BAIT

VIP1

F2J6.6, F2J6_6, SUE3, VIRE2-INTERACTING PROTEIN, VIRE2-interacting protein 1, sulphate utilization efficiency 3, AT1G43700
VIRE2-interacting protein 1
Arabidopsis thaliana (Columbia)
PREY

AT2G31370

T28P16.14, T28P16_14
putative transcription factor PosF21
GO Process (1)
GO Function (2)
GO Component (1)

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

Analysis of functions of VIP1 and its close homologs in osmosensory responses of Arabidopsis thaliana.

Tsugama D, Liu S, Takano T

VIP1 is a bZIP protein in Arabidopsis thaliana. VIP1 accumulates in the nucleus under hypo-osmotic conditions and interacts with the promoters of hypo-osmolarity-responsive genes, CYP707A1 and CYP707A3 (CYP707A1/3), but neither overexpression of VIP1 nor truncation of its DNA-binding region affects the expression of CYP707A3 in vivo, raising the possibility that VIP and other proteins are functionally redundant. Here we show ... [more]

PLoS ONE Aug. 06, 2014; 9(8);e103930 [Pubmed: 25093810]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
VIP1 AT2G31370
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