{PDOC51269} {PS51269; COMM} {BEGIN} *********************** * COMM domain profile * *********************** COMM (copper metabolism gene MURR1) domain proteins constitute a family initially identified as interacting partners of COMMD1 (previously known as MURR1), the prototype member of this protein family. COMMD1 is a multifunctional protein that has been shown to participate in two apparently distinct activities, regulation of the transcription factor NF-kappa-B and control of copper metabolism. The family is defined by the presence of a C- terminal motif termed COMM domain, which functions as an interface for protein-protein interactions. The proteins designated as COMMD or COMM domain containing 1-10 are extensively conserved in multicellular eukaryotic organisms [1,2]. The leucine-rich, 70-85 amino acid long COMM domain is predicted to form a beta-sheet [1]. The profile we developed covers the entire COMM domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: November 2006 / First entry. [ 1] Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A., Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S. "COMMD proteins, a novel family of structural and functional homologs of MURR1." J. Biol. Chem. 280:22222-22232(2005). PubMed=15799966; DOI=10.1074/jbc.M501928200 [ 2] de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., Duckett C.S., Wijmenga C., Klomp L.W.J. "Characterization of COMMD protein-protein interactions in NF-kappaB signalling." Biochem. J. 398:63-71(2006). PubMed=16573520; DOI=10.1042/BJ20051664 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}