Literature summary for 2.3.2.31 extracted from

Zhang, Y.; Liao, X.H.; Xie, H.Y.; Shao, Z.M.; Li, D.Q.
RBR-type E3 ubiquitin ligase RNF144A targets PARP1 for ubiquitin-dependent degradation and regulates PARP inhibitor sensitivity in breast cancer cells (2017), Oncotarget, 8, 94505-94518 .

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Application

Application	Comment	Organism
medicine	isoform RNF144A interacts with poly(ADP-ribose) polymerase PARP1 through its carboxy-terminal region containing the transmembrane domain, and targets PARP1 for ubiquitination and subsequent proteasomal degradation. Induced expression of RNF144A decreases PARP1 protein levels and renders breast cancer cells resistant to the clinical-grade PARP inhibitor olaparib. Knockdown of endogenous RNF144A increases PARP1 protein levels and enhances cellular sensitivity to olaparib	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293T cell	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P50876	isoform RNF144A	-

Synonyms

Synonyms	Comment	Organism
RNF144A	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	isoform RNF144A interacts with poly(ADP-ribose) polymerase PARP1, a DNA repair protein, through its carboxy-terminal region containing the transmembrane domain, and targets PARP1 for ubiquitination and subsequent proteasomal degradation. Induced expression of RNF144A decreases PARP1 protein levels and renders breast cancer cells resistant to the clinical-grade PARP inhibitor olaparib. Knockdown of endogenous RNF144A increases PARP1 protein levels and enhances cellular sensitivity to olaparib	Homo sapiens

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Release 2023.1 (January 2023)