PREY

CDKN1B

CDKN4, KIP1, MEN1B, MEN4, P27KIP1
cyclin-dependent kinase inhibitor 1B (p27, Kip1)
GO Process (23)
GO Function (4)
GO Component (5)
Homo sapiens

Biochemical Activity (Ubiquitination)

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.

Publication

Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation.

Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA

Cullin-RING ligases (CRLs) comprise the largest ubiquitin E3 subclass, in which a central cullin subunit links a substrate-binding adaptor with an E2-binding RING. Covalent attachment of the ubiquitin-like protein NEDD8 to a conserved C-terminal domain (ctd) lysine stimulates CRL ubiquitination activity and prevents binding of the inhibitor CAND1. Here we report striking conformational rearrangements in the crystal structure of NEDD8~Cul5(ctd)-Rbx1 ... [more]

Cell Sep. 19, 2008; 134(6);995-1006 [Pubmed: 18805092]

Throughput

  • Low Throughput

Additional Notes

  • E2:Cdc34
  • Figure S10

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDKN1B RBX1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High-BioGRID
3443909

Curated By

  • BioGRID