Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Protein binding and signaling properties of RIN1 suggest a unique effector function.

Han L, Wong D, Dhaka A, Afar D, White M, Xie W, Herschman H, Witte O, Colicelli J

Human RIN1 was first characterized as a RAS binding protein based on the properties of its carboxyl-terminal domain. We now show that full-length RIN1 interacts with activated RAS in mammalian cells and defines a minimum region of 434 aa required for efficient RAS binding. RIN1 interacts with the "effector domain" of RAS and employs some RAS determinants that are common ... [more]

Proc. Natl. Acad. Sci. U.S.A. May. 13, 1997; 94(10);4954-9 [Pubmed: 9144171]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

YWHAB

Gene Ontology Biological Process

Gene Ontology Molecular Function

enzyme binding [ISO]histone deacetylase binding [ISO]phosphoprotein binding [ISO]phosphoserine binding [ISO]protein C-terminus binding [ISO]protein binding [IPI]protein complex binding [ISO]protein domain specific binding [IDA, ISO]transcription corepressor activity [ISO]

Gene Ontology Cellular Component

RIN1