Literature summary extracted from

Porte, S.; Crosas, E.; Yakovtseva, E.; Biosca, J.A.; Farres, J.; Fernandez, M.R.; Pares, X.
MDR quinone oxidoreductases: the human and yeast zeta-crystallins (2009), Chem. Biol. Interact., 178, 288-294.

Localization

EC Number	Localization	Comment	Organism	GeneOntology No.	Textmining
1.6.5.5	cytoplasm	-	Homo sapiens	5737	-
1.6.5.5	cytoplasm	localizes in both cytoplasm and nucleus	Saccharomyces cerevisiae	5737	-
1.6.5.5	additional information	not in nucleus	Homo sapiens	-	-
1.6.5.5	nucleus	localizes in both cytoplasm and nucleus	Saccharomyces cerevisiae	5634	-

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.6.5.5	Homo sapiens	Q08257	-	-
1.6.5.5	Saccharomyces cerevisiae	P38230	-	-

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.6.5.5	HeLa cell	-	Homo sapiens	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.6.5.5	zeta-Crystallin	-	Homo sapiens
1.6.5.5	zeta-Crystallin	-	Saccharomyces cerevisiae
1.6.5.5	Zta1p	-	Saccharomyces cerevisiae

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.6.5.5	NADPH	interference of NADPH on Zta1p binding to RNA is much lower than that of NADPH on human zeta-crystallin, consistent with a weaker binding of NADPH to the yeast enzyme	Saccharomyces cerevisiae
1.6.5.5	NADPH	NADPH, but not NADH, competitively prevents binding of zeta-crystallin to RNA, suggesting that the cofactor-binding site is involved in RNA binding	Homo sapiens

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Release 2023.1 (January 2023)