Ontology highlight
ABSTRACT:
SUBMITTER: Lorick KL
PROVIDER: S-EPMC18039 | biostudies-literature | 1999 Sep
REPOSITORIES: biostudies-literature
Lorick K L KL Jensen J P JP Fang S S Ong A M AM Hatakeyama S S Weissman A M AM
Proceedings of the National Academy of Sciences of the United States of America 19990901 20
A RING finger-containing protein (AO7) that binds ubiquitin-conjugating enzymes (E2s) and is a substrate for E2-dependent ubiquitination was identified. Mutations of cation-coordinating residues within AO7's RING finger abolished ubiquitination, as did chelation of zinc. Several otherwise-unrelated RING finger proteins, including BRCA1, Siah-1, TRC8, NF-X1, kf-1, and Praja1, were assessed for their ability to facilitate E2-dependent ubiquitination. In all cases, ubiquitination was observed. The ...[more]