot
proteins
sequence_length
408
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000269|PubMed:29459785, ECO:0000269|PubMed:30388443}.
uniprot
proteins
transmembrane_region
TRANSMEM 11..38; /note="Helical; Name=Helix 1"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 59..78; /note="Helical; Name=Helix 2"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 92..118; /note="Helical; Name=Helix 3"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 122..143; /note="Helical; Name=Helix 4"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 167..186; /note="Helical; Name=Helix 5"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 193..213; /note="Helical; Name=Helix 6"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 219..242; /note="Helical; Name=Helix 7"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 251..269; /note="Helical; Name=Helix 8"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 272..293; /note="Helical; Name=Helix 9"; /evidence="ECO:0000269|PubMed:29459785"; TRANSMEM 376..400; /note="Helical; Name=Helix 10"; /evidence="ECO:0000269|PubMed:29459785
uniprot
proteins