DXO
entrez
1797
canonical
uniprot
O77932
canonical
ensembl
ENSG00000204348
resolver
ensembl
ENSG00000206346
resolver
ensembl
ENSG00000224313
resolver
ensembl
ENSG00000225682
resolver
ensembl
ENSG00000234798
resolver
ensembl
ENSG00000236765
resolver
ensp
ENSP00000337759
resolver
ensp
ENSP00000364498
resolver
ensp
ENSP00000364505
resolver
ensp
ENSP00000372820
resolver
ensp
ENSP00000382818
resolver
ensp
ENSP00000382819
resolver
ensp
ENSP00000391123
resolver
ensp
ENSP00000391349
resolver
ensp
ENSP00000391532
resolver
ensp
ENSP00000394167
resolver
ensp
ENSP00000395262
resolver
ensp
ENSP00000400173
resolver
ensp
ENSP00000401315
resolver
ensp
ENSP00000406143
resolver
ensp
ENSP00000410404
resolver
ensp
ENSP00000411380
resolver
ensp
ENSP00000413860
resolver
ensp
ENSP00000415675
resolver
ensp
ENSP00000638351
resolver
ensp
ENSP00000721734
resolver
enst
ENST00000337523
resolver
enst
ENST00000375349
resolver
enst
ENST00000375356
resolver
enst
ENST00000383330
resolver
enst
ENST00000399936
resolver
enst
ENST00000399937
resolver
enst
ENST00000414092
resolver
enst
ENST00000419797
resolver
enst
ENST00000426498
resolver
enst
ENST00000427627
resolver
enst
ENST00000427690
resolver
enst
ENST00000432110
resolver
enst
ENST00000439989
resolver
enst
ENST00000443250
resolver
enst
ENST00000446967
resolver
enst
ENST00000453742
resolver
enst
ENST00000454430
resolver
enst
ENST00000458308
resolver
enst
ENST00000968292
resolver
genesymbol
DXO
resolver
genesymbol_syn
DOM3L
resolver
genesymbol_syn
DOM3Z
resolver
genesymbol_syn
NG6
resolver
hgnc
HGNC:2992
resolver
uniprot
A2CER3
resolver
uniprot
B0UZ80
resolver
uniprot
O15004
resolver
uniprot
O78127
resolver
uniprot
O78128
resolver
uniprot
Q5ST60
resolver
uniprot
Q6IPZ2
resolver
uniprot
Q9NPK4
resolver
uniprot_entry
DXO_HUMAN
resolver
uniprot_sec
A2CER3
resolver
uniprot_sec
B0UZ80
resolver
uniprot_sec
O15004
resolver
uniprot_sec
O78127
resolver
uniprot_sec
O78128
resolver
uniprot_sec
Q5ST60
resolver
uniprot_sec
Q6IPZ2
resolver
uniprot_sec
Q9NPK4
resolver
amino_acid_sequence
MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK
uniprot
proteins
ec_number
3.1.13.-
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
function
FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed:28283058). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:28283058). Preferentially acts on NAD-capped transcripts in response to environmental stress (PubMed:31101919). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (By similarity). Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control (By similarity). Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:29601584). In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA (By similarity). Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:29601584). Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity). Exhibits decapping activity towards FAD-capped RNAs (PubMed:32374864). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:O70348, ECO:0000269|PubMed:28283058, ECO:0000269|PubMed:29601584, ECO:0000269|PubMed:31101919, ECO:0000269|PubMed:32374864}.
uniprot
proteins
mass_dalton
44929
uniprot
proteins
mutagenesis
MUTAGEN 7..8; /note="KR->AA: Impaired subcellular location, leading to localization both in cytoplasm and nucleus."; /evidence="ECO:0000269|PubMed:29601584"; MUTAGEN 236; /note="D->A: Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-253."; /evidence="ECO:0000269|PubMed:29601584"; MUTAGEN 253; /note="E->A: Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-236."; /evidence="ECO:0000269|PubMed:29601584
uniprot
proteins
protein_family
DXO/Dom3Z family
uniprot
proteins
pubmed
10686478
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21750099
uniprot
proteins
pubmed
28283058
uniprot
proteins
pubmed
29601584
uniprot
proteins
pubmed
31101919
uniprot
proteins
pubmed
32374864
uniprot
proteins
pubmed
9799600
uniprot
proteins
sequence_length
396
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21750099, ECO:0000269|PubMed:29601584}.
uniprot
proteins