Literature summary for 2.7.8.17 extracted from

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 (2013), Proc. Natl. Acad. Sci. USA, 110, 10246-10251.

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Cloned(Commentary)

Cloned (Comment)	Organism
plasmids encoding WT and K732N alpha/beta cDNA with C-terminal V5/His tags are generated and transfected into HEK-293 cells and monitoring of the proteolytic cleavage of the alpha/beta precursor by the appearance of the mature V5-tagged beta-subunit. Recombinant expression of wild-type and mutant GST-DMAP domain	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
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	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
Golgi apparatus	-	Homo sapiens	5794	-

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose	Homo sapiens	substrates are lysosomal acid hydrolases	UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q3T906 AND Q9UJJ9	alpha/beta-, and gamma-subunit encoding genes	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	proteolytic cleavage of the alpha/beta enzyme precursor	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetyl-D-glucosamine + alpha-methyl-D-mannoside	-	Homo sapiens	UMP + 6-(N-acetyl-D-glucosaminyl-phospho)-alpha-methyl D-mannoside	-	?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose	substrates are lysosomal acid hydrolases	Homo sapiens	UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose	-	?
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme 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	Homo sapiens	UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose	-	?

Subunits

Subunits	Comment	Organism
heterohexamer	alpha2beta2gamma2	Homo sapiens

Synonyms

Synonyms	Comment	Organism
GlcNAc-1-phosphotransferase	-	Homo sapiens
UDP-GlcNAc:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase	-	Homo sapiens

General Information

General Information	Comment	Organism
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	Homo sapiens
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	Homo sapiens

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Release 2023.1 (January 2023)