Literature summary for 3.1.3.1 extracted from

Sultana, S.; Al-Shawafi, H.A.; Makita, S.; Sohda, M.; Amizuka, N.; Takagi, R.; Oda, K.
An asparagine at position 417 of tissue-nonspecific alkaline phosphatase is essential for its structure and function as revealed by analysis of the N417S mutation associated with severe hypophosphatasia (2013), Mol. Genet. Metab., 109, 282-288.

Search for more literature for 3.1.3.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in COS-1 cells and CHO K1 Tet-On cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N417D	mutation abolishes the dimerization without perturbing its cell surface localization	Homo sapiens
N417E	mutation abolishes the dimerization without perturbing its cell surface localization	Homo sapiens
N417S	mutation associated with severe hypophosphatasia, mutants lack enzymic activity. Mutant undergoes N-linked oligosaccharide processing and appears on the cell surface similar to wild-type. Mutant fails to assemble into a dimer structure, which is needed for the catalytic function	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell surface	-	Homo sapiens	9986	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P05186	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	mature form of 80 ka bears complex-type oligosaccharides. The 80 kDa form is sensitive to neuraminidase, but is resistant to treatment with Endo H	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)