EIF3D_HUMAN
ID EIF3D_HUMAN Reviewed; 548 AA.
AC O15371; A8MWD3; B2R7D4; B4DTF8; B4DVY1; Q3MJD9; Q5M9Q6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003};
DE Short=eIF3d {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 7 {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=eIF-3-zeta {ECO:0000255|HAMAP-Rule:MF_03003};
DE AltName: Full=eIF3 p66;
GN Name=EIF3D {ECO:0000255|HAMAP-Rule:MF_03003};
GN Synonyms=EIF3S7 {ECO:0000255|HAMAP-Rule:MF_03003};
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).
RC TISSUE=Liver;
RX PubMed=9341143; DOI=10.1074/jbc.272.43.27042;
RA Asano K., Vornlocher H.-P., Richter-Cook N.J., Merrick W.C.,
RA Hinnebusch A.G., Hershey J.W.B.;
RT "Structure of cDNAs encoding human eukaryotic initiation factor 3 subunits.
RT Possible roles in RNA binding and macromolecular assembly.";
RL J. Biol. Chem. 272:27042-27052(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Placenta, and Stomach;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lung, Muscle, Skin, and Uterus;
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 [8]
RP INTERACTION WITH NORWALK VIRUS VPG PROTEIN (MICROBIAL INFECTION).
RX PubMed=12773399; DOI=10.1093/emboj/cdg251;
RA Daughenbaugh K.F., Fraser C.S., Hershey J.W., Hardy M.E.;
RT "The genome-linked protein VPg of the Norwalk virus binds eIF3, suggesting
RT its role in translation initiation complex recruitment.";
RL EMBO J. 22:2852-2859(2003).
RN [9]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [10]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.m605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [11]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [12]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=18056426; DOI=10.1101/gad.439507;
RA Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
RT "The mechanism of an exceptional case of reinitiation after translation of
RT a long ORF reveals why such events do not generally occur in mammalian mRNA
RT translation.";
RL Genes Dev. 21:3149-3162(2007).
RN [13]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
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-529, AND IDENTIFICATION BY
RP 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 [17]
RP FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE
RP EIF-3 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, AND
RP IDENTIFICATION BY MASS 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, 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 [22]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=25370813; DOI=10.1042/bsr20140078;
RA Yu X., Zheng B., Chai R.;
RT "Lentivirus-mediated knockdown of eukaryotic translation initiation factor
RT 3 subunit D inhibits proliferation of HCT116 colon cancer cells.";
RL Biosci. Rep. 34:E00161-E00161(2014).
RN [23]
RP IDENTIFICATION BY 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 [24]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=25322666; DOI=10.1002/bab.1305;
RA Li H., Zhou F., Wang H., Lin D., Chen G., Zuo X., Sun L., Zhang X.,
RA Yang S.;
RT "Knockdown of EIF3D suppresses proliferation of human melanoma cells
RT through G2/M phase arrest.";
RL Biotechnol. Appl. Biochem. 62:615-620(2015).
RN [25]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=25682860; DOI=10.1111/cbdd.12542;
RA Ren M., Zhou C., Liang H., Wang X., Xu L.;
RT "RNAi-mediated silencing of eif3d alleviates proliferation and migration of
RT glioma U251 and U87MG cells.";
RL Chem. Biol. Drug Des. 86:715-722(2015).
RN [26]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=26617750;
RA Fan Y., Guo Y.;
RT "Knockdown of eIF3D inhibits breast cancer cell proliferation and invasion
RT through suppressing the Wnt/beta-catenin signaling pathway.";
RL Int. J. Clin. Exp. Pathol. 8:10420-10427(2015).
RN [27]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=26008152; DOI=10.1007/s12032-015-0625-8;
RA Lin Z., Xiong L., Lin Q.;
RT "Knockdown of eIF3d inhibits cell proliferation through G2/M phase arrest
RT in non-small cell lung cancer.";
RL Med. Oncol. 32:183-183(2015).
RN [28]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=26036682; DOI=10.1007/s12032-015-0518-x;
RA Gao Y., Teng J., Hong Y., Qu F., Ren J., Li L., Pan X., Chen L., Yin L.,
RA Xu D., Cui X.;
RT "The oncogenic role of EIF3D is associated with increased cell cycle
RT progression and motility in prostate cancer.";
RL Med. Oncol. 32:518-518(2015).
RN [29]
RP FUNCTION, AND IDENTIFICATION IN THE EIF-3 COMPLEX.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [30]
RP POSSIBLE INVOLVEMENT IN CANCER.
RX PubMed=27035563; DOI=10.3892/ijo.2016.3459;
RA Pan X.W., Chen L., Hong Y., Xu D.F., Liu X., Li L., Huang Y., Cui L.M.,
RA Gan S.S., Yang Q.W., Huang H., Qu F.J., Ye J.Q., Wang L.H., Cui X.G.;
RT "EIF3D silencing suppresses renal cell carcinoma tumorigenesis via inducing
RT G2/M arrest through downregulation of Cyclin B1/CDK1 signaling.";
RL Int. J. Oncol. 48:2580-2590(2016).
RN [31]
RP FUNCTION, DOMAIN, RNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF ASP-249; 262-VAL-TYR-263 AND 317-THR--HIS-321.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [32]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
RN [33]
RP VARIANT CYS-310.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC -!- FUNCTION: mRNA cap-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, a complex required for several
CC steps in the initiation of protein synthesis of a specialized
CC repertoire of mRNAs (PubMed:27462815). The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A,
CC eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation
CC complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the
CC 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex
CC is also required for disassembly and recycling of post-termination
CC ribosomal complexes and subsequently prevents premature joining of the
CC 40S and 60S ribosomal subunits prior to initiation (PubMed:18599441,
CC PubMed:25849773). The eIF-3 complex specifically targets and initiates
CC translation of a subset of mRNAs involved in cell proliferation,
CC including cell cycling, differentiation and apoptosis, and uses
CC different modes of RNA stem-loop binding to exert either translational
CC activation or repression (PubMed:25849773). In the eIF-3 complex, EIF3D
CC specifically recognizes and binds the 7-methylguanosine cap of a subset
CC of mRNAs (PubMed:27462815). {ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: (Microbial infection) In case of FCV infection, plays a role
CC in the ribosomal termination-reinitiation event leading to the
CC translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. {ECO:0000255|HAMAP-
CC Rule:MF_03003, ECO:0000269|PubMed:12773399,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Norwalk virus VPg protein
CC (PubMed:12773399). {ECO:0000269|PubMed:12773399}.
CC -!- INTERACTION:
CC O15371; O15084: ANKRD28; NbExp=3; IntAct=EBI-353818, EBI-359567;
CC O15371; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-353818, EBI-724373;
CC O15371; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-353818, EBI-11977221;
CC O15371; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-353818, EBI-10961624;
CC O15371; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-353818, EBI-739624;
CC O15371; Q92997: DVL3; NbExp=3; IntAct=EBI-353818, EBI-739789;
CC O15371; P60228: EIF3E; NbExp=6; IntAct=EBI-353818, EBI-347740;
CC O15371; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-353818, EBI-5916454;
CC O15371; Q9NSC5: HOMER3; NbExp=8; IntAct=EBI-353818, EBI-748420;
CC O15371; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-353818, EBI-10961706;
CC O15371; O75031: HSF2BP; NbExp=3; IntAct=EBI-353818, EBI-7116203;
CC O15371; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-353818, EBI-14069005;
CC O15371; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-353818, EBI-741037;
CC O15371; Q6PF18: MORN3; NbExp=3; IntAct=EBI-353818, EBI-9675802;
CC O15371; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-353818, EBI-11522433;
CC O15371; Q8WV24: PHLDA1; NbExp=2; IntAct=EBI-353818, EBI-738731;
CC O15371; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-353818, EBI-79165;
CC O15371; P62487: POLR2G; NbExp=3; IntAct=EBI-353818, EBI-347928;
CC O15371; Q04864: REL; NbExp=3; IntAct=EBI-353818, EBI-307352;
CC O15371; P21673: SAT1; NbExp=3; IntAct=EBI-353818, EBI-711613;
CC O15371; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-353818, EBI-1105213;
CC O15371; P36406: TRIM23; NbExp=3; IntAct=EBI-353818, EBI-740098;
CC O15371; P14373: TRIM27; NbExp=6; IntAct=EBI-353818, EBI-719493;
CC O15371; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-353818, EBI-527853;
CC O15371; Q9Q2G4: ORF; Xeno; NbExp=5; IntAct=EBI-353818, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O15371-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15371-2; Sequence=VSP_055473;
CC Name=3;
CC IsoId=O15371-3; Sequence=VSP_055474;
CC -!- DOMAIN: The RNA gate region regulates mRNA cap recognition to prevent
CC promiscuous mRNA-binding before assembly of EIF3D into the full
CC eukaryotic translation initiation factor 3 (eIF-3) complex.
CC {ECO:0000305|PubMed:27462815}.
CC -!- MASS SPECTROMETRY: Mass=63972.9; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=64046.7; Mass_error=1.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- DISEASE: Note=Defects in EIF3D are associated with some cancers, such
CC as prostate, breast and colon cancers. Disease susceptibility may be
CC associated with variants affecting the gene represented in this entry.
CC Down-regulation inhibits proliferation of cancers (PubMed:25370813,
CC PubMed:25322666, PubMed:25682860, PubMed:26617750, PubMed:26008152,
CC PubMed:26036682, PubMed:27035563). {ECO:0000269|PubMed:25322666,
CC ECO:0000269|PubMed:25370813, ECO:0000269|PubMed:25682860,
CC ECO:0000269|PubMed:26008152, ECO:0000269|PubMed:26036682,
CC ECO:0000269|PubMed:26617750, ECO:0000269|PubMed:27035563}.
CC -!- SIMILARITY: Belongs to the eIF-3 subunit D family. {ECO:0000255|HAMAP-
CC Rule:MF_03003}.
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DR EMBL; U54558; AAD03466.1; -; mRNA.
DR EMBL; BT007381; AAP36045.1; -; mRNA.
DR EMBL; CR456489; CAG30375.1; -; mRNA.
DR EMBL; AK300199; BAG61970.1; -; mRNA.
DR EMBL; AK301284; BAG62843.1; -; mRNA.
DR EMBL; AK312939; BAG35781.1; -; mRNA.
DR EMBL; AL022313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60109.1; -; Genomic_DNA.
DR EMBL; BC000328; AAH00328.1; -; mRNA.
DR EMBL; BC000469; AAH00469.1; -; mRNA.
DR EMBL; BC014912; AAH14912.1; -; mRNA.
DR EMBL; BC080515; AAH80515.1; -; mRNA.
DR EMBL; BC093100; AAH93100.1; -; mRNA.
DR EMBL; BC093686; AAH93686.1; -; mRNA.
DR EMBL; BC101477; AAI01478.1; -; mRNA.
DR CCDS; CCDS13930.1; -. [O15371-1]
DR RefSeq; NP_003744.1; NM_003753.3. [O15371-1]
DR PDB; 6YBD; EM; 3.30 A; x=1-548.
DR PDB; 6YBS; EM; 3.10 A; x=1-548.
DR PDB; 6ZMW; EM; 3.70 A; x=1-548.
DR PDB; 6ZON; EM; 3.00 A; D=1-548.
DR PDB; 6ZP4; EM; 2.90 A; N=1-548.
DR PDB; 6ZVJ; EM; 3.80 A; D=1-527.
DR PDB; 7A09; EM; 3.50 A; N=1-548.
DR PDBsum; 6YBD; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; O15371; -.
DR SMR; O15371; -.
DR BioGRID; 114213; 187.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; O15371; -.
DR DIP; DIP-32870N; -.
DR IntAct; O15371; 100.
DR MINT; O15371; -.
DR STRING; 9606.ENSP00000216190; -.
DR MoonProt; O15371; -.
DR GlyGen; O15371; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O15371; -.
DR MetOSite; O15371; -.
DR PhosphoSitePlus; O15371; -.
DR SwissPalm; O15371; -.
DR BioMuta; EIF3D; -.
DR EPD; O15371; -.
DR jPOST; O15371; -.
DR MassIVE; O15371; -.
DR MaxQB; O15371; -.
DR PaxDb; O15371; -.
DR PeptideAtlas; O15371; -.
DR PRIDE; O15371; -.
DR ProteomicsDB; 2242; -.
DR ProteomicsDB; 48614; -. [O15371-1]
DR ProteomicsDB; 5301; -.
DR Antibodypedia; 25691; 276 antibodies from 32 providers.
DR DNASU; 8664; -.
DR Ensembl; ENST00000216190.13; ENSP00000216190.8; ENSG00000100353.18. [O15371-1]
DR Ensembl; ENST00000405442.5; ENSP00000385812.1; ENSG00000100353.18. [O15371-1]
DR GeneID; 8664; -.
DR KEGG; hsa:8664; -.
DR MANE-Select; ENST00000216190.13; ENSP00000216190.8; NM_003753.4; NP_003744.1.
DR UCSC; uc003apr.4; human. [O15371-1]
DR CTD; 8664; -.
DR DisGeNET; 8664; -.
DR GeneCards; EIF3D; -.
DR HGNC; HGNC:3278; EIF3D.
DR HPA; ENSG00000100353; Low tissue specificity.
DR MIM; 603915; gene.
DR neXtProt; NX_O15371; -.
DR OpenTargets; ENSG00000100353; -.
DR PharmGKB; PA162384740; -.
DR VEuPathDB; HostDB:ENSG00000100353; -.
DR eggNOG; KOG2479; Eukaryota.
DR GeneTree; ENSGT00390000002667; -.
DR HOGENOM; CLU_024521_2_0_1; -.
DR InParanoid; O15371; -.
DR OMA; PDGWGPC; -.
DR OrthoDB; 1030308at2759; -.
DR PhylomeDB; O15371; -.
DR TreeFam; TF101519; -.
DR PathwayCommons; O15371; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; O15371; -.
DR SIGNOR; O15371; -.
DR BioGRID-ORCS; 8664; 810 hits in 1092 CRISPR screens.
DR ChiTaRS; EIF3D; human.
DR GeneWiki; EIF3D; -.
DR GenomeRNAi; 8664; -.
DR Pharos; O15371; Tbio.
DR PRO; PR:O15371; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O15371; protein.
DR Bgee; ENSG00000100353; Expressed in body of pancreas and 211 other tissues.
DR ExpressionAtlas; O15371; baseline and differential.
DR Genevisible; O15371; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0071541; C:eukaryotic translation initiation factor 3 complex, eIF3m; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0098808; F:mRNA cap binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0002191; P:cap-dependent translational initiation; IDA:UniProtKB.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:1902416; P:positive regulation of mRNA binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0045727; P:positive regulation of translation; IPI:ParkinsonsUK-UCL.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
DR HAMAP; MF_03003; eIF3d; 1.
DR InterPro; IPR007783; eIF3d.
DR PANTHER; PTHR12399; PTHR12399; 1.
DR Pfam; PF05091; eIF-3_zeta; 1.
DR PIRSF; PIRSF016281; EIF-3_zeta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Host-virus interaction; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..548
FT /note="Eukaryotic translation initiation factor 3 subunit
FT D"
FT /id="PRO_0000123520"
FT REGION 285..299
FT /note="RNA gate"
FT /evidence="ECO:0000250|UniProtKB:K7IM66"
FT REGION 523..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..548
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O70194"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT VAR_SEQ 54..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055473"
FT VAR_SEQ 137..151
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055474"
FT VARIANT 310
FT /note="R -> C (in dbSNP:rs745920273)"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074184"
FT MUTAGEN 249
FT /note="D->Q: Reduced binding to JUN mRNA; when associated
FT with 262-I-A-263."
FT /evidence="ECO:0000269|PubMed:27462815"
FT MUTAGEN 262..263
FT /note="VY->IA: Reduced binding to JUN mRNA; when associated
FT with Q-249."
FT /evidence="ECO:0000269|PubMed:27462815"
FT MUTAGEN 317..321
FT /note="TYINH->EYENA: Reduced binding to JUN mRNA."
FT /evidence="ECO:0000269|PubMed:27462815"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:6YBD"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 237..241
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 309..322
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 357..361
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 371..374
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 401..405
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 409..412
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 430..441
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 445..456
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 463..471
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 484..497
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 503..507
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:6YBS"
SQ SEQUENCE 548 AA; 63973 MW; 7FE0448EC3BE1711 CRC64;
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS
SQFGGGSQYA YFHEEDESSF QLVDTARTQK TAYQRNRMRF AQRNLRRDKD RRNMLQFNLQ
ILPKSAKQKE RERIRLQKKF QKQFGVRQKW DQKSQKPRDS SVEVRSDWEV KEEMDFPQLM
KMRYLEVSEP QDIECCGALE YYDKAFDRIT TRSEKPLRSI KRIFHTVTTT DDPVIRKLAK
TQGNVFATDA ILATLMSCTR SVYSWDIVVQ RVGSKLFFDK RDNSDFDLLT VSETANEPPQ
DEGNSFNSPR NLAMEATYIN HNFSQQCLRM GKERYNFPNP NPFVEDDMDK NEIASVAYRY
RRWKLGDDID LIVRCEHDGV MTGANGEVSF INIKTLNEWD SRHCNGVDWR QKLDSQRGAV
IATELKNNSY KLARWTCCAL LAGSEYLKLG YVSRYHVKDS SRHVILGTQQ FKPNEFASQI
NLSVENAWGI LRCVIDICMK LEEGKYLILK DPNKQVIRVY SLPDGTFSSD EDEEEEEEEE
EEEEEEET
