BAIT

TP53

BCC7, LFS1, P53, TRP53
tumor protein p53
GO Process (61)
GO Function (25)
GO Component (14)

Gene Ontology Biological Process

Homo sapiens

Proximity Label-MS

An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

Genome-wide CRISPR screens identify novel regulators of wild-type and mutant p53 stability.

Lue Y, Cho T, Mukherjee S, Suarez CF, Gonzalez-Foutel NS, Malik A, Martinez S, Dervovic D, Oh RH, Langille E, Al-Zahrani KN, Hoeg L, Lin ZY, Tsai R, Mbamalu G, Rotter V, Ashton-Prolla P, Moffat J, Chemes LB, Gingras AC, Oren M, Durocher D, Schramek D

Tumor suppressor p53 (TP53) is frequently mutated in cancer, often resulting not only in loss of its tumor-suppressive function but also acquisition of dominant-negative and even oncogenic gain-of-function traits. While wild-type p53 levels are tightly regulated, mutants are typically stabilized in tumors, which is crucial for their oncogenic properties. Here, we systematically profiled the factors that regulate protein stability of ... [more]

Mol Syst Biol Jun. 01, 2024; 20(6);719-740 [Pubmed: 38580884]

Throughput

  • High Throughput

Additional Notes

  • BioID
  • High confidence BioID interactions had a minimum unique mass spectral count of 2 and SAINT BFDR score =< 0.01
  • MG132 proteasome inhibitor treatment
  • TP53_R273H mutant

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CSNK2B TP53
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
2533412
TP53 CSNK2B
PCA
PCA

A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.

High-BioGRID
662332

Curated By

  • BioGRID