DCPS
entrez
28960
canonical
uniprot
Q96C86
canonical
ensembl
ENSG00000110063
resolver
ensp
ENSP00000263579
resolver
ensp
ENSP00000531281
resolver
enst
ENST00000263579
resolver
genesymbol
DCPS
resolver
genesymbol_syn
DCS1
resolver
genesymbol_syn
HINT5
resolver
hgnc
HGNC:29812
resolver
uniprot
A0A384MTI8
resolver
uniprot
Q8NHL8
resolver
uniprot
Q9Y2S5
resolver
uniprot_entry
A0A384MTI8_HUMAN
resolver
uniprot_entry
DCPS_HUMAN
resolver
uniprot_sec
Q8NHL8
resolver
uniprot_sec
Q9Y2S5
resolver
activity_regulation
ACTIVITY REGULATION: The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro. Inhibited by 2,4-diaminoquinazoline. {ECO:0000269|PubMed:18839960, ECO:0000269|PubMed:22985415}.
uniprot
proteins
amino_acid_sequence
MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNEASGDGDGEDAVVILEKTPFQVEQVAQLLTGSPELQLQFSNDIYSTYHLFPPRQLNDVKTTVVYPATEKHLQKYLRQDLRLIRETGDDYRNITLPHLESQSLSIQWVYNILDKKAEADRIVFENPDPSDGFVLIPDLKWNQQQLDDLYLIAICHRRGIRSLRDLTPEHLPLLRNILHQGQEAILQRYRMKGDHLRVYLHYLPSYYHLHVHFTALGFEAPGSGVERAHLLAEVIENLECDPRHYQQRTLTFALRADDPLLKLLQEAQQS
uniprot
proteins
disease_involvement
DISEASE: Al-Raqad syndrome (ARS) [MIM:616459]: A syndrome characterized by delayed psychomotor development, moderate to severe intellectual disability, poor or absent speech, microcephaly, congenital hypotonia, and severe growth delay. {ECO:0000269|PubMed:25701870, ECO:0000269|PubMed:25712129}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.1.59
uniprot
proteins
function
FUNCTION: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415). May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240). Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death. {ECO:0000269|PubMed:11747811, ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:12871939, ECO:0000269|PubMed:14523240, ECO:0000269|PubMed:15273322, ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:15769464, ECO:0000269|PubMed:16140270, ECO:0000269|PubMed:18426921, ECO:0000269|PubMed:22985415}.
uniprot
proteins
mass_dalton
38609
uniprot
proteins
mutagenesis
MUTAGEN 10..13; /note="Missing: Increases cytoplasmic localization."; /evidence="ECO:0000269|PubMed:18426921"; MUTAGEN 58; /note="R->A: Increases decapping activity to 125% of wild-type."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 61; /note="I->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 63; /note="F->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 83; /note="I->A: Strongly reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 85; /note="E->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 108; /note="F->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 110; /note="N->A: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 113; /note="Y->A: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 128; /note="K->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 138; /note="K->D: Increases decapping activity to 250% of wild-type."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 145; /note="R->A: Increases decapping activity to 180% of wild-type."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 146; /note="Q->P: Increases decapping activity to 140% of wild-type."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 148; /note="L->A: Inhibits nuclear export to the cytoplasm."; /evidence="ECO:0000269|PubMed:18426921"; MUTAGEN 150; /note="L->A: Inhibits nuclear export to the cytoplasm."; /evidence="ECO:0000269|PubMed:18426921"; MUTAGEN 175; /note="W->A: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 185; /note="E->A: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 204; /note="P->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 205; /note="D->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 206; /note="L->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 207; /note="K->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 207; /note="K->R: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 217; /note="Y->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 217; /note="Y->F: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 268; /note="H->N: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 272; /note="S->A: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 273; /note="Y->A: Reduces decapping activity."; /evidence="ECO:0000269|PubMed:15769464"; MUTAGEN 273; /note="Y->F: Activates decapping activity to 120% of wild-type."; /evidence="ECO:0000269|PubMed:15769464"; MUTAGEN 277; /note="H->N: Loss of decapping activity. Does not inhibit cap structure and capped RNA binding. Preferentially hydrolyzes cap structure (m7GpppG) at least 2500-fold more efficiently than capped RNA (m7Gppp-RNA)."; /evidence="ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:15068804, ECO:0000269|PubMed:15273322"; MUTAGEN 279; /note="H->N: Loss of decapping activity."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 294; /note="R->A,K: No effect."; /evidence="ECO:0000269|PubMed:15068804"; MUTAGEN 322; /note="R->A: No effect."; /evidence="ECO:0000269|PubMed:15068804
uniprot
proteins
protein_family
HIT family
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
11747811
uniprot
proteins
pubmed
12198172
uniprot
proteins
pubmed
12871939
uniprot
proteins
pubmed
14523240
uniprot
proteins
pubmed
15068804
uniprot
proteins
pubmed
15273322
uniprot
proteins
pubmed
15383679
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15769464
uniprot
proteins
pubmed
16140270
uniprot
proteins
pubmed
18426921
uniprot
proteins
pubmed
18725266
uniprot
proteins
pubmed
18839960
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22985415
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25701870
uniprot
proteins
pubmed
25712129
uniprot
proteins
sequence_length
337
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.
uniprot
proteins