Literature summary for 3.4.24.87 extracted from

Peyvandi, F.; Lavoretano, S.; Palla, R.; Valsecchi, C.; Merati, G.; De Cristofaro, R.; Rossi, E.; Mannuccio Mannucci, P.
Mechanisms of the interaction between two ADAMTS13 gene mutations leading to severe deficiency of enzymatic activity (2006), Hum. Mutat., 27, 330-336.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes in HEK 293 and COS-7 cells	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
G1239V	mutation leads to a secretion defect causing intracellular accumulation of the protease	Homo sapiens
V88M	mutation leads to a defect of secretion of the protease associated with a reduction of enzymatic activity	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
endoplasmic reticulum	homogeneous distribution of wild-type ADAMTS13 in cis-Golgi and endoplasmic reticulum compartments. Reduction of ADAMTS13(Val88Met) in both compartments. ADAMTS13(Gly1239Val) fails to reach the cis-Golgi compartment and remains in the endoplasmic reticulum	Homo sapiens	5783	-
Golgi apparatus	homogeneous distribution of wild-type ADAMTS13 in cis-Golgi and endoplasmic reticulum compartments. Reduction of ADAMTS13(Val88Met) in both compartments. ADAMTS13(Gly1239Val) fails to reach the cis-Golgi compartment and remains in the endoplasmic reticulum	Homo sapiens	5794	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	genetic analysis of a woman with a family history of chronic recurrent thrombotic thrombocytopenic purpurea and undetectable plasma levels of ADAMTS13 reveals two missense mutations in the heterozygous state: Val88Met substitution in the metalloprotease domain and Gly1239Val substitution in the first CUB domain of ADAMTS13	-

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Release 2023.1 (January 2023)