BAIT

CDKNX

Xic-1, Xic1, p27XIC1, p28
cyclin-dependent kinase inhibitor xic1
GO Process (0)
GO Function (0)
GO Component (0)
Xenopus laevis
PREY

CDK2

eg1
cyclin-dependent kinase 2
GO Process (0)
GO Function (0)
GO Component (0)
Xenopus laevis

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

The C-terminal domain of the Xenopus cyclin-dependent kinase inhibitor, p27Xic1, is both necessary and sufficient for phosphorylation-independent proteolysis.

Chuang LC, Zhu XN, Herrera CR, Tseng HM, Pfleger CM, Block K, Yew PR

Cell cycle progression is regulated by cyclin-dependent kinases (CDKs), cyclins, and CDK inhibitors. In the frog, Xenopus laevis, the CDK inhibitor p27(Xic1) (Xic1) inhibits DNA synthesis by negatively regulating CDK2-cyclin E. Using the frog egg extract as a model system for the study of Xic1, studies have demonstrated that Xic1 protein levels are regulated by nuclear ubiquitination and proteolysis. To ... [more]

J. Biol. Chem. Oct. 21, 2005; 280(42);35290-8 [Pubmed: 16118210]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDK2 CDKNX
Affinity Capture-Western
Affinity Capture-Western

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Low-BioGRID
-
CDKNX CDK2
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-

Curated By

  • BioGRID