Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

m7GpppX diphosphatase (EC 3.6.1.59) (DCS-1) (Decapping scavenger enzyme) (Hint-related 7meGMP-directed hydrolase) (Histidine triad nucleotide-binding protein 5) (Histidine triad protein member 5) (HINT-5) (Scavenger mRNA-decapping enzyme DcpS)

 DCPS_HUMAN              Reviewed;         337 AA.
Q96C86; Q8NHL8; Q9Y2S5;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=m7GpppX diphosphatase;
EC=3.6.1.59;
AltName: Full=DCS-1;
AltName: Full=Decapping scavenger enzyme;
AltName: Full=Hint-related 7meGMP-directed hydrolase;
AltName: Full=Histidine triad nucleotide-binding protein 5;
AltName: Full=Histidine triad protein member 5;
Short=HINT-5;
AltName: Full=Scavenger mRNA-decapping enzyme DcpS;
Name=DCPS; Synonyms=DCS1, HINT5; ORFNames=HSPC015;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Huang C.-H., Peng J., Chen H., Chen Y.;
"Cloning and characterization of a novel member of the histidine triad
protein family (HINT-5) in different vertebrate species.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS
SPECTROMETRY, MUTAGENESIS OF HIS-277, AND SUBUNIT.
PubMed=12198172; DOI=10.1093/emboj/cdf448;
Liu H., Rodgers N.D., Jiao X., Kiledjian M.;
"The scavenger mRNA decapping enzyme DcpS is a member of the HIT
family of pyrophosphatases.";
EMBO J. 21:4699-4708(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=12871939; DOI=10.1074/jbc.M306355200;
Kwasnicka D.A., Krakowiak A., Thacker C., Brenner C., Vincent S.R.;
"Coordinate expression of NADPH-dependent flavin reductase, Fre-1, and
Hint-related 7meGMP-directed hydrolase, DCS-1.";
J. Biol. Chem. 278:39051-39058(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-73.
TISSUE=Bone marrow;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-11; 129-138 AND 243-255, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V.;
Submitted (JAN-2010) to UniProtKB.
[7]
FUNCTION, AND INTERACTION WITH EXOSOME PROTEINS.
PubMed=11747811; DOI=10.1016/S0092-8674(01)00592-X;
Wang Z., Kiledjian M.;
"Functional link between the mammalian exosome and mRNA decapping.";
Cell 107:751-762(2001).
[8]
FUNCTION.
PubMed=14523240; DOI=10.1073/pnas.1635192100;
van Dijk E., Le Hir H., Seraphin B.;
"DcpS can act in the 5'-3' mRNA decay pathway in addition to the 3'-5'
pathway.";
Proc. Natl. Acad. Sci. U.S.A. 100:12081-12086(2003).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-277.
PubMed=15273322; DOI=10.1261/rna.7660804;
Liu S.-W., Jiao X., Liu H., Gu M., Lima C.D., Kiledjian M.;
"Functional analysis of mRNA scavenger decapping enzymes.";
RNA 10:1412-1422(2004).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
PubMed=15383679; DOI=10.1261/rna.7690504;
Cohen L.S., Mikhli C., Friedman C., Jankowska-Anyszka M.,
Stepinski J., Darzynkiewicz E., Davis R.E.;
"Nematode m7GpppG and m3(2,2,7)GpppG decapping: activities in Ascaris
embryos and characterization of C. elegans scavenger DcpS.";
RNA 10:1609-1624(2004).
[11]
FUNCTION IN CYTOTOXICITY INHIBITION, INDUCTION, AND INTERACTION WITH
NDOR1.
PubMed=16140270; DOI=10.1016/j.bbrc.2005.08.129;
Kwasnicka-Crawford D.A., Vincent S.R.;
"Role of a novel dual flavin reductase (NR1) and an associated
histidine triad protein (DCS-1) in menadione-induced cytotoxicity.";
Biochem. Biophys. Res. Commun. 336:565-571(2005).
[12]
FUNCTION IN SPLICING, MUTAGENESIS OF 10-LYS--ARG-13; LEU-148 AND
LEU-150, AND SUBCELLULAR LOCATION.
PubMed=18426921; DOI=10.1261/rna.1008208;
Shen V., Liu H., Liu S.W., Jiao X., Kiledjian M.;
"DcpS scavenger decapping enzyme can modulate pre-mRNA splicing.";
RNA 14:1132-1142(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18725266; DOI=10.1016/j.biochi.2008.07.009;
Mariller C., Hardiville S., Hoedt E., Benaissa M., Mazurier J.,
Pierce A.;
"Proteomic approach to the identification of novel delta-lactoferrin
target genes: Characterization of DcpS, an mRNA scavenger decapping
enzyme.";
Biochimie 91:109-122(2009).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-142, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ENZYME
REGULATION.
PubMed=22985415; DOI=10.1021/bi300781g;
Wypijewska A., Bojarska E., Lukaszewicz M., Stepinski J.,
Jemielity J., Davis R.E., Darzynkiewicz E.;
"7-Methylguanosine diphosphate (m(7)GDP) is not hydrolyzed but
strongly bound by decapping scavenger (dcpS) enzymes and potently
inhibits their activity.";
Biochemistry 51:8003-8013(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
INVOLVEMENT IN ARS.
PubMed=25712129; DOI=10.1093/hmg/ddv067;
Ng C.K., Shboul M., Taverniti V., Bonnard C., Lee H., Eskin A.,
Nelson S.F., Al-Raqad M., Altawalbeh S., Seraphin B., Reversade B.;
"Loss of the scavenger mRNA decapping enzyme DCPS causes syndromic
intellectual disability with neuromuscular defects.";
Hum. Mol. Genet. 24:3163-3171(2015).
[23]
INVOLVEMENT IN ARS, VARIANT ARS MET-316, AND CHARACTERIZATION OF
VARIANT ARS MET-316.
PubMed=25701870; DOI=10.1093/hmg/ddv069;
Ahmed I., Buchert R., Zhou M., Jiao X., Mittal K., Sheikh T.I.,
Scheller U., Vasli N., Rafiq M.A., Brohi M.Q., Mikhailov A., Ayaz M.,
Bhatti A., Sticht H., Nasr T., Carter M.T., Uebe S., Reis A., Ayub M.,
John P., Kiledjian M., Vincent J.B., Jamra R.A.;
"Mutations in DCPS and EDC3 in autosomal recessive intellectual
disability indicate a crucial role for mRNA decapping in
neurodevelopment.";
Hum. Mol. Genet. 24:3172-3180(2015).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT ASN-277 IN COMPLEX
WITH SUBSTRATE, SUBUNIT, AND MUTAGENESIS OF ARG-58; ILE-61; PHE-63;
ILE-83; GLU-85; PHE-108; ASN-110; TYR-113; LYS-128; LYS-138; ARG-145;
GLN-146; TRP-175; GLU-185; PRO-204; ASP-205; LEU-206; LYS-207;
TYR-217; HIS-268; SER-272; HIS-277; HIS-279; ARG-294 AND ARG-322.
PubMed=15068804; DOI=10.1016/S1097-2765(04)00180-7;
Gu M., Fabrega C., Liu S.-W., Liu H., Kiledjian M., Lima C.D.;
"Insights into the structure, mechanism, and regulation of scavenger
mRNA decapping activity.";
Mol. Cell 14:67-80(2004).
[25]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
FUNCTION, SUBUNIT, AND MUTAGENESIS OF TYR-273.
PubMed=15769464; DOI=10.1016/j.jmb.2005.01.062;
Chen N., Walsh M.A., Liu Y., Parker R., Song H.;
"Crystal structures of human DcpS in ligand-free and m7GDP-bound forms
suggest a dynamic mechanism for scavenger mRNA decapping.";
J. Mol. Biol. 347:707-718(2005).
[26]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 38-337 IN COMPLEX WITH
SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
PubMed=18839960; DOI=10.1021/cb800120t;
Singh J., Salcius M., Liu S.W., Staker B.L., Mishra R., Thurmond J.,
Michaud G., Mattoon D.R., Printen J., Christensen J., Bjornsson J.M.,
Pollok B.A., Kiledjian M., Stewart L., Jarecki J., Gurney M.E.;
"DcpS as a therapeutic target for spinal muscular atrophy.";
ACS Chem. Biol. 3:711-722(2008).
-!- 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}.
-!- CATALYTIC ACTIVITY: A 5'-(N(7)-methyl 5'-triphosphoguanosine)-
[mRNA] + H(2)O = N(7)-methylguanosine 5'-phosphate + a 5'-
diphospho-[mRNA]. {ECO:0000269|PubMed:15273322,
ECO:0000269|PubMed:15383679, ECO:0000269|PubMed:18839960,
ECO:0000269|PubMed:22985415}.
-!- ENZYME 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}.
-!- SUBUNIT: Homodimer. Associates with components of the exosome
multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4.
Interacts with NDOR1. {ECO:0000269|PubMed:11747811,
ECO:0000269|PubMed:12198172, ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15769464, ECO:0000269|PubMed:16140270,
ECO:0000269|PubMed:18839960}.
-!- 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.
-!- TISSUE SPECIFICITY: Detected in liver, brain, kidney, testis and
prostate. {ECO:0000269|PubMed:12871939}.
-!- INDUCTION: Up-regulated by menadione. Up-regulated by the
transcription factor LTF isoform delta-lactoferrin (at protein
level). {ECO:0000269|PubMed:16140270,
ECO:0000269|PubMed:18725266}.
-!- DOMAIN: The C-terminal histidine triad (HIT) motif and the N-
terminal domain are required for the decapping activity. The N-
terminus is necessary but not sufficient for binding cap
structures. {ECO:0000269|PubMed:15273322}.
-!- 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 mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the HIT family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AH010984; AAK91763.1; -; Genomic_DNA.
EMBL; AY040771; AAK91765.1; -; mRNA.
EMBL; AF532613; AAM90310.1; -; mRNA.
EMBL; AY077684; AAL77216.1; -; mRNA.
EMBL; AF077201; AAD26996.1; -; mRNA.
EMBL; BC014532; AAH14532.1; -; mRNA.
CCDS; CCDS8473.1; -.
RefSeq; NP_054745.1; NM_014026.4.
UniGene; Hs.504249; -.
UniGene; Hs.651497; -.
PDB; 1ST0; X-ray; 1.90 A; A/B=1-337.
PDB; 1ST4; X-ray; 2.02 A; A/B=1-337.
PDB; 1XML; X-ray; 2.00 A; A/B=1-337.
PDB; 1XMM; X-ray; 2.50 A; A/B/C/D=1-337.
PDB; 3BL7; X-ray; 2.31 A; A/B=38-337.
PDB; 3BL9; X-ray; 1.80 A; A/B=38-337.
PDB; 3BLA; X-ray; 2.60 A; A/B=38-337.
PDB; 4QDE; X-ray; 2.90 A; A/B/C/D=2-337.
PDB; 4QDV; X-ray; 2.80 A; A/B/C/D=2-337.
PDB; 4QEB; X-ray; 3.21 A; A/B/C/D=2-337.
PDBsum; 1ST0; -.
PDBsum; 1ST4; -.
PDBsum; 1XML; -.
PDBsum; 1XMM; -.
PDBsum; 3BL7; -.
PDBsum; 3BL9; -.
PDBsum; 3BLA; -.
PDBsum; 4QDE; -.
PDBsum; 4QDV; -.
PDBsum; 4QEB; -.
ProteinModelPortal; Q96C86; -.
SMR; Q96C86; -.
BioGrid; 118787; 38.
IntAct; Q96C86; 6.
STRING; 9606.ENSP00000263579; -.
BindingDB; Q96C86; -.
ChEMBL; CHEMBL1949488; -.
DrugBank; DB01649; 7-Methyl-Gpppa.
DrugBank; DB03958; 7-methyl-guanosine-5'-triphosphate-5'-guanosine.
DrugBank; DB01960; 7n-Methyl-8-Hydroguanosine-5'-Diphosphate.
DrugBank; DB03593; N7-Methyl-Guanosine-5'-Monophosphate.
iPTMnet; Q96C86; -.
PhosphoSitePlus; Q96C86; -.
BioMuta; DCPS; -.
DMDM; 116241325; -.
REPRODUCTION-2DPAGE; IPI00335385; -.
EPD; Q96C86; -.
MaxQB; Q96C86; -.
PaxDb; Q96C86; -.
PeptideAtlas; Q96C86; -.
PRIDE; Q96C86; -.
DNASU; 28960; -.
Ensembl; ENST00000263579; ENSP00000263579; ENSG00000110063.
GeneID; 28960; -.
KEGG; hsa:28960; -.
UCSC; uc001qdp.3; human.
CTD; 28960; -.
DisGeNET; 28960; -.
EuPathDB; HostDB:ENSG00000110063.8; -.
GeneCards; DCPS; -.
HGNC; HGNC:29812; DCPS.
HPA; HPA039632; -.
HPA; HPA058597; -.
MalaCards; DCPS; -.
MIM; 610534; gene.
MIM; 616459; phenotype.
neXtProt; NX_Q96C86; -.
OpenTargets; ENSG00000110063; -.
PharmGKB; PA134863866; -.
eggNOG; KOG3969; Eukaryota.
eggNOG; COG5075; LUCA.
GeneTree; ENSGT00390000003924; -.
HOGENOM; HOG000182411; -.
HOVERGEN; HBG051322; -.
InParanoid; Q96C86; -.
KO; K12584; -.
OMA; IWCEKSH; -.
OrthoDB; EOG091G0DTP; -.
PhylomeDB; Q96C86; -.
TreeFam; TF105622; -.
BRENDA; 3.6.1.59; 2681.
Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
ChiTaRS; DCPS; human.
EvolutionaryTrace; Q96C86; -.
GeneWiki; DCPS_(gene); -.
GenomeRNAi; 28960; -.
PRO; PR:Q96C86; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110063; -.
CleanEx; HS_DCPS; -.
Genevisible; Q96C86; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IBA:GO_Central.
GO; GO:0004532; F:exoribonuclease activity; TAS:Reactome.
GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
GO; GO:0000340; F:RNA 7-methylguanosine cap binding; IDA:UniProtKB.
GO; GO:0036245; P:cellular response to menadione; IDA:UniProtKB.
GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
GO; GO:0043928; P:exonucleolytic nuclear-transcribed mRNA catabolic process involved in deadenylation-dependent decay; TAS:Reactome.
GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0043069; P:negative regulation of programmed cell death; IDA:UniProtKB.
GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; TAS:UniProtKB.
InterPro; IPR008594; DcpS/DCS2.
InterPro; IPR019808; Histidine_triad_CS.
InterPro; IPR036265; HIT-like_sf.
InterPro; IPR011145; Scavenger_mRNA_decap_enz_N.
PANTHER; PTHR12978; PTHR12978; 1.
Pfam; PF05652; DcpS; 1.
PIRSF; PIRSF028973; Scavenger_mRNA_decap_enz; 1.
SUPFAM; SSF102860; SSF102860; 1.
SUPFAM; SSF54197; SSF54197; 1.
PROSITE; PS00892; HIT_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Hydrolase;
Mental retardation; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 337 m7GpppX diphosphatase.
/FTId=PRO_0000109794.
REGION 268 279 Substrate binding.
MOTIF 10 13 nuclear localization signal (NLS).
MOTIF 142 154 nuclear export sequence (NES).
MOTIF 275 279 Histidine triad motif.
ACT_SITE 277 277 Nucleophile.
BINDING 175 175 Substrate. {ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15769464}.
BINDING 185 185 Substrate. {ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15769464}.
BINDING 205 205 Substrate. {ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15769464}.
BINDING 207 207 Substrate. {ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15769464}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DAR7}.
MOD_RES 138 138 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 142 142 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 73 73 G -> E (in dbSNP:rs11557735).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027958.
VARIANT 316 316 T -> M (in ARS; results in a severe
decrease of decapase activity;
dbSNP:rs137941190).
{ECO:0000269|PubMed:25701870}.
/FTId=VAR_073956.
MUTAGEN 10 13 Missing: Increases cytoplasmic
localization.
{ECO:0000269|PubMed:18426921}.
MUTAGEN 58 58 R->A: Increases decapping activity to
125% of wild-type.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 61 61 I->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 63 63 F->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 83 83 I->A: Strongly reduces decapping
activity. {ECO:0000269|PubMed:15068804}.
MUTAGEN 85 85 E->A: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 108 108 F->A: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 110 110 N->A: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 113 113 Y->A: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 128 128 K->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 138 138 K->D: Increases decapping activity to
250% of wild-type.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 145 145 R->A: Increases decapping activity to
180% of wild-type.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 146 146 Q->P: Increases decapping activity to
140% of wild-type.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 148 148 L->A: Inhibits nuclear export to the
cytoplasm. {ECO:0000269|PubMed:18426921}.
MUTAGEN 150 150 L->A: Inhibits nuclear export to the
cytoplasm. {ECO:0000269|PubMed:18426921}.
MUTAGEN 175 175 W->A: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 185 185 E->A: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 204 204 P->A: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 205 205 D->A: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 206 206 L->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 207 207 K->A: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 207 207 K->R: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 217 217 Y->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 217 217 Y->F: Reduces decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 268 268 H->N: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 272 272 S->A: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 273 273 Y->A: Reduces decapping activity.
{ECO:0000269|PubMed:15769464}.
MUTAGEN 273 273 Y->F: Activates decapping activity to
120% of wild-type.
{ECO:0000269|PubMed:15769464}.
MUTAGEN 277 277 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). {ECO:0000269|PubMed:12198172,
ECO:0000269|PubMed:15068804,
ECO:0000269|PubMed:15273322}.
MUTAGEN 279 279 H->N: Loss of decapping activity.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 294 294 R->A,K: No effect.
{ECO:0000269|PubMed:15068804}.
MUTAGEN 322 322 R->A: No effect.
{ECO:0000269|PubMed:15068804}.
CONFLICT 69 69 N -> K (in Ref. 1; AAK91763).
{ECO:0000305}.
STRAND 43 45 {ECO:0000244|PDB:1ST0}.
STRAND 48 56 {ECO:0000244|PDB:3BL9}.
TURN 57 60 {ECO:0000244|PDB:3BL9}.
STRAND 61 67 {ECO:0000244|PDB:3BL9}.
STRAND 79 86 {ECO:0000244|PDB:3BL9}.
HELIX 91 98 {ECO:0000244|PDB:3BL9}.
STRAND 103 110 {ECO:0000244|PDB:3BL9}.
STRAND 113 119 {ECO:0000244|PDB:3BL9}.
HELIX 122 124 {ECO:0000244|PDB:3BL9}.
STRAND 127 132 {ECO:0000244|PDB:3BL9}.
HELIX 137 143 {ECO:0000244|PDB:3BL9}.
STRAND 148 153 {ECO:0000244|PDB:3BL9}.
HELIX 155 160 {ECO:0000244|PDB:3BL9}.
HELIX 162 167 {ECO:0000244|PDB:3BL9}.
HELIX 174 180 {ECO:0000244|PDB:3BL9}.
STRAND 183 185 {ECO:0000244|PDB:3BL9}.
HELIX 186 188 {ECO:0000244|PDB:3BL9}.
STRAND 191 193 {ECO:0000244|PDB:3BL9}.
TURN 196 198 {ECO:0000244|PDB:3BL9}.
STRAND 200 204 {ECO:0000244|PDB:3BL9}.
HELIX 213 215 {ECO:0000244|PDB:1XML}.
STRAND 217 225 {ECO:0000244|PDB:3BL9}.
HELIX 230 232 {ECO:0000244|PDB:3BL9}.
HELIX 235 237 {ECO:0000244|PDB:3BL9}.
HELIX 238 256 {ECO:0000244|PDB:3BL9}.
HELIX 260 262 {ECO:0000244|PDB:3BL9}.
STRAND 263 270 {ECO:0000244|PDB:3BL9}.
STRAND 272 275 {ECO:0000244|PDB:3BL9}.
STRAND 277 282 {ECO:0000244|PDB:3BL9}.
TURN 292 294 {ECO:0000244|PDB:3BL9}.
STRAND 295 297 {ECO:0000244|PDB:3BL9}.
HELIX 298 307 {ECO:0000244|PDB:3BL9}.
HELIX 311 314 {ECO:0000244|PDB:3BL9}.
STRAND 317 322 {ECO:0000244|PDB:3BL9}.
HELIX 326 333 {ECO:0000244|PDB:3BL9}.
SEQUENCE 337 AA; 38609 MW; C9C5A33C212D7A52 CRC64;
MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK
IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP
PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL
DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL
LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE
VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS


Related products :

Catalog number Product name Quantity
EIAAB10638 DCPS,DCS1,DCS-1,HINT5,HINT-5,Hint-related 7meGMP-directed hydrolase,Histidine triad protein member 5,Pig,Scavenger mRNA-decapping enzyme DcpS,Sus scrofa
EIAAB10641 Bos taurus,Bovine,DCPS,DCS1,DCS-1,HINT5,HINT-5,Hint-related 7meGMP-directed hydrolase,Histidine triad protein member 5,Scavenger mRNA-decapping enzyme DcpS
EIAAB10642 Dcps,Dcs1,DCS-1,Hint5,HINT-5,Hint-related 7meGMP-directed hydrolase,Histidine triad protein member 5,Rat,Rattus norvegicus,Scavenger mRNA-decapping enzyme DcpS
EIAAB10639 Dcps,Dcs1,DCS-1,Hint5,HINT-5,Hint-related 7meGMP-directed hydrolase,Histidine triad protein member 5,Mouse,Mus musculus,Scavenger mRNA-decapping enzyme DcpS
EIAAB10640 DCPS,DCS1,DCS-1,HINT5,HINT-5,Hint-related 7meGMP-directed hydrolase,Histidine triad protein member 5,Homo sapiens,HSPC015,Human,Scavenger mRNA-decapping enzyme DcpS
CSB-EL006558HU Human Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit 96T
G8971 Scavenger mRNA-decapping enzyme DcpS (DCPS), Human, ELISA Kit 96T
CSB-EL006558RA Rat Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit SpeciesRat 96T
CSB-EL006558MO Mouse Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit 96T
CSB-EL006558PI Pig Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit SpeciesPig 96T
CSB-EL006558BO Bovine Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit 96T
G8970 Scavenger mRNA-decapping enzyme DcpS (DCPS), Bovine, ELISA Kit 96T
G8972 Scavenger mRNA-decapping enzyme DcpS (DCPS), Mouse, ELISA Kit 96T
CSB-EL006558RA Rat Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit 96T
G8973 Scavenger mRNA-decapping enzyme DcpS (DCPS), Pig, ELISA Kit 96T
G8974 Scavenger mRNA-decapping enzyme DcpS (DCPS), Rat, ELISA Kit 96T
CSB-EL006558MO Mouse Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit SpeciesMouse 96T
DCPS_RAT ELISA Kit FOR Scavenger mRNA-decapping enzyme DcpS; organism: Rat; gene name: Dcps 96T
CSB-EL006558BO Bovine Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit SpeciesBovine 96T
CSB-EL006558HU Human Scavenger mRNA-decapping enzyme DcpS(DCPS) ELISA kit SpeciesHuman 96T
DCPS_MOUSE ELISA Kit FOR Scavenger mRNA-decapping enzyme DcpS; organism: Mouse; gene name: Dcps 96T
28-134 Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts 0.1 mg
29-052 Decapping is a key step in general and regulated mRNA decay. The protein encoded by this gene is a decapping enzyme. This protein and another decapping enzyme form a decapping complex, which interacts 0.1 mg
DCST1 DCPS Gene decapping enzyme, scavenger
10-663-45591 Fragile Histidine Triad (FHIT) Human - EC 3.6.1.29; Diadenosine 5'.5'''-P1.P3-triphosphate hydrolase; Dinucleosidetriphosphatase; AP3A hydrolase; AP3AASE; Fragile histidine triad protein N_A 0.01 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur