Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC51269COMM domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC51269
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 β-sheet [1].
The profile we developed covers the entire COMM domain.
Last update:November 2006 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | 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. |
| Title | COMMD proteins, a novel family of structural and functional homologs of MURR1. | |
| Source | J. Biol. Chem. 280:22222-22232(2005). | |
| PubMed ID | 15799966 | |
| DOI | 10.1074/jbc.M501928200 |
| 2 | Authors | de Bie P. van de Sluis B. Burstein E. Duran K.J. Berger R. Duckett C.S. Wijmenga C. Klomp L.W.J. |
| Title | Characterization of COMMD protein-protein interactions in NF-kappaB signalling. | |
| Source | Biochem. J. 398:63-71(2006). | |
| PubMed ID | 16573520 | |
| DOI | 10.1042/BJ20051664 |
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