BAIT

EIR1

AGR, AGR1, AGRAVITROPIC ROOT, AGRAVITROPIC ROOT 1, ARABIDOPSIS THALIANA PIN-FORMED 2, ATPIN2, AUXIN TRANSPORT PROTEIN EIR1, ETHYLENE INSENSITIVE ROOT 1, MUL3.3, MUL3_3, PIN-FORMED 2, PIN2, POLAR-AUXIN-TRANSPORT EFFLUX COMPONENT AGRAVITROPIC 1, WAV6, WAVY ROOTS 6, AT5G57090
auxin efflux carrier component 2
Arabidopsis thaliana (Columbia)
PREY

AT1G50370

F14I3.5, F14I3_5
phytochrome-associated serine/threonine protein phosphatase 1
GO Process (0)
GO Function (1)
GO Component (1)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

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

A PP6-Type Phosphatase Holoenzyme Directly Regulates PIN Phosphorylation and Auxin Efflux in Arabidopsis.

Dai M, Zhang C, Kania U, Chen F, Xue Q, McCray T, Li G, Qin G, Wakeley M, Terzaghi W, Wan J, Zhao Y, Xu J, Friml J, Deng XW, Wang H

The directional transport of the phytohormone auxin depends on the phosphorylation status and polar localization of PIN-FORMED (PIN) auxin efflux proteins. While PINIOD (PID) kinase is directly involved in the phosphorylation of PIN proteins, the phosphatase holoenzyme complexes that dephosphorylate PIN proteins remain elusive. Here, we demonstrate that mutations simultaneously disrupting the function of Arabidopsis thaliana FyPP1 (for Phytochrome-associated serine/threonine ... [more]

Unknown Jun. 21, 2012; 0(0); [Pubmed: 22715043]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
EIR1 AT1G50370
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.

Low-BioGRID
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Curated By

  • BioGRID