BAIT

SH3RF1

POSH, RNF142, SH3MD2
SH3 domain containing ring finger 1
GO Process (3)
GO Function (1)
GO Component (1)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex.

Figueroa C, Tarras S, Taylor J, Vojtek AB

We demonstrate that POSH, a scaffold for the JNK signaling pathway, binds to Akt2. A POSH mutant that is unable to bind Akt2 (POSH W489A) exhibits enhanced-binding to MLK3, and this increase in binding is accompanied by increased activation of the JNK signaling pathway. In addition, we show that the association of MLK3 with POSH is increased upon inhibition of ... [more]

J. Biol. Chem. Nov. 28, 2003; 278(48);47922-7 [Pubmed: 14504284]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
AKT2 SH3RF1
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
716205
AKT2 SH3RF1
Two-hybrid
Two-hybrid

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.

Low-BioGRID
-
AKT2 SH3RF1
Two-hybrid
Two-hybrid

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.

High-BioGRID
2709500

Curated By

  • BioGRID