EIF3J_HUMAN
ID EIF3J_HUMAN Reviewed; 258 AA.
AC O75822; B4DUI3; F5H425; Q9BUD2; Q9H8Q2; Q9UI65;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit J {ECO:0000255|HAMAP-Rule:MF_03009};
DE Short=eIF3j {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 1 {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=eIF-3-alpha {ECO:0000255|HAMAP-Rule:MF_03009};
DE AltName: Full=eIF3 p35 {ECO:0000255|HAMAP-Rule:MF_03009};
GN Name=EIF3J {ECO:0000255|HAMAP-Rule:MF_03009};
GN Synonyms=EIF3S1 {ECO:0000255|HAMAP-Rule:MF_03009}; ORFNames=PRO0391;
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), PARTIAL PROTEIN SEQUENCE, AND
RP INTERACTION WITH EIF3A.
RX PubMed=9822659; DOI=10.1074/jbc.273.48.31901;
RA Block K.L., Vornlocher H.-P., Hershey J.W.B.;
RT "Characterization of cDNAs encoding the p44 and p35 subunits of human
RT translation initiation factor eIF3.";
RL J. Biol. Chem. 273:31901-31908(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP THR-141.
RC TISSUE=Ovarian carcinoma, and Skeletal muscle;
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 MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
RP PROTEIN SEQUENCE OF 2-27; 99-119; 123-133 AND 199-210, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-258 (ISOFORM 1).
RC TISSUE=Fetal liver;
RA Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 50 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH EIF3K.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [9]
RP INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
RX PubMed=14688252; DOI=10.1074/jbc.m312745200;
RA Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
RA Hershey J.W.B.;
RT "The j-subunit of human translation initiation factor eIF3 is required for
RT the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits
RT in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [10]
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 [11]
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, 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 [14]
RP INTERACTION WITH EIF3B AND THE 40S RIBOSOMAL SUBUNIT.
RX PubMed=17190833; DOI=10.1074/jbc.m610860200;
RA ElAntak L., Tzakos A.G., Locker N., Lukavsky P.J.;
RT "Structure of eIF3b RNA recognition motif and its interaction with eIF3j:
RT structural insights into the recruitment of eIF3b to the 40 S ribosomal
RT subunit.";
RL J. Biol. Chem. 282:8165-8174(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, 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 [16]
RP INTERACTION WITH THE 40S RIBOSOMAL SUBUNIT.
RX PubMed=17588516; DOI=10.1016/j.molcel.2007.05.019;
RA Fraser C.S., Berry K.E., Hershey J.W.B., Doudna J.A.;
RT "eIF3j is located in the decoding center of the human 40S ribosomal
RT subunit.";
RL Mol. Cell 26:811-819(2007).
RN [17]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT
RP SER-11; SER-13; SER-20 AND THR-109, 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP 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 [20]
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 [21]
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=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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-254, AND IDENTIFICATION BY
RP 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 [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11; SER-13; THR-109 AND SER-127, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [24]
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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-11; SER-13 AND THR-109, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [26]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [27]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-109 AND SER-127, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [29]
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 [30]
RP FUNCTION OF 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 [31]
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 [32]
RP FUNCTION OF THE EIF-3 COMPLEX.
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 [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
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 [35]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 141-220.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human translation initiation factor 3, subunit 1
RT alpha.";
RL Submitted (JAN-2008) to the PDB data bank.
CC -!- FUNCTION: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is required for several steps in the initiation
CC of protein synthesis (PubMed:25849773, PubMed:27462815). The eIF-3
CC complex associates with the 40S ribosome and facilitates the
CC recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to
CC form the 43S pre-initiation complex (43S PIC). The eIF-3 complex
CC stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for
CC AUG recognition. The eIF-3 complex is also required for disassembly and
CC recycling of post-termination ribosomal complexes and subsequently
CC prevents premature joining of the 40S and 60S ribosomal subunits prior
CC to initiation. 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).
CC {ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
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_03009, ECO:0000269|PubMed:14519125,
CC ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16766523,
CC ECO:0000269|PubMed:17190833, ECO:0000269|PubMed:17322308,
CC ECO:0000269|PubMed:17588516, ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:9822659}.
CC -!- INTERACTION:
CC O75822; P61221: ABCE1; NbExp=3; IntAct=EBI-366647, EBI-2510446;
CC O75822; P68400: CSNK2A1; NbExp=3; IntAct=EBI-366647, EBI-347804;
CC O75822; P55884: EIF3B; NbExp=5; IntAct=EBI-366647, EBI-366696;
CC O75822; O75822: EIF3J; NbExp=3; IntAct=EBI-366647, EBI-366647;
CC O75822; Q04637: EIF4G1; NbExp=2; IntAct=EBI-366647, EBI-73711;
CC O75822; Q16236: NFE2L2; NbExp=5; IntAct=EBI-366647, EBI-2007911;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03009}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75822-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75822-2; Sequence=VSP_054593;
CC Name=3;
CC IsoId=O75822-3; Sequence=VSP_054776;
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03009,
CC ECO:0000269|PubMed:17322308}.
CC -!- MASS SPECTROMETRY: Mass=29293.2; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=28974.2; Mass_error=0.3; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit J family. {ECO:0000255|HAMAP-
CC Rule:MF_03009}.
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DR EMBL; U97670; AAC78729.1; -; mRNA.
DR EMBL; AK023388; BAB14555.1; -; mRNA.
DR EMBL; AK300659; BAG62345.1; -; mRNA.
DR EMBL; CR606839; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC009996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002719; AAH02719.1; -; mRNA.
DR EMBL; AF090923; AAF24039.1; -; mRNA.
DR CCDS; CCDS10111.1; -. [O75822-1]
DR CCDS; CCDS61612.1; -. [O75822-2]
DR CCDS; CCDS61613.1; -. [O75822-3]
DR RefSeq; NP_001271264.1; NM_001284335.1. [O75822-2]
DR RefSeq; NP_001271265.1; NM_001284336.1. [O75822-3]
DR RefSeq; NP_003749.2; NM_003758.3. [O75822-1]
DR PDB; 2KRB; NMR; -; B=45-55.
DR PDB; 3BPJ; X-ray; 1.85 A; A/B/C/D=141-220.
DR PDB; 6YBW; EM; 3.10 A; z=1-258.
DR PDB; 6ZMW; EM; 3.70 A; z=1-258.
DR PDB; 6ZVJ; EM; 3.80 A; G/J=1-258.
DR PDBsum; 2KRB; -.
DR PDBsum; 3BPJ; -.
DR PDBsum; 6YBW; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZVJ; -.
DR AlphaFoldDB; O75822; -.
DR SMR; O75822; -.
DR BioGRID; 114218; 86.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; O75822; -.
DR DIP; DIP-31117N; -.
DR IntAct; O75822; 46.
DR MINT; O75822; -.
DR STRING; 9606.ENSP00000261868; -.
DR GlyGen; O75822; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75822; -.
DR MetOSite; O75822; -.
DR PhosphoSitePlus; O75822; -.
DR SwissPalm; O75822; -.
DR BioMuta; EIF3J; -.
DR EPD; O75822; -.
DR jPOST; O75822; -.
DR MassIVE; O75822; -.
DR MaxQB; O75822; -.
DR PaxDb; O75822; -.
DR PeptideAtlas; O75822; -.
DR PRIDE; O75822; -.
DR ProteomicsDB; 26447; -.
DR ProteomicsDB; 50215; -. [O75822-1]
DR ProteomicsDB; 5189; -.
DR Antibodypedia; 24232; 180 antibodies from 28 providers.
DR DNASU; 8669; -.
DR Ensembl; ENST00000261868.10; ENSP00000261868.5; ENSG00000104131.13. [O75822-1]
DR Ensembl; ENST00000424492.7; ENSP00000414548.3; ENSG00000104131.13. [O75822-3]
DR Ensembl; ENST00000535391.5; ENSP00000440221.1; ENSG00000104131.13. [O75822-2]
DR GeneID; 8669; -.
DR KEGG; hsa:8669; -.
DR MANE-Select; ENST00000261868.10; ENSP00000261868.5; NM_003758.4; NP_003749.2.
DR UCSC; uc001ztv.4; human. [O75822-1]
DR CTD; 8669; -.
DR DisGeNET; 8669; -.
DR GeneCards; EIF3J; -.
DR HGNC; HGNC:3270; EIF3J.
DR HPA; ENSG00000104131; Tissue enhanced (skeletal).
DR MIM; 603910; gene.
DR neXtProt; NX_O75822; -.
DR OpenTargets; ENSG00000104131; -.
DR PharmGKB; PA162384902; -.
DR VEuPathDB; HostDB:ENSG00000104131; -.
DR eggNOG; KOG4813; Eukaryota.
DR GeneTree; ENSGT00390000018400; -.
DR HOGENOM; CLU_085806_2_1_1; -.
DR InParanoid; O75822; -.
DR OMA; HYGLFLE; -.
DR PhylomeDB; O75822; -.
DR TreeFam; TF101514; -.
DR PathwayCommons; O75822; -.
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; O75822; -.
DR SIGNOR; O75822; -.
DR BioGRID-ORCS; 8669; 455 hits in 1078 CRISPR screens.
DR ChiTaRS; EIF3J; human.
DR EvolutionaryTrace; O75822; -.
DR GeneWiki; EIF3J; -.
DR GenomeRNAi; 8669; -.
DR Pharos; O75822; Tbio.
DR PRO; PR:O75822; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O75822; protein.
DR Bgee; ENSG00000104131; Expressed in gastrocnemius and 203 other tissues.
DR ExpressionAtlas; O75822; baseline and differential.
DR Genevisible; O75822; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IC:UniProtKB.
DR Gene3D; 1.10.246.60; -; 1.
DR HAMAP; MF_03009; eIF3j; 1.
DR InterPro; IPR023194; eIF3-like_dom_sf.
DR InterPro; IPR013906; eIF3j.
DR PANTHER; PTHR21681; PTHR21681; 1.
DR Pfam; PF08597; eIF3_subunit; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Initiation factor; Isopeptide bond;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..258
FT /note="Eukaryotic translation initiation factor 3 subunit
FT J"
FT /id="PRO_0000123506"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..69
FT /note="Sufficient for interaction with EIF3B"
FT REGION 217..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..258
FT /note="Promotes stable association with the 40S ribosome"
FT COILED 70..135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009"
FT COMPBIAS 39..61
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308, ECO:0000269|Ref.6,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308"
FT MOD_RES 109
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03009,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 50..98
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_054776"
FT VAR_SEQ 137..191
FT /note="GVNNAVYGIDAMNPSSRDDFTEFGKLLKDKITQYEKSLYYASFLEVLVRDVC
FT ISL -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054593"
FT VARIANT 141
FT /note="A -> T (in dbSNP:rs2303578)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_034007"
FT CONFLICT 40
FT /note="E -> G (in Ref. 1; AAC78729)"
FT /evidence="ECO:0000305"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 76..95
FT /evidence="ECO:0007829|PDB:6YBW"
FT HELIX 115..134
FT /evidence="ECO:0007829|PDB:6YBW"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:3BPJ"
FT HELIX 153..167
FT /evidence="ECO:0007829|PDB:3BPJ"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3BPJ"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:3BPJ"
FT HELIX 193..212
FT /evidence="ECO:0007829|PDB:3BPJ"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6YBW"
SQ SEQUENCE 258 AA; 29062 MW; 83624235424445AA CRC64;
MAAAAAAAGD SDSWDADAFS VEDPVRKVGG GGTAGGDRWE GEDEDEDVKD NWDDDDDEKK
EEAEVKPEVK ISEKKKIAEK IKEKERQQKK RQEEIKKRLE EPEEPKVLTP EEQLADKLRL
KKLQEESDLE LAKETFGVNN AVYGIDAMNP SSRDDFTEFG KLLKDKITQY EKSLYYASFL
EVLVRDVCIS LEIDDLKKIT NSLTVLCSEK QKQEKQSKAK KKKKGVVPGG GLKATMKDDL
ADYGGYDGGY VQDYEDFM
