BAIT

NPLOC4

Npl4
nuclear protein localization 4 homolog (S. cerevisiae)
GO Process (2)
GO Function (4)
GO Component (3)
Rattus norvegicus
PREY

VCP

3110001E05, CDC48, p97, p97/VCP, RP23-124L1.5
valosin containing protein
GO Process (19)
GO Function (13)
GO Component (15)
Mus musculus

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy.

Bebeacua C, Foerster A, McKeown C, Meyer HH, Zhang X, Freemont PS

p97 is a key regulator of numerous cellular pathways and associates with ubiquitin-binding adaptors to remodel ubiquitin-modified substrate proteins. How adaptor binding to p97 is coordinated and how adaptors contribute to substrate remodeling is unclear. Here we present the 3D electron cryomicroscopy reconstructions of the major Ufd1-Npl4 adaptor in complex with p97. Our reconstructions show that p97-Ufd1-Npl4 is highly dynamic ... [more]

Proc. Natl. Acad. Sci. U.S.A. Jan. 24, 2012; 109(4);1098-103 [Pubmed: 22232657]

Throughput

  • Low Throughput

Additional Notes

  • 3D reconstructions and CryoEM Analysis

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NPLOC4 VCP
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
-

Curated By

  • BioGRID