BAIT

P38B

186F5S, BG:DS00797.3, CG7393, D-p38, D-p38 MAPK, D-p38b, Dm p38b, Dmel\CG7393, Dmp38b, Dp38, Dp38b, ESTS:186F5S, Mpk34C, anon-sts23, p38, p38 MAPK, p38 beta, p38Kb, p38beta, Dmel_CG7393
p38b MAP kinase
Drosophila melanogaster
PREY

PTP-ER

CG9856, Dmel\CG9856, ER2-5, Dmel_CG9856
Protein tyrosine phosphatase-ERK/Enhancer of Ras1
Drosophila melanogaster

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.

Publication

High-resolution protein interaction map of the Drosophila melanogaster p38 mitogen-activated protein kinases reveals limited functional redundancy.

Belozerov VE, Lin ZY, Gingras AC, McDermott JC, Michael Siu KW

Functional redundancy is a pivotal mechanism that supports the robustness of biological systems at a molecular, cellular, and organismal level. The extensive prevalence of redundancy in molecular networks has been highlighted by recent systems biology studies; however, a detailed mechanistic understanding of redundant functions in specific signaling modules is often missing. We used affinity purification of protein complexes coupled to ... [more]

Mol. Cell. Biol. Sep. 01, 2012; 32(18);3695-706 [Pubmed: 22801366]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
P38B PTP-ER
Two-hybrid
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.

High-BioGRID
-

Curated By