BAIT

TNFRSF1A

CD120a, FPF, TNF-R, TNF-R-I, TNF-R1, TNF-R55, TNF-alphaR1, TNFAR, TNFR60, TNFRI, TNFRp55, TNFalpha-R1, Tnfr-2, Tnfr1, p55, p55-R
tumor necrosis factor receptor superfamily, member 1a
GO Process (23)
GO Function (5)
GO Component (13)
Mus musculus
PREY

UBC

2700054O04Rik, AI194771, Rps27a, TI-225, Uba52, Ubb
ubiquitin C
GO Process (1)
GO Function (3)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Mus musculus

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.

Publication

SPATA2 restricts OTULIN-dependent LUBAC activity independently of CYLD.

Griewahn L, Mueller-Foxworth M, Peintner L, Wissler M, Weiss M, Brauns-Schubert P, Massoumi R, Borner C, Gross O, Yabal M, Charvet C, Maurer U

SPATA2 mediates the recruitment of CYLD to immune receptor complexes by bridging the interaction of CYLD with the linear ubiquitylation assembly complex (LUBAC) component HOIP. Whether SPATA2 exhibits functions independently of CYLD is unclear. Here, we show that, while Cyld-/- and Spata2-/- mice are viable, double mutants exhibit highly penetrant perinatal lethality, indicating independent functions of SPATA2 and CYLD. Cyld-/-Spata2-/- ... [more]

Cell Rep Jan. 31, 2023; 42(1);111961 [Pubmed: 36640323]

Throughput

  • Low Throughput

Additional Notes

  • #LPPI
  • Likely protein-protein interaction
  • TNFR1 complex IP'd by pulling down TNF

Curated By

  • BioGRID