NUDT12
entrez
83594
canonical
uniprot
Q9BQG2
canonical
ensembl
ENSG00000112874
resolver
ensp
ENSP00000230792
resolver
ensp
ENSP00000424521
resolver
ensp
ENSP00000550057
resolver
ensp
ENSP00000550058
resolver
genesymbol
NUDT12
resolver
hgnc
HGNC:18826
resolver
uniprot
B3KUW2
resolver
uniprot
B4E1W3
resolver
uniprot
Q8TAL7
resolver
uniprot_entry
NUD12_HUMAN
resolver
uniprot_sec
B3KUW2
resolver
uniprot_sec
B4E1W3
resolver
uniprot_sec
Q8TAL7
resolver
amino_acid_sequence
MSSVKRSLKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSDLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLLNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWHSRYKFCPTCGNATKIEEGGYKRLCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDARWFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
ec_number
3.6.1.22
uniprot
proteins
function
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:31875550). 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 (PubMed:12790796). May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (PubMed:12790796). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity). {ECO:0000250|UniProtKB:Q9DCN1, ECO:0000269|PubMed:12790796, ECO:0000269|PubMed:31101919, ECO:0000269|PubMed:31875550}.
uniprot
proteins
mass_dalton
52076
uniprot
proteins
mutagenesis
MUTAGEN 281; /note="Y->A: Loss of homodimerization; when associated with A-283; A-284; A-287 and A-384."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 283; /note="F->A: Loss of homodimerization; when associated with A-281; A-284; A-287 and A-384."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 284; /note="C->A: Loss of homodimerization; when associated with A-281; A-283; A-287 and A-384."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 287; /note="C->A: Loss of homodimerization; when associated with A-281; A-283; A-284 and A-384."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 318; /note="Y->A: Partial loss of decapping activity towards NAD-capped RNAs."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 356; /note="F->A: Loss of decapping activity towards NAD-capped RNAs."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 370; /note="E->Q: Loss of decapping activity towards NAD-capped RNAs."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 374; /note="E->Q: Loss of decapping activity towards NAD-capped RNAs."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 384; /note="Y->A: No effect on decapping activity towards NAD-capped RNAs. Loss of homodimerization; when associated with A-281; A-283; A-284 and A-287."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 390; /note="W->A: Partial loss of decapping activity towards NAD-capped RNAs."; /evidence="ECO:0000269|PubMed:31875550"; MUTAGEN 460..462; /note="Missing: Abolishes localization to peroxisomes."; /evidence="ECO:0000269|PubMed:12790796
uniprot
proteins
protein_family
NudC subfamily
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
12790796
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
31101919
uniprot
proteins
pubmed
31875550
uniprot
proteins
sequence_length
462
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12790796}. Peroxisome {ECO:0000269|PubMed:12790796}. Cytoplasmic granule {ECO:0000269|PubMed:31875550}. Note=Localizes to cytoplasmic granules in the presence of BLMH. {ECO:0000269|PubMed:31875550}.
uniprot
proteins