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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: NAD-capped RNA hydrolase NUDT12

UniprotKB/SwissProt ID: Q9DCN1 (Q9DCN1)

Gene Name: Nudt12

Organism: Mus musculus (Mouse)

Function: mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:31101919, PubMed:32432673). The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:31101919). Preferentially acts on NAD-capped transcripts in response to nutrient stress (PubMed:31101919). Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP (By similarity). May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (PubMed:31875550)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Peroxisome. Cytoplasmic granule

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002110 Ankyrin_rpt
IPR036770 Ankyrin_rpt-contain_sf
IPR050241 NAD-cap_RNA_hydrolase_NudC
IPR015375 NADH_PPase-like_N
IPR049734 NudC-like_C
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom
IPR015376 Znr_NADH_PPase

The S-nitrosylation sites of Q9DCN1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 177 ESSQQPEVRL C QLNYPDVKGY  CCCCCCCHHH H HHHHHHHHHH  2.79% 21278135