The BACK domain in BTB-kelch proteins.
A novel conserved motif--the BACK (for BTB and C-terminal Kelch) domain--is found in the majority of proteins that contain both the BTB domain and kelch repeats. Many kelch-repeat proteins are involved in organization of the cytoskeleton via interaction with actin and intermediate filaments, whereas BTB domains have multiple cellular roles, including recruitment to E3 ubiquitin ligase complexes. The identification of the BACK domain in BTB and kelch proteins, and its high conservation across metazoan genomes, suggest an important function for this domain with a possible role in substrate orientation in Cullin3-based E3 ligase complexes.
Stogios
Peter J
PJ
Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, Canada M5G 2M9.
Privé
Gilbert G
GG
D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism; D016678:Genome; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry / Q000378:metabolism
D000199:Actins; D029721:Drosophila Proteins; D008840:Microfilament Proteins; C080353:kel protein, Drosophila; D044767:Ubiquitin-Protein Ligases