Primary Information |
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| BoMiProt ID | Bomi7359 |
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| Protein Name | NAD-capped RNA hydrolase NUDT12 |
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| Organism | Bos taurus |
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| Uniprot ID | Q29RH3 |
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| Milk Fraction | Whey |
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| Ref Sequence ID | NP_001040073.1 |
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| Aminoacid Length | 444 |
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| Molecular Weight | 50119 |
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| FASTA Sequence |
Download |
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| Gene Name | NUDT12 |
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| Gene ID | 617720 |
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| Protein Existence Status | reviewed |
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Secondary Information |
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| Protein Function | Nudt12 in complex with the deNADding product AMP and three Mg2+ ions at 1.6 Å resolution provides insights into the molecular basis of the deNADding activity in the NAD pyrophosphate. |
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| Biochemical Properties | NUDT12 is active only as homodimers, with each monomer contributing to creation of the two functional catalytic pockets. We identify an ∼600-kDa dodecamer complex between bleomycin hydrolase (BLMH) and NUDT12, with BLMH being required for localization of NUDT12 to a few discrete cytoplasmic granules that are distinct from P-bodies. |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| NA |
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Additional Comments | , loss of Nudt12 results in a significant upregulation of circadian clock transcripts in mouse liver. |
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| Bibliography | 1.Grudzien-Nogalska E, Wu Y, Jiao X, Cui H, Mateyak MK, Hart RP, Tong L, Kiledjian M. Structural and mechanistic basis of mammalian Nudt12 RNA deNADding. Nat Chem Biol. 2019 Jun;15(6):575-582. doi: 10.1038/s41589-019-0293-7. Epub 2019 May 17. PMID: 31101919; PMCID: PMC6527130. |
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