Literature summary for 2.3.2.27 extracted from

Vander Kooi, C.W.; Ohi, M.D.; Rosenberg, J.A.; Oldham, M.L.; Newcomer, M.E.; Gould, K.L.; Chazin, W.J.
The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases (2006), Biochemistry, 45, 121-130.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of fragment Prp19(1-133), which contains both the N-terminal U-box and central coiled-coil domain, to 1.38 A resolution. The Prp19 U-box domain exists in a dimeric state in the context of intact Prp19. The hydrophobic character of the dimer interface is due to residues Leu15, Ile22, Val51, and Ile53. All four positions are conserved long-chain hydrophobic residues	Saccharomyces cerevisiae

Protein Variants

Protein Variants	Comment	Organism
L15E	mutant in U-box domain interface, abrogates U-box dimer formation and is lethal in vivo	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	P32523	isoform Prp19	-

Synonyms

Synonyms	Comment	Organism
pre-mRNA-splicing factor 19	-	Saccharomyces cerevisiae
PRP19	-	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)