DCP1A_HUMAN
ID DCP1A_HUMAN Reviewed; 582 AA.
AC Q9NPI6; B4DHN9; U3KQM8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=mRNA-decapping enzyme 1A;
DE EC=3.6.1.62 {ECO:0000269|PubMed:12417715};
DE AltName: Full=Smad4-interacting transcriptional co-activator;
DE AltName: Full=Transcription factor SMIF;
GN Name=DCP1A; Synonyms=SMIF;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF ASP-20 AND
RP ARG-59, INTERACTION WITH DCP1B; DCP2 AND UPF1, SUBCELLULAR LOCATION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=12417715; DOI=10.1128/mcb.22.23.8114-8121.2002;
RA Lykke-Andersen J.;
RT "Identification of a human decapping complex associated with hUpf proteins
RT in nonsense-mediated decay.";
RL Mol. Cell. Biol. 22:8114-8121(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SMAD4,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=11836524; DOI=10.1038/ncb753;
RA Bai R.-Y., Koester C., Ouyang T., Hahn S.A., Hammerschmidt M., Peschel C.,
RA Duyster J.;
RT "SMIF, a Smad4-interacting protein that functions as a co-activator in
RT TGFbeta signalling.";
RL Nat. Cell Biol. 4:181-190(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Caudate nucleus, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH A COMPLEX CONTAINING ENZYMES
RP INVOLVED IN MRNA DECAY.
RX PubMed=12515382;
RA Ingelfinger D., Arndt-Jovin D.J., Luehrmann R., Achsel T.;
RT "The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes
RT Dcp1/2 and Xrnl in distinct cytoplasmic foci.";
RL RNA 8:1489-1501(2002).
RN [7]
RP INTERACTION WITH ZFP36L1.
RX PubMed=15687258; DOI=10.1101/gad.1282305;
RA Lykke-Andersen J., Wagner E.;
RT "Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay
RT activation domains in the proteins TTP and BRF-1.";
RL Genes Dev. 19:351-361(2005).
RN [8]
RP INTERACTION WITH EDC3; DCP2; EDC4 AND DDX6, AND SUBCELLULAR LOCATION.
RX PubMed=16364915; DOI=10.1016/j.molcel.2005.10.031;
RA Fenger-Groen M., Fillman C., Norrild B., Lykke-Andersen J.;
RT "Multiple processing body factors and the ARE binding protein TTP activate
RT mRNA decapping.";
RL Mol. Cell 20:905-915(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-334 AND THR-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-353, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-315; SER-319;
RP SER-334; SER-353; THR-401; SER-522; SER-523; SER-525 AND THR-531, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP INTERACTION WITH PNRC2.
RX PubMed=19150429; DOI=10.1016/j.molcel.2008.11.022;
RA Cho H., Kim K.M., Kim Y.K.;
RT "Human proline-rich nuclear receptor coregulatory protein 2 mediates an
RT interaction between mRNA surveillance machinery and decapping complex.";
RL Mol. Cell 33:75-86(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-315; SER-319;
RP SER-522; SER-523; SER-525 AND THR-531, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319; SER-353 AND
RP SER-422, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH ZC3HAV1 AND DDX17.
RX PubMed=21876179; DOI=10.1073/pnas.1101676108;
RA Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T.,
RA Gao G.;
RT "Zinc-finger antiviral protein inhibits HIV-1 infection by selectively
RT targeting multiply spliced viral mRNAs for degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-315; THR-348;
RP SER-353; THR-401; SER-522; SER-523; SER-525 AND THR-531, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP INTERACTION WITH DHX34.
RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020;
RA Hug N., Caceres J.F.;
RT "The RNA helicase DHX34 activates NMD by promoting a transition from the
RT surveillance to the decay-inducing complex.";
RL Cell Rep. 8:1845-1856(2014).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-376, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [24]
RP INTERACTION WITH NBDY.
RX PubMed=27918561; DOI=10.1038/nchembio.2249;
RA D'Lima N.G., Ma J., Winkler L., Chu Q., Loh K.H., Corpuz E.O., Budnik B.A.,
RA Lykke-Andersen J., Saghatelian A., Slavoff S.A.;
RT "A human microprotein that interacts with the mRNA decapping complex.";
RL Nat. Chem. Biol. 13:174-180(2017).
RN [25]
RP FUNCTION.
RX PubMed=33813271; DOI=10.1016/j.bbrc.2021.03.117;
RA Ibayashi M., Aizawa R., Tsukamoto S.;
RT "mRNA decapping factor Dcp1a is essential for embryonic growth in mice.";
RL Biochem. Biophys. Res. Commun. 555:128-133(2021).
CC -!- FUNCTION: Necessary for the degradation of mRNAs, both in normal mRNA
CC turnover and in nonsense-mediated mRNA decay (PubMed:12417715). Removes
CC the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-
CC phosphorylated mRNA fragment and 7m-GDP (PubMed:12417715). Contributes
CC to the transactivation of target genes after stimulation by TGFB1
CC (PubMed:11836524). Essential for embryonic development
CC (PubMed:33813271). {ECO:0000269|PubMed:11836524,
CC ECO:0000269|PubMed:12417715, ECO:0000269|PubMed:33813271}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside
CC in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) +
CC N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692,
CC Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461;
CC EC=3.6.1.62; Evidence={ECO:0000269|PubMed:12417715};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485;
CC Evidence={ECO:0000305|PubMed:12417715};
CC -!- SUBUNIT: Forms a complex with EDC3, DCP2, DDX6 and EDC4/HEDLS, within
CC this complex directly interacts with EDC3 (PubMed:16364915). Part of a
CC cytoplasmic complex containing proteins involved in mRNA decay,
CC including XRN1 and LSM1 (PubMed:12515382). Interacts with DCP1B
CC (PubMed:12417715). Interacts with DCP2 (PubMed:12417715). Interacts
CC with DDX17 in an RNA-independent manner (PubMed:21876179). Interacts
CC with PNRC2 (PubMed:19150429). Interacts with SMAD4 (PubMed:11836524).
CC Interacts with UPF1 (PubMed:12417715). Interacts with ZC3HAV1
CC (PubMed:21876179). Interacts with ZFP36L1 (PubMed:15687258). Interacts
CC with NBDY (PubMed:27918561). Interacts with DHX34; the interaction is
CC RNA-independent (PubMed:25220460). {ECO:0000269|PubMed:11836524,
CC ECO:0000269|PubMed:12417715, ECO:0000269|PubMed:12515382,
CC ECO:0000269|PubMed:15687258, ECO:0000269|PubMed:16364915,
CC ECO:0000269|PubMed:19150429, ECO:0000269|PubMed:21876179,
CC ECO:0000269|PubMed:25220460, ECO:0000269|PubMed:27918561}.
CC -!- INTERACTION:
CC Q9NPI6; O95429: BAG4; NbExp=5; IntAct=EBI-374238, EBI-2949658;
CC Q9NPI6; Q9NPI6: DCP1A; NbExp=9; IntAct=EBI-374238, EBI-374238;
CC Q9NPI6; Q8IZD4: DCP1B; NbExp=8; IntAct=EBI-374238, EBI-521595;
CC Q9NPI6; Q8IU60: DCP2; NbExp=16; IntAct=EBI-374238, EBI-521577;
CC Q9NPI6; P26196: DDX6; NbExp=9; IntAct=EBI-374238, EBI-351257;
CC Q9NPI6; Q96F86: EDC3; NbExp=14; IntAct=EBI-374238, EBI-997311;
CC Q9NPI6; Q6P2E9: EDC4; NbExp=11; IntAct=EBI-374238, EBI-1006038;
CC Q9NPI6; Q14192: FHL2; NbExp=10; IntAct=EBI-374238, EBI-701903;
CC Q9NPI6; A0A0U1RRE5: NBDY; NbExp=4; IntAct=EBI-374238, EBI-27058088;
CC Q9NPI6; Q92636: NSMAF; NbExp=2; IntAct=EBI-374238, EBI-2947053;
CC Q9NPI6; Q86TB9: PATL1; NbExp=2; IntAct=EBI-374238, EBI-2562092;
CC Q9NPI6; Q9NPJ4: PNRC2; NbExp=11; IntAct=EBI-374238, EBI-726549;
CC Q9NPI6; Q9NPJ4-1: PNRC2; NbExp=6; IntAct=EBI-374238, EBI-16018718;
CC Q9NPI6; P43351: RAD52; NbExp=5; IntAct=EBI-374238, EBI-706448;
CC Q9NPI6; Q96K30: RITA1; NbExp=4; IntAct=EBI-374238, EBI-2836148;
CC Q9NPI6; Q13485: SMAD4; NbExp=5; IntAct=EBI-374238, EBI-347263;
CC Q9NPI6; Q92900: UPF1; NbExp=13; IntAct=EBI-374238, EBI-373471;
CC Q9NPI6; P26651: ZFP36; NbExp=2; IntAct=EBI-374238, EBI-374248;
CC Q9NPI6; F4HZB2: SPI; Xeno; NbExp=2; IntAct=EBI-374238, EBI-3386960;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:12417715,
CC ECO:0000269|PubMed:12515382, ECO:0000269|PubMed:16364915}. Nucleus
CC {ECO:0000269|PubMed:11836524, ECO:0000269|PubMed:12417715}. Note=Co-
CC localizes with NANOS3 in the processing bodies (By similarity).
CC Predominantly cytoplasmic, in processing bodies (PB) (PubMed:16364915).
CC Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on
CC interaction with SMAD4 (PubMed:11836524).
CC {ECO:0000250|UniProtKB:Q91YD3, ECO:0000269|PubMed:11836524,
CC ECO:0000269|PubMed:16364915}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NPI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NPI6-2; Sequence=VSP_057206;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, lung, skeletal
CC muscle, liver, kidney and pancreas. {ECO:0000269|PubMed:11836524}.
CC -!- SIMILARITY: Belongs to the DCP1 family. {ECO:0000305}.
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DR EMBL; AY146651; AAN62763.1; -; mRNA.
DR EMBL; AJ275986; CAB77023.1; -; mRNA.
DR EMBL; AK001969; BAA92008.1; -; mRNA.
DR EMBL; AK295205; BAG58201.1; -; mRNA.
DR EMBL; AC097015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007439; AAH07439.1; -; mRNA.
DR CCDS; CCDS46847.2; -. [Q9NPI6-1]
DR CCDS; CCDS74946.1; -. [Q9NPI6-2]
DR RefSeq; NP_001277133.1; NM_001290204.1. [Q9NPI6-2]
DR RefSeq; NP_001277134.1; NM_001290205.1.
DR RefSeq; NP_001277135.1; NM_001290206.1.
DR RefSeq; NP_001277136.1; NM_001290207.1.
DR RefSeq; NP_060873.4; NM_018403.6. [Q9NPI6-1]
DR PDB; 2WX3; X-ray; 2.31 A; A/B/C=539-582.
DR PDB; 4B6H; X-ray; 2.60 A; A/B=1-130.
DR PDBsum; 2WX3; -.
DR PDBsum; 4B6H; -.
DR AlphaFoldDB; Q9NPI6; -.
DR SMR; Q9NPI6; -.
DR BioGRID; 120914; 172.
DR CORUM; Q9NPI6; -.
DR DIP; DIP-31292N; -.
DR IntAct; Q9NPI6; 51.
DR MINT; Q9NPI6; -.
DR STRING; 9606.ENSP00000476046; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q9NPI6; 8 sites, 1 O-linked glycan (8 sites).
DR iPTMnet; Q9NPI6; -.
DR PhosphoSitePlus; Q9NPI6; -.
DR BioMuta; DCP1A; -.
DR DMDM; 296434475; -.
DR EPD; Q9NPI6; -.
DR jPOST; Q9NPI6; -.
DR MassIVE; Q9NPI6; -.
DR MaxQB; Q9NPI6; -.
DR PeptideAtlas; Q9NPI6; -.
DR PRIDE; Q9NPI6; -.
DR ProteomicsDB; 82020; -. [Q9NPI6-1]
DR Antibodypedia; 73473; 389 antibodies from 34 providers.
DR DNASU; 55802; -.
DR Ensembl; ENST00000294241.10; ENSP00000476046.2; ENSG00000272886.6. [Q9NPI6-2]
DR Ensembl; ENST00000610213.6; ENSP00000476386.1; ENSG00000272886.6. [Q9NPI6-1]
DR GeneID; 55802; -.
DR KEGG; hsa:55802; -.
DR MANE-Select; ENST00000610213.6; ENSP00000476386.1; NM_018403.7; NP_060873.4.
DR UCSC; uc021wzk.3; human. [Q9NPI6-1]
DR CTD; 55802; -.
DR DisGeNET; 55802; -.
DR GeneCards; DCP1A; -.
DR HGNC; HGNC:18714; DCP1A.
DR HPA; ENSG00000272886; Low tissue specificity.
DR MIM; 607010; gene.
DR neXtProt; NX_Q9NPI6; -.
DR OpenTargets; ENSG00000272886; -.
DR PharmGKB; PA134931379; -.
DR VEuPathDB; HostDB:ENSG00000272886; -.
DR eggNOG; KOG2868; Eukaryota.
DR GeneTree; ENSGT00940000158818; -.
DR HOGENOM; CLU_030030_0_0_1; -.
DR InParanoid; Q9NPI6; -.
DR OMA; TPQHDQM; -.
DR OrthoDB; 1509316at2759; -.
DR PhylomeDB; Q9NPI6; -.
DR PathwayCommons; Q9NPI6; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
DR Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; Q9NPI6; -.
DR BioGRID-ORCS; 55802; 9 hits in 182 CRISPR screens.
DR ChiTaRS; DCP1A; human.
DR EvolutionaryTrace; Q9NPI6; -.
DR GeneWiki; DCP1A; -.
DR GenomeRNAi; 55802; -.
DR Pharos; Q9NPI6; Tbio.
DR PRO; PR:Q9NPI6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NPI6; protein.
DR Bgee; ENSG00000272886; Expressed in oocyte and 206 other tissues.
DR ExpressionAtlas; Q9NPI6; baseline and differential.
DR Genevisible; Q9NPI6; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR GO; GO:0110156; P:methylguanosine-cap decapping; IMP:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IEA:InterPro.
DR GO; GO:1903608; P:protein localization to cytoplasmic stress granule; IMP:AgBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010334; Dcp1.
DR InterPro; IPR031953; mRNA_decap_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR16290; PTHR16290; 1.
DR Pfam; PF06058; DCP1; 1.
DR Pfam; PF16741; mRNA_decap_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Hydrolase; Methylation;
KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..582
FT /note="mRNA-decapping enzyme 1A"
FT /id="PRO_0000189632"
FT REGION 132..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91YD3"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 376
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q91YD3"
FT MOD_RES 531
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 171..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057206"
FT MUTAGEN 20
FT /note="D->A: Lowers decapping activity."
FT /evidence="ECO:0000269|PubMed:12417715"
FT MUTAGEN 59
FT /note="R->A: Lowers decapping activity."
FT /evidence="ECO:0000269|PubMed:12417715"
FT CONFLICT 483
FT /note="P -> Q (in Ref. 4; AC097015/AC112218)"
FT HELIX 1..19
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 23..39
FT /evidence="ECO:0007829|PDB:4B6H"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 44..63
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4B6H"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:4B6H"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:4B6H"
FT HELIX 539..557
FT /evidence="ECO:0007829|PDB:2WX3"
FT HELIX 559..571
FT /evidence="ECO:0007829|PDB:2WX3"
SQ SEQUENCE 582 AA; 63278 MW; 26480D0B10CE7C72 CRC64;
MEALSRAGQE MSLAALKQHD PYITSIADLT GQVALYTFCP KANQWEKTDI EGTLFVYRRS
ASPYHGFTIV NRLNMHNLVE PVNKDLEFQL HEPFLLYRNA SLSIYSIWFY DKNDCHRIAK
LMADVVEEET RRSQQAARDK QSPSQANGCS DHRPIDILEM LSRAKDEYER NQMGDSNISS
PGLQPSTQLS NLGSTETLEE MPSGSQDKSA PSGHKHLTVE ELFGTSLPKE QPAVVGLDSE
EMERLPGDAS QKEPNSFLPF PFEQLGGAPQ SETLGVPSAA HHSVQPEITT PVLITPASIT
QSNEKHAPTY TIPLSPVLSP TLPAEAPTAQ VPPSLPRNST MMQAVKTTPR QRSPLLNQPV
PELSHASLIA NQSPFRAPLN VTNTAGTSLP SVDLLQKLRL TPQHDQIQTQ PLGKGAMVAS
FSPAAGQLAT PESFIEPPSK TAAARVAASA SLSNMVLAPL QSMQQNQDPE VFVQPKVLSS
AIPVAGAPLV TATTTAVSSV LLAPSVFQQT VTRSSDLERK ASSPSPLTIG TPESQRKPSI
ILSKSQLQDT LIHLIKNDSS FLSTLHEVYL QVLTKNKDNH NL
