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 27-MAR-2024, entry version 184. 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 ROTAVIRUS A NON-STRUCTURAL PROTEIN 2 (MICROBIAL RP INFECTION), AND INTERACTION WITH ROTAVIRUS A NON-STRUCTURAL PROTEIN 5 RP (MICROBIAL INFECTION). RX PubMed=30258011; DOI=10.1128/jvi.01363-18; RA Dhillon P., Rao C.D.; RT "Rotavirus Induces Formation of Remodeled Stress Granules and P Bodies and RT Their Sequestration in Viroplasms To Promote Progeny Virus Production."; RL J. Virol. 92:0-0(2018). RN [30] 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 -!- SUBUNIT: (Microbial infection) Interacts with rotavirus A non- CC structural protein 2; this interaction probably plays a role in the CC sequestration of EDC4 in viral factories (PubMed:30258011). Interacts CC with rotavirus A non-structural protein 5; this interaction probably CC plays a role in its sequestration in viral factories (PubMed:30258011). CC {ECO:0000269|PubMed:30258011}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 215. DR ComplexPortal; CPX-2870; RNA decapping and exonuclease complex, DCP1A variant. DR ComplexPortal; CPX-7341; RNA decapping and exonuclease complex, DCP1B variant. DR CORUM; Q6P2E9; -. DR DIP; DIP-31192N; -. DR IntAct; Q6P2E9; 71. 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; 9606-ENSP00000351811; -. DR PeptideAtlas; Q6P2E9; -. DR ProteomicsDB; 66897; -. [Q6P2E9-1] DR ProteomicsDB; 66898; -. [Q6P2E9-2] DR Pumba; Q6P2E9; -. DR Antibodypedia; 29657; 178 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 AGR; HGNC:17157; -. 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; VIAMHVK; -. DR OrthoDB; 2911539at2759; -. 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; 269 hits in 1161 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 96 other cell types or tissues. DR ExpressionAtlas; Q6P2E9; baseline and differential. 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; 6.10.140.270; -; 1. DR Gene3D; 1.10.220.100; conserved c-terminal region of ge- 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR045152; EDC4-like. DR InterPro; IPR049404; EDC4_C. DR InterPro; IPR044938; EDC4_C_sf. DR InterPro; IPR032401; EDC4_WD40. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR15598; ENHANCER OF MRNA-DECAPPING PROTEIN 4; 1. DR PANTHER; PTHR15598:SF5; ENHANCER OF MRNA-DECAPPING PROTEIN 4; 1. DR Pfam; PF21289; EDC4_C; 1. DR Pfam; PF16529; Ge1_WD40; 1. DR SMART; SM00320; WD40; 3. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50082; WD_REPEATS_2; 1. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q6P2E9; HS. 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 //