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m7GpppN-mRNA hydrolase (EC 3.6.1.62) (Nucleoside diphosphate-linked moiety X motif 20) (Nudix motif 20) (mRNA-decapping enzyme 2) (hDpc)

 DCP2_HUMAN              Reviewed;         420 AA.
Q8IU60; C9J778; Q6P2D4; Q7Z5W5; Q8NBG5;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
22-NOV-2017, entry version 143.
RecName: Full=m7GpppN-mRNA hydrolase {ECO:0000305};
EC=3.6.1.62 {ECO:0000269|PubMed:12486012, ECO:0000269|PubMed:12923261, ECO:0000269|PubMed:21070968};
AltName: Full=Nucleoside diphosphate-linked moiety X motif 20;
Short=Nudix motif 20;
AltName: Full=mRNA-decapping enzyme 2;
Short=hDpc;
Name=DCP2; Synonyms=NUDT20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
GLU-148, SUBCELLULAR LOCATION, INTERACTION WITH DCP1A AND UPF1, AND
VARIANT LEU-16.
PubMed=12417715; DOI=10.1128/MCB.22.23.8114-8121.2002;
Lykke-Andersen J.;
"Identification of a human decapping complex associated with hUpf
proteins in nonsense-mediated decay.";
Mol. Cell. Biol. 22:8114-8121(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
147-GLU-GLU-148, SUBCELLULAR LOCATION, ASSOCIATION WITH POLYSOMES, AND
VARIANT LEU-16.
TISSUE=Erythroleukemia;
PubMed=12218187; DOI=10.1073/pnas.192445599;
Wang Z., Jiao X., Carr-Schmid A., Kiledjian M.;
"The hDcp2 protein is a mammalian mRNA decapping enzyme.";
Proc. Natl. Acad. Sci. U.S.A. 99:12663-12668(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-16.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
LEU-16.
TISSUE=Blood, and Uterus;
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]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=12486012; DOI=10.1093/emboj/cdf678;
van Dijk E., Cougot N., Meyer S., Babajko S., Wahle E., Seraphin B.;
"Human Dcp2: a catalytically active mRNA decapping enzyme located in
specific cytoplasmic structures.";
EMBO J. 21:6915-6924(2002).
[7]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH A COMPLEX CONTAINING
ENZYMES INVOLVED IN MRNA DECAY.
PubMed=12515382;
Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.;
"The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
Dcp1/2 and Xrnl in distinct cytoplasmic foci.";
RNA 8:1489-1501(2002).
[8]
FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, IDENTIFICATION IN A MRNA
DECAY COMPLEX WITH UPF1; UPF2 AND UPF3B, AND SUBCELLULAR LOCATION.
PubMed=14527413; DOI=10.1016/S1097-2765(03)00349-6;
Lejeune F., Li X., Maquat L.E.;
"Nonsense-mediated mRNA decay in mammalian cells involves decapping,
deadenylating, and exonucleolytic activities.";
Mol. Cell 12:675-687(2003).
[9]
FUNCTION, RNA-BINDING, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=12923261; DOI=10.1261/rna.5690503;
Piccirillo C., Khanna R., Kiledjian M.;
"Functional characterization of the mammalian mRNA decapping enzyme
hDcp2.";
RNA 9:1138-1147(2003).
[10]
INTERACTION WITH DCP1A AND DCP1B.
PubMed=15231747; DOI=10.1101/gr.2122004;
Lehner B., Sanderson C.M.;
"A protein interaction framework for human mRNA degradation.";
Genome Res. 14:1315-1323(2004).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH DCP1A.
PubMed=15067023; DOI=10.1083/jcb.200309008;
Cougot N., Babajko S., Seraphin B.;
"Cytoplasmic foci are sites of mRNA decay in human cells.";
J. Cell Biol. 165:31-40(2004).
[12]
SUBCELLULAR LOCATION.
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).
[13]
INTERACTION WITH ZFP36L1.
PubMed=15687258; DOI=10.1101/gad.1282305;
Lykke-Andersen J., Wagner E.;
"Recruitment and activation of mRNA decay enzymes by two ARE-mediated
decay activation domains in the proteins TTP and BRF-1.";
Genes Dev. 19:351-361(2005).
[14]
INTERACTION WITH DCP1A; EDC3; EDC4 AND DDX6, AND SUBCELLULAR LOCATION.
PubMed=16364915; DOI=10.1016/j.molcel.2005.10.031;
Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.;
"Multiple processing body factors and the ARE binding protein TTP
activate mRNA decapping.";
Mol. Cell 20:905-915(2005).
[15]
INTERACTION WITH APOBEC3G.
PubMed=16699599; DOI=10.1371/journal.ppat.0020041;
Wichroski M.J., Robb G.B., Rana T.M.;
"Human retroviral host restriction factors APOBEC3G and APOBEC3F
localize to mRNA processing bodies.";
PLoS Pathog. 2:E41-E41(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-284, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
INTERACTION WITH TRIM21.
PubMed=18361920; DOI=10.1016/j.bbrc.2008.03.075;
Yamochi T., Ohnuma K., Hosono O., Tanaka H., Kanai Y., Morimoto C.;
"SSA/Ro52 autoantigen interacts with Dcp2 to enhance its decapping
activity.";
Biochem. Biophys. Res. Commun. 370:195-199(2008).
[18]
FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
PubMed=18172165; DOI=10.1101/gad.1622708;
Mullen T.E., Marzluff W.F.;
"Degradation of histone mRNA requires oligouridylation followed by
decapping and simultaneous degradation of the mRNA both 5' to 3' and
3' to 5'.";
Genes Dev. 22:50-65(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247; SER-249
AND SER-284, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
FUNCTION AS A DECAPPING ENZYME, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
Song M.G., Li Y., Kiledjian M.;
"Multiple mRNA decapping enzymes in mammalian cells.";
Mol. Cell 40:423-432(2010).
[22]
SUBCELLULAR LOCATION, AND INTERACTION WITH LIMD1; WTIP AND AJUBA.
PubMed=20616046; DOI=10.1073/pnas.0914987107;
James V., Zhang Y., Foxler D.E., de Moor C.H., Kong Y.W., Webb T.M.,
Self T.J., Feng Y., Lagos D., Chu C.Y., Rana T.M., Morley S.J.,
Longmore G.D., Bushell M., Sharp T.V.;
"LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for
microRNA-mediated gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 107:12499-12504(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
INTERACTION WITH ZC3HAV1 AND DDX17.
PubMed=21876179; DOI=10.1073/pnas.1101676108;
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L.,
Zheng Y.T., Gao G.;
"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
targeting multiply spliced viral mRNAs for degradation.";
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247 AND
SER-249, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-284, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[27]
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).
[28]
FUNCTION, MUTAGENESIS OF SER-249, AND PHOSPHORYLATION AT SER-249.
PubMed=26098573; DOI=10.1038/ncb3189;
Hu G., McQuiston T., Bernard A., Park Y.D., Qiu J., Vural A.,
Zhang N., Waterman S.R., Blewett N.H., Myers T.G., Maraia R.J.,
Kehrl J.H., Uzel G., Klionsky D.J., Williamson P.R.;
"A conserved mechanism of TOR-dependent RCK-mediated mRNA degradation
regulates autophagy.";
Nat. Cell Biol. 17:930-942(2015).
[29]
INTERACTION WITH NBDY.
PubMed=27918561; DOI=10.1038/nchembio.2249;
D'Lima N.G., Ma J., Winkler L., Chu Q., Loh K.H., Corpuz E.O.,
Budnik B.A., Lykke-Andersen J., Saghatelian A., Slavoff S.A.;
"A human microprotein that interacts with the mRNA decapping
complex.";
Nat. Chem. Biol. 13:174-180(2017).
-!- FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of
the cap structure on mRNAs (PubMed:12417715, PubMed:12218187,
PubMed:12923261, PubMed:21070968). 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). 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).
Blocks autophagy in nutrient-rich conditions by repressing the
expression of ATG-related genes through degration 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}.
-!- CATALYTIC ACTIVITY: 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA]
+ H(2)O = N(7)-methylguanosine 5'-diphosphate + 5'-phospho-[mRNA].
{ECO:0000269|PubMed:12486012, ECO:0000269|PubMed:12923261,
ECO:0000269|PubMed:21070968}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:12923261};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12923261};
Note=Mn(2+) ion is required for highest activity. Can also utilize
magnesium ions. {ECO:0000269|PubMed:12923261};
-!- SUBUNIT: Found in a mRNA decay complex with LSM1, LSM3, LSM4,
EXOSC2, EXOSC4, EXOSC10, PARN, XRN1, CNOT6, UPF1, UPF2 and UPF3B
(PubMed:12417715, PubMed:12515382, PubMed:14527413). Forms a
complex with DCP1A, EDC3, DDX6 and EDC4/HEDLS, within this complex
directly interacts with EDC4/HEDLS (PubMed:15231747,
PubMed:15067023, PubMed:16364915). Interacts with DPC1B
(PubMed:15231747). Interacts (via N-terminus and C-terminus) with
TRIM21 (via N-terminus and C-terminus) (PubMed:18361920).
Associates with polysomes (PubMed:12218187). Interacts with LIMD1,
WTIP and AJUBA (PubMed:20616046). Interacts with DDX17 in an RNA-
dependent manner (PubMed:21876179). Interacts with ZC3HAV1
(PubMed:21876179). Interacts with APOBEC3G in an RNA-dependent
manner (PubMed:16699599). Interacts with ZFP36L1 (via N-terminus)
(PubMed:15687258). Interacts with NBDY (PubMed:27918561).
{ECO:0000269|PubMed:12218187, ECO:0000269|PubMed:12417715,
ECO:0000269|PubMed:12515382, ECO:0000269|PubMed:14527413,
ECO:0000269|PubMed:15067023, ECO:0000269|PubMed:15231747,
ECO:0000269|PubMed:15687258, ECO:0000269|PubMed:16364915,
ECO:0000269|PubMed:16699599, ECO:0000269|PubMed:18361920,
ECO:0000269|PubMed:20616046, ECO:0000269|PubMed:21876179,
ECO:0000269|PubMed:27918561}.
-!- INTERACTION:
Q9NPI6:DCP1A; NbExp=10; IntAct=EBI-521577, EBI-374238;
Q8IZD4:DCP1B; NbExp=3; IntAct=EBI-521577, EBI-521595;
Q6P2E9:EDC4; NbExp=4; IntAct=EBI-521577, EBI-1006038;
Q92900:UPF1; NbExp=3; IntAct=EBI-521577, EBI-373471;
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8IU60-1; Sequence=Displayed;
Name=2;
IsoId=Q8IU60-2; Sequence=VSP_012908;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain and testis. Not detected in
heart (at protein level). {ECO:0000269|PubMed:21070968}.
-!- PTM: Phosphorylated at ser-249 in a MTOR-dependent manner
(PubMed:26098573).
-!- SIMILARITY: Belongs to the Nudix hydrolase family. DCP2 subfamily.
{ECO:0000305}.
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EMBL; AY146650; AAN62762.1; -; mRNA.
EMBL; AY135173; AAN08884.1; -; mRNA.
EMBL; AK090564; BAC03479.1; -; mRNA.
EMBL; AC008536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC045596; AAH45596.1; -; mRNA.
EMBL; BC064593; AAH64593.1; -; mRNA.
CCDS; CCDS34210.1; -. [Q8IU60-1]
CCDS; CCDS56377.1; -. [Q8IU60-2]
RefSeq; NP_001229306.1; NM_001242377.1.
RefSeq; NP_689837.2; NM_152624.5.
UniGene; Hs.443875; -.
PDB; 5MP0; X-ray; 1.63 A; D=95-260.
PDBsum; 5MP0; -.
ProteinModelPortal; Q8IU60; -.
SMR; Q8IU60; -.
BioGrid; 127944; 67.
CORUM; Q8IU60; -.
DIP; DIP-31126N; -.
IntAct; Q8IU60; 16.
STRING; 9606.ENSP00000373715; -.
iPTMnet; Q8IU60; -.
PhosphoSitePlus; Q8IU60; -.
BioMuta; DCP2; -.
DMDM; 269849560; -.
EPD; Q8IU60; -.
MaxQB; Q8IU60; -.
PaxDb; Q8IU60; -.
PeptideAtlas; Q8IU60; -.
PRIDE; Q8IU60; -.
DNASU; 167227; -.
Ensembl; ENST00000389063; ENSP00000373715; ENSG00000172795.
Ensembl; ENST00000515408; ENSP00000425770; ENSG00000172795.
GeneID; 167227; -.
KEGG; hsa:167227; -.
UCSC; uc003kqh.4; human. [Q8IU60-1]
CTD; 167227; -.
EuPathDB; HostDB:ENSG00000172795.15; -.
GeneCards; DCP2; -.
HGNC; HGNC:24452; DCP2.
HPA; CAB011677; -.
HPA; HPA057676; -.
MIM; 609844; gene.
neXtProt; NX_Q8IU60; -.
PharmGKB; PA134898646; -.
eggNOG; KOG2937; Eukaryota.
eggNOG; COG0494; LUCA.
HOGENOM; HOG000005974; -.
HOVERGEN; HBG051321; -.
InParanoid; Q8IU60; -.
KO; K12613; -.
OrthoDB; EOG091G05Q0; -.
PhylomeDB; Q8IU60; -.
TreeFam; TF314180; -.
BRENDA; 3.6.1.62; 2681.
Reactome; R-HSA-380994; ATF4 activates genes.
Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
Reactome; R-HSA-450604; KSRP (KHSRP) binds and destabilizes mRNA.
ChiTaRS; DCP2; human.
GeneWiki; DCP2; -.
GenomeRNAi; 167227; -.
PRO; PR:Q8IU60; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000172795; -.
CleanEx; HS_DCP2; -.
ExpressionAtlas; Q8IU60; baseline and differential.
Genevisible; Q8IU60; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000932; C:P-body; IDA:MGI.
GO; GO:0016442; C:RISC complex; IDA:MGI.
GO; GO:0004534; F:5'-3' exoribonuclease activity; IMP:BHF-UCL.
GO; GO:0016896; F:exoribonuclease activity, producing 5'-phosphomonoesters; TAS:Reactome.
GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
GO; GO:0070034; F:telomerase RNA binding; IC:BHF-UCL.
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:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IMP:BHF-UCL.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:1904872; P:regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
InterPro; IPR007722; DCP2_BoxA.
InterPro; IPR036189; DCP2_BoxA_sf.
InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
InterPro; IPR020084; NUDIX_hydrolase_CS.
InterPro; IPR000086; NUDIX_hydrolase_dom.
Pfam; PF05026; DCP2; 1.
Pfam; PF00293; NUDIX; 1.
SMART; SM01125; DCP2; 1.
SUPFAM; SSF140586; SSF140586; 1.
SUPFAM; SSF55811; SSF55811; 1.
PROSITE; PS51462; NUDIX; 1.
PROSITE; PS00893; NUDIX_BOX; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Hydrolase; Manganese; Metal-binding; Nonsense-mediated mRNA decay;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
RNA-binding.
CHAIN 1 420 m7GpppN-mRNA hydrolase.
/FTId=PRO_0000057051.
DOMAIN 95 226 Nudix hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00794}.
MOTIF 129 150 Nudix box.
METAL 144 144 Manganese. {ECO:0000250}.
METAL 148 148 Manganese. {ECO:0000250}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 315 349 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012908.
VARIANT 16 16 F -> L (in dbSNP:rs33555).
{ECO:0000269|PubMed:12218187,
ECO:0000269|PubMed:12417715,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_059528.
MUTAGEN 147 147 E->Q: Loss of decapping activity; when
associated with Q-148.
MUTAGEN 148 148 E->Q: Strongly reduced decapping
activity. {ECO:0000269|PubMed:12417715}.
MUTAGEN 249 249 S->A: Leads to the accumulation of
autophagosomes under normal growth
conditions.
{ECO:0000269|PubMed:26098573}.
MUTAGEN 249 249 S->D: Leads to reduced autophagosome
formation under autophagy-inducing
conditions.
{ECO:0000269|PubMed:26098573}.
CONFLICT 103 103 I -> V (in Ref. 3; BAC03479).
{ECO:0000305}.
STRAND 99 105 {ECO:0000244|PDB:5MP0}.
STRAND 109 116 {ECO:0000244|PDB:5MP0}.
HELIX 119 121 {ECO:0000244|PDB:5MP0}.
STRAND 123 125 {ECO:0000244|PDB:5MP0}.
STRAND 127 130 {ECO:0000244|PDB:5MP0}.
HELIX 137 149 {ECO:0000244|PDB:5MP0}.
TURN 154 156 {ECO:0000244|PDB:5MP0}.
STRAND 162 167 {ECO:0000244|PDB:5MP0}.
STRAND 170 177 {ECO:0000244|PDB:5MP0}.
TURN 191 193 {ECO:0000244|PDB:5MP0}.
STRAND 196 201 {ECO:0000244|PDB:5MP0}.
HELIX 202 204 {ECO:0000244|PDB:5MP0}.
HELIX 213 215 {ECO:0000244|PDB:5MP0}.
TURN 224 228 {ECO:0000244|PDB:5MP0}.
HELIX 229 243 {ECO:0000244|PDB:5MP0}.
SEQUENCE 420 AA; 48457 MW; 78925E9E4FF0F6C8 CRC64;
METKRVEIPG SVLDDFCSRF ILHIPSEERD NAIRVCFQIE LAHWFYLDFY MQNTPGLPQC
GIRDFAKAVF SHCPFLLPQG EDVEKVLDEW KEYKMGVPTY GAIILDETLE NVLLVQGYLA
KSGWGFPKGK VNKEEAPHDC AAREVFEETG FDIKDYICKD DYIELRINDQ LARLYIIPGI
PKDTKFNPKT RREIRNIEWF SIEKLPCHRN DMTPKSKLGL APNKFFMAIP FIRPLRDWLS
RRFGDSSDSD NGFSSTGSTP AKPTVEKLSR TKFRHSQQLF PDGSPGDQWV KHRQPLQQKP
YNNHSEMSDL LKGKNQSMRG NGRKQYQDSP NQKKRTNGLQ PAKQQNSLMK CEKKLHPRKL
QDNFETDAVY DLPSSSEDQL LEHAEGQPVA CNGHCKFPFS SRAFLSFKFD HNAIMKILDL


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