Literature summary for 2.3.1.78 extracted from

Fedele, A.O.; Isenmann, S.; Kamei, M.; Snel, M.F.; Trim, P.J.; Proud, C.G.; Hopwood, J.J.
Lysosomal N-acetyltransferase interacts with ALIX and is detected in extracellular vesicles (2018), Biochim. Biophys. Acta, 1865, 1451-1464 .

Search for more literature for 2.3.1.78

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293 and HEK-293T cell	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endosome	HGSNAT coimmunoprecipitates with antibodies to ALIX, which is associated with the endosomal sorting complexes required for transport proteins	Homo sapiens	5768	-
lysosome	-	Homo sapiens	5764	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q68CP4	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
fibroblast	primary fibroblast	Homo sapiens	-
urine	extracellular vesicles isolated from urine	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
HGSNAT	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	mutation of a putative LYPXnL-based binding site within HGSNAT for the V-domain of ALIX ablates association of HGSNAT with ALIX, posttranslational maturation, and transport through the endolysosomal network. A mutation within the V-domain of ALIX demonstrates enhanced HGSNAT association. HGSNAT still coimmunoprecipitates with truncations of ALIX lacking the V-domain. Knockdown of ALIX does not inhibit HGSNAT trafficking through the endo-lysosomal network	Homo sapiens

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Release 2023.1 (January 2023)