BAIT

RHAG

CD241, RH2, RH50A, Rh50, Rh50GP, SLC42A1
Rh-associated glycoprotein
Homo sapiens
PREY

ANK1

ANK, SPH1, SPH2
ankyrin 1, erythrocytic
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Rh-RhAG/ankyrin-R, a new interaction site between the membrane bilayer and the red cell skeleton, is impaired by Rh(null)-associated mutation.

Nicolas V, Le Van Kim C, Gane P, Birkenmeier C, Cartron JP, Colin Y, Mouro-Chanteloup I

Several studies suggest that the Rh complex represents a major interaction site between the membrane lipid bilayer and the red cell skeleton, but little is known about the molecular basis of this interaction. We report here that ankyrin-R is capable of interacting directly with the C-terminal cytoplasmic domain of Rh and RhAG polypeptides. We first show that the primary defect ... [more]

J. Biol. Chem. Jul. 11, 2003; 278(28);25526-33 [Pubmed: 12719424]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
ANK1 RHAG
Two-hybrid
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.

Low-BioGRID
-

Curated By

  • BioGRID