EDC4_HUMAN
ID EDC4_HUMAN Reviewed; 1401 AA.
AC Q6P2E9; A6NGM1; A8K4T4; Q13025; Q13826; Q6ZR12; Q7Z6H7;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Enhancer of mRNA-decapping protein 4;
DE AltName: Full=Autoantigen Ge-1;
DE AltName: Full=Autoantigen RCD-8;
DE AltName: Full=Human enhancer of decapping large subunit;
DE Short=Hedls;
GN Name=EDC4; Synonyms=HEDLS;
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), AND SUBCELLULAR LOCATION.
RX PubMed=7520377; DOI=10.1006/clin.1994.1156;
RA Bloch D.B., Rabkina D., Quertermous T., Bloch K.D.;
RT "The immunoreactive region in a novel autoantigen contains a nuclear
RT localization sequence.";
RL Clin. Immunol. Immunopathol. 72:380-389(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Duodenum, Skin, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 421-1401 (ISOFORMS 1/2), AND SUBCELLULAR
RP LOCATION.
RX PubMed=9067524; DOI=10.1046/j.1365-2249.1997.d01-955.x;
RA Garcia-Lozano J.R., Gonzalez-Escribano M.F., Wichmann I., Nunez-Roldan A.;
RT "Cytoplasmic detection of a novel protein containing a nuclear localization
RT sequence by human autoantibodies.";
RL Clin. Exp. Immunol. 107:501-506(1997).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP INTERACTION WITH DCP1A; DCP1B; DCP2; DDX6 AND EDC3, SUBCELLULAR LOCATION,
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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 IDENTIFICATION BY 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-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION BY
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-871, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-821;
RP SER-844; SER-871 AND SER-879, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-879, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-729; SER-741;
RP SER-875; SER-879 AND SER-892, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP 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 [22]
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 [23]
RP IDENTIFICATION BY 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-6; SER-583; SER-585;
RP THR-693; SER-729; SER-844; SER-967 AND SER-1380, AND IDENTIFICATION BY MASS
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560; SER-565; SER-708;
RP SER-725; THR-727; SER-729; SER-871 AND SER-879, AND IDENTIFICATION BY MASS
RP 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [27]
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 [28]
RP INTERACTION WITH LSM14A.
RX PubMed=29510985; DOI=10.15252/embj.201797869;
RA Brandmann T., Fakim H., Padamsi Z., Youn J.Y., Gingras A.C., Fabian M.R.,
RA Jinek M.;
RT "Molecular architecture of LSM14 interactions involved in the assembly of
RT mRNA silencing complexes.";
RL EMBO J. 37:0-0(2018).
RN [29]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
CC -!- FUNCTION: In the process of mRNA degradation, seems to play a role in
CC mRNA decapping. Component of a complex containing DCP2 and DCP1A which
CC functions in decapping of ARE-containing mRNAs. Promotes complex
CC formation between DCP1A and DCP2. Enhances the catalytic activity of
CC DCP2 (in vitro). {ECO:0000269|PubMed:16364915}.
CC -!- SUBUNIT: Part of a decapping complex consisting of DCP1A, DCP2, EDC3,
CC EDC4 and probably DDX6. Part of a complex consisting of DCP1A, EDC3,
CC EDC4 and DDX6. Part of a complex consisting of DCP1B, EDC3, EDC4 and
CC DDX6. Interacts with DCP2 (PubMed:16364915). Interacts with RC3H1 (By
CC similarity). Interacts with NBDY (PubMed:27918561). Interacts with
CC TEX19 (By similarity). Interacts with LSM14A (PubMed:29510985).
CC Interacts with DDX6 (PubMed:31422817). {ECO:0000250|UniProtKB:Q3UJB9,
CC ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:27918561,
CC ECO:0000269|PubMed:29510985, ECO:0000269|PubMed:31422817}.
CC -!- INTERACTION:
CC Q6P2E9; Q9H9G7: AGO3; NbExp=2; IntAct=EBI-1006038, EBI-2267883;
CC Q6P2E9; Q13057: COASY; NbExp=3; IntAct=EBI-1006038, EBI-745967;
CC Q6P2E9; Q9NPI6: DCP1A; NbExp=11; IntAct=EBI-1006038, EBI-374238;
CC Q6P2E9; Q8IU60: DCP2; NbExp=8; IntAct=EBI-1006038, EBI-521577;
CC Q6P2E9; Q8IU60-2: DCP2; NbExp=2; IntAct=EBI-1006038, EBI-521590;
CC Q6P2E9; P19525: EIF2AK2; NbExp=2; IntAct=EBI-1006038, EBI-640775;
CC Q6P2E9; A0A0U1RRE5: NBDY; NbExp=11; IntAct=EBI-1006038, EBI-27058088;
CC Q6P2E9; Q8IZH2: XRN1; NbExp=4; IntAct=EBI-1006038, EBI-372406;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:16364915,
CC ECO:0000269|PubMed:9067524}. Nucleus {ECO:0000269|PubMed:7520377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6P2E9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P2E9-2; Sequence=VSP_023412;
CC -!- SIMILARITY: Belongs to the WD repeat EDC4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA21833.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB51444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH53598.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L26339; AAA21833.1; ALT_FRAME; mRNA.
DR EMBL; AK128582; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK291049; BAF83738.1; -; mRNA.
DR EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83183.1; -; Genomic_DNA.
DR EMBL; BC043616; AAH43616.1; -; mRNA.
DR EMBL; BC053598; AAH53598.1; ALT_INIT; mRNA.
DR EMBL; BC064567; AAH64567.1; -; mRNA.
DR EMBL; U17474; AAB51444.1; ALT_INIT; mRNA.
DR CCDS; CCDS10849.1; -. [Q6P2E9-1]
DR PIR; I52882; I52882.
DR RefSeq; NP_055144.3; NM_014329.4. [Q6P2E9-1]
DR AlphaFoldDB; Q6P2E9; -.
DR SMR; Q6P2E9; -.
DR BioGRID; 117171; 180.
DR CORUM; Q6P2E9; -.
DR DIP; DIP-31192N; -.
DR IntAct; Q6P2E9; 64.
DR MINT; Q6P2E9; -.
DR STRING; 9606.ENSP00000351811; -.
DR GlyGen; Q6P2E9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P2E9; -.
DR MetOSite; Q6P2E9; -.
DR PhosphoSitePlus; Q6P2E9; -.
DR SwissPalm; Q6P2E9; -.
DR BioMuta; EDC4; -.
DR DMDM; 74758241; -.
DR EPD; Q6P2E9; -.
DR jPOST; Q6P2E9; -.
DR MassIVE; Q6P2E9; -.
DR MaxQB; Q6P2E9; -.
DR PaxDb; Q6P2E9; -.
DR PeptideAtlas; Q6P2E9; -.
DR PRIDE; Q6P2E9; -.
DR ProteomicsDB; 66897; -. [Q6P2E9-1]
DR ProteomicsDB; 66898; -. [Q6P2E9-2]
DR Antibodypedia; 29657; 162 antibodies from 27 providers.
DR DNASU; 23644; -.
DR Ensembl; ENST00000358933.10; ENSP00000351811.5; ENSG00000038358.15. [Q6P2E9-1]
DR GeneID; 23644; -.
DR KEGG; hsa:23644; -.
DR MANE-Select; ENST00000358933.10; ENSP00000351811.5; NM_014329.5; NP_055144.3.
DR UCSC; uc002eur.4; human. [Q6P2E9-1]
DR CTD; 23644; -.
DR DisGeNET; 23644; -.
DR GeneCards; EDC4; -.
DR HGNC; HGNC:17157; EDC4.
DR HPA; ENSG00000038358; Low tissue specificity.
DR MIM; 606030; gene.
DR neXtProt; NX_Q6P2E9; -.
DR OpenTargets; ENSG00000038358; -.
DR PharmGKB; PA145148958; -.
DR VEuPathDB; HostDB:ENSG00000038358; -.
DR eggNOG; KOG1916; Eukaryota.
DR GeneTree; ENSGT00510000047791; -.
DR HOGENOM; CLU_005166_0_0_1; -.
DR InParanoid; Q6P2E9; -.
DR OMA; QQVNLMT; -.
DR OrthoDB; 1424637at2759; -.
DR PhylomeDB; Q6P2E9; -.
DR TreeFam; TF350715; -.
DR PathwayCommons; Q6P2E9; -.
DR Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
DR SignaLink; Q6P2E9; -.
DR BioGRID-ORCS; 23644; 256 hits in 1081 CRISPR screens.
DR ChiTaRS; EDC4; human.
DR GenomeRNAi; 23644; -.
DR Pharos; Q6P2E9; Tbio.
DR PRO; PR:Q6P2E9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6P2E9; protein.
DR Bgee; ENSG00000038358; Expressed in right hemisphere of cerebellum and 94 other tissues.
DR ExpressionAtlas; Q6P2E9; baseline and differential.
DR Genevisible; Q6P2E9; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; IDA:MGI.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IBA:GO_Central.
DR Gene3D; 1.10.220.100; -; 1.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045152; EDC4-like.
DR InterPro; IPR044938; EDC4_C.
DR InterPro; IPR032401; EDC4_WD40.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR15598; PTHR15598; 1.
DR Pfam; PF16529; Ge1_WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1401
FT /note="Enhancer of mRNA-decapping protein 4"
FT /id="PRO_0000278962"
FT REPEAT 121..164
FT /note="WD 1"
FT REPEAT 167..206
FT /note="WD 2"
FT REPEAT 217..269
FT /note="WD 3"
FT REPEAT 287..326
FT /note="WD 4"
FT REPEAT 335..385
FT /note="WD 5"
FT REPEAT 389..426
FT /note="WD 6"
FT REPEAT 432..475
FT /note="WD 7"
FT REGION 23..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..934
FT /note="Sufficient for nuclear localization"
FT COILED 954..1025
FT /evidence="ECO:0000255"
FT COMPBIAS 662..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 821
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:24275569"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 879
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UJB9"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023412"
FT CONFLICT 271..272
FT /note="ML -> IV (in Ref. 1; AAA21833)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="S -> N (in Ref. 6; AAB51444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018..1019
FT /note="QL -> HW (in Ref. 1; AAA21833)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160..1161
FT /note="KA -> NG (in Ref. 1; AAA21833)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1401 AA; 151661 MW; 0790BB8ADF488356 CRC64;
MASCASIDIE DATQHLRDIL KLDRPAGGPS AESPRPSSAY NGDLNGLLVP DPLCSGDSTS
ANKTGLRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI VASSDSSISS KARGSNKVKI
QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR AANNGSAMVR VISVSTSERT LLKGFTGSVA
DLAFAHLNSP QLACLDEAGN LFVWRLALVN GKIQEEILVH IRQPEGTPLN HFRRIIWCPF
IPEESEDCCE ESSPTVALLH EDRAEVWDLD MLRSSHSTWP VDVSQIKQGF IVVKGHSTCL
SEGALSPDGT VLATASHDGY VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC LLFCDNHKKQ
DPDVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI FSSVSVPPSL KVCLDLSAEY
LILSDVQRKV LYVMELLQNQ EEGHACFSSI SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA
EEENDSLGAD GTHGAGAMES AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLPTHTA
HEDFTFGESR PELGSEGLGS AAHGSQPDLR RIVELPAPAD FLSLSSETKP KLMTPDAFMT
PSASLQQITA SPSSSSSGSS SSSSSSSSSL TAVSAMSSTS AVDPSLTRPP EELTLSPKLQ
LDGSLTMSSS GSLQASPRGL LPGLLPAPAD KLTPKGPGQV PTATSALSLE LQEVEPLGLP
QASPSRTRSP DVISSASTAL SQDIPEIASE ALSRGFGSSA PEGLEPDSMA SAASALHLLS
PRPRPGPELG PQLGLDGGPG DGDRHNTPSL LEAALTQEAS TPDSQVWPTA PDITRETCST
LAESPRNGLQ EKHKSLAFHR PPYHLLQQRD SQDASAEQSD HDDEVASLAS ASGGFGTKVP
APRLPAKDWK TKGSPRTSPK LKRKSKKDDG DAAMGSRLTE HQVAEPPEDW PALIWQQQRE
LAELRHSQEE LLQRLCTQLE GLQSTVTGHV ERALETRHEQ EQRRLERALA EGQQRGGQLQ
EQLTQQLSQA LSSAVAGRLE RSIRDEIKKT VPPCVSRSLE PMAGQLSNSV ATKLTAVEGS
MKENISKLLK SKNLTDAIAR AAADTLQGPM QAAYREAFQS VVLPAFEKSC QAMFQQINDS
FRLGTQEYLQ QLESHMKSRK AREQEAREPV LAQLRGLVST LQSATEQMAA TVAGSVRAEV
QHQLHVAVGS LQESILAQVQ RIVKGEVSVA LKEQQAAVTS SIMQAMRSAA GTPVPSAHLD
CQAQQAHILQ LLQQGHLNQA FQQALTAADL NLVLYVCETV DPAQVFGQPP CPLSQPVLLS
LIQQLASDLG TRTDLKLSYL EEAVMHLDHS DPITRDHMGS VMAQVRQKLF QFLQAEPHNS
LGKAARRLSL MLHGLVTPSL P
