BAIT

THAP11

CTG-B43a, CTG-B45d, RONIN, HRIHFB2206
THAP domain containing 11
GO Process (0)
GO Function (3)
GO Component (3)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

PSMC5

S8, SUG-1, SUG1, TBP10, TRIP1, p45, p45/SUG
proteasome (prosome, macropain) 26S subunit, ATPase, 5
GO Process (25)
GO Function (5)
GO Component (10)
Homo sapiens

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.

Publication

Construction and characterization of a normalized yeast two-hybrid library derived from a human protein-coding clone collection.

DeGrado-Warren J, Dufford M, Chen J, Bartel PL, Shattuck D, Frech GC

The nuclear yeast two-hybrid (Y2H) system is the most widely used technology for detecting interactions between proteins. A common approach is to screen specific test proteins (baits) against large compilations of randomly cloned proteins (prey libraries). For eukaryotic organisms, libraries have traditionally been generated using messenger RNA (mRNA) extracted from various tissues and cells. Here we present a library construction ... [more]

BioTechniques Feb. 01, 2008; 44(2);265-73 [Pubmed: 18330356]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PSMC5 THAP11
Affinity Capture-MS
Affinity Capture-MS

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 is identified by mass spectrometric methods.

High0.9999BioGRID
2227113
PSMC5 THAP11
Affinity Capture-MS
Affinity Capture-MS

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 is identified by mass spectrometric methods.

High0.9999BioGRID
3112005

Curated By

  • BioGRID