Literature summary for 2.3.2.27 extracted from

Riley, B.E.; Lougheed, J.C.; Callaway, K.; Velasquez, M.; Brecht, E.; Nguyen, L.; Shaler, T.; Walker, D.; Yang, Y.; Regnstrom, K.; Diep, L.; Zhang, Z.; Chiou, S.; Bova, M.; Artis, D.R.; Yao, N.; Baker, J.; Yednock, T.; Johnston, J.A.
Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases (2013), Nat. Commun., 4, 1982.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization of isoform parkin protein residues 141-465 including RING 0 and RING-between-RING domains. The protein is assembled into two compact domain groups separated by linkers. The catalytic network consists of residues C431 and H433. Parkin functions as a RING/HECT hybrid ubiquitin ligase	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C431A	mutation eliminates parkin-catalyzed degradation of mitochondria	Homo sapiens
C431S	mutation eliminates parkin-catalyzed degradation of mitochondria. Mutant forms an ubiquitin oxyester only in presence of mitochondrial toxin CCCP	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60260	isoform parkin	-

Synonyms

Synonyms	Comment	Organism
Parkin	-	Homo sapiens
Parkinson juvenile disease protein 2	-	Homo sapiens

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Release 2023.1 (January 2023)