BAIT

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)
PREY

RCN1

ATB BETA BETA, EER1, ENHANCED ETHYLENE RESPONSE 1, F2J7.19, F2J7_19, PHOSPHOPROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT A, REGA, ROOTS CURL IN NPA, SERINE/THREONINE PROTEIN PHOSPHATASE TYPE 2A REGULATORY SUBUNIT A, AT1G25490
serine/threonine-protein phosphatase 2A regulatory subunit A alpha isoform
Arabidopsis thaliana (Columbia)

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

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
AT1G50370 RCN1
Affinity Capture-Western
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.

Low-BioGRID
-
AT1G50370 RCN1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

Low-BioGRID
-
AT1G50370 RCN1
Co-fractionation
Co-fractionation

Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.

High0.6849BioGRID
2918902

Curated By

  • BioGRID