Full text data of EIF3I
EIF3I
(EIF3S2, TRIP1)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 3 subunit I; eIF3i (Eukaryotic translation initiation factor 3 subunit 2; TGF-beta receptor-interacting protein 1; TRIP-1; eIF-3-beta; eIF3 p36)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 3 subunit I; eIF3i (Eukaryotic translation initiation factor 3 subunit 2; TGF-beta receptor-interacting protein 1; TRIP-1; eIF-3-beta; eIF3 p36)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q13347
ID EIF3I_HUMAN Reviewed; 325 AA.
AC Q13347;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit I;
DE Short=eIF3i;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 2;
DE AltName: Full=TGF-beta receptor-interacting protein 1;
DE Short=TRIP-1;
DE AltName: Full=eIF-3-beta;
DE AltName: Full=eIF3 p36;
GN Name=EIF3I; Synonyms=EIF3S2, TRIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT factor 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
RT type 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 269-280 AND 283-298, AND MASS 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
RT for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
RT subunits in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASS
RP SPECTROMETRY.
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
RT 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.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and 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 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
RP COMPLEX, 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.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 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
RP 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
RT interaction 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 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
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3.
CC -!- INTERACTION:
CC Q6UXB4:CLEC4G; NbExp=3; IntAct=EBI-354047, EBI-2114729;
CC P55884:EIF3B; NbExp=4; IntAct=EBI-354047, EBI-366696;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- PTM: Phosphorylated by TGF-beta type II receptor.
CC -!- MASS SPECTROMETRY: Mass=36501.9; Method=Unknown; Range=1-325;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=36503.2; Mass_error=0.4; Method=MALDI;
CC Range=1-325; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family.
CC -!- SIMILARITY: Contains 5 WD repeats.
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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 PIR; S60335; S60335.
DR RefSeq; NP_003748.1; NM_003757.2.
DR UniGene; Hs.530096; -.
DR ProteinModelPortal; Q13347; -.
DR SMR; Q13347; 1-324.
DR DIP; DIP-31116N; -.
DR IntAct; Q13347; 22.
DR MINT; MINT-5004513; -.
DR STRING; 9606.ENSP00000362688; -.
DR PhosphoSite; Q13347; -.
DR DMDM; 2494895; -.
DR DOSAC-COBS-2DPAGE; Q13347; -.
DR OGP; Q13347; -.
DR PaxDb; Q13347; -.
DR PeptideAtlas; Q13347; -.
DR PRIDE; Q13347; -.
DR DNASU; 8668; -.
DR Ensembl; ENST00000373586; ENSP00000362688; ENSG00000084623.
DR GeneID; 8668; -.
DR KEGG; hsa:8668; -.
DR UCSC; uc001bur.4; human.
DR CTD; 8668; -.
DR GeneCards; GC01P032687; -.
DR HGNC; HGNC:3272; EIF3I.
DR HPA; HPA029939; -.
DR HPA; HPA029940; -.
DR MIM; 603911; gene.
DR neXtProt; NX_Q13347; -.
DR PharmGKB; PA162384875; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000231322; -.
DR HOVERGEN; HBG000900; -.
DR InParanoid; Q13347; -.
DR KO; K03246; -.
DR OMA; IFEEEIG; -.
DR PhylomeDB; Q13347; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; Q13347; -.
DR ChiTaRS; EIF3I; human.
DR GeneWiki; EIF3I; -.
DR GenomeRNAi; 8668; -.
DR NextBio; 32515; -.
DR PRO; PR:Q13347; -.
DR ArrayExpress; Q13347; -.
DR Bgee; Q13347; -.
DR CleanEx; HS_EIF3I; -.
DR Genevestigator; Q13347; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 4.
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 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; Ubl conjugation;
KW WD repeat.
FT CHAIN 1 325 Eukaryotic translation initiation factor
FT 3 subunit I.
FT /FTId=PRO_0000051036.
FT REPEAT 8 47 WD 1.
FT REPEAT 50 91 WD 2.
FT REPEAT 144 183 WD 3.
FT REPEAT 186 225 WD 4.
FT REPEAT 283 324 WD 5.
FT MOD_RES 264 264 N6-acetyllysine.
FT MOD_RES 308 308 Phosphotyrosine.
FT CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with 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
//
ID EIF3I_HUMAN Reviewed; 325 AA.
AC Q13347;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 138.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit I;
DE Short=eIF3i;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 2;
DE AltName: Full=TGF-beta receptor-interacting protein 1;
DE Short=TRIP-1;
DE AltName: Full=eIF-3-beta;
DE AltName: Full=eIF3 p36;
GN Name=EIF3I; Synonyms=EIF3S2, TRIP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT factor 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
RT type 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 269-280 AND 283-298, AND MASS 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
RT for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
RT subunits in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASS
RP SPECTROMETRY.
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
RT 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.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and 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 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
RP COMPLEX, 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.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 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
RP 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
RT interaction 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 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
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3.
CC -!- INTERACTION:
CC Q6UXB4:CLEC4G; NbExp=3; IntAct=EBI-354047, EBI-2114729;
CC P55884:EIF3B; NbExp=4; IntAct=EBI-354047, EBI-366696;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- PTM: Phosphorylated by TGF-beta type II receptor.
CC -!- MASS SPECTROMETRY: Mass=36501.9; Method=Unknown; Range=1-325;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=36503.2; Mass_error=0.4; Method=MALDI;
CC Range=1-325; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit I family.
CC -!- SIMILARITY: Contains 5 WD repeats.
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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 PIR; S60335; S60335.
DR RefSeq; NP_003748.1; NM_003757.2.
DR UniGene; Hs.530096; -.
DR ProteinModelPortal; Q13347; -.
DR SMR; Q13347; 1-324.
DR DIP; DIP-31116N; -.
DR IntAct; Q13347; 22.
DR MINT; MINT-5004513; -.
DR STRING; 9606.ENSP00000362688; -.
DR PhosphoSite; Q13347; -.
DR DMDM; 2494895; -.
DR DOSAC-COBS-2DPAGE; Q13347; -.
DR OGP; Q13347; -.
DR PaxDb; Q13347; -.
DR PeptideAtlas; Q13347; -.
DR PRIDE; Q13347; -.
DR DNASU; 8668; -.
DR Ensembl; ENST00000373586; ENSP00000362688; ENSG00000084623.
DR GeneID; 8668; -.
DR KEGG; hsa:8668; -.
DR UCSC; uc001bur.4; human.
DR CTD; 8668; -.
DR GeneCards; GC01P032687; -.
DR HGNC; HGNC:3272; EIF3I.
DR HPA; HPA029939; -.
DR HPA; HPA029940; -.
DR MIM; 603911; gene.
DR neXtProt; NX_Q13347; -.
DR PharmGKB; PA162384875; -.
DR eggNOG; COG2319; -.
DR HOGENOM; HOG000231322; -.
DR HOVERGEN; HBG000900; -.
DR InParanoid; Q13347; -.
DR KO; K03246; -.
DR OMA; IFEEEIG; -.
DR PhylomeDB; Q13347; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR SignaLink; Q13347; -.
DR ChiTaRS; EIF3I; human.
DR GeneWiki; EIF3I; -.
DR GenomeRNAi; 8668; -.
DR NextBio; 32515; -.
DR PRO; PR:Q13347; -.
DR ArrayExpress; Q13347; -.
DR Bgee; Q13347; -.
DR CleanEx; HS_EIF3I; -.
DR Genevestigator; Q13347; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
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.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF00400; WD40; 4.
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 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Isopeptide bond; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Repeat; Ubl conjugation;
KW WD repeat.
FT CHAIN 1 325 Eukaryotic translation initiation factor
FT 3 subunit I.
FT /FTId=PRO_0000051036.
FT REPEAT 8 47 WD 1.
FT REPEAT 50 91 WD 2.
FT REPEAT 144 183 WD 3.
FT REPEAT 186 225 WD 4.
FT REPEAT 283 324 WD 5.
FT MOD_RES 264 264 N6-acetyllysine.
FT MOD_RES 308 308 Phosphotyrosine.
FT CROSSLNK 282 282 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with 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
//
MIM
603911
*RECORD*
*FIELD* NO
603911
*FIELD* TI
*603911 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT I; EIF3I
;;TGF-BETA RECEPTOR-INTERACTING PROTEIN 1; TRIP1;;
read moreEIF3-p36;;
EIF3-BETA;;
EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 2, FORMERLY; EIF3S2,
FORMERLY
*FIELD* TX
Eukaryotic initiation factor 3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits in mammals. See p66
(EIF3S7; 603915). In S. cerevisiae, the p39 subunit of eIF3 contains WD
repeats, which are thought to mediate protein-protein interactions. The
p39 protein appears to be essential for maintaining the integrity of the
yeast eIF3 complex. The mammalian eIF3-p36 subunit is homologous to
yeast p39. By searching an EST database for sequences corresponding to
the partial protein sequence of rabbit p36, Asano et al. (1997)
identified a cDNA encoding human p36. The predicted 325-amino acid human
protein shares 46% identity with yeast p39. Like p39, p36 contains 5 WD
repeats and 2 less conserved WD repeat elements. The authors found that
the p116 (603917), p110 (603916), and p36 subunits localize on 40S
ribosomes in cells active in translation and coimmunoprecipitate with
p170 (602039), indicating that these proteins are integral components of
eIF3. Northern blot analysis revealed that p36 is expressed as a 1.6-kb
mRNA in HeLa cells. Galli-Stauber et al. (1998) reported that the p36
gene contains 11 exons and spans 9 kb.
Transforming growth factor-beta (TGF-beta; see 190180) signaling is
mediated by the type I (RI; 190181) and type II (RII; 190182) TGF-beta
serine/threonine kinase receptors, which are able to form a heteromeric
complex. Chen et al. (1995) identified eIF3-p36 as TRIP1 (TGF-beta
receptor-interacting protein-1), a protein that specifically associates
with RII. The association with RII requires RII's kinase activity,
suggesting that receptor autophosphorylation creates a binding site for
TRIP1. Since TRIP1 is phosphorylated on serine and threonine by the
receptor kinase, the authors proposed that TRIP1 plays a role in
TGF-beta signaling. Northern blot analysis indicated that TRIP1 was
expressed as a 1.6-kb mRNA in all human fetal tissues tested. In mouse
embryos, the immunolocalization patterns of TRIP1 and RII were well
correlated, further supporting a functional correlation between both
proteins.
By fluorescence in situ hybridization, Galli-Stauber et al. (1998)
mapped the TRIP1 gene to 1p34.1 and a TRIP1 pseudogene to 7q32.
*FIELD* RF
1. Asano, K.; Kinzy, T. G.; Merrick, W. C.; Hershey, J. W. B.: Conservation
and diversity of eukaryotic translation initiation factor eIF3. J.
Biol. Chem. 272: 1101-1109, 1997.
2. Chen, R.-H.; Miettinen, P. J.; Maruoka, E. M.; Choy, L.; Derynck,
R.: A WD-domain protein that is associated with and phosphorylated
by the type II TGF-beta receptor. Nature 377: 548-552, 1995.
3. Galli-Stauber, C.; Raho, G.; Rossi, D.; Corona, D. F. V.; Pirola,
B.; Bonaglia, M. C.; Zuffardi, O.; Sorrentino, V.: Genomic structure
and chromosomal location of the human TGF-beta-receptor interacting
protein-1 (TRIP-1) gene to 1p34.1. FEBS Lett. 426: 279-282, 1998.
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 10/02/2007
cwells: 9/17/2003
alopez: 6/17/1999
*RECORD*
*FIELD* NO
603911
*FIELD* TI
*603911 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT I; EIF3I
;;TGF-BETA RECEPTOR-INTERACTING PROTEIN 1; TRIP1;;
read moreEIF3-p36;;
EIF3-BETA;;
EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 2, FORMERLY; EIF3S2,
FORMERLY
*FIELD* TX
Eukaryotic initiation factor 3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits in mammals. See p66
(EIF3S7; 603915). In S. cerevisiae, the p39 subunit of eIF3 contains WD
repeats, which are thought to mediate protein-protein interactions. The
p39 protein appears to be essential for maintaining the integrity of the
yeast eIF3 complex. The mammalian eIF3-p36 subunit is homologous to
yeast p39. By searching an EST database for sequences corresponding to
the partial protein sequence of rabbit p36, Asano et al. (1997)
identified a cDNA encoding human p36. The predicted 325-amino acid human
protein shares 46% identity with yeast p39. Like p39, p36 contains 5 WD
repeats and 2 less conserved WD repeat elements. The authors found that
the p116 (603917), p110 (603916), and p36 subunits localize on 40S
ribosomes in cells active in translation and coimmunoprecipitate with
p170 (602039), indicating that these proteins are integral components of
eIF3. Northern blot analysis revealed that p36 is expressed as a 1.6-kb
mRNA in HeLa cells. Galli-Stauber et al. (1998) reported that the p36
gene contains 11 exons and spans 9 kb.
Transforming growth factor-beta (TGF-beta; see 190180) signaling is
mediated by the type I (RI; 190181) and type II (RII; 190182) TGF-beta
serine/threonine kinase receptors, which are able to form a heteromeric
complex. Chen et al. (1995) identified eIF3-p36 as TRIP1 (TGF-beta
receptor-interacting protein-1), a protein that specifically associates
with RII. The association with RII requires RII's kinase activity,
suggesting that receptor autophosphorylation creates a binding site for
TRIP1. Since TRIP1 is phosphorylated on serine and threonine by the
receptor kinase, the authors proposed that TRIP1 plays a role in
TGF-beta signaling. Northern blot analysis indicated that TRIP1 was
expressed as a 1.6-kb mRNA in all human fetal tissues tested. In mouse
embryos, the immunolocalization patterns of TRIP1 and RII were well
correlated, further supporting a functional correlation between both
proteins.
By fluorescence in situ hybridization, Galli-Stauber et al. (1998)
mapped the TRIP1 gene to 1p34.1 and a TRIP1 pseudogene to 7q32.
*FIELD* RF
1. Asano, K.; Kinzy, T. G.; Merrick, W. C.; Hershey, J. W. B.: Conservation
and diversity of eukaryotic translation initiation factor eIF3. J.
Biol. Chem. 272: 1101-1109, 1997.
2. Chen, R.-H.; Miettinen, P. J.; Maruoka, E. M.; Choy, L.; Derynck,
R.: A WD-domain protein that is associated with and phosphorylated
by the type II TGF-beta receptor. Nature 377: 548-552, 1995.
3. Galli-Stauber, C.; Raho, G.; Rossi, D.; Corona, D. F. V.; Pirola,
B.; Bonaglia, M. C.; Zuffardi, O.; Sorrentino, V.: Genomic structure
and chromosomal location of the human TGF-beta-receptor interacting
protein-1 (TRIP-1) gene to 1p34.1. FEBS Lett. 426: 279-282, 1998.
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 10/02/2007
cwells: 9/17/2003
alopez: 6/17/1999