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O43432

- IF4G3_HUMAN

UniProt

O43432 - IF4G3_HUMAN

Protein

Eukaryotic translation initiation factor 4 gamma 3

Gene

EIF4G3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Probable component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome. Thought to be a functional homolog of EIF4G1.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei699 – 7002Cleavage; by enterovirus/rhinovirus protease 2A
    Sitei700 – 7012Cleavage; by foot-and-mouth disease virus leader protease

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. RNA cap binding Source: ProtInc
    3. translation factor activity, nucleic acid binding Source: ProtInc
    4. translation initiation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. positive regulation of meiosis I Source: Ensembl
    3. positive regulation of protein phosphorylation Source: Ensembl
    4. positive regulation of translation Source: Ensembl
    5. regulation of translational initiation Source: ProtInc
    6. spermatogenesis Source: Ensembl
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Host-virus interaction, Protein biosynthesis, Translation regulation

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4 gamma 3
    Short name:
    eIF-4-gamma 3
    Short name:
    eIF-4G 3
    Short name:
    eIF4G 3
    Alternative name(s):
    eIF-4-gamma II
    Short name:
    eIF4GII
    Gene namesi
    Name:EIF4G3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3298. EIF4G3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. eukaryotic translation initiation factor 4F complex Source: ProtInc

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi756 – 7561R → D: Reduces binding to EIF4A; when associated with D-759 and D-764. 1 Publication
    Mutagenesisi759 – 7591R → D: Reduces binding to EIF4A; when associated with D-756 and D-764. 1 Publication
    Mutagenesisi764 – 7641K → D: Reduces binding to EIF4A; when associated with D-756 and D-759. 1 Publication
    Mutagenesisi814 – 8141R → D: Reduces binding to EIF4A; when associated with D-820. 1 Publication
    Mutagenesisi820 – 8201K → D: Reduces binding to EIF4A; when associated with D-814. 1 Publication
    Mutagenesisi834 – 8352RK → DD: Reduces binding to IRES.

    Organism-specific databases

    PharmGKBiPA27724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15851585Eukaryotic translation initiation factor 4 gamma 3PRO_0000213329Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei168 – 1681PhosphothreonineBy similarity
    Modified residuei230 – 2301Phosphoserine2 Publications
    Modified residuei232 – 2321Phosphoserine2 Publications
    Modified residuei267 – 2671PhosphoserineBy similarity
    Modified residuei495 – 4951Phosphoserine7 Publications
    Modified residuei1156 – 11561Phosphoserine; by CaMK11 Publication

    Post-translational modificationi

    Following infection by certain enteroviruses, rhinoviruses and aphthoviruses, EIF4G1 is cleaved by the viral protease 2A, or the leader protease in the case of aphthoviruses. This shuts down the capped cellular mRNA transcription.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43432.
    PaxDbiO43432.
    PRIDEiO43432.

    PTM databases

    PhosphoSiteiO43432.

    Miscellaneous databases

    PMAP-CutDBO43432.

    Expressioni

    Gene expression databases

    ArrayExpressiO43432.
    BgeeiO43432.
    CleanExiHS_EIF4G3.
    GenevestigatoriO43432.

    Organism-specific databases

    HPAiHPA025031.
    HPA025039.
    HPA025041.

    Interactioni

    Subunit structurei

    Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a complex with EIF4E. eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114220. 16 interactions.
    DIPiDIP-33245N.
    IntActiO43432. 12 interactions.
    MINTiMINT-85560.
    STRINGi9606.ENSP00000264211.

    Structurei

    Secondary structure

    1
    1585
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi746 – 76217
    Helixi770 – 7778
    Helixi785 – 80117
    Helixi803 – 8053
    Helixi806 – 81611
    Helixi833 – 84816
    Helixi885 – 90016
    Turni901 – 9033
    Helixi907 – 91913
    Helixi923 – 94018
    Turni943 – 9453
    Helixi946 – 96116
    Helixi967 – 98115
    Turni982 – 9843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HU3X-ray2.37A745-1003[»]
    ProteinModelPortaliO43432.
    SMRiO43432. Positions 136-161, 745-986, 1214-1551.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43432.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati745 – 78339HEAT 1Add
    BLAST
    Domaini755 – 983229MIF4GPROSITE-ProRule annotationAdd
    BLAST
    Repeati784 – 83148HEAT 2Add
    BLAST
    Repeati832 – 90574HEAT 3Add
    BLAST
    Repeati906 – 94439HEAT 4Add
    BLAST
    Repeati945 – 98440HEAT 5Add
    BLAST
    Domaini1221 – 1343123MIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1416 – 1585170W2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 16229PABPC1-bindingAdd
    BLAST
    Regioni619 – 63012EIF4E-bindingBy similarityAdd
    BLAST
    Regioni699 – 1019321eIF3/EIF4A-bindingBy similarityAdd
    BLAST
    Regioni1433 – 1585153EIF4A-bindingBy similarityAdd
    BLAST
    Regioni1571 – 158515Necessary but not sufficient for MKNK1-bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili447 – 47529Sequence AnalysisAdd
    BLAST
    Coiled coili994 – 102330Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 5 HEAT repeats.Curated
    Contains 1 MI domain.PROSITE-ProRule annotation
    Contains 1 MIF4G domain.Curated
    Contains 1 W2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG301289.
    HOVERGENiHBG052083.
    InParanoidiO43432.
    KOiK03260.
    OMAiICKKSCS.
    OrthoDBiEOG7D59N2.
    PhylomeDBiO43432.
    TreeFamiTF101527.

    Family and domain databases

    Gene3Di1.25.40.180. 3 hits.
    InterProiIPR016024. ARM-type_fold.
    IPR003891. Initiation_fac_eIF4g_MI.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    IPR003307. W2_domain.
    [Graphical view]
    PfamiPF02847. MA3. 1 hit.
    PF02854. MIF4G. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view]
    SMARTiSM00515. eIF5C. 1 hit.
    SM00544. MA3. 1 hit.
    SM00543. MIF4G. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.
    PROSITEiPS51366. MI. 1 hit.
    PS51363. W2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43432-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNSQPQTRSP FFQRPQIQPP RATIPNSSPS IRPGAQTPTA VYQANQHIMM     50
    VNHLPMPYPV PQGPQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG 100
    PGDFPNAYGT PFYPSQPVYQ SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG 150
    GKDITEEIMS GGGSRNPTPP IGRPTSTPTP PQQLPSQVPE HSPVVYGTVE 200
    SAHLAASTPV TAASDQKQEE KPKPDPVLKS PSPVLRLVLS GEKKEQEGQT 250
    SETTAIVSIA ELPLPPSPTT VSSVARSTIA APTSSALSSQ PIFTTAIDDR 300
    CELSSPREDT IPIPSLTSCT ETSDPLPTNE NDDDICKKPC SVAPNDIPLV 350
    SSTNLINEIN GVSEKLSATE SIVEIVKQEV LPLTLELEIL ENPPEEMKLE 400
    CIPAPITPST VPSFPPTPPT PPASPPHTPV IVPAAATTVS SPSAAITVQR 450
    VLEEDESIRT CLSEDAKEIQ NKIEVEADGQ TEEILDSQNL NSRRSPVPAQ 500
    IAITVPKTWK KPKDRTRTTE EMLEAELELK AEEELSIDKV LESEQDKMSQ 550
    GFHPERDPSD LKKVKAVEEN GEEAEPVRNG AESVSEGEGI DANSGSTDSS 600
    GDGVTFPFKP ESWKPTDTEG KKQYDREFLL DFQFMPACIQ KPEGLPPISD 650
    VVLDKINQPK LPMRTLDPRI LPRGPDFTPA FADFGRQTPG GRGVPLLNVG 700
    SRRSQPGQRR EPRKIITVSV KEDVHLKKAE NAWKPSQKRD SQADDPENIK 750
    TQELFRKVRS ILNKLTPQMF NQLMKQVSGL TVDTEERLKG VIDLVFEKAI 800
    DEPSFSVAYA NMCRCLVTLK VPMADKPGNT VNFRKLLLNR CQKEFEKDKA 850
    DDDVFEKKQK ELEAASAPEE RTRLHDELEE AKDKARRRSI GNIKFIGELF 900
    KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFEKAKPRMD 950
    QYFNQMEKIV KERKTSSRIR FMLQDVIDLR LCNWVSRRAD QGPKTIEQIH 1000
    KEAKIEEQEE QRKVQQLMTK EKRRPGVQRV DEGGWNTVQG AKNSRVLDPS 1050
    KFLKITKPTI DEKIQLVPKA QLGSWGKGSS GGAKASETDA LRSSASSLNR 1100
    FSALQPPAPS GSTPSTPVEF DSRRTLTSRG SMGREKNDKP LPSATARPNT 1150
    FMRGGSSKDL LDNQSQEEQR REMLETVKQL TGGVDVERNS TEAERNKTRE 1200
    SAKPEISAMS AHDKAALSEE ELERKSKSII DEFLHINDFK EAMQCVEELN 1250
    AQGLLHVFVR VGVESTLERS QITRDHMGQL LYQLVQSEKL SKQDFFKGFS 1300
    ETLELADDMA IDIPHIWLYL AELVTPMLKE GGISMRELTI EFSKPLLPVG 1350
    RAGVLLSEIL HLLCKQMSHK KVGALWREAD LSWKDFLPEG EDVHNFLLEQ 1400
    KLDFIESDSP CSSEALSKKE LSAEELYKRL EKLIIEDKAN DEQIFDWVEA 1450
    NLDEIQMSSP TFLRALMTAV CKAAIIADSS TFRVDTAVIK QRVPILLKYL 1500
    DSDTEKELQA LYALQASIVK LDQPANLLRM FFDCLYDEEV ISEDAFYKWE 1550
    SSKDPAEQNG KGVALKSVTA FFTWLREAEE ESEDN 1585
    Length:1,585
    Mass (Da):176,652
    Last modified:March 1, 2001 - v2
    Checksum:iEA483139373DCA5C
    GO
    Isoform 2 (identifier: O43432-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         11-11: F → FAAGPRPPHHQF
         499-504: AQIAIT → ETSNEC
         505-1585: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:515
    Mass (Da):55,227
    Checksum:i0B4E961F10F62EA0
    GO
    Isoform 3 (identifier: O43432-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         10-10: P → PGGFRPIQ
         182-182: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,591
    Mass (Da):177,280
    Checksum:iA6A4BEC78E05CC92
    GO
    Isoform 4 (identifier: O43432-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         219-498: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,305
    Mass (Da):146,871
    Checksum:iEDF74715CD55642D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591M → I in AAH30578. (PubMed:15489334)Curated
    Sequence conflicti333 – 3331D → G in AAH30578. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti378 – 3781Q → R.
    Corresponds to variant rs35731992 [ dbSNP | Ensembl ].
    VAR_048924
    Natural varianti496 – 4961P → A.
    Corresponds to variant rs35176330 [ dbSNP | Ensembl ].
    VAR_034009
    Natural varianti1185 – 11851D → E.
    Corresponds to variant rs2230572 [ dbSNP | Ensembl ].
    VAR_048925

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei10 – 101P → PGGFRPIQ in isoform 3. 1 PublicationVSP_043447
    Alternative sequencei11 – 111F → FAAGPRPPHHQF in isoform 2. 1 PublicationVSP_010487
    Alternative sequencei182 – 1821Missing in isoform 3. 1 PublicationVSP_043448
    Alternative sequencei219 – 498280Missing in isoform 4. 1 PublicationVSP_054502Add
    BLAST
    Alternative sequencei499 – 5046AQIAIT → ETSNEC in isoform 2. 1 PublicationVSP_010488
    Alternative sequencei505 – 15851081Missing in isoform 2. 1 PublicationVSP_010489Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012072 mRNA. Translation: AAC02903.2.
    AL031005 Genomic DNA. No translation available.
    AL358392, AL606477, AL627311 Genomic DNA. Translation: CAI12155.1.
    AL606477, AL358392, AL627311 Genomic DNA. Translation: CAI12534.1.
    AL627311, AL358392, AL606477 Genomic DNA. Translation: CAI14553.1.
    AL672037 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94956.1.
    BC030578 mRNA. Translation: AAH30578.1.
    BC094683 mRNA. Translation: AAH94683.1.
    BC136643 mRNA. Translation: AAI36644.1.
    Z34918 mRNA. Translation: CAA84397.1.
    CCDSiCCDS214.1. [O43432-1]
    CCDS55580.1. [O43432-3]
    CCDS59192.1. [O43432-2]
    PIRiS49172.
    RefSeqiNP_001185730.1. NM_001198801.1.
    NP_001185731.1. NM_001198802.1. [O43432-3]
    NP_001185732.1. NM_001198803.1. [O43432-2]
    NP_003751.2. NM_003760.4. [O43432-1]
    UniGeneiHs.467084.
    Hs.732241.

    Genome annotation databases

    EnsembliENST00000264211; ENSP00000264211; ENSG00000075151. [O43432-1]
    ENST00000356916; ENSP00000349386; ENSG00000075151. [O43432-2]
    ENST00000374935; ENSP00000364071; ENSG00000075151. [O43432-4]
    ENST00000400422; ENSP00000383274; ENSG00000075151. [O43432-1]
    ENST00000602326; ENSP00000473510; ENSG00000075151. [O43432-3]
    GeneIDi8672.
    KEGGihsa:8672.
    UCSCiuc001bec.3. human. [O43432-1]
    uc001bee.3. human. [O43432-3]
    uc001beh.3. human. [O43432-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF012072 mRNA. Translation: AAC02903.2 .
    AL031005 Genomic DNA. No translation available.
    AL358392 , AL606477 , AL627311 Genomic DNA. Translation: CAI12155.1 .
    AL606477 , AL358392 , AL627311 Genomic DNA. Translation: CAI12534.1 .
    AL627311 , AL358392 , AL606477 Genomic DNA. Translation: CAI14553.1 .
    AL672037 Genomic DNA. No translation available.
    CH471134 Genomic DNA. Translation: EAW94956.1 .
    BC030578 mRNA. Translation: AAH30578.1 .
    BC094683 mRNA. Translation: AAH94683.1 .
    BC136643 mRNA. Translation: AAI36644.1 .
    Z34918 mRNA. Translation: CAA84397.1 .
    CCDSi CCDS214.1. [O43432-1 ]
    CCDS55580.1. [O43432-3 ]
    CCDS59192.1. [O43432-2 ]
    PIRi S49172.
    RefSeqi NP_001185730.1. NM_001198801.1.
    NP_001185731.1. NM_001198802.1. [O43432-3 ]
    NP_001185732.1. NM_001198803.1. [O43432-2 ]
    NP_003751.2. NM_003760.4. [O43432-1 ]
    UniGenei Hs.467084.
    Hs.732241.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HU3 X-ray 2.37 A 745-1003 [» ]
    ProteinModelPortali O43432.
    SMRi O43432. Positions 136-161, 745-986, 1214-1551.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114220. 16 interactions.
    DIPi DIP-33245N.
    IntActi O43432. 12 interactions.
    MINTi MINT-85560.
    STRINGi 9606.ENSP00000264211.

    PTM databases

    PhosphoSitei O43432.

    Proteomic databases

    MaxQBi O43432.
    PaxDbi O43432.
    PRIDEi O43432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264211 ; ENSP00000264211 ; ENSG00000075151 . [O43432-1 ]
    ENST00000356916 ; ENSP00000349386 ; ENSG00000075151 . [O43432-2 ]
    ENST00000374935 ; ENSP00000364071 ; ENSG00000075151 . [O43432-4 ]
    ENST00000400422 ; ENSP00000383274 ; ENSG00000075151 . [O43432-1 ]
    ENST00000602326 ; ENSP00000473510 ; ENSG00000075151 . [O43432-3 ]
    GeneIDi 8672.
    KEGGi hsa:8672.
    UCSCi uc001bec.3. human. [O43432-1 ]
    uc001bee.3. human. [O43432-3 ]
    uc001beh.3. human. [O43432-2 ]

    Organism-specific databases

    CTDi 8672.
    GeneCardsi GC01M021132.
    HGNCi HGNC:3298. EIF4G3.
    HPAi HPA025031.
    HPA025039.
    HPA025041.
    MIMi 603929. gene.
    neXtProti NX_O43432.
    PharmGKBi PA27724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301289.
    HOVERGENi HBG052083.
    InParanoidi O43432.
    KOi K03260.
    OMAi ICKKSCS.
    OrthoDBi EOG7D59N2.
    PhylomeDBi O43432.
    TreeFami TF101527.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.

    Miscellaneous databases

    ChiTaRSi EIF4G3. human.
    EvolutionaryTracei O43432.
    GeneWikii EIF4G3.
    GenomeRNAii 8672.
    NextBioi 32529.
    PMAP-CutDB O43432.
    PROi O43432.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43432.
    Bgeei O43432.
    CleanExi HS_EIF4G3.
    Genevestigatori O43432.

    Family and domain databases

    Gene3Di 1.25.40.180. 3 hits.
    InterProi IPR016024. ARM-type_fold.
    IPR003891. Initiation_fac_eIF4g_MI.
    IPR016021. MIF4-like_typ_1/2/3.
    IPR003890. MIF4G-like_typ-3.
    IPR003307. W2_domain.
    [Graphical view ]
    Pfami PF02847. MA3. 1 hit.
    PF02854. MIF4G. 1 hit.
    PF02020. W2. 1 hit.
    [Graphical view ]
    SMARTi SM00515. eIF5C. 1 hit.
    SM00544. MA3. 1 hit.
    SM00543. MIF4G. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    PROSITEi PS51366. MI. 1 hit.
    PS51363. W2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel functional human eukaryotic translation initiation factor 4G."
      Gradi A., Imataka H., Svitkin Y.V., Rom E., Raught B., Morino S., Sonenberg N.
      Mol. Cell. Biol. 18:334-342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EIF4A; EIF4E AND EIF3.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 2; 3 AND 4).
      Tissue: PNS and Testis.
    5. "Characterization of secretory proteins of human ovarian follicle cells by cDNA cloning."
      Klaudiny J.J., von der Kammer H.H., Scheit K.K.
      Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 887-1585 (ISOFORM 1).
      Tissue: Ovary.
    6. "A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation."
      Imataka H., Gradi A., Sonenberg N.
      EMBO J. 17:7480-7489(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PABPC1.
    7. "Phosphorylation screening identifies translational initiation factor 4GII as an intracellular target of Ca(2+)/calmodulin-dependent protein kinase I."
      Qin H., Raught B., Sonenberg N., Goldstein E.G., Edelman A.M.
      J. Biol. Chem. 278:48570-48579(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1156 BY CAMK1.
    8. "Human rhin4ovirus 2A proteinase cleavage sites in eukaryotic initiation factors (eIF) 4GI and eIF4GII are different."
      Gradi A., Svitkin Y.V., Sommergruber W., Imataka H., Morino S., Skern T., Sonenberg N.
      J. Virol. 77:5026-5029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY RHINOVIRUS PROTEASE.
    9. "Cleavage of eukaryotic translation initiation factor 4GII within foot-and-mouth disease virus-infected cells: identification of the L-protease cleavage site in vitro."
      Gradi A., Foeger N., Strong R., Svitkin Y.V., Sonenberg N., Skern T., Belsham G.J.
      J. Virol. 78:3271-3278(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY FOOT-AND-MOUTH DISEASE VIRUS PROTEASE.
    10. "eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation."
      Gingras A.-C., Raught B., Sonenberg N.
      Annu. Rev. Biochem. 68:913-963(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. "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 SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-232 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII."
      Miura T., Shiratori Y., Shimma N.
      J. Biomol. NMR 27:279-280(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 621-637 IN COMPLEX WITH EIF4E.
    21. "A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery."
      Marcotrigiano J., Lomakin I.B., Sonenberg N., Pestova T.V., Hellen C.U.T., Burley S.K.
      Mol. Cell 7:193-203(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) OF 745-986, MUTAGENESIS OF ARG-756; ARG-759; LYS-764; ARG-814; LYS-820 AND 834-ARG-LYS-835.

    Entry informationi

    Entry nameiIF4G3_HUMAN
    AccessioniPrimary (citable) accession number: O43432
    Secondary accession number(s): B9EGQ7
    , Q15597, Q504Z1, Q5SWC3, Q8NEN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 136 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3