EIF3I_HUMAN
ID EIF3I_HUMAN Reviewed; 325 AA.
AC Q13347;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit I {ECO:0000255|HAMAP-Rule:MF_03008};
DE Short=eIF3i {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 2 {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=TGF-beta receptor-interacting protein 1;
DE Short=TRIP-1;
DE AltName: Full=eIF-3-beta {ECO:0000255|HAMAP-Rule:MF_03008};
DE AltName: Full=eIF3 p36 {ECO:0000255|HAMAP-Rule:MF_03008};
GN Name=EIF3I {ECO:0000255|HAMAP-Rule:MF_03008};
GN Synonyms=EIF3S2 {ECO:0000255|HAMAP-Rule:MF_03008}, TRIP1;
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].
RC TISSUE=Brain;
RX PubMed=8995409; DOI=10.1074/jbc.272.28.17668;
RA Asano K., Kinzy T.G., Merrick W.C., Hershey J.W.B.;
RT "Conservation and diversity of eukaryotic translation initiation factor
RT eIF3.";
RL J. Biol. Chem. 272:1101-1109(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7566156; DOI=10.1038/377548a0;
RA Chen R.H., Miettinen P.J., Maruka E.M., Choy L., Derynck R.;
RT "A WD-domain protein that is associated with and phosphorylated by the type
RT II TGF-beta receptor.";
RL Nature 377:548-552(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Muscle;
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 [4]
RP PROTEIN SEQUENCE OF 269-280 AND 283-298, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP INTERACTION WITH EIF3B.
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 [6]
RP INTERACTION WITH EIF3B.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
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 [9]
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 [10]
RP FUNCTION, AND 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 [11]
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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-264, 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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219, AND IDENTIFICATION BY
RP 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 [16]
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 [17]
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 [18]
RP FUNCTION.
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 [19]
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).
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:17581632, PubMed:25849773,
CC PubMed:27462815). The eIF-3 complex associates with the 40S ribosome
CC and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-
CC tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The
CC eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning
CC of the mRNA for AUG recognition. The eIF-3 complex is also required for
CC disassembly and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S ribosomal
CC subunits prior to initiation (PubMed:17581632). The eIF-3 complex
CC specifically targets and initiates translation of a subset of mRNAs
CC involved in cell proliferation, including cell cycling, differentiation
CC and apoptosis, and uses different modes of RNA stem-loop binding to
CC exert either translational activation or repression (PubMed:25849773).
CC {ECO:0000255|HAMAP-Rule:MF_03008, ECO:0000269|PubMed:17581632,
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_03008, ECO:0000269|PubMed:14519125,
CC ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16766523,
CC ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:25849773}.
CC -!- INTERACTION:
CC Q13347; P55212: CASP6; NbExp=3; IntAct=EBI-354047, EBI-718729;
CC Q13347; Q6UXB4: CLEC4G; NbExp=3; IntAct=EBI-354047, EBI-2114729;
CC Q13347; P55884: EIF3B; NbExp=7; IntAct=EBI-354047, EBI-366696;
CC Q13347; O75821: EIF3G; NbExp=3; IntAct=EBI-354047, EBI-366632;
CC Q13347; P42858: HTT; NbExp=13; IntAct=EBI-354047, EBI-466029;
CC Q13347; P13473-2: LAMP2; NbExp=3; IntAct=EBI-354047, EBI-21591415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03008}.
CC -!- PTM: Phosphorylated by TGF-beta type II receptor. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
CC -!- MASS SPECTROMETRY: Mass=36501.9; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=36503.2; Mass_error=0.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family. {ECO:0000255|HAMAP-
CC Rule:MF_03008}.
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DR EMBL; U39067; AAC97144.1; -; mRNA.
DR EMBL; U36764; AAC50224.1; -; mRNA.
DR EMBL; BC000413; AAH00413.1; -; mRNA.
DR EMBL; BC003140; AAH03140.1; -; mRNA.
DR CCDS; CCDS357.1; -.
DR PIR; S60335; S60335.
DR RefSeq; NP_003748.1; NM_003757.3.
DR PDB; 6YBT; EM; 6.00 A; 2=1-325.
DR PDB; 6ZMW; EM; 3.70 A; 2=1-325.
DR PDB; 6ZON; EM; 3.00 A; I=1-325.
DR PDB; 6ZP4; EM; 2.90 A; I=1-325.
DR PDB; 6ZVJ; EM; 3.80 A; I=1-316.
DR PDB; 7A09; EM; 3.50 A; I=1-325.
DR PDBsum; 6YBT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 7A09; -.
DR AlphaFoldDB; Q13347; -.
DR SMR; Q13347; -.
DR BioGRID; 114217; 176.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; Q13347; -.
DR DIP; DIP-31116N; -.
DR IntAct; Q13347; 86.
DR MINT; Q13347; -.
DR STRING; 9606.ENSP00000362688; -.
DR ChEMBL; CHEMBL4295814; -.
DR GlyGen; Q13347; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13347; -.
DR MetOSite; Q13347; -.
DR PhosphoSitePlus; Q13347; -.
DR SwissPalm; Q13347; -.
DR BioMuta; EIF3I; -.
DR DMDM; 2494895; -.
DR DOSAC-COBS-2DPAGE; Q13347; -.
DR OGP; Q13347; -.
DR EPD; Q13347; -.
DR jPOST; Q13347; -.
DR MassIVE; Q13347; -.
DR PaxDb; Q13347; -.
DR PeptideAtlas; Q13347; -.
DR PRIDE; Q13347; -.
DR ProteomicsDB; 59333; -.
DR Antibodypedia; 31260; 177 antibodies from 27 providers.
DR DNASU; 8668; -.
DR Ensembl; ENST00000676801.1; ENSP00000503348.1; ENSG00000084623.12.
DR Ensembl; ENST00000677202.1; ENSP00000504034.1; ENSG00000084623.12.
DR Ensembl; ENST00000677701.1; ENSP00000503539.1; ENSG00000084623.12.
DR Ensembl; ENST00000677711.1; ENSP00000504061.1; ENSG00000084623.12.
DR Ensembl; ENST00000677760.1; ENSP00000502867.1; ENSG00000084623.12.
DR GeneID; 8668; -.
DR KEGG; hsa:8668; -.
DR MANE-Select; ENST00000677711.2; ENSP00000504061.1; NM_003757.4; NP_003748.1.
DR CTD; 8668; -.
DR DisGeNET; 8668; -.
DR GeneCards; EIF3I; -.
DR HGNC; HGNC:3272; EIF3I.
DR HPA; ENSG00000084623; Low tissue specificity.
DR MIM; 603911; gene.
DR neXtProt; NX_Q13347; -.
DR OpenTargets; ENSG00000084623; -.
DR PharmGKB; PA162384875; -.
DR VEuPathDB; HostDB:ENSG00000084623; -.
DR eggNOG; KOG0643; Eukaryota.
DR GeneTree; ENSGT00940000161371; -.
DR HOGENOM; CLU_043845_0_0_1; -.
DR InParanoid; Q13347; -.
DR OMA; VWFSHNG; -.
DR OrthoDB; 866359at2759; -.
DR PhylomeDB; Q13347; -.
DR TreeFam; TF101515; -.
DR PathwayCommons; Q13347; -.
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; Q13347; -.
DR SIGNOR; Q13347; -.
DR BioGRID-ORCS; 8668; 805 hits in 1057 CRISPR screens.
DR ChiTaRS; EIF3I; human.
DR GeneWiki; EIF3I; -.
DR GenomeRNAi; 8668; -.
DR Pharos; Q13347; Tbio.
DR PRO; PR:Q13347; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13347; protein.
DR Bgee; ENSG00000084623; Expressed in islet of Langerhans and 205 other tissues.
DR ExpressionAtlas; Q13347; baseline and differential.
DR Genevisible; Q13347; 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; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR HAMAP; MF_03008; eIF3i; 1.
DR InterPro; IPR027525; eIF3i.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Isopeptide bond; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..325
FT /note="Eukaryotic translation initiation factor 3 subunit
FT I"
FT /id="PRO_0000051036"
FT REPEAT 1..39
FT /note="WD 1"
FT REPEAT 43..81
FT /note="WD 2"
FT REPEAT 87..127
FT /note="WD 3"
FT REPEAT 135..175
FT /note="WD 4"
FT REPEAT 180..217
FT /note="WD 5"
FT REPEAT 221..267
FT /note="WD 6"
FT REPEAT 275..316
FT /note="WD 7"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 308
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT CROSSLNK 282
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
SQ SEQUENCE 325 AA; 36502 MW; 02797BB72A752A96 CRC64;
MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
FVSFFDLRDP SQIDNNEPYM KIPCNDSKIT SAVWGPLGEC IIAGHESGEL NQYSAKSGEV
LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
SSGGEDGYVR IHYFDPQYFE FEFEA
