BAIT

RHBDL2

RRP2
rhomboid, veinlet-like 2 (Drosophila)
GO Process (0)
GO Function (1)
GO Component (1)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens

Biochemical Activity (Proteolytic Processing)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2.

Pascall JC, Brown KD

Rhomboid-1 is a serine protease that cleaves the membrane domain of the Drosophila EGF-family protein, Spitz, to release a soluble growth factor. Several vertebrate rhomboid-like proteins have been identified, although their substrates and functions remain unknown. The human rhomboid, RHBDL2, cleaves the membrane domain of Drosophila Spitz when the proteins are co-expressed in mammalian cells. However, the membrane domains of ... [more]

Biochem. Biophys. Res. Commun. Apr. 23, 2004; 317(1);244-52 [Pubmed: 15047175]

Throughput

  • Low Throughput

Curated By

  • BioGRID