Activation of ADP-ribosylation factors (ARFs) is mediated by guanine nucleotide-exchange proteins, which accelerate conversion of inactive ARF-GDP to active ARF-GTP. ARF domain protein (ARD1), a 64-kDa GTPase with a C-terminal ADP-ribosylation factor domain, is localized to lysosomes and the Golgi apparatus. When ARD1 was used as bait to screen a human liver cDNA library using the yeast two-hybrid system, a ... [more]

J. Biol. Chem. Jul. 14, 2000; 275(28);21331-9 [Pubmed: 10748148]

Throughput

Low Throughput

Curated By

BioGRID

Interaction Summary

TRIM23

Gene Ontology Biological Process

Gene Ontology Molecular Function

GDP binding [IDA]GTP binding [IDA]GTPase activity [IDA]enzyme activator activity [TAS]identical protein binding [IPI]protein binding [IPI]ubiquitin-protein transferase activity [IDA]

Gene Ontology Cellular Component

CYTH2

Gene Ontology Biological Process

Gene Ontology Molecular Function

ARF guanyl-nucleotide exchange factor activity [IBA, ISS]inositol 1,4,5 trisphosphate binding [ISS]protein binding [IPI]

Gene Ontology Cellular Component

Reconstituted Complex

Publication

Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1).

Throughput

Curated By

GDP binding [IDA]
GTP binding [IDA]
GTPase activity [IDA]
enzyme activator activity [TAS]
identical protein binding [IPI]
protein binding [IPI]
ubiquitin-protein transferase activity [IDA]

ARF guanyl-nucleotide exchange factor activity [IBA, ISS]
inositol 1,4,5 trisphosphate binding [ISS]
protein binding [IPI]