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Enhancer of mRNA-decapping protein 4 (Autoantigen Ge-1) (Autoantigen RCD-8) (Human enhancer of decapping large subunit) (Hedls)

 EDC4_HUMAN              Reviewed;        1401 AA.
Q6P2E9; A6NGM1; A8K4T4; Q13025; Q13826; Q6ZR12; Q7Z6H7;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
18-JUL-2018, entry version 149.
RecName: Full=Enhancer of mRNA-decapping protein 4;
AltName: Full=Autoantigen Ge-1;
AltName: Full=Autoantigen RCD-8;
AltName: Full=Human enhancer of decapping large subunit;
Short=Hedls;
Name=EDC4; Synonyms=HEDLS;
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), AND SUBCELLULAR LOCATION.
PubMed=7520377; DOI=10.1006/clin.1994.1156;
Bloch D.B., Rabkina D., Quertermous T., Bloch K.D.;
"The immunoreactive region in a novel autoantigen contains a nuclear
localization sequence.";
Clin. Immunol. Immunopathol. 72:380-389(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Trachea;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Duodenum, Skin, and Testis;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 421-1401 (ISOFORMS 1/2), AND SUBCELLULAR
LOCATION.
PubMed=9067524; DOI=10.1046/j.1365-2249.1997.d01-955.x;
Garcia-Lozano J.R., Gonzalez-Escribano M.F., Wichmann I.,
Nunez-Roldan A.;
"Cytoplasmic detection of a novel protein containing a nuclear
localization sequence by human autoantibodies.";
Clin. Exp. Immunol. 107:501-506(1997).
[7]
INTERACTION WITH DCP1A; DCP1B; DCP2; DDX6 AND EDC3, SUBCELLULAR
LOCATION, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-871, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723; SER-725; THR-821;
SER-844; SER-871 AND SER-879, 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).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729 AND SER-879, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-729; SER-741;
SER-875; SER-879 AND SER-892, 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).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-125, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[20]
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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-6; SER-583;
SER-585; THR-693; SER-729; SER-844; SER-967 AND SER-1380, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560; SER-565; SER-708;
SER-725; THR-727; SER-729; SER-871 AND SER-879, AND 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).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
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: In the process of mRNA degradation, seems to play a role
in mRNA decapping. Component of a complex containing DCP2 and
DCP1A which functions in decapping of ARE-containing mRNAs.
Promotes complex formation between DCP1A and DCP2. Enhances the
catalytic activity of DCP2 (in vitro).
{ECO:0000269|PubMed:16364915}.
-!- SUBUNIT: Part of a decapping complex consisting of DCP1A, DCP2,
EDC3, EDC4 and probably DDX6. Part of a complex consisting of
DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B,
EDC3, EDC4 and DDX6. Interacts with DCP2 (PubMed:16364915).
Interacts with RC3H1 (By similarity). Interacts with NBDY
(PubMed:27918561). Interacts with TEX19 (By similarity).
{ECO:0000250|UniProtKB:Q3UJB9, ECO:0000269|PubMed:16364915,
ECO:0000269|PubMed:27918561}.
-!- INTERACTION:
Q9H9G7:AGO3; NbExp=2; IntAct=EBI-1006038, EBI-2267883;
Q13057:COASY; NbExp=3; IntAct=EBI-1006038, EBI-745967;
Q9NPI6:DCP1A; NbExp=10; IntAct=EBI-1006038, EBI-374238;
Q8IU60:DCP2; NbExp=4; IntAct=EBI-1006038, EBI-521577;
P19525:EIF2AK2; NbExp=2; IntAct=EBI-1006038, EBI-640775;
-!- SUBCELLULAR LOCATION: Cytoplasm, P-body
{ECO:0000269|PubMed:16364915, ECO:0000269|PubMed:9067524}. Nucleus
{ECO:0000269|PubMed:7520377}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6P2E9-1; Sequence=Displayed;
Name=2;
IsoId=Q6P2E9-2; Sequence=VSP_023412;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the WD repeat EDC4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA21833.1; Type=Frameshift; Positions=1189; Evidence={ECO:0000305};
Sequence=AAB51444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH53598.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L26339; AAA21833.1; ALT_FRAME; mRNA.
EMBL; AK128582; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK291049; BAF83738.1; -; mRNA.
EMBL; AC040162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83183.1; -; Genomic_DNA.
EMBL; BC043616; AAH43616.1; -; mRNA.
EMBL; BC053598; AAH53598.1; ALT_INIT; mRNA.
EMBL; BC064567; AAH64567.1; -; mRNA.
EMBL; U17474; AAB51444.1; ALT_INIT; mRNA.
CCDS; CCDS10849.1; -. [Q6P2E9-1]
PIR; I52882; I52882.
RefSeq; NP_055144.3; NM_014329.4. [Q6P2E9-1]
UniGene; Hs.75682; -.
ProteinModelPortal; Q6P2E9; -.
BioGrid; 117171; 98.
CORUM; Q6P2E9; -.
DIP; DIP-31192N; -.
IntAct; Q6P2E9; 36.
MINT; Q6P2E9; -.
STRING; 9606.ENSP00000351811; -.
iPTMnet; Q6P2E9; -.
PhosphoSitePlus; Q6P2E9; -.
SwissPalm; Q6P2E9; -.
BioMuta; EDC4; -.
DMDM; 74758241; -.
EPD; Q6P2E9; -.
MaxQB; Q6P2E9; -.
PaxDb; Q6P2E9; -.
PeptideAtlas; Q6P2E9; -.
PRIDE; Q6P2E9; -.
ProteomicsDB; 66897; -.
ProteomicsDB; 66898; -. [Q6P2E9-2]
Ensembl; ENST00000358933; ENSP00000351811; ENSG00000038358. [Q6P2E9-1]
GeneID; 23644; -.
KEGG; hsa:23644; -.
UCSC; uc002eur.4; human. [Q6P2E9-1]
CTD; 23644; -.
EuPathDB; HostDB:ENSG00000038358.14; -.
GeneCards; EDC4; -.
HGNC; HGNC:17157; EDC4.
HPA; HPA041164; -.
HPA; HPA043038; -.
MIM; 606030; gene.
neXtProt; NX_Q6P2E9; -.
OpenTargets; ENSG00000038358; -.
PharmGKB; PA145148958; -.
eggNOG; KOG1916; Eukaryota.
eggNOG; ENOG410XP6V; LUCA.
GeneTree; ENSGT00510000047791; -.
HOVERGEN; HBG053855; -.
InParanoid; Q6P2E9; -.
KO; K12616; -.
OMA; SAHLDCQ; -.
OrthoDB; EOG091G036X; -.
PhylomeDB; Q6P2E9; -.
TreeFam; TF350715; -.
Reactome; R-HSA-430039; mRNA decay by 5' to 3' exoribonuclease.
ChiTaRS; EDC4; human.
GenomeRNAi; 23644; -.
PMAP-CutDB; Q6P2E9; -.
PRO; PR:Q6P2E9; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000038358; -.
CleanEx; HS_EDC4; -.
ExpressionAtlas; Q6P2E9; baseline and differential.
Genevisible; Q6P2E9; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000932; C:P-body; IDA:MGI.
GO; GO:0031087; P:deadenylation-independent 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.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR032401; EDC4_WD40.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF16529; Ge1_WD40; 1.
SMART; SM00320; WD40; 3.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS50082; WD_REPEATS_2; 1.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1401 Enhancer of mRNA-decapping protein 4.
/FTId=PRO_0000278962.
REPEAT 121 164 WD 1.
REPEAT 167 206 WD 2.
REPEAT 217 269 WD 3.
REPEAT 287 326 WD 4.
REPEAT 335 385 WD 5.
REPEAT 389 426 WD 6.
REPEAT 432 475 WD 7.
REGION 913 934 Sufficient for nuclear localization.
COILED 954 1025 {ECO:0000255}.
COMPBIAS 602 676 Ser-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 125 125 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 560 560 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 565 565 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 676 676 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UJB9}.
MOD_RES 693 693 Phosphothreonine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 727 727 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 741 741 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332}.
MOD_RES 821 821 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 844 844 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 871 871 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 879 879 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 887 887 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UJB9}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UJB9}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 967 967 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1380 1380 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 381 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_023412.
CONFLICT 271 272 ML -> IV (in Ref. 1; AAA21833).
{ECO:0000305}.
CONFLICT 621 621 S -> N (in Ref. 6; AAB51444).
{ECO:0000305}.
CONFLICT 1018 1019 QL -> HW (in Ref. 1; AAA21833).
{ECO:0000305}.
CONFLICT 1160 1161 KA -> NG (in Ref. 1; AAA21833).
{ECO:0000305}.
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


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