DBC1 |
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| SMART accession number: | SM01122
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| Description: |
DBC1 and it homologs from diverse eukaryotes are a catalytically inactive version of the Nudix hydrolase (MutT) domain ((PUBMED:18418069)). DBC1 is predicted to bind NAD metabolites and regulate the activity of SIRT1 or related deacetylases by sensing the soluble products or substrates of the NAD-dependent deacetylation reaction ((PUBMED:18418069)). |
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| Family alignment: |
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There are 79
DBC1 domains in 79 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Cellular role (predicted cellular role)
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Cellular role: metabolism
- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Anantharaman V, Aravind L
- Analysis of DBC1 and its homologs suggests a potential mechanism for regulationof sirtuin domain deacetylases by NAD metabolites.
- Cell Cycle. 2008; 7: 1467-72
- Display abstract
Deleted in Breast Cancer-1 (DBC1) and its paralog CARP-1 are large multi-domainproteins, with a nuclear or perinuclear localization, and a role in promotingapoptosis upon processing by caspases. Recent studies on human DBC1 show that it is a specific inhibitor of the sirtuin-type deacetylase, Sirt1, whichdeacetylates histones and p53. Using sensitive sequence profile searches andHMM-HMM comparisons we show that the central conserved globular domain present inthe DBC1 and it homologs from diverse eukaryotes is a catalytically inactiveversion of the Nudix hydrolase (MutT) domain. Given that Nudix domains are known to bind nucleoside diphosphate sugars and NAD, we predict that this domain inDBC1 and its homologs binds NAD metabolites such as ADP-ribose. Hence, we proposethat DBC1 and its homologs are likely to regulate the activity of SIRT1 orrelated deacetylases by sensing the soluble products or substrates of theNAD-dependent deacetylation reaction. The complex domain architectures of themembers of the DBC1 family, which include fusions to the RNA-binding S1-likedomain, the DNA-binding SAP domain and EF-hand domains, suggest that they arelikely to function as integrators of distinct regulatory signals includingchromatin protein modification, soluble compounds in NAD metabolism, apoptoticstimuli and RNA recognition.
- Links (links to other resources describing this domain)
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