DCP2
entrez
167227
canonical
uniprot
Q8IU60
canonical
ensembl
ENSG00000172795
resolver
ensp
ENSP00000373715
resolver
ensp
ENSP00000425770
resolver
ensp
ENSP00000715027
resolver
ensp
ENSP00000744713
resolver
genesymbol
DCP2
resolver
genesymbol_syn
NUDT20
resolver
hgnc
HGNC:24452
resolver
uniprot
C9J778
resolver
uniprot
Q6P2D4
resolver
uniprot
Q7Z5W5
resolver
uniprot
Q8NBG5
resolver
uniprot_entry
DCP2_HUMAN
resolver
uniprot_sec
C9J778
resolver
uniprot_sec
Q6P2D4
resolver
uniprot_sec
Q7Z5W5
resolver
uniprot_sec
Q8NBG5
resolver
amino_acid_sequence
METKRVEIPGSVLDDLCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL
uniprot
proteins
ec_number
3.6.1.62
uniprot
proteins
function
FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:12218187, PubMed:12417715, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12486012, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:14527413). Plays a role in replication-dependent histone mRNA degradation (PubMed:18172165). Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping (PubMed:28002401). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:26098573). {ECO:0000269|PubMed:12218187, ECO:0000269|PubMed:12417715, ECO:0000269|PubMed:12486012, ECO:0000269|PubMed:12923261, ECO:0000269|PubMed:14527413, ECO:0000269|PubMed:18172165, ECO:0000269|PubMed:21070968, ECO:0000269|PubMed:26098573, ECO:0000269|PubMed:28002401}.
uniprot
proteins
mass_dalton
48423
uniprot
proteins
mutagenesis
MUTAGEN 147; /note="E->Q: Loss of decapping activity; when associated with Q-148."; MUTAGEN 148; /note="E->Q: Strongly reduced decapping activity."; /evidence="ECO:0000269|PubMed:12417715"; MUTAGEN 249; /note="S->A: Leads to the accumulation of autophagosomes under normal growth conditions."; /evidence="ECO:0000269|PubMed:26098573"; MUTAGEN 249; /note="S->D: Leads to reduced autophagosome formation under autophagy-inducing conditions."; /evidence="ECO:0000269|PubMed:26098573
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at ser-249 in a MTOR-dependent manner (PubMed:26098573).
uniprot
proteins
protein_family
DCP2 subfamily
uniprot
proteins
protein_family
Nudix hydrolase family
uniprot
proteins
pubmed
12218187
uniprot
proteins
pubmed
12417715
uniprot
proteins
pubmed
12486012
uniprot
proteins
pubmed
12515382
uniprot
proteins
pubmed
12923261
uniprot
proteins
pubmed
14527413
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15067023
uniprot
proteins
pubmed
15231747
uniprot
proteins
pubmed
15273322
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15687258
uniprot
proteins
pubmed
16364915
uniprot
proteins
pubmed
16699599
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18172165
uniprot
proteins
pubmed
18361920
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20616046
uniprot
proteins
pubmed
21070968
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21876179
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26098573
uniprot
proteins
pubmed
27918561
uniprot
proteins
pubmed
28002401
uniprot
proteins
pubmed
31875550
uniprot
proteins
sequence_length
420
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:15067023, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:20616046}. Nucleus {ECO:0000269|PubMed:15273322}. Note=Predominantly cytoplasmic, in processing bodies (PB) (PubMed:15273322). A minor amount is nuclear (PubMed:15273322). {ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:20616046}.
uniprot
proteins