BAIT

PIP1;4

A_IG005I10.2, A_IG005I10_2, F5I10.2, F5I10_2, PIP1E, PLASMA MEMBRANE INTRINSIC PROTEIN 1E, TMP-C, TRANSMEMBRANE PROTEIN C, plasma membrane intrinsic protein 1;4, AT4G00430
plasma membrane intrinsic protein 1;4
GO Process (3)
GO Function (1)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)
PREY

PIP3

PIP2;7, PIP3A, PLASMA MEMBRANE INTRINSIC PROTEIN 2;7, PLASMA MEMBRANE INTRINSIC PROTEIN 3, PLASMA MEMBRANE INTRINSIC PROTEIN 3A, SIMIP, T12J5.9, AT4G35100
plasma membrane intrinsic protein 3
GO Process (2)
GO Function (2)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

Evidence for network evolution in an Arabidopsis interactome map.

Braun P, Carvunis AR, Charloteaux B, Dreze M, Ecker JR, Hill DE, Roth FP, Vidal M, Galli M, Balumuri P, Bautista V, Chesnut JD, Kim RC, de los Reyes C, Gilles P, Kim CJ, Matrubutham U, Mirchandani J, Olivares E, Patnaik S, Quan R, Ramaswamy G, Shinn P, Swamilingiah GM, Wu S, Ecker JR, Dreze M, Byrdsong D, Dricot A, Duarte M, Gebreab F, Gutierrez BJ, MacWilliams A, Monachello D, Mukhtar MS, Poulin MM, Reichert P, Romero V, Tam S, Waaijers S, Weiner EM, Vidal M, Hill DE, Braun P, Galli M, Carvunis AR, Cusick ME, Dreze M, Romero V, Roth FP, Tasan M, Yazaki J, Braun P, Ecker JR, Carvunis AR, Ahn YY, Barabási AL, Charloteaux B, Chen H, Cusick ME, Dangl JL, Dreze M, Ecker JR, Fan C, Gai L, Galli M, Ghoshal G, Hao T, Hill DE, Lurin C, Milenkovic T, Moore J, Mukhtar MS, Pevzner SJ, Przulj N, Rabello S, Rietman EA, Rolland T, Roth FP, Santhanam B, Schmitz RJ, Spooner W, Stein J, Tasan M, Vandenhaute J, Ware D, Braun P, Vidal M.

Plants have unique features that evolved in response to their environments and ecosystems. A full account of the complex cellular networks that underlie plant-specific functions is still missing. We describe a proteome-wide binary protein-protein interaction map for the interactome network of the plant Arabidopsis thaliana containing about 6200 highly reliable interactions between about 2700 proteins. A global organization of plant ... [more]

Science Jul. 29, 2011; 333(6042);601-7 [Pubmed: 21798944]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
PIP3 PIP1;4
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.

High-BioGRID
1251904

Curated By

  • BioGRID