CBS domain superfamily
IPR046342
Definition
CBS domains are evolutionarily conserved structural domains found in a variety of non functionally-related proteins from all kingdoms of life. These domains pair together to form a intramolecular dimeric structure (CBS pair), termed Bateman domain [[cite:PMID:10200156], [cite:PMID:16275737], [cite:PMID:24161944], [cite:PMID:14722609]]. CBS domains have been shown to bind mainly ligands with an adenosyl group such as AMP, ATP and S-AdoMet, but may also bind metal ions, or nucleic acids [[cite:PMID:24161944], [cite:PMID:14722619]]. Hence, they play an essential role in the regulation of the activities of numerous proteins, and mutations in them are associated with several hereditary diseases [[cite:PMID:29037129], [cite:PMID:16275737], [cite:PMID:14722619]]. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl-carrying ligands. The region containing the CBS domains in cystathionine-beta synthase is involved in regulation by S-AdoMet PMID:11524006. CBS domain pairs from AMPK bind AMP or ATP PMID:14722619. The CBS domains from IMPDH, which bind ATP, have shown to have a role in the regulation of adenylate nucleotide synthesis [[cite:PMID:14722619], [cite:PMID:19153081]].
17 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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