BAIT

LP1

ARABIDOPSIS THALIANA LIPID TRANSFER PROTEIN 1, ATLTP1, LIPID TRANSFER PROTEIN 1, LTP1, T6A23.26, T6A23_26, AT2G38540
non-specific lipid-transfer protein 1
GO Process (1)
GO Function (1)
GO Component (5)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Arabidopsis thaliana (Columbia)
PREY

CAM1

ACAM-1, K22F20.20, K22F20_20, TCH1, TOUCH 1, calmodulin 1, AT5G37780
calmodulin 1
GO Process (2)
GO Function (1)
GO Component (2)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Identification of non-specific lipid transfer protein-1 as a calmodulin-binding protein in Arabidopsis.

Wang Z, Xie W, Chi F, Li C

Although non-specific lipid transfer proteins (nsLTPs) are widely present in plants, their functions and regulations have not been fully understood. In this report, Arabidopsis nsLTP1 was cloned and expressed to investigate its binding to calmodulin (CaM). Gel overlay assays revealed that recombinant nsLTP1 bound to CaM in a calcium-independent manner. The association of nsLTP1 and CaM was corroborated using CaM-Sepharose ... [more]

FEBS Lett. Mar. 14, 2005; 579(7);1683-7 [Pubmed: 15757661]

Throughput

  • Low Throughput

Additional Notes

  • hit species/izozyme is unspecified

Curated By

  • BioGRID