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O75821

- EIF3G_HUMAN

UniProt

O75821 - EIF3G_HUMAN

Protein

Eukaryotic translation initiation factor 3 subunit G

Gene

EIF3G

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. This subunit can bind 18S rRNA.

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. translation initiation factor activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. formation of translation preinitiation complex Source: UniProtKB-HAMAP
    3. gene expression Source: Reactome
    4. regulation of translational initiation Source: UniProtKB-HAMAP
    5. translation Source: Reactome
    6. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 3 subunit GUniRule annotation
    Short name:
    eIF3gUniRule annotation
    Alternative name(s):
    Eukaryotic translation initiation factor 3 RNA-binding subunitUniRule annotation
    Short name:
    eIF-3 RNA-binding subunitUniRule annotation
    Eukaryotic translation initiation factor 3 subunit 4UniRule annotation
    eIF-3-deltaUniRule annotation
    eIF3 p42UniRule annotation
    eIF3 p44UniRule annotation
    Gene namesi
    Name:EIF3GUniRule annotation
    Synonyms:EIF3S4UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3274. EIF3G.

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus 1 PublicationUniRule annotation. Cytoplasmperinuclear region 1 PublicationUniRule annotation
    Note: Colocalizes with AIFM1 in the nucleus and perinuclear region.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
    3. eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
    4. eukaryotic translation initiation factor 3 complex Source: UniProtKB
    5. nucleus Source: UniProtKB-SubCell
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162384827.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 320319Eukaryotic translation initiation factor 3 subunit GPRO_0000123510Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphothreonine2 PublicationsUniRule annotation
    Modified residuei41 – 411Phosphothreonine3 PublicationsUniRule annotation
    Modified residuei42 – 421Phosphoserine3 PublicationsUniRule annotation

    Post-translational modificationi

    Phosphorylated. Phosphorylation is enhanced upon serum stimulation.3 PublicationsUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75821.
    PaxDbiO75821.
    PeptideAtlasiO75821.
    PRIDEiO75821.

    PTM databases

    PhosphoSiteiO75821.

    Expressioni

    Gene expression databases

    ArrayExpressiO75821.
    BgeeiO75821.
    CleanExiHS_EIF3G.
    GenevestigatoriO75821.

    Organism-specific databases

    HPAiHPA041997.

    Interactioni

    Subunit structurei

    Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and EIF3H of module B, thereby linking the three modules. EIF3J is a labile subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1 under conditions of nutrient depletion. Mitogenic stimulation leads to binding and activation of a complex composed of MTOR and RPTOR, leading to phosphorylation and release of RPS6KB1 and binding of EIF4B to eIF-3. Interacts (via C-terminus) with AIFM1 (via N-terminus).8 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIFM1O958319EBI-366632,EBI-356440
    EIF3BP558844EBI-366632,EBI-366696

    Protein-protein interaction databases

    BioGridi114215. 41 interactions.
    DIPiDIP-31115N.
    IntActiO75821. 24 interactions.
    MINTiMINT-3001737.
    STRINGi9606.ENSP00000253108.

    Structurei

    Secondary structure

    1
    320
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi236 – 24510
    Helixi252 – 2565
    Turni260 – 2623
    Beta strandi265 – 2728
    Beta strandi274 – 2763
    Beta strandi278 – 28912
    Helixi290 – 29910
    Turni300 – 3023
    Beta strandi311 – 3166

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQ0NMR-A231-320[»]
    ProteinModelPortaliO75821.
    SMRiO75821. Positions 228-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75821.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini239 – 31779RRMUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the eIF-3 subunit G family.UniRule annotation
    Contains 1 RRM (RNA recognition motif) domain.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000239560.
    HOVERGENiHBG026850.
    InParanoidiO75821.
    KOiK03248.
    OMAiWKASNED.
    OrthoDBiEOG75QR4G.
    PhylomeDBiO75821.
    TreeFamiTF101516.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    HAMAPiMF_03006. eIF3g.
    InterProiIPR017334. eIF3_g.
    IPR024675. eIF3g_N.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PANTHERiPTHR10352. PTHR10352. 1 hit.
    PfamiPF12353. eIF3g. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037949. Transl_init_eIF-3_RNA-bind. 1 hit.
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O75821-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG    50
    APLPPPKEVI NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK 100
    NWKKFGNSEF DPPGPNVATT TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK 150
    GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK ELAEQLGLST GEKEKLPGEL 200
    EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT IRVTNLSEDT 250
    RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV 300
    SGFGYDHLIL NVEWAKPSTN 320
    Length:320
    Mass (Da):35,611
    Last modified:September 19, 2002 - v2
    Checksum:i7D7226FEDE9D6FBB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti293 – 2931A → R in AAC78728. (PubMed:9822659)Curated

    Mass spectrometryi

    Molecular mass is 35639.8 Da from positions 1 - 320. 1 Publication
    Molecular mass is 35481.1±0.4 Da from positions 1 - 320. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96074 mRNA. Translation: AAC78728.1.
    AF020833 mRNA. Translation: AAB71866.1.
    AF092453 Genomic DNA. Translation: AAG15396.1.
    AF094850 mRNA. Translation: AAG15419.1.
    BT006889 mRNA. Translation: AAP35535.1.
    BC000733 mRNA. Translation: AAH00733.1.
    BC008469 mRNA. Translation: AAH08469.1.
    CCDSiCCDS12227.1.
    RefSeqiNP_003746.2. NM_003755.3.
    UniGeneiHs.529059.

    Genome annotation databases

    EnsembliENST00000253108; ENSP00000253108; ENSG00000130811.
    GeneIDi8666.
    KEGGihsa:8666.
    UCSCiuc002mnd.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96074 mRNA. Translation: AAC78728.1 .
    AF020833 mRNA. Translation: AAB71866.1 .
    AF092453 Genomic DNA. Translation: AAG15396.1 .
    AF094850 mRNA. Translation: AAG15419.1 .
    BT006889 mRNA. Translation: AAP35535.1 .
    BC000733 mRNA. Translation: AAH00733.1 .
    BC008469 mRNA. Translation: AAH08469.1 .
    CCDSi CCDS12227.1.
    RefSeqi NP_003746.2. NM_003755.3.
    UniGenei Hs.529059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQ0 NMR - A 231-320 [» ]
    ProteinModelPortali O75821.
    SMRi O75821. Positions 228-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114215. 41 interactions.
    DIPi DIP-31115N.
    IntActi O75821. 24 interactions.
    MINTi MINT-3001737.
    STRINGi 9606.ENSP00000253108.

    PTM databases

    PhosphoSitei O75821.

    Proteomic databases

    MaxQBi O75821.
    PaxDbi O75821.
    PeptideAtlasi O75821.
    PRIDEi O75821.

    Protocols and materials databases

    DNASUi 8666.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253108 ; ENSP00000253108 ; ENSG00000130811 .
    GeneIDi 8666.
    KEGGi hsa:8666.
    UCSCi uc002mnd.3. human.

    Organism-specific databases

    CTDi 8666.
    GeneCardsi GC19M010225.
    HGNCi HGNC:3274. EIF3G.
    HPAi HPA041997.
    MIMi 603913. gene.
    neXtProti NX_O75821.
    PharmGKBi PA162384827.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000239560.
    HOVERGENi HBG026850.
    InParanoidi O75821.
    KOi K03248.
    OMAi WKASNED.
    OrthoDBi EOG75QR4G.
    PhylomeDBi O75821.
    TreeFami TF101516.

    Enzyme and pathway databases

    Reactomei REACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
    REACT_1797. Formation of a pool of free 40S subunits.
    REACT_1979. Translation initiation complex formation.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF3G. human.
    EvolutionaryTracei O75821.
    GeneWikii EIF3G.
    GenomeRNAii 8666.
    NextBioi 32507.
    PROi O75821.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75821.
    Bgeei O75821.
    CleanExi HS_EIF3G.
    Genevestigatori O75821.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    HAMAPi MF_03006. eIF3g.
    InterProi IPR017334. eIF3_g.
    IPR024675. eIF3g_N.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    PANTHERi PTHR10352. PTHR10352. 1 hit.
    Pfami PF12353. eIF3g. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037949. Transl_init_eIF-3_RNA-bind. 1 hit.
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3."
      Block K.L., Vornlocher H.-P., Hershey J.W.B.
      J. Biol. Chem. 273:31901-31908(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF3A, RNA-BINDING.
    2. "Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells."
      Bandyopadhyay A., Maitra U.
      Nucleic Acids Res. 27:1331-1337(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH EIF5, RNA-BINDING.
    3. "Molecular cloning, genomic structure and chromosomal localization of a novel human RNA binding protein gene homologous to a tumor necrosis factor alpha inducible transcript in mouse."
      Chen W., Blough R.I., Winkelmann J.C.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain and Placenta.
    6. "Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3."
      Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.
      Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B.
    7. "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro."
      Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B.
      J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF3B.
    8. "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
      Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
      RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)."
      Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W., Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.
      FEBS Lett. 580:6375-6383(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AIFM1.
    11. "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
      LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
      J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Reconstitution reveals the functional core of mammalian eIF3."
      Masutani M., Sonenberg N., Yokoyama S., Imataka H.
      EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
    13. "Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
      Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.
      Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41 AND SER-42, MASS SPECTROMETRY.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
      Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E., Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B., Doudna J.A., Robinson C.V.
      Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY.
    16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structural roles for human translation factor eIF3 in initiation of protein synthesis."
      Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
      Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
    22. "Solution structure of RNA binding domain in eukaryotic translation initiation factor 3 subunit 4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 231-320.

    Entry informationi

    Entry nameiEIF3G_HUMAN
    AccessioniPrimary (citable) accession number: O75821
    Secondary accession number(s): O14801, Q969U5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Translation initiation factors
      List of translation initiation factor entries
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3