Information on EC 2.7.8.15 -

Information on EC 2.7.8.15 - UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase:

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EC NUMBER	COMMENTARY
2.7.8.15	-

RECOMMENDED NAME	GeneOntology No.
UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase	GO:0003975

REACTION	REACTION DIAGRAM	COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		-	-	-	-

REACTION TYPE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
substituted phospho group transfer	-	-	-	-
substituted phospho group transfer	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	-	-	703322

PATHWAY	KEGG Link	MetaCyc Link
dolichyl-diphosphooligosaccharide biosynthesis	-	MANNOSYL-CHITO-DOLICHOL-BIOSYNTHESIS

SYSTEMATIC NAME	IUBMB Comments
UDP-N-acetyl-D-glucosamine:dolichyl-phosphate N-acetyl-D-glucosaminephosphotransferase	-

SYNONYMS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-dolichyl phosphate	-	-	-	-
chitobiosylpyrophosphoryldolichol synthase	-	-	-	-
Dol-P dependent GlcNAc-1-P transferase	Saccharomyces cerevisiae	-	enzyme is encoded by ALG7	661252
dolichol phosphate N-acetylglucosamine-1-phosphotransferase	-	-	-	-
dolichol-P-dependent N-acetylglucosamine-1-P transferase	-	-	-	-
dolichol-P-dependent N-acetylglucosamine-1-phosphate transferase	-	-	-	-
DPAGT1	-	-	-	-
DPAGT1	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	-	-	703322
G1PT	-	-	-	-
GlcNAc-1-P transferase	-	-	-	-
GlcNAc-1-P transferase	Cricetulus griseus, Mesocricetus auratus	-	-	673891
GlcNAc-phosphotransferase	Homo sapiens	-	encoded by genes GNPTAB and GNPTG, deficiency causes mucolipidosis II	691880
GPT	-	-	-	-
GPT	Saccharomyces cerevisiae	-	-	661252
GPT	Cricetulus griseus	-	-	673891, 703322
GPT	Mesocricetus auratus	-	-	673891
GPT	Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus	-	-	703322
L-G1PT	-	-	-	-
N-acetylglucosamine-1-phosphate transferase	-	-	-	-
N-acetylglucosamine-1-phosphotransferase	Homo sapiens	-	-	691880
UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase	-	-	-	-
UDP-acetylglucosamine-dolichol phosphate acetylglucosamine-1-phosphotransferase	-	-	-	-
UDP-GlcNAc:dolichol phosphate GlcNAc-1-phosphate transferase	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	-	-	703322
UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase	-	-	-	-
UDP-GlcNAc:dolichyl-P GlcNAc1P transferase	-	-	-	-
UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase	-	-	-	-
UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase	-	-	-	-
UDPGlcNAc:dolichol phosphate N-acetylglucosamine 1-phosphate transferase	-	-	-	-

CAS REGISTRY NUMBER	COMMENTARY
70431-08-2	-

ORGANISM	COMMENTARY	LITERATURE	SEQUENCE CODE	SEQUENCE DB	SOURCE
Acanthamoeba castellanii	-	645349	-	-
Aspergillus niger	N402	645357	-	-
Bos taurus	-	645350, 703322	-	-
Cricetulus griseus	-	645359, 645360, 645361, 645364, 645366, 645367, 673891, 703322	-	-
Glycine max	-	645354, 645356	-	-
Homo sapiens	-	645362, 703322	-	-
Homo sapiens	french Canadian founder population in Saguenay-Lac-Saint-Jean (Quebec, Canada) with mucolipidosis II carrier rate at 1/39 (highest worldwide)	691880	-	-
Mesocricetus auratus	-	673891	-	-
Mus musculus	-	645363, 645365, 703322	-	-
Rattus norvegicus	-	645352, 645355, 703322	-	-
Saccharomyces cerevisiae	-	645358, 661252	-	-
Saccharomyces cerevisiae	X2180-1A	645348	-	-
Sus scrofa	-	645351, 645353	-	-

GENERAL INFORMATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
physiological function	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	-	GPT is involved in glycosylation of proteins on asparagine amino acids	703322

SUBSTRATE	PRODUCT	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY/ Substrate	LITERATURE/ Substrate	COMMENTARY/ Product	LITERATURE/ Product	Reversibility r=reversible ir=irreversible ?=not specified
UDP-GlcNAc + dolichyl phosphate	UMP + GlcNAc-diphosphodolichol		Cricetulus griseus	-	-	673891	initiating subsequent synthesis of Glc3Man9GlcNAc2-diphosphodolichol	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645359	-	645359	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645360	-	645360	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645361	-	645361	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645364	-	645364	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645366	-	645366	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	645367	-	645367	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus	-	-	703322	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Mus musculus	-	-	645363	-	645363	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Mus musculus	-	-	645365	-	645365	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Mus musculus	-	-	703322	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Homo sapiens	-	-	645362	-	645362	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Homo sapiens	-	-	703322	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Rattus norvegicus	-	-	645352	-	645352	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Rattus norvegicus	-	-	645355	-	645355	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Rattus norvegicus	-	-	703322	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Sus scrofa	-	-	645351	-	645351	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Sus scrofa	-	-	645353	-	645353	?, r
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Saccharomyces cerevisiae	-	-	645348	-	645348	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Saccharomyces cerevisiae	-	-	645358	-	645358	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Bos taurus	-	-	645350	-	645350	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Bos taurus	-	-	703322	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Aspergillus niger	-	-	645357	-	645357	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Glycine max	-	-	645354	-	645354	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Glycine max	-	-	645356	-	645356	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Mesocricetus auratus	-	-	673891	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Acanthamoeba castellanii	-	-	645349	-	645349	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme catalyzes the comitted step for N-linked glycosylation	645364	-	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme catalyzes the comitted step for N-linked glycosylation	645366	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Homo sapiens	-	deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij	645362	-	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Mus musculus	-	first enzyme in the dolichol pathway of protein N-glycosylation. The all-trans-retinoic acid induction of the enzyme has a regulatory impact on the dolichol pathway	645363	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Saccharomyces cerevisiae	-	the enzyme initiates the dolichol pathway of protein N-glycosylation. A 2.5- to 4fold reduction in enzyme activity gives rise to distinct phenotypes, whose severity is inversely related to the level of enzyme activity. These phenotypes include hypersensitivity to tunicamycin, enlarged cell size, extensive aggregation, lack of typical stationary arrest and defective spore germination	645358	-	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Aspergillus niger	-	the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides	645357	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Mus musculus	-	enzyme activity, immunoreactive GPT, and GPT mRNA are modulated in parallel during development and stimulated to a similar extent by a combination of insulin, hydrocortisone and prolactin in mouse mammary gland	645365	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Saccharomyces cerevisiae	-	first enzyme of dolichol pathway	645348	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Bos taurus	-	enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins	645350	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation	645361	-	-	?
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme is encoded by ALG7, whose expression affects the extent of N-glycosylation and secretion of proteins	645359	-	-	?
additional information	?	-	Saccharomyces cerevisiae	-	alg7 mutants show diminished activity of GPT, reduced steady-state levels of lipid-linked oligosaccharides and hypoglycosylated carboxypeptidase Y. Mutants also lack mitochondrial DNA including the genes that encode the components of the respiratory machinery	661252	-	-	-
additional information	?	-	Cricetulus griseus	-	overexpression of GPT in CHO-K1 cells does not go along with accumulation of intermediate Man5GlcNAc2-diphosphodolichol because of alteration of levels of oligosaccharide-diphosphodolichol and monosaccharide-phosphodolichol or through GPT enzymatic activity and excessive dolichyl phosphate consumption but rather may interfere with utilization of mannose- and glucosephosphodolichol	673891	-	-	-

NATURAL SUBSTRATES	NATURAL PRODUCTS	REACTION DIAGRAM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY SUBSTRATE	LITERATURE (Substrate)	COMMENTARY PRODUCT	LITERATURE (Product)
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	UMP + N-acetyl-D-glucosaminyl-diphosphodolichol		Cricetulus griseus, Mus musculus, Homo sapiens, Rattus norvegicus, Bos taurus	-	-	703322	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme catalyzes the comitted step for N-linked glycosylation	645364, 645366	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Homo sapiens	-	deficiency of UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij	645362	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Mus musculus	-	first enzyme in the dolichol pathway of protein N-glycosylation. The all-trans-retinoic acid induction of the enzyme has a regulatory impact on the dolichol pathway	645363	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Saccharomyces cerevisiae	-	the enzyme initiates the dolichol pathway of protein N-glycosylation. A 2.5- to 4fold reduction in enzyme activity gives rise to distinct phenotypes, whose severity is inversely related to the level of enzyme activity. These phenotypes include hypersensitivity to tunicamycin, enlarged cell size, extensive aggregation, lack of typical stationary arrest and defective spore germination	645358	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Aspergillus niger	-	the enzyme catalyzes the first step in the assembly of dolichol-linked oligosaccharides	645357	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Mus musculus	-	enzyme activity, immunoreactive GPT, and GPT mRNA are modulated in parallel during development and stimulated to a similar extent by a combination of insulin, hydrocortisone and prolactin in mouse mammary gland	645365	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Saccharomyces cerevisiae	-	first enzyme of dolichol pathway	645348	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Bos taurus	-	enzyme initiates the dolichol cycle for the biosynthesis of asparagine-linked glycoproteins	645350	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme catalyzes the key step in the assembly of oligosaccharide-lipid intermediates in N-linked glycosylation	645361	-	-
UDP-N-acetyl-D-glucosamine + dolichyl phosphate	?		Cricetulus griseus	-	the enzyme is encoded by ALG7, whose expression affects the extent of N-glycosylation and secretion of proteins	645359	-	-
additional information	?	-	Saccharomyces cerevisiae	-	alg7 mutants show diminished activity of GPT, reduced steady-state levels of lipid-linked oligosaccharides and hypoglycosylated carboxypeptidase Y. Mutants also lack mitochondrial DNA including the genes that encode the components of the respiratory machinery	661252	-	-

COFACTOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

METALS and IONS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
Ca2+	Saccharomyces cerevisiae	-	divalent metal required, Ca2+ is less effective as Mg2+	645348
Ca2+	Sus scrofa	-	less effective than Mn2+ or Mg2+	645351
Ca2+	Glycine max	-	1-2 mM, weak stimulation	645354
Mg2+	Saccharomyces cerevisiae	-	divalent metal required, optimal activity in presence of Mg2+	645348
Mg2+	Acanthamoeba castellanii	-	divalent cation required for dialyzed enzyme, maximal activity in presence of 8-10 mM	645349
Mg2+	Bos taurus	-	stimulates	645350
Mg2+	Sus scrofa	-	either Mn2+, 1 mM, or Mg2+, 10 mM, required for optimal activity	645351
Mg2+	Glycine max	-	10 mM required for optimal activity	645354
Mn2+	Saccharomyces cerevisiae	-	divalent metal required, Mn2+ is less effective as Mg2+	645348
Mn2+	Acanthamoeba castellanii	-	divalent cation required for dialyzed enzyme, Mg2+ or Mn2+	645349
Mn2+	Bos taurus	-	stimulates	645350
Mn2+	Sus scrofa	-	either Mn2+, 1 mM, or Mg2+, 10 mM, required for optimal activity	645351
Mn2+	Glycine max	-	1-2 mM, weak stimulation	645354

INHIBITORS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
Amphomycin	Glycine max	-	-	645354	2D-image
Ca2+	Glycine max	-	above 2 mM	645354	2D-image
Diumycin	Acanthamoeba castellanii	-	-	645349	-
Diumycin	Bos taurus	-	-	645350	-
Diumycin	Glycine max	-	-	645354	-
dolichyl phosphate	Bos taurus	-	at high concentrations	645350	2D-image
GDP-mannose	Glycine max	-	-	645354	2D-image
GDP-mannose	Glycine max	-	slight	645356	2D-image
GDP-mannose	Mesocricetus auratus	-	5 residues of mannose from GDP-mannose	673891	2D-image
GTP	Glycine max	-	0.4 mM, 25-30% inhibition, enzyme from tunicamycin-resistant cells, no inhibition of wild-type enzyme up to 0.4 mM	645356	2D-image
Hg2+	Bos taurus	-	partially reversed by dithiothreitol	645350	2D-image
iodoacetamide	Bos taurus	-	-	645350	2D-image
Mn2+	Glycine max	-	above 2 mM	645354	2D-image
NEM	Sus scrofa	-	protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate and Mn2+ are added before addition of the sulfhydryl reagent	645351	2D-image
PCMB	Bos taurus	-	-	645350	2D-image
PCMB	Sus scrofa	-	protected to the extent of about 50% when all of the substrates, UDP-GlcNAc, dolichyl phosphate anf Mn2+ are added before addition of the sulfhydryl reagent	645351	2D-image
PCMB	Glycine max	-	the enzyme from tunicamycin-resistant cells is equally sensitive to tunicamycin as the wilde-type enzyme	645356	2D-image
phosphatidylcholine	Glycine max	-	-	645354	2D-image
phosphatidylethanolamine	Glycine max	-	-	645354	2D-image
phosphatidylserine	Glycine max	-	-	645354	2D-image
Showdomycin	Glycine max	-	-	645354	2D-image
Triton X-100	Rattus norvegicus	-	substrate protects from inhibition	645355	2D-image
Tunicamycin	Saccharomyces cerevisiae	-	1 mM, complete inhibition	645348	2D-image
Tunicamycin	Bos taurus	-	-	645350, 703322	2D-image
Tunicamycin	Sus scrofa	-	0.00005-0.0001 mg/ml, 50% inhibition, noncompetitive with respect to UDP-GlcNAc or dolichyl phosphate, both directions	645353	2D-image
Tunicamycin	Glycine max	-	-	645354	2D-image
Tunicamycin	Rattus norvegicus	-	-	645355, 703322	2D-image
Tunicamycin	Mesocricetus auratus	-	-	673891	2D-image
Tunicamycin	Cricetulus griseus, Homo sapiens, Mus musculus	-	-	703322	2D-image
UDP	Saccharomyces cerevisiae	-	1 mM, 55% inhibition	645348	2D-image
UDP	Bos taurus	-	-	645350	2D-image
UDP-GlcNAc	Glycine max	-	strong inhibition	645356	2D-image
UDP-glucose	Bos taurus	-	-	645350	2D-image
UDP-glucose	Glycine max	-	-	645354	2D-image
UDP-hexanolamine	Bos taurus	-	-	645350	2D-image
UDP-xylose	Bos taurus	-	-	645350	2D-image
UMP	Saccharomyces cerevisiae	-	1 mM, 45% inhibition	645348	2D-image
UMP	Bos taurus	-	-	645350	2D-image

ACTIVATING COMPOUND	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
ATP	Glycine max	-	0.01-0.025 mM, stimulates activity of tunicamycin-resistant cells about 20-30%	645356	2D-image
cardiolipin	Rattus norvegicus	-	stimulates activity of enzyme in endoplasmic membrane vesicles, due to better solubilization of the dolichol phosphate	645355	2D-image
Dolichyl-phosphoryl-mannose	Bos taurus	-	stimulates	645350	2D-image
Dolichyl-phosphoryl-mannose	Sus scrofa	-	stimulates	645351	2D-image
GDP-mannose	Sus scrofa	-	stimulates by protecting the substrate UDP-GlcNAc from degradation	645351	2D-image
Monogalactosyldiglyceride	Rattus norvegicus	-	stimulates activity of enzyme in endoplasmic membrane vesicles	645355	2D-image
phosphatidylcholine	Sus scrofa	-	0.001 mM/ml, 30-40% inhibition	645353	2D-image
phosphatidylethanolamine	Rattus norvegicus	-	stimulates activity of enzyme in endoplasmic membrane vesicles	645355	2D-image
phosphatidylglycerol	Sus scrofa	-	solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine	645351	2D-image
phosphatidylglycerol	Glycine max	-	2- to 3fold maximal stimulation at 0.06 mg/ml	645354	2D-image
phosphatidylglycerol	Glycine max	-	activity is slightly enhanced	645356	2D-image
phosphatidylinositol	Sus scrofa	-	solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine	645351	2D-image
phosphatidylinositol	Glycine max	-	stimulates	645354	2D-image
phosphatidylserine	Sus scrofa	-	solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine	645351	2D-image
Phospholipid	Sus scrofa	-	solubilized enzyme is stimulated by exogenously added phospholipids in order of increasing activity: phosphatidylglycerol, phosphatidylinositol, phosphatidylserine	645351	2D-image
Phospholipid	Rattus norvegicus	-	endogenous microsomal phospholipid is required for reaction to proceed normally in rat lung microsomes	645352	2D-image

KM VALUE [mM]	KM VALUE [mM] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
0.0007	-	dolichyl phosphate	Sus scrofa	-	37�C	645353	2D-image
0.001	-	dolichyl phosphate	Saccharomyces cerevisiae	-	pH 7.5	645348	2D-image
0.001	-	dolichyl phosphate	Sus scrofa	-	pH 7.5, 37�C	645351	2D-image
0.0045	-	dolichyl phosphate	Acanthamoeba castellanii	-	pH 7.4, 30�C	645349	2D-image
0.0062	-	dolichyl phosphate	Glycine max	-	pH 7.5, 37�C	645354	2D-image
0.016	-	dolichyl phosphate	Bos taurus	-	pH 7.6, 37�C	645350	2D-image
0.0001	-	UDP-GlcNAc	Sus scrofa	-	pH 7.5, 37�C	645351	2D-image
0.0002	-	UDP-GlcNAc	Sus scrofa	-	37�C	645353	2D-image
0.00042	-	UDP-GlcNAc	Glycine max	-	pH 7.5, 37�C	645354	2D-image
0.0005	-	UDP-GlcNAc	Acanthamoeba castellanii	-	pH 7.4, 30�C	645349	2D-image
0.0045	-	UDP-GlcNAc	Bos taurus	-	pH 7.6, 37�C	645350	2D-image
0.015	-	UDP-GlcNAc	Saccharomyces cerevisiae	-	pH 7.5	645348	2D-image
0.18	-	dolichyl phosphate	Saccharomyces cerevisiae	-	pH 7.5	645348	2D-image
additional information	-	additional information	Rattus norvegicus	-	Km-value for dolichyl phosphate: 0.005 mg/0.1 ml	645355	-

TURNOVER NUMBER [1/s]	TURNOVER NUMBER MAXIMUM[1/s]	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

kcat/KM VALUE [1/mMs^-1]	kcat/KM VALUE [1/mMs^-1] Maximum	SUBSTRATE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

Ki VALUE [mM]	Ki VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

IC50 VALUE [mM]	IC50 VALUE [mM] Maximum	INHIBITOR	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg]	SPECIFIC ACTIVITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	-	Bos taurus	-	-	645350

pH OPTIMUM	pH MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
7.2	7.6	Glycine max	-	-	645354
7.4	7.6	Bos taurus	-	-	645350
7.4	7.6	Sus scrofa	-	-	645351
7.4	7.8	Acanthamoeba castellanii	-	-	645349
7.5	-	Saccharomyces cerevisiae	-	-	645348

pH RANGE	pH RANGE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
6.5	8.5	Saccharomyces cerevisiae	-	pH 6.5: about 60% of maximal activity, pH 8.5: about 35% of maximal activity	645348
7	8.7	Acanthamoeba castellanii	-	pH 6.0: no activity, pH 7.0: 85% of maximal activity, pH 8.7: 64% of maximal activity	645349

TEMPERATURE OPTIMUM	TEMPERATURE OPTIMUM MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
30	-	Acanthamoeba castellanii	-	-	645349
40	-	Rattus norvegicus	-	with 0.5% Triton X-100 in the assay mixture	645355
60	-	Rattus norvegicus	-	with either dioleoylphosphatidylethanolamine or cardiolipin in the assay mixture	645355

TEMPERATURE RANGE	TEMPERATURE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
25	40	Acanthamoeba castellanii	-	0�C: no activity, 15�C: 11% of maximal activity, 25�C: 73% of maximal activity, 35�C: 96% of maximal activity, 40�C: 57% of maximal activity	645349

pI VALUE	pI VALUE MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

SOURCE TISSUE	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE	SOURCE
aorta	Sus scrofa	-	-	645351, 645353
brain	Cricetulus griseus	-	-	645359
cell culture	Acanthamoeba castellanii	-	-	645349
cell culture	Glycine max	-	-	645354
cell culture	Glycine max	-	the tunicamycin resistant cells have a greater than 40fold increase in the activity of the enzyme UDP-GlcNAc:dolichyl-P GlcNAc1P transferase. Increase in enzyme activity is due to an increased production of the enzyme	645356
CHO cell	Cricetulus griseus	-	-	645359, 645360, 645364, 645366, 645367, 703322
CHO-K1 cell	Cricetulus griseus, Mesocricetus auratus	-	-	673891
cyst	Acanthamoeba castellanii	-	-	645349
heart	Cricetulus griseus	-	-	645359
kidney	Cricetulus griseus	-	-	645359
liver	Rattus norvegicus	-	-	645355
lung	Rattus norvegicus	-	-	645352, 703322
lung	Cricetulus griseus	-	-	645359
lung	Homo sapiens	-	-	703322
mammary gland	Bos taurus	-	lactating	645350
mammary gland	Mus musculus	-	-	645365, 703322
mammary gland	Bos taurus	-	-	703322
P-19 cell	Mus musculus	-	-	645363
spleen	Cricetulus griseus	-	-	645359
submandibular gland	Cricetulus griseus	-	-	645359

LOCALIZATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	GeneOntology No.	LITERATURE	SOURCE
endoplasmic reticulum	Rattus norvegicus	-	-	5783	645355
endoplasmic reticulum	Cricetulus griseus	-	-	5783	645364
endoplasmic reticulum	Cricetulus griseus	-	the enzyme has multiple transmembrane spans and a critical cytosolic loop	5783	645366
endoplasmic reticulum	Cricetulus griseus	-	an enzyme with multiple transmembrane spans	5783	645367
membrane	Saccharomyces cerevisiae	-	-	16020	645348
membrane	Cricetulus griseus	-	enzyme with multiple transmembrane spans	16020	645367
membrane	Cricetulus griseus, Mus musculus	-	-	16020	703322
microsome	Saccharomyces cerevisiae	-	-	-	645348
microsome	Bos taurus	-	-	-	645350
microsome	Sus scrofa	-	-	-	645351, 645353
microsome	Rattus norvegicus	-	-	-	645352, 703322
microsome	Glycine max	-	-	-	645354
microsome	Cricetulus griseus	-	microsomal membranes	-	673891
rough endoplasmic reticulum	Cricetulus griseus, Mus musculus	-	-	5791	703322

PDB	SCOP	CATH	ORGANISM
No entries in this field

MOLECULAR WEIGHT	MOLECULAR WEIGHT MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
34000	-	Cricetulus griseus	-	monomer, determined by SDS-PAGE and Western blot analysis	703322
44700	-	Homo sapiens	-	-	703322
46000	-	Bos taurus	-	determined by SDS-PAGE and Western Blot analysis	703322
46470	-	Mus musculus	-	theoretical	703322
50000	-	Bos taurus	-	determined by SDS-PAGE and Western Blot analysis	703322
67000	-	Cricetulus griseus	-	assumed to be a dimeric form, determined by SDS-PAGE and Western blot analysis	703322
70000	-	Bos taurus	-	suggested to be a biological precursor or the degraded native enzyme, determined by SDS-PAGE and Western blot analysis	703322
79400	-	Rattus norvegicus	-	-	703322
330000	360000	Bos taurus	-	large molecular mass of the enzyme can be due to aggregation of the hydrophobic, membrane-derived enzyme rather than resulting from subunit interaction, gel filtration	645350
additional information	-	Cricetulus griseus	-	ALG7 1.5 kb mRNAs appears to be initiated at a start site downstream from that used by the 1.9 and 2.2 kb species and located bentween two in-frame ATG codons. Translation of these transcripts in vitro provides supporting evidence that the 1.5 and 1.9 kb transcripts are translationally competent, giving rise to related protein isoforms with different lengths of their NH2-terminal domains. The 1.9 kb mRNA serves in the synthesis of 36000 Da and 24000 Da species, as well as a low abundance 32000 Da protein. The 1.5 kb transcript gives rise to a translation product of 32000 Da	645359

SUBUNITS	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
?	Glycine max	-	x * 39000, SDS-PAGE	645356
?	Aspergillus niger	-	x * 51400, calculation from nucleotide sequence	645357
dimer	Cricetulus griseus	-	2 * 34000, the 67000 Da enzyme form is a homodimer of UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase or perhaps a hetero-oligomer with another microsomal component	645367
additional information	Bos taurus	-	results indicate that either 70000 MW band in SDS-PAGE is a precursor form of the enzyme or this polypeptide, representing the native enzyme or its subunit, is proteolyzed to smaller, enzymatically active peptides of 50000 Da and 46000 Da during purification	645350

POSTTRANSLATIONAL MODIFICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
additional information	Bos taurus	-	the enzyme is not a glycoprotein of the asparagine-linked type	645350

Crystallization/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

pH STABILITY	pH STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

TEMPERATURE STABILITY	TEMPERATURE STABILITY MAXIMUM	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
30	-	Acanthamoeba castellanii	-	1 h, stable	645349
35	-	Glycine max	-	the enzyme from tunicamycin-resistant cells is significantly less stable than the wild-type enzyme	645356
40	-	Glycine max	-	the enzyme from tunicamycin-resistant cells is significantly less stable than the wild-type enzyme	645356

GENERAL STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
purified enzyme is resistant to digestion with either endo-beta-N-acetylglucosaminidase H or F	Bos taurus	-	645350
a 1:4 dilution leads to a 65% loss of activity	Saccharomyces cerevisiae	-	645348

ORGANIC SOLVENT	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

OXIDATION STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

STORAGE STABILITY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-20�C or -70�C, stable for 2 weeks	Acanthamoeba castellanii	-	645349
4�C, completely stable for 9-10 days. No significant loss of activity after 63 days in presence of NaN3	Acanthamoeba castellanii	-	645349
4�C, solubilized enzyme loses most of its activity within 12 h	Bos taurus	-	645350
-20�C, solubilized enzyme loses 96% of its activity after 6 days, only 20% loss of activity after 6 days in presence of 0.07 mM UDP-GlcNAc	Saccharomyces cerevisiae	-	645348
0-4�C, 20% glycerol, 0.02 mg phosphatidylglycerol/mg of protein, less than 20% loss of activity after 6 days. In absence of both glycerol and phosphatidylglycerol the enzyme is quite unstable and loses most of its activity within 24 h	Sus scrofa	-	645351

Purification/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	-	703322
partial	Sus scrofa	-	645351

Cloned/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
-	Aspergillus niger	-	645357
for expression in Saccharomyces cerevisiae	Bos taurus	-	703322
-	Cricetulus griseus	-	703322
plasmid shuffling procedure in Schizosaccharomyces pombe for analyzing site-directed mutations in the cDNA of L-G1PT for their effect on enzymatic activity	Cricetulus griseus	-	645361
for expression in Saccharomyces cerevisiae	Homo sapiens	-	703322
-	Mus musculus, Rattus norvegicus	-	703322

EXPRESSION	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

ENGINEERING	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
A263D	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
D252A	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residues is essential for activity	645359
D252A/F254I	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residues are essential for activity	645359
D252A/L102F	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residues are essential for activity	645359
DELTA395-408	Cricetulus griseus	-	mutation fully eliminates enzyme expression in vivo	645364
DELTA398-408	Cricetulus griseus	-	removal of the last 11 amino acids 398-408 from the enzyme has no significant effect on the catalytic activity, thermal stability, tunicamycin binding, reticular localization, or consumption of cellular dolichol phosphate	645364
F249A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
F257A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
F395L/S396M/I397W	Cricetulus griseus	-	expression of the mutant enzyme	645364
F395L/S396M/I397W/DELTA398-408	Cricetulus griseus	-	mutation fully eliminates enzyme expression in vivo	645364
K125A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
N182A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
N182A/I186M	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residues are essential for activity	645359
N182A/W122R	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residues are essential for activity	645359
N185A	Cricetulus griseus	-	mutation does not allows plasmid shuffling, indicating that the residue is essential for activity	645359
R123A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
R303K	Cricetulus griseus	-	catalytically inactive mutant enzyme, this mutant can be expressed in CHO-K1 cells and can bind tunicamycin efficiently, indicative of proper folding. The R303K mutant can inhibit exogenously expressed normal enzyme	645367
R303K	Cricetulus griseus	-	catalytically inactive mutant	703322
W122R	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
Y256A	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
Y170C	Homo sapiens	-	mutant enzyme has almost no activity	645362
Y256A/F286S	Cricetulus griseus	-	mutation allows plasmid shuffling, indicating that the residue is not essential for activity	645359
additional information	Homo sapiens	-	c.3503_3504delTC: heterozygous, two-nucleotide deletion in exon 19, causes frameshift and premature translational stop (p.L1168QfsX5), detected by PCR in all tested parents of children with mucolipidosis II	691880

Renatured/COMMENTARY	ORGANISM	UNIPROT ACCESSION NO.	LITERATURE
No entries in this field

APPLICATION	ORGANISM	UNIPROT ACCESSION NO.	COMMENTARY	LITERATURE
No entries in this field

DISEASE	TITLE OF PUBLICATION	LINK TO PUBMED
Carcinoma	Aberrant amplification of the crosstalk between canonical Wnt signaling and N-glycosylation gene DPAGT1 promotes oral cancer.	PubMed
Carcinoma	Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer.	PubMed
Carcinoma, Hepatocellular	Elevated carbohydrate phosphotransferase activity in human hepatoma and phosphorylation of cathepsin D.	PubMed
Carcinoma, Squamous Cell	Aberrant amplification of the crosstalk between canonical Wnt signaling and N-glycosylation gene DPAGT1 promotes oral cancer.	PubMed
Carcinoma, Squamous Cell	N-glycosylation gene DPAGT1 is a target of the Wnt/beta-catenin signaling pathway.	PubMed
Carcinoma, Squamous Cell	Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer.	PubMed
Congenital, Hereditary, and Neonatal Diseases and Abnormalities	Deficiency of UDP-GlcNAc:Dolichol Phosphate N-Acetylglucosamine-1 Phosphate Transferase (DPAGT1) causes a novel congenital disorder of Glycosylation Type Ij.	PubMed
Genetic Diseases, Inborn	[Mucolipidoses type II. Case report]	PubMed
Leukemia	Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.	PubMed
Leukemia, Myelogenous, Chronic, BCR-ABL Positive	Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.	PubMed
Leukemia, Myeloid, Acute	Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.	PubMed
Lysosomal Storage Diseases	Inheritance, biochemical abnormalities, and clinical features of feline mucolipidosis II: the first animal model of human I-cell disease.	PubMed
Lysosomal Storage Diseases	Lysosomal enzyme phosphorylation in human fibroblasts. Kinetic parameters offer a biochemical rationale for two distinct defects in the uridine diphospho-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase.	PubMed
Metabolic Diseases	Lysosomal storage causes cellular dysfunction In mucolipidosis II skin fibroblasts.	PubMed
Mouth Neoplasms	Aberrant amplification of the crosstalk between canonical Wnt signaling and N-glycosylation gene DPAGT1 promotes oral cancer.	PubMed
Mouth Neoplasms	Overexpression of DPAGT1 leads to aberrant N-glycosylation of E-cadherin and cellular discohesion in oral cancer.	PubMed
Mucolipidoses	A key enzyme in the biogenesis of lysosomes is a protease that regulates cholesterol metabolism.	PubMed
Mucolipidoses	Abnormal expressions of the subunits of the UDP-N-acetylglucosamine: lysosomal enzyme, N-acetylglucosamine-1-phosphotransferase, result in the formation of cytoplasmic vacuoles resembling those of the I-cells.	PubMed
Mucolipidoses	Acid sphingomyelinase: relation of 93lysine residue on the ratio of intracellular to secreted enzyme activity.	PubMed
Mucolipidoses	Correction of mucolipidosis III in vitro by gene transfer.	PubMed
Mucolipidoses	Demonstration of the heterozygous state for I-cell disease and pseudo-Hurler polydystrophy by assay of N-acetylglucosaminylphosphotransferase in white blood cells and fibroblasts.	PubMed
Mucolipidoses	Identification of a variant of mucolipidosis III (pseudo-Hurler polydystrophy): a catalytically active N-acetylglucosaminylphosphotransferase that fails to phosphorylate lysosomal enzymes.	PubMed
Mucolipidoses	Identification of mutations in the GNPTA (MGC4170) gene coding for GlcNAc-phosphotransferase alpha/beta subunits in Korean patients with mucolipidosis type II or type IIIA.	PubMed
Mucolipidoses	Inheritance, biochemical abnormalities, and clinical features of feline mucolipidosis II: the first animal model of human I-cell disease.	PubMed
Mucolipidoses	Inhibition of autophagosome formation restores mitochondrial function in mucolipidosis II and III skin fibroblasts.	PubMed
Mucolipidoses	Light and heavy lysosomes: characterization of N-acetyl-beta-D-hexosaminidase isolated from normal and I-cell disease lymphoblasts.	PubMed
Mucolipidoses	Loss of N-acetylglucosamine-1-phosphotransferase gamma subunit due to intronic mutation in GNPTG causes mucolipidosis type III gamma: Implications for molecular and cellular diagnostics.	PubMed
Mucolipidoses	Lysosomal enzyme phosphorylation in human fibroblasts. Kinetic parameters offer a biochemical rationale for two distinct defects in the uridine diphospho-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase.	PubMed
Mucolipidoses	Lysosomal storage causes cellular dysfunction In mucolipidosis II skin fibroblasts.	PubMed
Mucolipidoses	Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts.	PubMed
Mucolipidoses	Missense mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTA) in a patient with mucolipidosis II induces changes in the size and cellular distribution of GNPTG.	PubMed
Mucolipidoses	Missense mutations in N-acetylglucosamine-1-phosphotransferase alpha/beta subunit gene in a patient with mucolipidosis III and a mild clinical phenotype.	PubMed
Mucolipidoses	Molecular analysis of the GNPTAB and GNPTG genes in 13 patients with mucolipidosis type II or type III - identification of eight novel mutations.	PubMed
Mucolipidoses	Mucolipidosis II (I-Cell Disease) and Mucolipidosis IIIA (Classical Pseudo-Hurler Polydystrophy) Are Caused by Mutations in the GlcNAc-Phosphotransferase alpha / beta -Subunits Precursor Gene.	PubMed
Mucolipidoses	Mucolipidosis II and III alpha/beta: mutation analysis of 40 Japanese patients showed genotype-phenotype correlation.	PubMed
Mucolipidoses	Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population.	PubMed
Mucolipidoses	Mucolipidosis type II in a domestic shorthair cat.	PubMed
Mucolipidoses	Origin and spread of a common deletion causing mucolipidosis type II: insights from patterns of haplotypic diversity.	PubMed
Mucolipidoses	Peripheral blood lymphocyte appearance in a case of I cell disease.	PubMed
Mucolipidoses	Phosphorylation of lysosomal enzymes in fibroblasts. Marked deficiency of N-acetylglucosamine-1-phosphotransferase in fibroblasts of patients with mucolipidosis III.	PubMed
Myasthenic Syndromes, Congenital	Mutations in DPAGT1 cause a limb-girdle congenital myasthenic syndrome with tubular aggregates.	PubMed
Myelodysplastic Syndromes	Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.	PubMed
Neoplasms	Aberrant amplification of the crosstalk between canonical Wnt signaling and N-glycosylation gene DPAGT1 promotes oral cancer.	PubMed
Neoplasms	UDP-N-acetylglucosamine: lysosomal enzyme precursor N-acetylglucosamine-1-phosphate transferase activities in human ovarian tumor tissue and some transformed cell lines.	PubMed
Neuroblastoma	Identification and characterization of human LL5A gene and mouse Ll5a gene in silico.	PubMed
Precursor Cell Lymphoblastic Leukemia-Lymphoma	Increased N-acetylglucosamine-1-phosphotransferase activity in sera from patients with leukemia.	PubMed
Stuttering	A role for inherited metabolic deficits in persistent developmental stuttering.	PubMed
Stuttering	Mutations in the lysosomal enzyme-targeting pathway and persistent stuttering.	PubMed

REF.	AUTHORS	TITLE	JOURNAL	VOL.	PAGES	YEAR	ORGANISM	LINK TO PUBMED	SOURCE
645348	Sharma, C.B.; Lehle, L.; Tanner, W.	Solubilization and characterization of the initial enzymes of the dolichol pathway from yeast	Eur. J. Biochem.	126	319-325	1982	Saccharomyces cerevisiae	PubMed
645349	Villemez, C.L.; Carlo, P.L.	Properties of a soluble polyprenyl phosphate. UDP-D-N-acetylglucosamine N-acetylglucosamine-1-phosphate transferase	J. Biol. Chem.	255	8174-8178	1980	Acanthamoeba castellanii	PubMed
645350	Shailubhai, K.; Dong-Yu, B.; Saxena, E.S.; Vijay, I.K.	Purification and characterization of UDP-N-acetyl-D-glucosamine:dolichol phosphate N-acetyl-D-glucosamine-1-phosphate transferase involved in the biosynthesis of asparagine-linked glycoproteins in the mammary gland	J. Biol. Chem.	263	15964-15972	1988	Bos taurus	PubMed
645351	Kaushal, G.P.; Elbein, A.D.	Purification and properties of UDP-GlcNAc:dolichyl-phosphate GlcNAc-1-phosphate transferase. Activation and inhibition of the enzyme	J. Biol. Chem.	260	16303-16309	1985	Sus scrofa	PubMed
645352	Plouhar, P.L.; Bretthauer, R.K.	A phospholipid requirement for dolichol pyrophosphate N-acetylglucosamine synthesis in phospholipase A2-treated rat lung microsomes	J. Biol. Chem.	257	8907-8911	1982	Rattus norvegicus	PubMed
645353	Heifetz, A.; Keenan, R.W.; Elbein, A.D.	Mechanism of action of tunicamycin on the UDP-GlcNAc:dolichyl-phosphate Glc-NAc-1-phosphate transferase	Biochemistry	18	2186-2192	1979	Sus scrofa	PubMed
645354	Kaushal, G.P.; Elbein, A.D.	Properties of solubilized UDP-GlcNAc:dolichyl phosphate-GlcNAc-1-P-transferase from soybean cultured cells	Plant Physiol.	82	748-752	1986	Glycine max	PubMed
645355	Chandra, N.C.; Doody, M.B.; Bretthauer, R.K.	Specific lipids enhance the activity of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase in rat liver endoplasmic reticulum membrane vesicles	Arch. Biochem. Biophys.	290	345-354	1991	Rattus norvegicus	PubMed
645356	Zeng, Y.; Elbein, A.D.	UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase is amplified in tunicamycin-resistant soybean cells	Eur. J. Biochem.	233	458-466	1995	Glycine max	PubMed
645357	Sorensen, T.K.; Dyer, P.S.; Fierro, F.; Laube, U.; Peberdy, J.F.	Characterisation of the gptA gene, encoding UDP N-acetylglucosamine: dolichol phosphate N-acetylglucosaminylphosphoryl transferase, from the filamentous fungus, Aspergillus niger	Biochim. Biophys. Acta	1619	89-97	2003	Aspergillus niger	PubMed
645358	Kukuruzinska, M.A.; Lennon, K.	Diminished activity of the first N-glycosylation enzyme, dolichol-P-dependent N-acetylglucosamine-1-P transferase (GPT), gives rise to mutant phenotypes in yeast	Biochim. Biophys. Acta	1247	51-59	1995	Saccharomyces cerevisiae	PubMed
645359	Mota, O.M.; Huang, G.T.; Kukuruzinska, M.A.	Developmental regulation and tissue-specific expression of hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase (GPT)	Biochem. Biophys. Res. Commun.	204	284-291	1994	Cricetulus griseus	PubMed
645360	Huang, G.T.; Lennon, K.; Kukuruzinska, M.A.	Characterization of multiple transcripts of the hamster dolichol-P-dependent N-acetylglucosamine-1-P transferase suggests functionally complex expression	Mol. Cell. Biochem.	181	97-106	1998	Cricetulus griseus	PubMed
645361	Scocca, J.R.; Krag, S.S.	Aspartic acid 252 and asparagine 185 are essential for activity of lipid N-acetylglucosaminylphosphate transferase	Glycobiology	7	1181-1191	1997	Cricetulus griseus	PubMed
645362	Wu, X.; Rush, J.S.; Karaoglu, D.; Krasnewich, D.; Lubinsky, M.S.; Waechter, C.J.; Gilmore, R.; Freeze, H.H.	Deficiency of UDP-GlcNAc: dolichol phosphate N-acetylglucosamine-1 phosphate transferase (DPAGT1) causes a novel congenital disorder of glycosylation type Ij	Hum. Mutat.	22	144-150	2003	Homo sapiens	PubMed
645363	Meissner, J.D.; Naumann, A.; Mueller, W.H.; Scheibe, R.J.	Regulation of UDP-N-acetylglucosamine:dolichyl-phosphate N-acetylglucosamine-1-phosphate transferase by retinoic acid in P19 cells	Biochem. J.	338	561-568	1999	Mus musculus	PubMed
645364	Zara, J.; Lehrman, M.A.	Role of the carboxyl terminus in stable expression of hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase	J. Biol. Chem.	269	19108-19115	1994	Cricetulus griseus	PubMed
645365	Rajput, B.; Ma, J.; Vijay, I.K.	Structure and organization of mouse GlcNAc-1-phosphate transferase gene	J. Biol. Chem.	269	9590-9597	1994	Mus musculus	PubMed
645366	Dan, N.; Middleton, R.B.; Lehrman, M.A.	Hamster UDP-N-acetylglucosamine:dolichol-P N acetylglucosamine-1-P transferase has multiple transmembrane spans and a critical cytosolic loop	J. Biol. Chem.	271	30717-30724	1996	Cricetulus griseus	PubMed
645367	Dan, N.; Lehrman, M.A.	Oligomerization of hamster UDP-GlcNAc:dolichol-P GlcNAc-1-P transferase, an enzyme with multiple transmembrane spans	J. Biol. Chem.	272	14214-14219	1997	Cricetulus griseus	PubMed
661252	Mendelsohn, R.D.; Helmerhorst, E.J.; Cipollo, J.F.; Kukuruzinska, M.A.	A hypomorphic allele of the first N-glycosylation gene, ALG7, causes mitochondrial defects in yeast	Biochim. Biophys. Acta	1723	33-44	2005	Saccharomyces cerevisiae	PubMed
673891	Gao, N.; Shang, J.; Lehrman, M.A.	Unexpected basis for impaired Glc3Man9GlcNAc2-P-P-dolichol biosynthesis by elevated expression of Glcnac-1-p transferase	Glycobiology	18	125-134	2007	Cricetulus griseus, Mesocricetus auratus	PubMed
691880	Plante, M.; Claveau, S.; Lepage, P.; Lavoie, E.M.; Brunet, S.; Roquis, D.; Morin, C.; Vezina, H.; Laprise, C.	Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population	Clin. Genet.	73	236-244	2008	Homo sapiens	PubMed
703322	Bretthauer, R.K.	Structure, expression, and regulation of UDP-GlcNAc: dolichol phosphate GlcNAc-1-phosphate transferase (DPAGT1)	Curr. Drug Targets	10	477-482	2009	Bos taurus, Cricetulus griseus, Homo sapiens, Mus musculus, Rattus norvegicus	PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.7.8.15)

NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM

IUBMB Enzyme Nomenclature

PROSITE Database of protein families and domains

SYSTERS

Protein Mutant Database

InterPro (database of protein families, domains and functional sites)

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