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(UDP)–N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
-
acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-glycoprotein
-
-
-
-
acetylglucosamine-1-phosphotransferase, uridine diphosphoacetylglucosamine-lysosomal enzyme precursor
-
-
-
-
GlcNAc-1-phosphotransferase
GlcNAc-phosphotransferase
-
lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase
-
-
-
-
M6P-forming GlcNAc-1-phosphotransferase
M6P-forming N-acetylglucosamine-1-phosphotransferase
N-acetylglucosamine-1-phosphate transferase
-
N-acetylglucosamine-1-phosphotransferase
N-acetylglucosaminyl phosphotransferase
-
-
-
-
N-acetylglucosaminylphosphotransferase
-
-
-
-
PT alpha/beta subunit precursor protein
-
UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
-
-
-
-
UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase
UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
UDP-GlcNAc:lysosomal enzymeN-acetylglucosamine-1-phosphotransferase
Q3T906 AND Q9UJJ9
-
UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase
-
-
-
-
UDP-N-acetylglucosamine:glycoprotein N-acetylglucosaminyl-1-phosphotransferase
-
-
-
-
UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
-
-
-
-
UDP-N-acetylglucosamine:lysosomal enzyme phosphotransferase
-
-
UDP-N-acetylglucosamine:lysosomal-enzyme-N-acetylglucosamine-1-phosphotransferase
-
GlcNAc-1-phosphotransferase

-
-
GlcNAc-1-phosphotransferase
-
-
GlcNAc-1-phosphotransferase
-
GlcNAc-1-phosphotransferase
Q3T906 AND Q9UJJ9
-
GlcNAc-1-phosphotransferase
-
GlcNAc-1-phosphotransferase
Q69ZN6 AND Q6S5C2
-
GlcNAc-1PT

Q3T906 AND Q9UJJ9
-
GlcNAc-1PT
Q69ZN6 AND Q6S5C2
-
M6P-forming GlcNAc-1-phosphotransferase

Q3T906 AND Q9UJJ9
-
M6P-forming GlcNAc-1-phosphotransferase
Q69ZN6 AND Q6S5C2
-
M6P-forming N-acetylglucosamine-1-phosphotransferase

Q3T906 AND Q9UJJ9
-
M6P-forming N-acetylglucosamine-1-phosphotransferase
Q69ZN6 AND Q6S5C2
-
N-acetylglucosamine-1-phosphotransferase

-
-
N-acetylglucosamine-1-phosphotransferase
-
UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase

-
-
-
-
UDP-GlcNAc:glycoprotein N-acetylglucosamine-1-phosphotransferase
-
-
UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase

-
-
UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase
-
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase

-
-
-
-
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
-
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
Q3T906 AND Q9UJJ9
-
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase
-
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malfunction

-
deletion of the Alg14 N-terminal region causes a severe growth defect at high temperature. Malfunction can be partially complemented by overexpression of Alg7
malfunction
-
extracts of two mutant cell lines transfer UDP-N-acetyl-D-glucosamine from N-acetyl-D-glucosamine to mannose residues at less than 5% the wild type value. In addition, the lysosomal hydrolases of these mutant clones fail to bind to a cation-independent mannose 6-phosphate receptor affinity column
malfunction
-
30% of the acid hydrolases of gamma gene knockout mice brain are phosphorylated at levels equivalent to that in wild-type brain, although 25% are poorly phosphorylated compared to wild-type. The rest of the acid hydrolases of the gamma-deficient sample are phosphorylated at an intermediate level. This shows that some acid hydrolases are highly dependent on the presence of the gamma subunit to acquire the Man-6-P, although others are well phosphorylated by the alpha/beta subunits alone
malfunction
-
mucolipidosis II (MLII) and III alpha/beta are autosomal-recessive diseases of childhood caused by mutations in GNPTAB encoding the alpha/beta-subunit precursor protein of the GlcNAc-1-phosphotransferase complex. Biological significance of eight selected disease-causing GNPTAB mutations found in MLII and MLIII alpha/beta patients in Brazil, overview. The frameshift E757KfsX1 and the non-sense R587X mutations result in a severe clinical phenotype in homozygosity. In addition to the loss of combinatorial cytosolic targeting motifs, luminal missense mutations located in the stealth region 2 of the alpha-subunit impair the transport of the alpha/beta-subunit precursor to the Golgi apparatus
malfunction
the lysosomal storage disorder ML III gamma is caused by defects in the gamma subunit of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. In patients with this disorder, most of the newly synthesized lysosomal enzymes are secreted rather than being sorted to lysosomes, resulting in increased levels of these enzymes in the plasma. Several missense mutations in GNPTG, the gene encoding the gamma subunit, are reported in mucolipidosis III gamma patients. gamma-Subunit deficient HeLa cells have greatly reduced levels of many lysosomal acid hydrolases compared with the parental HeLa cells and display a lysosomal storage phenotype
malfunction
-
some mutations in the Stealth domain harboring the catalytic site greatly impaires the activity of the enzyme without affecting its Golgi localization and proteolytic processing. Missense mutations in conserved cysteine residues in the Notch repeat 1 domain do not affect the catalytic activity but impair mannose phosphorylation of certain lysosomal hydrolases
malfunction
-
some mutations in the Stealth domain harboring the catalytic site greatly impaires the activity of the enzyme without affecting its Golgi localization and proteolytic processing. Missense mutations in conserved cysteine residues in the Notch repeat 1 domain do not affect the catalytic activity but impair mannose phosphorylation of certain lysosomal hydrolases
malfunction
mucolipidoses II and III (ML II and MLIII) are lysosomal disorders in which the mannose 6-phosphate recognition marker is absent from lysosomal hydrolases and other glycoproteins due to mutations in GNPTAB, which encodes two of three subunits of the heterohexameric enzyme, N-acetylglucosamine-1-phosphotransferase. Both disorders are caused by the same gene, but ML II represents the more severe phenotype. Bone manifestations of ML II include hip dysplasia, scoliosis, rickets and osteogenesis imperfecta, phhentype overview. A recombinant adeno-associated viral vector (AAV2/8-GNPTAB) confers high and prolonged gene expression of GNPTAB and thereby influence the pathology in the cartilage and bone tissue of a GNPTAB knock out (KO) mouse model. AAV8-mediated expression of N-acetylglucosamine-1-phosphate transferase attenuates bone loss in a mouse model of mucolipidosis II with significant increases in bone mineral density and content
malfunction
-
recombinant GlcNAc-1-phosphotransferase containing a missense mutation in the DMAP interaction domain (Lys732Asn) identified in a patient with mucolipidosis II exhibits full activity toward the simple sugar alpha-methyl D-mannoside but impaired phosphorylation activity toward acid hydrolases, recombinant expression of the K732N mutant in a zebrafish model of mucolipidosis II fails to correct the phenotypic abnormalities
malfunction
-
loss of function results in impaired lysosomal targeting of these acid hydrolases and decreased lysosomal degradation. Two mucolipidosis III patient missense mutations, Lys4Gln and Ser15Tyr, in the N-terminal cytoplasmic tail of the alpha-subunit of phosphotransferase impair retention of the catalytically active enzyme in the Golgi complex. This results in mistargeting of the mutant enzymes to lysosomes, where they are degraded, or to the cell surface and release into the medium. The mislocalization of the active enzymes is the basis for mucolipidosis III alphabeta in a subset of patients
physiological function

-
the enzyme modifies lysosomal hydrolases with mannose 6-phosphate targeting signals. The proteolytic cleavage of alpha/beta-subunit precursor protein is a prerequisite for the catalytic activity of the GlcNAc-1-phosphotransferase and therefore plays an important role in the biogenesis of lysosomes
physiological function
the enzyme tags lysosomal enzymes with the mannose 6-phosphate lysosomal targeting signal. The gamma-subunit is required for efficient phosphorylation of a subset of the lysosomal enzymes
physiological function
-
the enzyme UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase is involved in lysosomal enzyme recognition. UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase tags newly synthesized lysosomal enzymes with mannose 6-phosphate recognition markers, which are required for their targeting to the endolysosomal system
physiological function
-
the enzyme UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase is involved in lysosomal enzyme recognition. UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase tags newly synthesized lysosomal enzymes with mannose 6-phosphate recognition markers, which are required for their targeting to the endolysosomal system
physiological function
-
the enzyme mediates the initial step in the addition of the mannose 6-phosphate targeting signal on newly synthesized lysosomal enzymes, which serves to direct the lysosomal enzymes to lysosomes. GlcNAc-1-phosphotransferase is able to distinguish the about 60 lysosomal enzymes from the numerous nonlysosomal glycoproteins with identical Asn-linked glycans, that lack a common structural motif. The two Notch repeat modules and the DNA methyltransferase-associated protein interaction domain of the alpha-subunit are key components of this recognition process. Different combinations of these domains are involved in binding to individual lysosomal enzymes. In the majority of instances the mannose 6-phosphate receptor homology domain of the gamma-subunit is required for optimal phosphorylation, the gamma-binding site is located on the alpha-subunit, the gamma-subunit binds to amino acids 535-694 of the alpha-subunit
physiological function
-
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the mannose 6-phosphate recognition signal on lysosomal acid hydrolases. The DMAP interaction domain of the alpha subunit functions in the selective recognition of acid hydrolase substrates
physiological function
-
the Golgi-localized enzyme mediates the first step in the synthesis of the mannose 6-phosphate recognition marker on lysosomal acid hydrolases
additional information

-
identification of domains of the enzyme involved in catalytic function, overview
additional information
-
identification of domains of the enzyme involved in catalytic function, overview
additional information
-
the lysosomal integral membrane protein type 2 (LIMP-2/SCARB2) is a mannose 6-phosphate-independent trafficking receptor for beta-glucocerebrosidase and no substrate of the enzyme, M6P-independent lysosomal sorting of LIMP-2, overview
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UDP-N-acetyl-D-glucosamine + alpha-L-fucosidase
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-methyl D-mannoside
UMP + 6-(N-acetyl-D-glucosaminyl-phospho)-alpha-methyl D-mannoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-methyl-D-mannoside
UMP + 6-(N-acetyl-D-glucosaminyl-phospho)-alpha-methyl D-mannoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + alpha-N-acetylglucosaminidase
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-hexosaminidase
UMP + ?
UDP-N-acetyl-D-glucosamine + cathepsin A
UMP + ?
-
capthepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
UDP-N-acetyl-D-glucosamine + DNase I
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-cathepsin Z D-mannose
UMP + lysosomal-cathepsin Z N-acetyl-D-glucosaminyl-phospho-D-mannose
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
UDP-N-acetyl-D-glucosamine + Man9GlcNAc1 oligosaccharide
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl alpha-D-mannopyranoside
UMP + methyl (6-O-alpha-N-acetyl-D-glucosaminylphospho)-alpha-D-mannopyranoside
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
UDP-N-acetyl-D-glucosamine + NPC2
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
UMP + ?
UDP-N-acetyl-D-glucosamine + pro-tripeptidyl peptidase
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ribonuclease B
UMP + ?
UDP-N-acetyl-D-glucosamine + RNase B
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + soybean agglutinin
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + thyroglobulin
UMP + ?
-
weak activity
-
-
?
UDP-N-acetyl-D-glucosamine + UDP-glucose
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin
?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin
UMP + ?
additional information
?
-
UDP-N-acetyl-D-glucosamine + beta-hexosaminidase

UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + beta-hexosaminidase
UMP + ?
-
the alpha-chain of beta-hexosaminidase is a poorer acceptor than the beta-chain, and the beta chain in the B isoenzyme is a better acceptor than the beta-chain in the A isoenzyme
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D

UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
-
substitution of two lysines (E203K/E267K) of the substrate cathepsin D stimulates mannose phosphorylation 116fold. Subtitution of additional residues in the beta loop particularly lysines, increase phosphorylation 4fold further
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + cathepsin D
UMP + ?
-
capthepsin A and cathepsin D have one closely related phosphotransferase recognition site represented by a structurally and topologically conserved beta-hairpin loop
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose

UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Q3T906 AND Q9UJJ9
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Q3T906 AND Q9UJJ9
-
localization of tagged protein products in the Golgi of wild-type and mutant enzymes expressing HeLa cells, overview
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
initial enzyme in biosynthesis of mannose 6-phosphate
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
substrates are lysosomal acid hydrolases
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
-
the specificity of the reaction is determined by the ability of the alpha/beta subunits to recognize a conformation-dependent protein determinant present on the acid hydrolases, the DNA methyltransferase-associated protein (DMAP) interaction domain of the alpha subunit functions in this recognition process. Recombinant GST-DMAP domain pulls down several acid hydrolases, but not nonlysosomal glycoproteins
-
-
?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose
UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Q69ZN6 AND Q6S5C2
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl alpha-D-mannopyranoside

UMP + methyl (6-O-alpha-N-acetyl-D-glucosaminylphospho)-alpha-D-mannopyranoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl alpha-D-mannopyranoside
UMP + methyl (6-O-alpha-N-acetyl-D-glucosaminylphospho)-alpha-D-mannopyranoside
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside

UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
-
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + methyl-alpha-D-mannoside
UMP + N-acetyl-D-glucosamine-phospho-(methyl-alpha-D-mannoside)
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin

UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ovalbumin
UMP + ?
-
weak activity
-
-
?
UDP-N-acetyl-D-glucosamine + ribonuclease B

UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + ribonuclease B
UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin

UMP + ?
-
-
-
-
?
UDP-N-acetyl-D-glucosamine + uteroferrin
UMP + ?
-
-
-
-
?
additional information

?
-
-
the enzyme catalyzes the initial step in the synthesis of the mannose 6-phosphate determinant required for efficient intracellular targeting of newly synthesized lysosomal hydrolase to the lysosome
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
the enzyme is specific for lysosomally destined acceptor glycoproteins
-
-
-
additional information
?
-
enzyme catalyzes modification of lysosomal enzymes with mannose 6-phosphate. This modification is catalyzed by UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase. The modified lysosomal enzymes are then targeted to the lysosome
-
-
-
additional information
?
-
-
the lysosomal integral membrane protein type 2 (LIMP-2/SCARB2) is a mannose 6-phosphate-independent trafficking receptor for beta-glucocerebrosidase and no substrate of the enzyme, M6P-independent lysosomal sorting of LIMP-2, overview. beta-Glucocerebrosidase is also no substrate for the enzyme
-
-
-
additional information
?
-
-
the critical step in lysosomal targeting of soluble lysosomal enzymes is the recognition by an UDP-N-acetylglucosamine:lysosomal enzyme-N-acetylglucosamine-1-phosphotransferase
-
-
-
additional information
?
-
-
UDPglucose is also a substrate with a catalytic efficiency about 12fold worse than UDP-GlcNAc. The enzyme phosphorylates lysosomal enzymes in an in vitro assay at least 100fold more efficiently than either other glycoproteins with similar carbohydrate chains or free oligosaccharides
-
-
-
additional information
?
-
-
the recognition and catalytic site of the phosphotransferase are located on different subunits
-
-
-
additional information
?
-
-
phosphorylated recognition markers in lysosomal enzymes appear to be synthesized by transfer of alpha-N-acetylglucosamine 1-phosphate groups to C6 hydroxyl of mannose residues in glycosylated enzyme precursors and a subsequent hydrolysis from the diester groups of the N-acetylglucosamine residue
-
-
-
UDP-N-acetyl-D-glucosamine + arylsulfatase A
additional information
-
-
binding of arylsulfatase A to the phosphotransferase is not restricted to a limited surface area but involves the simultaneous recognition of large parts of arylsulfatase A
-
-
?
UDP-N-acetyl-D-glucosamine + arylsulfatase A
additional information
-
-
mature arylsulfatase A from human urine
formation of GlcNAc(alpha1)phospho(6)mannose diesters in high mannose oligosaccharides in arylsulfatase A
?
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0.03 - 0.11
cathepsin D
-
0.75 - 1.55
Man9GlcNAc1 oligosaccharide
0.5 - 0.75
methyl alpha-D-mannopyranoside
0.008 - 0.038
pro-tripeptidyl peptidase
-
0.0041 - 0.005
soybean agglutinin
-
0.011 - 0.033
uteroferrin
0.03
cathepsin D

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.11
cathepsin D
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.0045
DNase I

-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.005
DNase I
-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.75
Man9GlcNAc1 oligosaccharide

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
1.55
Man9GlcNAc1 oligosaccharide
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
0.5
methyl alpha-D-mannopyranoside

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
0.75
methyl alpha-D-mannopyranoside
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
0.44
NPC2

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.62
NPC2
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.008
pro-tripeptidyl peptidase

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.038
pro-tripeptidyl peptidase
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.042
RNase B

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.05
RNase B
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.0041
soybean agglutinin

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.005
soybean agglutinin
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.011
uteroferrin

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
0.033
uteroferrin
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
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0.23 - 0.266
Man9GlcNAc1 oligosaccharide
0.0166
methyl alpha-D-mannopyranoside
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
0.075 - 0.36
pro-tripeptidyl peptidase
-
0.09
RNase B
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.005
soybean agglutinin
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase; pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
1.2
cathepsin D

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
4.45
cathepsin D
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.08
DNase I

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.15
DNase I
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.23
Man9GlcNAc1 oligosaccharide

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
0.266
Man9GlcNAc1 oligosaccharide
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
1.25
NPC2

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
1.7
NPC2
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.075
pro-tripeptidyl peptidase

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
-
0.36
pro-tripeptidyl peptidase
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
-
0.45
uteroferrin

-
pH 7.4, 37°C, alpha2beta2 GlcNAc-1-phosphotransferase
1
uteroferrin
-
pH 7.4, 37°C, alpha2beta2gamma2 GlcNAc-1-phosphotransferase
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C447Y
-
site-directed mutagenesis, the mutation does not affect the catalytic activity of the GlcNAc-1-phosphotransferase. Enzyme-deficient embryos rescued with C447Y mRNA only corrects 84% of mutational features, and embryos rescued with the mutant mRNA appear visually different, i.e. shorter, from embryos rescued with wild-type mRNA
C473S
-
site-directed mutagenesis, the mutation does not affect the catalytic activity of the GlcNAc-1-phosphotransferase. Enzyme-deficient embryos rescued with C473S mRNA only corrects 80% of mutational features, and embryos rescued with the mutant mRNA appear visually different, i.e. shorter, from embryos rescued with wild-type mRNA
A592T
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, that has no effect on the mutant enzyme
A955V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
A955V/K928R
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
C142S
-
mutant expressed as dimer
C142Y
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
C157S
-
mutant expressed as dimer
C157S/C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer
C169S
-
mutant expressed as dimer
C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer. Mutant is localised in the Golgi apparatus, indicating that dimerization is not essential for endoplasmic reticulum exit of the gamma-subunit. Monomeric C245S mutant does not assemble with endogenous GlcNAc-1-phosphotransferase 1 subunits
C442Y
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C461G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C468S
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the Notch 1 mutant is efficiently delivered to the Golgi complex and the alphabeta precursor undergoes proteolytic cleavage
C523R
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
C84S
-
mutant expressed as dimer
C84S/C157S
-
mutant expressed as dimer
C84S/C157S/C245S
-
mutant can be detected as 36 kDa monomeric form but not as a dimer
D1018G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
D190V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
D407A
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant in the Stealth domain trafficks to the Golgi
D407A/A663G
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
F374L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
G106S
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
G126S
naturally occuring mutation of the gamma-subunit that causes misfolding of the gamma-subunit, the misfolded protein is retained in the endoplasmic reticulum, where it forms aggregates, and fails to rescue the lysososmal targeting of lysosomal acid glycosidases
G575R
-
naturally occuring missense mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant shows 3% of wild-type activity
H956Y
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
I348L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant behaves similar to the wild-type enzyme
K1236A/R1237A/K1238A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
L1001P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant partially exits from the endoplasmic reticulum and is almost inactive
L1054V
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
L5A/L6A
-
replacement of the N-terminal dileucine motif with alanine residues results in a significant reduction of the PT alpha/beta-subunit precursor protein cleavage. Densitometric evaluation of intensities of immunoreactive bands show that the formation of the beta-subunit is reduced by 46% compared with the wild-type construct. Mutant mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
L5A/L6A/R1253A/I1254A/R1255A
-
double mutant containing a mutation of N-terminal and C-terminal endoplasmic reticulum export motif shows a strong inhibitory effect on cleavage of the PT alpha/beta-subunit precursor protein. Mutation leads to retention in the endoplasmic reticulum
L5A/L6A/R1253L/I1254L/R1255X
-
the transfer of the dileucine motif to the C-terminal domain replacing the dibasic-based motif 1253RIR1255 in combination with the substitution of the N-terminal dileucine motif, blocks the endoplasmic exit and the subsequent proteolytic cleavage to mature PT beta-subunit
L5R/L6R/R1253A/I1254A/R1255A
-
substitution of the N-terminal L-Leu/L-Leu motif by dibasic-based motifs RIR or RR in combination with alanine substitution of the C-terminal motif prevents the alpha/beta-subunit precursor protein from reaching the Golgi apparatus for cleavage
L785W
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the DMAP interaction domain mutation has full activity toward alpha-MM but impaired ability to phosphorylate lysosomal acid hydrolases
N1153S
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
N115Q
-
electrophoretic migration similar to wild-type at 34 kDa, mutant sensitive to PNGase F treatment
N88Q
-
electrophoretic migration similar to wild-type at 34 kDa, mutant sensitive to PNGase F treatment
N88Q/N115Q
-
electrophoretic migration at 31 kDa, double mutant insensitive to PNGase F treatment, non-glycosylated polypeptide. Non-glycosylated gamma-subunits do not colocalize with the Golgi apparatus marker GM130
Q926P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
R1242A/R1243A/R1244A
-
by mutation of the arginine motif in beta subunit it is shown that this signal is not a functional endoplasmic reticulum retention signal
R1244A/R1245A/R1246A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
R1253A/I1254A/R1255A
-
mutant containing a mutation of C-terminal endoplasmic reticulum export motif mainly co-localizes with the cis-Golgi marker protein but fails to co-distribute with the endoplasmic reticulum protein marker
R334L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant fails to exit from the endoplasmic reticulum and is inactive
R334Q
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant fails to exit from the endoplasmic reticulum and is inactive
R587P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the R587P mutant shifts from a predominant endoplasmic reticulum localization to a predominant Golgi localization
R925A
-
mutation results in an uncleavable PT alpha/beta-subunit precursor protein. Mutant co-localizes mainly with the cis-Golgi marker protein, no detection in endoplasmic reticulum
R986C
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant in the Stealth domain trafficks to the Golgi
S15Y
-
naturally occurring mutation in the N-terminal cytoplasmic tail of the alpha-subunit leading to a mislocated enzyme, mistargeting of the mutant enzymes to lysosomes, where they are degraded, or to the cell surface and release into the medium, but the mutant enzyme shows 41% of wild-type activity. Half-life of the mutant is decreased compared to the wild-type enzyme
T1223del
-
naturally occurig heterozygous mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant T1223del is correctly transported and proteolytically cleaved into mature alpha- and beta-subunits exhibiting 85% of GlcNAc-1-phosphotransferase activity of the wild-type enzyme
T286M
naturally occuring mutation of the gamma-subunit that does not alter the gamma-subunit function, the mutant variant enters the Golgi like the wild-type enzyme
T644M
-
naturally occuring heterozygous mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant T644M is correctly transported and proteolytically cleaved into mature alpha- and beta-subunits exhibiting 50% of GlcNAc-1-phosphotransferase activity of the wild-type enzyme
V182D
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
V182D/Q205P
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
W81L
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, that has no effect on the mutant enzyme
DELTA1-47
-
N-terminal region (residues 1-47) of Saccharomyces cerevisiae Alg14 localizes its green fluorescent protein fusion to the endoplasmic reticulum membrane. Coimmunoprecipitation demonstrates that the N-terminal region of Alg14 is required for direct interaction with Alg7
G163A/G165A
-
mutant fails to rescue a loss of Alg14 function. Mutant is inactivated by loss of conserved G-loop
V131A/I135A/V139A/V143A/V146A/F150A
-
a mutant in which six hydrophobic residues are replaced with L-Ala is able to rescue the loss of Alg14 function, indicating that the mutated hydrophobic residues do not have a deleterious effect on Alg14 activity. Growth of these cells is extremely slow at 30°C
V131I/I135L/V139I/V143I/V146I/F150L
-
a mutant in which six hydrophobic residues are replaced with L-Ala is able to rescue the loss of Alg14 function
C505Y

-
naturally occuring missense mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients. The mutant shows 7% of wild-type activity
C505Y
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
I403T

-
naturally occuring missense mutation identified in Brazilian mucolipidosis MLII/MLIII alpha/beta patients, lack of processing of the mutant alpha/beta-subunit precursor I403T
I403T
-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant partially exits from the endoplasmic reticulum and is almost inactive
K1236M

-
proteolytic cleavage of mutant is not affected. Mutant is localised mainly in the Golgi apparatus
K1236M
-
site-directed mutagenesis, mutation involved in enzyme dysfunction
K4Q

-
patient mutation K4Q impairs the endoplasmic reticulum export of the PT alpha/beta-subunit precursor protein. Mutant shows reduced levels of the PT beta-subunit. Mutant is localised in the Golgi apparatus and in the endoplasmic reticulum
K4Q
-
naturally occurring mutation in the N-terminal cytoplasmic tail of the alpha-subunit leading to a mislocated enzyme, mistargeting of the mutant enzymes to lysosomes, where they are degraded, or to the cell surface and release into the medium, the mutant enzymes shows 32% of wild-type activity. The mutant K4Q alphabeta phosphotransferase contains increased complex-type N-linked glycans. Half-life of the mutant is decreased compared to the wild-type enzyme
K732N

-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the DMAP interaction domain mutation has full activity toward alpha-MM but impaired ability to phosphorylate lysosomal acid hydrolases
K732N
-
naturally occurring mutation in the DMAP interaction domain of the alpha-subunit identified in a patient with mucolipidosis II, the mutant exhibits full activity toward the simple sugar alpha-methyl D-mannoside but impaired phosphorylation activity toward acid hydrolases. The K732N mutation does not impair the transport of the alpha/beta precursor from the endoplasmic reticulum to the Golgi, nor the proteolytic cleavage that generates the alpha and beta subunits. Recombinant expression of the K732N mutant in a zebrafish model of mucolipidosis II fails to correct the phenotypic abnormalities
S399F

-
site-directed mutagenesis, mutation involved in enzyme dysfunction, the mutant partially exits from the endoplasmic reticulum and is almost inactive
S399F
-
a naturally occurring mucolipidosis III, MLIII, alphabeta mutant, the mutant enzyme remains in the endoplasmic reticulum and is not translocated to the Golgi due to reduced proteolytic cleavage of the precursor
additional information

-
generation of GNPTAB-deficient zebrafish, comprehensive analysis of the remaining missense mutations in GNPTAB reported in human mucolipidosis II and III alphabeta-patients using cell- and zebrafish-based approaches
additional information
-
the frameshift E757KfsX1 and the non-sense R587X mutations result in the retention of enzymatically inactive truncated precursor proteins in the endoplasmic reticulum due to loss of cytosolic endoplasmic reticulum exit motifs consistent with a severe clinical phenotype in homozygosity. Subcellular localization study of wild-type and mutant enzymes, as well as isolated alpha- and beta-subunits, overview
additional information
-
generation of GNPTAB-deficient zebrafish, comprehensive analysis of the remaining missense mutations in GNPTAB reported in human mucolipidosis II and III alphabeta-patients using cell- and zebrafish-based approaches; mutations in the GNPTAB gene give rise to the severe lysosomal storage disorder mucolipidosis II (I-cell disease) and the attenuated mucolipidosis III alphabeta (pseudo-Hurler polydystrophy). Subcellular localization ofalphabeta-phosphotransferase Stealth domain is altered compared to wild-type in HeLa cells
additional information
-
construction of GNPTAB-/- and GNPTG-/- mutant enzymes, all three alleles of GNPTAB are disrupted with one allele having a 17-bp deletion, c.216_232del, whereas the other two alleles have a 1-bp deletion c.221delC. The gamma-subunit-deficient DELTAN1-DMAP mutant has catalytic activity but is unable to phosphorylate lysosomal enzymes. Deletion of Notch 2 strongly inhibits phosphorylation of all the glycosidases, whereas deletion of Notch 1 is less detrimental, with levels of phosphorylation ranging from 100% down to 60% of wild-type activity. The effect of deleting the DMAP interaction domain is also variable, ranging from a 10% decrease in phosphorylation relative to wild-type to a 64% decrease in alpha-Man phosphorylation. Deletion of the S2 domain, which results in the loss of binding of the gamma-subunit, strongly inhibits phosphorylation of all the glycosidases
additional information
generation of GNTPAB knock-out mice
additional information
Q69ZN6 AND Q6S5C2
generation of GlcNAc-1-phosphotransferase-defective mice and enzyme-defective mouse embryonic fibroblasts
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adenylate kinase deficiency
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.
Apraxias
A study of the role of the FOXP2 and CNTNAP2 genes in persistent developmental stuttering.
Cardiomyopathies
A splicing mutation in the alpha/beta GlcNAc-1-phosphotransferase gene results in an adult onset form of mucolipidosis III associated with sensory neuropathy and cardiomyopathy.
Dyslexia
Association study of stuttering candidate genes GNPTAB, GNPTG and NAGPA with dyslexia in Chinese population.
Lysosomal Storage Diseases
Exome sequencing for mucolipidosis III: Detection of a novel GNPTAB gene mutation in a patient with a very mild phenotype.
Lysosomal Storage Diseases
GNPTAB missense mutations cause loss of GlcNAc-1-phosphotransferase activity in mucolipidosis type II through distinct mechanisms.
Lysosomal Storage Diseases
Mice lacking mannose 6-phosphate uncovering enzyme activity have a milder phenotype than mice deficient for N-acetylglucosamine-1-phosphotransferase activity.
Lysosomal Storage Diseases
Mice Lacking {alpha}/{beta} Subunits of GlcNAc-1-Phosphotransferase Exhibit Growth Retardation, Retinal Degeneration, and Secretory Cell Lesions.
Lysosomal Storage Diseases
Mucolipidosis II and III alpha/beta in Brazil: analysis of the GNPTAB gene.
Lysosomal Storage Diseases
Ultrastructural Analysis of Neuronal and Non-neuronal Lysosomal Storage in Mucolipidosis Type II Knock-in Mice.
Metabolic Diseases
Knockout of Lysosomal Enzyme-Targeting Gene Causes Abnormalities in Mouse Pup Isolation Calls.
Mucolipidoses
A compound heterozygous GNPTAB mutation causes mucolipidosis II with marked hair color change in a Han Chinese baby.
Mucolipidoses
A de novo or germline mutation in a family with Mucolipidosis III gamma: Implications for molecular diagnosis and genetic counseling.
Mucolipidoses
A novel intermediate mucolipidosis II/III?? caused by GNPTAB mutation in the cytosolic N-terminal domain.
Mucolipidoses
A novel single-chain antibody fragment for detection of mannose 6-phosphate-containing proteins: application in mucolipidosis type II patients and mice.
Mucolipidoses
A novel splice site mutation in the GNPTAB gene in an Iranian patient with mucolipidosis II ?/?.
Mucolipidoses
A role for inherited metabolic deficits in persistent developmental stuttering.
Mucolipidoses
A splicing mutation in the alpha/beta GlcNAc-1-phosphotransferase gene results in an adult onset form of mucolipidosis III associated with sensory neuropathy and cardiomyopathy.
Mucolipidoses
AAV8-mediated expression of N-acetylglucosamine-1-phosphate transferase attenuates bone loss in a mouse model of mucolipidosis II.
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.
Mucolipidoses
Alu-Alu Recombination Underlying the First Large Genomic Deletion in GlcNAc-Phosphotransferase Alpha/Beta (GNPTAB) Gene in a MLII Alpha/Beta Patient.
Mucolipidoses
An Alu insertion in compound heterozygosity with a microduplication in GNPTAB gene underlies Mucolipidosis II.
Mucolipidoses
Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site.
Mucolipidoses
Analysis of Mucolipidosis II/III GNPTAB Missense Mutations Identifies Domains of UDP-GlcNAc:lysosomal Enzyme GlcNAc-1-phosphotransferase Involved in Catalytic Function and Lysosomal Enzyme Recognition.
Mucolipidoses
Characterization of the mutant N-acetylglucosaminylphosphotransferase in I-cell disease and pseudo-Hurler polydystrophy: complementation analysis and kinetic studies.
Mucolipidoses
Clinical, biochemical and molecular characterization of Korean patients with mucolipidosis II/III and successful prenatal diagnosis.
Mucolipidoses
Compensatory expression of human N-Acetylglucosaminyl-1-phosphotransferase subunits in mucolipidosis type III gamma.
Mucolipidoses
Compensatory expression of human N-acetylglucosaminyl-1-phosphotransferase subunits in mucolipidosis type III gamma.
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.
Mucolipidoses
Elevated Bone Turnover in an Infantile Patient with Mucolipidosis II; No Association with Hyperparathyroidism.
Mucolipidoses
Enigmatic in vivo GlcNAc-1-phosphotransferase (GNPTG) transcript correction to wild type in two mucolipidosis III gamma siblings homozygous for nonsense mutations.
Mucolipidoses
Enzyme-specific differences in mannose phosphorylation between GlcNAc-1-phosphotransferase ?? and ? subunit deficient zebrafish support cathepsin proteases as early mediators of mucolipidosis pathology.
Mucolipidoses
Exome sequencing for mucolipidosis III: Detection of a novel GNPTAB gene mutation in a patient with a very mild phenotype.
Mucolipidoses
Fibroblasts from patients with I-cell disease and pseudo-Hurler polydystrophy are deficient in uridine 5'-diphosphate-N-acetylglucosamine: glycoprotein N-acetylglucosaminylphosphotransferase activity.
Mucolipidoses
Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases.
Mucolipidoses
GNPTAB missense mutations cause loss of GlcNAc-1-phosphotransferase activity in mucolipidosis type II through distinct mechanisms.
Mucolipidoses
Identification of a variant of mucolipidosis III (pseudo-Hurler polydystrophy): a catalytically active N-acetylglucosaminylphosphotransferase that fails to phosphorylate lysosomal enzymes.
Mucolipidoses
Identification of compound heterozygous mutations in GNPTG in three siblings of a Chinese family with mucolipidosis type III gamma.
Mucolipidoses
Knockout of Lysosomal Enzyme-Targeting Gene Causes Abnormalities in Mouse Pup Isolation Calls.
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.
Mucolipidoses
Mannose-6-phosphate pathway: A review on its role in lysosomal function and dysfunction.
Mucolipidoses
Mice Lacking {alpha}/{beta} Subunits of GlcNAc-1-Phosphotransferase Exhibit Growth Retardation, Retinal Degeneration, and Secretory Cell Lesions.
Mucolipidoses
Mislocalization of phosphotransferase as a cause of mucolipidosis III ??.
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.
Mucolipidoses
Molecular analysis of cell lines from patients with mucolipidosis II and mucolipidosis III.
Mucolipidoses
Molecular analysis of the GlcNac-1-phosphotransferase.
Mucolipidoses
Molecular analysis of the GNPTAB and GNPTG genes in 13 patients with mucolipidosis type II or type III - identification of eight novel mutations.
Mucolipidoses
Molecular characterization of 22 novel UDP-N-acetylglucosamine-1-phosphate transferase alpha- and beta-subunit (GNPTAB) gene mutations causing mucolipidosis types IIalpha/beta and IIIalpha/beta in 46 patients.
Mucolipidoses
Mucolipidosis II and III alpha/beta in Brazil: analysis of the GNPTAB gene.
Mucolipidoses
Mucolipidosis II and III alpha/beta: mutation analysis of 40 Japanese patients showed genotype-phenotype correlation.
Mucolipidoses
Mucolipidosis II is caused by mutations in GNPTA encoding the alpha/beta GlcNAc-1-phosphotransferase.
Mucolipidoses
Mucolipidosis II-related mutations inhibit the exit from the endoplasmic reticulum and proteolytic cleavage of GlcNAc-1-phosphotransferase precursor protein (GNPTAB).
Mucolipidoses
Mucolipidosis II: a single causal mutation in the N-acetylglucosamine-1-phosphotransferase gene (GNPTAB) in a French Canadian founder population.
Mucolipidoses
Mucolipidosis III GNPTG missense mutations cause misfolding of the ? subunit of GlcNAc-1-phosphotransferase.
Mucolipidoses
Mucolipidosis in a Chinese family with compound heterozygous mutations at the GNPTAB gene.
Mucolipidoses
Mucolipidosis type II ?/? with a homozygous missense mutation in the GNPTAB gene.
Mucolipidoses
Mucolipidosis type II in a domestic shorthair cat.
Mucolipidoses
Mucolipidosis Type II Secondary to GNPTAB Gene Deletion from India.
Mucolipidoses
Mucolipidosis types II and III and non-syndromic stuttering are associated with different variants in the same genes.
Mucolipidoses
Mutation Analysis of 16 Mucolipidosis II and III Alpha/Beta Chinese Children Revealed Genotype-Phenotype Correlations.
Mucolipidoses
Neonatal mucolipidosis type II alpha/beta due to compound heterozygosity for a known and novel GNPTAB mutation, and a concomitant heterozygous change in SERPINF1 inherited from the mother.
Mucolipidoses
Next Generation Sequencing identifies mutations in GNPTG gene as a cause of familial form of scleroderma-like disease.
Mucolipidoses
Pitfalls in the prenatal diagnosis of mucolipidosis II alpha/beta: A case report.
Mucolipidoses
Site-1 protease and lysosomal homeostasis.
Mucolipidoses
Solving a case of allelic dropout in the GNPTAB gene: implications in the molecular diagnosis of mucolipidosis type III alpha/beta.
Mucolipidoses
The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module.
Mucolipidoses
Three novel homozygous mutations in the GNPTG gene that cause mucolipidosis type III gamma.
Mucolipidoses
Two homozygous nonsense mutations of GNPTAB gene in two Chinese families with mucolipidosis II alpha/beta using targeted next-generation sequencing.
Mucolipidoses
Ultrastructural Analysis of Neuronal and Non-neuronal Lysosomal Storage in Mucolipidosis Type II Knock-in Mice.
Mucolipidoses
Using next-generation sequencing for the diagnosis of rare disorders: a family with retinitis pigmentosa and skeletal abnormalities.
Myopia
Novel Myopia Genes and Pathways Identified From Syndromic Forms of Myopia.
Retinal Degeneration
Mice Lacking {alpha}/{beta} Subunits of GlcNAc-1-Phosphotransferase Exhibit Growth Retardation, Retinal Degeneration, and Secretory Cell Lesions.
Retinitis Pigmentosa
Using next-generation sequencing for the diagnosis of rare disorders: a family with retinitis pigmentosa and skeletal abnormalities.
Stuttering
A Mutation Associated with Stuttering Alters Mouse Pup Ultrasonic Vocalizations.
Stuttering
A role for inherited metabolic deficits in persistent developmental stuttering.
Stuttering
A study of the role of the FOXP2 and CNTNAP2 genes in persistent developmental stuttering.
Stuttering
Association study of stuttering candidate genes GNPTAB, GNPTG and NAGPA with dyslexia in Chinese population.
Stuttering
Genetic approaches to understanding the causes of stuttering.
Stuttering
Genetics of Speech and Language Disorders.
Stuttering
Mucolipidosis types II and III and non-syndromic stuttering are associated with different variants in the same genes.
Stuttering
Mutations in the lysosomal enzyme-targeting pathway and persistent stuttering.
Stuttering
Variants in GNPTAB, GNPTG and NAGPA genes are associated with stutterers.
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Ben-Yoseph, Y.; Potier, M.; Pack, B.A.; Mitchell, D.A.; Melancon, S.B.; Nadler, H.L.
Molecular size of N-acetylglucosaminylphosphotransferase and alpha-N-acetylglucosaminyl phosphodiesterase as determined in situ in Golgi membranes by radiation inactivation
Biochem. J.
235
883-886
1986
Homo sapiens
brenda
Waheed, A.; Pohlmann, R.; Hasilik, A.; von Figura, K.
Subcellular location of two enzymes involved in the synthesis of phosphorylated recognition markers in lysosomal enzymes
J. Biol. Chem.
256
4150-4152
1981
Rattus norvegicus
brenda
Hiller, A.M.; Koro, L.A.; Marchase, R.B.
Glucose-1-phosphotransferase and N-acetylglucosamine-1-phosphotransferase have distinct acceptor specificities
J. Biol. Chem.
262
4377-4381
1987
Homo sapiens
brenda
Waheed, A.; Hasilik, A.; von Figura, K.
UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1-phosphotransferase. Partial purification and characterization of the rat liver Golgi enzyme
J. Biol. Chem.
257
12322-12331
1982
Rattus norvegicus
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Homo sapiens
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Rattus norvegicus
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Cricetulus griseus
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Homo sapiens, Mus musculus, Ovis aries, Rattus norvegicus
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Guillen, E.; Quesada-Allue, L.A.; Couso, R.O.
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Ceratitis capitata, Ceratitis capitata ARG-17
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Mus musculus
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Bos taurus
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Bos taurus
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Identification of UDP-N-acetylglucosamine-phosphotransferase-binding sites on the lysosomal proteases, cathepsins A, B, and D
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Rattus norvegicus
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Sun, Q.; Li, J.; Wang, C.; Huang, X.; Huang, H.; Du, D.; Liang, Y.; Han, H.
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Mus musculus, Mus musculus (Q6S5C2)
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Homo sapiens
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Homo sapiens, Homo sapiens (Q3T906)
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Homo sapiens (Q3T906)
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Homo sapiens, Homo sapiens (Q3T906)
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Alg14 organizes the formation of a multiglycosyltransferase complex involved in initiation of lipid-linked oligosaccharide biosynthesis
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2012
Saccharomyces cerevisiae
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Qian, Y.; West, C.M.; Kornfeld, S.
UDP-GlcNAc:Glycoprotein N-acetylglucosamine-1-phosphotransferase mediates the initial step in the formation of the methylphosphomannosyl residues on the high mannose oligosaccharides of Dictyostelium discoideum glycoproteins
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Dictyostelium discoideum
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Qian, Y.; Lee, I.; Lee, W.; Qian, M.; Kudo, M.; Canfield, W.; Lobel, P.; Kornfeld, S.
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Homo sapiens
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Encarnacao, M.; Kollmann, K.; Trusch, M.; Braulke, T.; Pohl, S.
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Homo sapiens
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Franke, M.; Braulke, T.; Storch, S.
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Homo sapiens, Homo sapiens (Q3T906)
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Velho, R.V.; De Pace, R.; Kluender, S.; Sperb-Ludwig, F.; Lourenco, C.M.; Schwartz, I.V.; Braulke, T.; Pohl, S.
Analyses of disease-related GNPTAB mutations define a novel GlcNAc-1-phosphotransferase interaction domain and an alternative site-1 protease cleavage site
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2015
Homo sapiens, Homo sapiens (Q3T906)
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van Meel, E.; Kornfeld, S.
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Homo sapiens, Homo sapiens (Q9UJJ9)
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Qian, Y.; van Meel, E.; Flanagan-Steet, H.; Yox, A.; Steet, R.; Kornfeld, S.
Analysis of mucolipidosis II/III GNPTAB missense mutations identifies domains of UDP-GlcNAc:lysosomal enzyme GlcNAc-1-phosphotransferase involved in catalytic function and lysosomal enzyme recognition
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Danio rerio, Homo sapiens, Homo sapiens (Q3T906)
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van Meel, E.; Lee, W.S.; Liu, L.; Qian, Y.; Doray, B.; Kornfeld, S.
Multiple domains of GlcNAc-1-phosphotransferase mediate recognition of lysosomal enzymes
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Homo sapiens (Q3T906 AND Q9UJJ9)
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Ko, A.R.; Jin, D.K.; Cho, S.Y.; Park, S.W.; Przybylska, M.; Yew, N.S.; Cheng, S.H.; Kim, J.S.; Kwak, M.J.; Kim, S.J.; Sohn, Y.B.
AAV8-mediated expression of N-acetylglucosamine-1-phosphate transferase attenuates bone loss in a mouse model of mucolipidosis II
Mol. Genet. Metab.
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2016
Mus musculus, Mus musculus (Q69ZN6)
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Qian, Y.; Flanagan-Steet, H.; van Meel, E.; Steet, R.; Kornfeld, S.A.
The DMAP interaction domain of UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase is a substrate recognition module
Proc. Natl. Acad. Sci. USA
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2013
Homo sapiens (Q3T906 AND Q9UJJ9)
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van Meel, E.; Qian, Y.; Kornfeld, S.A.
Mislocalization of phosphotransferase as a cause of mucolipidosis III alphabeta
Proc. Natl. Acad. Sci. USA
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3532-3537
2014
Homo sapiens, Homo sapiens (Q3T906)
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Blanz, J.; Zunke, F.; Markmann, S.; Damme, M.; Braulke, T.; Saftig, P.; Schwake, M.
Mannose 6-phosphate-independent lysosomal sorting of LIMP-2
Traffic
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1127-1136
2015
Homo sapiens (Q3T906 AND Q9UJJ9), Mus musculus, Mus musculus (Q69ZN6 AND Q6S5C2)
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