FEATURES

FAMILY

DESCRIPTION

Also known as GID4_HUMAN, GID4, C17orf39, VID24. Substrate-recognition subunit of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1 (Probable) (PubMed:29911972). Binds proteins and peptides with a Pro/N-degron consisting of an unmodified N-terminal Pro followed by a small residue, and has the highest affinity for the peptide Pro-Gly-Leu-Trp (PubMed:29632410). Binds peptides with an N-terminal sequence of the type Pro-[Ala, Gly]-[Leu, Met, Gln, Ser, Tyr]-[Glu, Gly, His, Ser, Val, Trp, Tyr]. Does not bind peptides with an acetylated N-terminal Pro residue (PubMed:29632410). Identified in the CTLH complex that contains GID4, RANBP9 and/or RANBP10, MKLN1, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, ARMC8, WDR26 and YPEL5 (PubMed:29911972). Within this complex, MAEA, RMND5A (or alternatively its paralog RMND5B), GID8, WDR26, and RANBP9 and/or RANBP10 form the catalytic core, while GID4, MKLN1, ARMC8 and YPEL5 have ancillary roles (PubMed:29911972).

EXTERNAL LINKS

GID4

Glucose-induced degradation protein 4 homolog

GID4

Molecular Synopsis