Literature summary for 1.6.5.5 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.

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Localization

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

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q08257	-	-
Saccharomyces cerevisiae	P38230	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HeLa cell	-	Homo sapiens	-

Synonyms

Synonyms	Comment	Organism
zeta-Crystallin	-	Homo sapiens
zeta-Crystallin	-	Saccharomyces cerevisiae
Zta1p	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
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
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)