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Q04637

- IF4G1_HUMAN

UniProt

Q04637 - IF4G1_HUMAN

Protein

Eukaryotic translation initiation factor 4 gamma 1

Gene

EIF4G1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 4 (20 Apr 2010)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei674 – 6752Cleavage; by foot-and-mouth disease virus leader protease
    Sitei681 – 6822Cleavage; by enterovirus/rhinovirus protease 2A

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular protein metabolic process Source: Reactome
    3. cytokine-mediated signaling pathway Source: Reactome
    4. gene expression Source: Reactome
    5. insulin receptor signaling pathway Source: Reactome
    6. mRNA metabolic process Source: Reactome
    7. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    8. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    9. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    10. regulation of translational initiation Source: UniProtKB
    11. RNA metabolic process Source: Reactome
    12. translation Source: Reactome
    13. translational initiation Source: Reactome
    14. 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.
    REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_6772. S6K1 signalling.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    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 4 gamma 1
    Short name:
    eIF-4-gamma 1
    Short name:
    eIF-4G 1
    Short name:
    eIF-4G1
    Alternative name(s):
    p220
    Gene namesi
    Name:EIF4G1
    Synonyms:EIF4F, EIF4G, EIF4GI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:3296. EIF4G1.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    Parkinson disease 18 (PARK18) [MIM:614251]: An autosomal dominant, late-onset form of Parkinson disease. Parkinson disease is a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability, as well as by a clinically significant response to treatment with levodopa. The pathology involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti502 – 5021A → V in PARK18. 1 Publication
    Corresponds to variant rs111290936 [ dbSNP | Ensembl ].
    VAR_066573
    Natural varianti1205 – 12051R → H in PARK18. 1 Publication
    Corresponds to variant rs112176450 [ dbSNP | Ensembl ].
    VAR_066579

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi174 – 1785KRERK → AAAAA: Loss of PABPC1 binding; when associated with 184-AAAA-187. 1 Publication
    Mutagenesisi180 – 1801I → A: Loss of PABPC1 binding. 2 Publications
    Mutagenesisi182 – 1821I → A: Loss of PABPC1 binding. 2 Publications
    Mutagenesisi184 – 1874DPNQ → AAAA: Loss of PABPC1 binding; when associated with 174-AAAAA-178. 1 Publication
    Mutagenesisi192 – 1921I → A: Loss of PABPC1 binding. 2 Publications
    Mutagenesisi196 – 1961I → A: Loss of PABPC1 binding. 2 Publications
    Mutagenesisi612 – 6121Y → A or F: Abolishes binding to EIF4E. 2 Publications
    Mutagenesisi617 – 6182LL → AA: Abolishes binding to EIF4E. 1 Publication
    Mutagenesisi682 – 6821G → A, V, W, R or E: Reduced cleavage by protease 2A from human rhinovirus 2. 2 Publications
    Mutagenesisi768 – 7681L → A: Abolishes binding to EIF4A; when associated with A-770 and A-775. 2 Publications
    Mutagenesisi771 – 7711L → A: Abolishes binding to EIF4A; when associated with A-767 and A-775. 2 Publications
    Mutagenesisi776 – 7761F → A: Abolishes binding to EIF4A; when associated with A-767 and A-770. 2 Publications
    Mutagenesisi842 – 8432LL → AA: Abolishes binding to EIF4A; when associated with A-850 and K-851. 1 Publication
    Mutagenesisi851 – 8522FE → AK: Abolishes binding to EIF4A; when associated with A-841 and A-842. 1 Publication
    Mutagenesisi896 – 8961L → A: Abolishes binding to EIF4A; when associated with A-92 and A-95. 2 Publications
    Mutagenesisi902 – 9021I → A: Abolishes binding to EIF4A; when associated with A-895 and A-95. 2 Publications
    Mutagenesisi905 – 9051L → A: Abolishes binding to EIF4A; when associated with A-895 and A-92. 2 Publications
    Mutagenesisi974 – 9741R → A: Abolishes binding to EIF4A; when associated with A-976. 2 Publications
    Mutagenesisi977 – 9771F → A: Abolishes binding to EIF4A; when associated with A-973. 2 Publications
    Mutagenesisi985 – 9851L → A: Slightly reduced binding to EIF4A; when associated with A-989. 2 Publications
    Mutagenesisi990 – 9901W → A: Slightly reduced binding to EIF4A; when associated with A-984. 2 Publications

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

    Organism-specific databases

    MIMi614251. phenotype.
    Orphaneti2828. Young adult-onset Parkinsonism.
    PharmGKBiPA27722.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 15991599Eukaryotic translation initiation factor 4 gamma 1PRO_0000007786Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei207 – 2071Phosphothreonine1 Publication
    Modified residuei223 – 2231Phosphothreonine1 Publication
    Modified residuei602 – 6021N6-acetyllysineBy similarity
    Modified residuei647 – 6471Phosphothreonine1 Publication
    Modified residuei1028 – 10281Phosphoserine2 Publications
    Modified residuei1092 – 10921Phosphoserine4 Publications
    Modified residuei1095 – 10951N6-acetyllysine1 Publication
    Modified residuei1145 – 11451Phosphoserine1 Publication
    Modified residuei1147 – 11471Phosphoserine1 Publication
    Modified residuei1185 – 11851Phosphoserine; by PKC/PRKCA3 Publications
    Modified residuei1187 – 11871Phosphoserine2 Publications
    Modified residuei1209 – 12091Phosphoserine3 Publications
    Modified residuei1211 – 12111Phosphothreonine2 Publications
    Modified residuei1231 – 12311Phosphoserine4 Publications
    Modified residuei1596 – 15961Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at multiple sites in vivo. Phosphorylation at Ser-1185 by PRKCA induces binding to MKNK1.7 Publications
    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.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ04637.
    PaxDbiQ04637.
    PRIDEiQ04637.

    PTM databases

    PhosphoSiteiQ04637.

    Miscellaneous databases

    PMAP-CutDBQ04637.

    Expressioni

    Gene expression databases

    ArrayExpressiQ04637.
    BgeeiQ04637.
    CleanExiHS_EIF4G1.
    GenevestigatoriQ04637.

    Organism-specific databases

    HPAiCAB014774.
    HPA028487.
    HPA043866.

    Interactioni

    Subunit structurei

    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. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. 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/EIF4G3 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. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with CIRBP and MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis. Interacts with RBM4. Interacts with HNRNPD/AUF1; the interaction requires RNA.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX3XO005713EBI-73711,EBI-353779
    EIF3JO758222EBI-73711,EBI-366647
    EIF4A1P608427EBI-73711,EBI-73449
    EIF4EP067302EBI-73711,EBI-73440
    HNRNPDQ14103-43EBI-73711,EBI-432545
    PABPC1P119402EBI-73711,EBI-81531

    Protein-protein interaction databases

    BioGridi108296. 60 interactions.
    DIPiDIP-1161N.
    IntActiQ04637. 35 interactions.
    MINTiMINT-135718.
    STRINGi9606.ENSP00000316879.

    Structurei

    Secondary structure

    1
    1599
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi181 – 1833
    Helixi185 – 1873
    Helixi193 – 1975
    Helixi614 – 6196
    Helixi1234 – 125623
    Helixi1259 – 12679
    Helixi1272 – 12743
    Helixi1275 – 128612
    Turni1287 – 12893
    Helixi1291 – 130616
    Helixi1312 – 132918
    Turni1330 – 13323
    Helixi1336 – 13449
    Helixi1345 – 13484
    Helixi1355 – 13628
    Turni1363 – 13653
    Helixi1366 – 13694
    Helixi1372 – 138716
    Helixi1389 – 139810
    Helixi1403 – 14053
    Helixi1413 – 14197
    Helixi1423 – 14253
    Helixi1439 – 145214
    Helixi1457 – 146711
    Helixi1470 – 14734
    Helixi1476 – 148914
    Beta strandi1494 – 14963
    Helixi1501 – 151414
    Helixi1518 – 153417
    Helixi1541 – 155111
    Helixi1557 – 15637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LJ2X-ray2.38C/D172-199[»]
    1UG3X-ray2.24A/B1233-1571[»]
    2W97X-ray2.29E/F609-622[»]
    4F02X-ray2.00C/F178-203[»]
    DisProtiDP00406.
    ProteinModelPortaliQ04637.
    SMRiQ04637. Positions 173-199, 751-991, 1234-1592.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ04637.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini565 – 792228MIF4GPROSITE-ProRule annotationAdd
    BLAST
    Domaini1241 – 1363123MIPROSITE-ProRule annotationAdd
    BLAST
    Domaini1433 – 1599167W2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni172 – 20029PABPC1-bindingAdd
    BLAST
    Regioni607 – 61812EIF4E-bindingAdd
    BLAST
    Regioni682 – 1085404eIF3/EIF4A-bindingAdd
    BLAST
    Regioni1450 – 1599150EIF4A-bindingAdd
    BLAST
    Regioni1585 – 159915Necessary but not sufficient for MKNK1-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi454 – 46714Poly-GluAdd
    BLAST
    Compositional biasi501 – 5044Poly-Ala

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG301289.
    HOVERGENiHBG052083.
    KOiK03260.
    OMAiGSNWVPR.
    OrthoDBiEOG7D59N2.
    PhylomeDBiQ04637.
    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 (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform A (identifier: Q04637-1) [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

    MNKAPQSTGP PPAPSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQH     50
    FYPSRAQPPS SAASRVQSAA PARPGPAAHV YPAGSQVMMI PSQISYPASQ 100
    GAYYIPGQGR STYVVPTQQY PVQPGAPGFY PGASPTEFGT YAGAYYPAQG 150
    VQQFPTGVAP TPVLMNQPPQ IAPKRERKTI RIRDPNQGGK DITEEIMSGA 200
    RTASTPTPPQ TGGGLEPQAN GETPQVAVIV RPDDRSQGAI IADRPGLPGP 250
    EHSPSESQPS SPSPTPSPSP VLEPGSEPNL AVLSIPGDTM TTIQMSVEES 300
    TPISRETGEP YRLSPEPTPL AEPILEVEVT LSKPVPESEF SSSPLQAPTP 350
    LASHTVEIHE PNGMVPSEDL EPEVESSPEL APPPACPSES PVPIAPTAQP 400
    EELLNGAPSP PAVDLSPVSE PEEQAKEVTA SMAPPTIPSA TPATAPSATS 450
    PAQEEEMEEE EEEEEGEAGE AGEAESEKGG EELLPPESTP IPANLSQNLE 500
    AAAATQVAVS VPKRRRKIKE LNKKEAVGDL LDAFKEANPA VPEVENQPPA 550
    GSNPGPESEG SGVPPRPEEA DETWDSKEDK IHNAENIQPG EQKYEYKSDQ 600
    WKPLNLEEKK RYDREFLLGF QFIFASMQKP EGLPHISDVV LDKANKTPLR 650
    PLDPTRLQGI NCGPDFTPSF ANLGRTTLST RGPPRGGPGG ELPRGPAGLG 700
    PRRSQQGPRK EPRKIIATVL MTEDIKLNKA EKAWKPSSKR TAADKDRGEE 750
    DADGSKTQDL FRRVRSILNK LTPQMFQQLM KQVTQLAIDT EERLKGVIDL 800
    IFEKAISEPN FSVAYANMCR CLMALKVPTT EKPTVTVNFR KLLLNRCQKE 850
    FEKDKDDDEV FEKKQKEMDE AATAEERGRL KEELEEARDI ARRRSLGNIK 900
    FIGELFKLKM LTEAIMHDCV VKLLKNHDEE SLECLCRLLT TIGKDLDFEK 950
    AKPRMDQYFN QMEKIIKEKK TSSRIRFMLQ DVLDLRGSNW VPRRGDQGPK 1000
    TIDQIHKEAE MEEHREHIKV QQLMAKGSDK RRGGPPGPPI SRGLPLVDDG 1050
    GWNTVPISKG SRPIDTSRLT KITKPGSIDS NNQLFAPGGR LSWGKGSSGG 1100
    SGAKPSDAAS EAARPATSTL NRFSALQQAV PTESTDNRRV VQRSSLSRER 1150
    GEKAGDRGDR LERSERGGDR GDRLDRARTP ATKRSFSKEV EERSRERPSQ 1200
    PEGLRKAASL TEDRDRGRDA VKREAALPPV SPLKAALSEE ELEKKSKAII 1250
    EEYLHLNDMK EAVQCVQELA SPSLLFIFVR HGVESTLERS AIAREHMGQL 1300
    LHQLLCAGHL STAQYYQGLY EILELAEDME IDIPHVWLYL AELVTPILQE 1350
    GGVPMGELFR EITKPLRPLG KAASLLLEIL GLLCKSMGPK KVGTLWREAG 1400
    LSWKEFLPEG QDIGAFVAEQ KVEYTLGEES EAPGQRALPS EELNRQLEKL 1450
    LKEGSSNQRV FDWIEANLSE QQIVSNTLVR ALMTAVCYSA IIFETPLRVD 1500
    VAVLKARAKL LQKYLCDEQK ELQALYALQA LVVTLEQPPN LLRMFFDALY 1550
    DEDVVKEDAF YSWESSKDPA EQQGKGVALK SVTAFFKWLR EAEEESDHN 1599
    Length:1,599
    Mass (Da):175,491
    Last modified:April 20, 2010 - v4
    Checksum:i324088B60863DA34
    GO
    Isoform B (identifier: Q04637-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

    Note: Produced by alternative initiation at Met-41 of isoform A.

    Show »
    Length:1,559
    Mass (Da):171,514
    Checksum:i22F62E219E629C0E
    GO
    Isoform C (identifier: Q04637-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-87: Missing.

    Note: Produced by alternative initiation at Met-88 of isoform A.

    Show »
    Length:1,512
    Mass (Da):166,619
    Checksum:i09DD6DC263462CB6
    GO
    Isoform D (identifier: Q04637-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-164: Missing.

    Note: Produced by alternative initiation at Met-165 of isoform A.

    Show »
    Length:1,435
    Mass (Da):158,517
    Checksum:i6F7E9DE4106E73B9
    GO
    Isoform E (identifier: Q04637-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-196: Missing.

    Note: Produced by alternative initiation at Met-197 of isoform A.

    Show »
    Length:1,403
    Mass (Da):154,805
    Checksum:i3E93A66EE3DFDDA9
    GO
    Isoform 7 (identifier: Q04637-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-196: Missing.
         696-696: P → PQ

    Note: Produced by alternative splicing.

    Show »
    Length:1,404
    Mass (Da):154,933
    Checksum:iE2CE3C54B5BB0A50
    GO
    Isoform 8 (identifier: Q04637-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         696-696: P → PQ

    Note: Produced by alternative splicing.

    Show »
    Length:1,600
    Mass (Da):175,619
    Checksum:i2B32EF7A6D50B657
    GO
    Isoform 9 (identifier: Q04637-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         48-48: R → RQGGFRSL

    Note: Produced by alternative splicing. Gene prediction based on EST data.

    Show »
    Length:1,606
    Mass (Da):176,237
    Checksum:iE4464821E0BA5FF6
    GO

    Sequence cautioni

    The sequence BAD18554.1 differs from that shown. Reason: Aberrant splicing.
    The sequence BAA02185.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAC78444.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAC82471.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301P → R in AAC78443. (PubMed:9755181)Curated
    Sequence conflicti138 – 1381F → L in AAL92872. (PubMed:14702039)Curated
    Sequence conflicti138 – 1381F → L in AAM69365. (PubMed:14702039)Curated
    Sequence conflicti149 – 1491Q → R in AAL92872. (PubMed:14702039)Curated
    Sequence conflicti149 – 1491Q → R in AAM69365. (PubMed:14702039)Curated
    Sequence conflicti214 – 2141G → S in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti462 – 4621E → D in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti468 – 4681A → V in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti474 – 4741A → G in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti479 – 4791G → R in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti604 – 6041L → P in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti604 – 6041L → P in AAL92872. (PubMed:14702039)Curated
    Sequence conflicti604 – 6041L → P in AAM69365. (PubMed:14702039)Curated
    Sequence conflicti604 – 6041L → P in AAC82471. (PubMed:9372926)Curated
    Sequence conflicti625 – 6262AS → CQ in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti693 – 6931P → A in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti696 – 6961P → A in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti764 – 7641V → W in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti878 – 8781G → E in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti894 – 8941R → C in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti1104 – 11041K → Q in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti1121 – 11211N → I in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti1185 – 11851S → T in BAA02185. (PubMed:1429670)Curated
    Sequence conflicti1384 – 13841C → Y in CAI46013. (PubMed:17974005)Curated
    Sequence conflicti1472 – 14721Missing in BAA02185. (PubMed:1429670)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711P → S.1 Publication
    Corresponds to variant rs113810947 [ dbSNP | Ensembl ].
    VAR_066571
    Natural varianti161 – 1611T → A.5 Publications
    Corresponds to variant rs13319149 [ dbSNP | Ensembl ].
    VAR_061147
    Natural varianti311 – 3111Y → C.1 Publication
    Corresponds to variant rs16858632 [ dbSNP | Ensembl ].
    VAR_055704
    Natural varianti432 – 4321M → V.4 Publications
    Corresponds to variant rs2178403 [ dbSNP | Ensembl ].
    VAR_063040
    Natural varianti466 – 4683Missing.
    VAR_066572
    Natural varianti502 – 5021A → V in PARK18. 1 Publication
    Corresponds to variant rs111290936 [ dbSNP | Ensembl ].
    VAR_066573
    Natural varianti686 – 6861G → C Found in patients with Parkinson disease; unknown pathological significance. 1 Publication
    Corresponds to variant rs112019125 [ dbSNP | Ensembl ].
    VAR_066574
    Natural varianti696 – 6961P → L in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036117
    Natural varianti806 – 8061I → V.1 Publication
    Corresponds to variant rs62287499 [ dbSNP | Ensembl ].
    VAR_066575
    Natural varianti829 – 8291T → S.1 Publication
    Corresponds to variant rs111500185 [ dbSNP | Ensembl ].
    VAR_066576
    Natural varianti1164 – 11641S → R Found in a patient with Parkinson disease; unknown pathological significance. 1 Publication
    Corresponds to variant rs113169049 [ dbSNP | Ensembl ].
    VAR_066577
    Natural varianti1197 – 11971R → W Found in a patient with Parkinson disease; unknown pathological significance. 1 Publication
    Corresponds to variant rs113388242 [ dbSNP | Ensembl ].
    VAR_066578
    Natural varianti1205 – 12051R → H in PARK18. 1 Publication
    Corresponds to variant rs112176450 [ dbSNP | Ensembl ].
    VAR_066579
    Natural varianti1229 – 12291P → A.1 Publication
    Corresponds to variant rs35629949 [ dbSNP | Ensembl ].
    VAR_061148
    Natural varianti1233 – 12331L → P.1 Publication
    Corresponds to variant rs2230570 [ dbSNP | Ensembl ].
    VAR_055705
    Natural varianti1257 – 12571N → S.1 Publication
    Corresponds to variant rs73053766 [ dbSNP | Ensembl ].
    VAR_066580

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 196196Missing in isoform E and isoform 7. 1 PublicationVSP_018723Add
    BLAST
    Alternative sequencei1 – 164164Missing in isoform D. CuratedVSP_018722Add
    BLAST
    Alternative sequencei1 – 8787Missing in isoform C. 1 PublicationVSP_018721Add
    BLAST
    Alternative sequencei1 – 4040Missing in isoform B. 1 PublicationVSP_018720Add
    BLAST
    Alternative sequencei48 – 481R → RQGGFRSL in isoform 9. CuratedVSP_047396
    Alternative sequencei696 – 6961P → PQ in isoform 7 and isoform 8. 4 PublicationsVSP_047397

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12686 mRNA. Translation: BAA02185.1. Frameshift.
    AY082886 mRNA. Translation: AAL92872.1.
    AF281070 mRNA. Translation: AAM69365.1.
    AK131407 mRNA. Translation: BAD18554.1. Sequence problems.
    BX647812 mRNA. Translation: CAI46013.1.
    AC078797 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78257.1.
    CH471052 Genomic DNA. Translation: EAW78259.1.
    CH471052 Genomic DNA. Translation: EAW78262.1.
    CH471052 Genomic DNA. Translation: EAW78263.1.
    CH471052 Genomic DNA. Translation: EAW78264.1.
    CH471052 Genomic DNA. Translation: EAW78265.1.
    CH471052 Genomic DNA. Translation: EAW78266.1.
    CH471052 Genomic DNA. Translation: EAW78267.1.
    AF002816 mRNA. Translation: AAC78443.1.
    AF004836 Genomic DNA. Translation: AAC78444.1. Different initiation.
    AF104913 mRNA. Translation: AAC82471.1. Different initiation.
    AJ001046 mRNA. Translation: CAA04500.1.
    CCDSiCCDS3259.1. [Q04637-1]
    CCDS3260.1. [Q04637-4]
    CCDS3261.1. [Q04637-5]
    CCDS46970.2. [Q04637-7]
    CCDS54687.1. [Q04637-9]
    CCDS54688.1. [Q04637-8]
    PIRiA44453.
    RefSeqiNP_004944.3. NM_004953.4. [Q04637-7]
    NP_886553.3. NM_182917.4.
    NP_937884.1. NM_198241.2.
    NP_937885.1. NM_198242.2. [Q04637-5]
    UniGeneiHs.433750.

    Genome annotation databases

    EnsembliENST00000319274; ENSP00000323737; ENSG00000114867. [Q04637-1]
    ENST00000342981; ENSP00000343450; ENSG00000114867. [Q04637-8]
    ENST00000346169; ENSP00000316879; ENSG00000114867. [Q04637-1]
    ENST00000350481; ENSP00000317600; ENSG00000114867. [Q04637-5]
    ENST00000352767; ENSP00000338020; ENSG00000114867. [Q04637-9]
    ENST00000382330; ENSP00000371767; ENSG00000114867. [Q04637-9]
    ENST00000392537; ENSP00000376320; ENSG00000114867. [Q04637-4]
    ENST00000414031; ENSP00000391935; ENSG00000114867. [Q04637-3]
    ENST00000424196; ENSP00000416255; ENSG00000114867. [Q04637-9]
    ENST00000434061; ENSP00000411826; ENSG00000114867. [Q04637-7]
    ENST00000435046; ENSP00000404754; ENSG00000114867. [Q04637-6]
    GeneIDi1981.
    KEGGihsa:1981.
    UCSCiuc003fnp.3. human. [Q04637-1]
    uc003fnv.4. human.
    uc003fnx.3. human.

    Polymorphism databases

    DMDMi294862538.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12686 mRNA. Translation: BAA02185.1 . Frameshift.
    AY082886 mRNA. Translation: AAL92872.1 .
    AF281070 mRNA. Translation: AAM69365.1 .
    AK131407 mRNA. Translation: BAD18554.1 . Sequence problems.
    BX647812 mRNA. Translation: CAI46013.1 .
    AC078797 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78257.1 .
    CH471052 Genomic DNA. Translation: EAW78259.1 .
    CH471052 Genomic DNA. Translation: EAW78262.1 .
    CH471052 Genomic DNA. Translation: EAW78263.1 .
    CH471052 Genomic DNA. Translation: EAW78264.1 .
    CH471052 Genomic DNA. Translation: EAW78265.1 .
    CH471052 Genomic DNA. Translation: EAW78266.1 .
    CH471052 Genomic DNA. Translation: EAW78267.1 .
    AF002816 mRNA. Translation: AAC78443.1 .
    AF004836 Genomic DNA. Translation: AAC78444.1 . Different initiation.
    AF104913 mRNA. Translation: AAC82471.1 . Different initiation.
    AJ001046 mRNA. Translation: CAA04500.1 .
    CCDSi CCDS3259.1. [Q04637-1 ]
    CCDS3260.1. [Q04637-4 ]
    CCDS3261.1. [Q04637-5 ]
    CCDS46970.2. [Q04637-7 ]
    CCDS54687.1. [Q04637-9 ]
    CCDS54688.1. [Q04637-8 ]
    PIRi A44453.
    RefSeqi NP_004944.3. NM_004953.4. [Q04637-7 ]
    NP_886553.3. NM_182917.4.
    NP_937884.1. NM_198241.2.
    NP_937885.1. NM_198242.2. [Q04637-5 ]
    UniGenei Hs.433750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LJ2 X-ray 2.38 C/D 172-199 [» ]
    1UG3 X-ray 2.24 A/B 1233-1571 [» ]
    2W97 X-ray 2.29 E/F 609-622 [» ]
    4F02 X-ray 2.00 C/F 178-203 [» ]
    DisProti DP00406.
    ProteinModelPortali Q04637.
    SMRi Q04637. Positions 173-199, 751-991, 1234-1592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108296. 60 interactions.
    DIPi DIP-1161N.
    IntActi Q04637. 35 interactions.
    MINTi MINT-135718.
    STRINGi 9606.ENSP00000316879.

    Chemistry

    BindingDBi Q04637.

    PTM databases

    PhosphoSitei Q04637.

    Polymorphism databases

    DMDMi 294862538.

    Proteomic databases

    MaxQBi Q04637.
    PaxDbi Q04637.
    PRIDEi Q04637.

    Protocols and materials databases

    DNASUi 1981.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319274 ; ENSP00000323737 ; ENSG00000114867 . [Q04637-1 ]
    ENST00000342981 ; ENSP00000343450 ; ENSG00000114867 . [Q04637-8 ]
    ENST00000346169 ; ENSP00000316879 ; ENSG00000114867 . [Q04637-1 ]
    ENST00000350481 ; ENSP00000317600 ; ENSG00000114867 . [Q04637-5 ]
    ENST00000352767 ; ENSP00000338020 ; ENSG00000114867 . [Q04637-9 ]
    ENST00000382330 ; ENSP00000371767 ; ENSG00000114867 . [Q04637-9 ]
    ENST00000392537 ; ENSP00000376320 ; ENSG00000114867 . [Q04637-4 ]
    ENST00000414031 ; ENSP00000391935 ; ENSG00000114867 . [Q04637-3 ]
    ENST00000424196 ; ENSP00000416255 ; ENSG00000114867 . [Q04637-9 ]
    ENST00000434061 ; ENSP00000411826 ; ENSG00000114867 . [Q04637-7 ]
    ENST00000435046 ; ENSP00000404754 ; ENSG00000114867 . [Q04637-6 ]
    GeneIDi 1981.
    KEGGi hsa:1981.
    UCSCi uc003fnp.3. human. [Q04637-1 ]
    uc003fnv.4. human.
    uc003fnx.3. human.

    Organism-specific databases

    CTDi 1981.
    GeneCardsi GC03P184032.
    HGNCi HGNC:3296. EIF4G1.
    HPAi CAB014774.
    HPA028487.
    HPA043866.
    MIMi 600495. gene.
    614251. phenotype.
    neXtProti NX_Q04637.
    Orphaneti 2828. Young adult-onset Parkinsonism.
    PharmGKBi PA27722.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301289.
    HOVERGENi HBG052083.
    KOi K03260.
    OMAi GSNWVPR.
    OrthoDBi EOG7D59N2.
    PhylomeDBi Q04637.
    TreeFami TF101527.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.
    REACT_1258. Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
    REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_6772. S6K1 signalling.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
    REACT_931. Ribosomal scanning and start codon recognition.

    Miscellaneous databases

    ChiTaRSi EIF4G1. human.
    EvolutionaryTracei Q04637.
    GeneWikii Eukaryotic_translation_initiation_factor_4_gamma.
    GenomeRNAii 1981.
    NextBioi 35489794.
    PMAP-CutDB Q04637.
    PROi Q04637.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q04637.
    Bgeei Q04637.
    CleanExi HS_EIF4G1.
    Genevestigatori Q04637.

    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. "Amino acid sequence of the human protein synthesis initiation factor eIF-4 gamma."
      Yan R., Rychlik W., Etchison D., Rhoads R.E.
      J. Biol. Chem. 267:23226-23231(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), VARIANT VAL-432.
      Tissue: Brain.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), INTERACTION WITH PABPC1.
    3. "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 C).
    4. "Generation of multiple isoforms of eukaryotic translation initiation factor 4GI by use of alternate translation initiation codons."
      Byrd M.P., Zamora M., Lloyd R.E.
      Mol. Cell. Biol. 22:4499-4511(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8), VARIANTS ALA-161 AND VAL-432, ALTERNATIVE INITIATION.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ALA-161.
      Tissue: Endometrial tumor.
    7. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Rotavirus RNA binding protein NSP3, interacts with eIF-4GI and evicts the poly(A) binding protein from eIF4F."
      Piron M., Vende P., Cohen J., Poncet D.
      EMBO J. 17:5811-5821(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-206, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-234, VARIANT ALA-161, INTERACTION WITH ROTAVIRAL NSP3.
    10. "Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A."
      Imataka H., Sonenberg N.
      Mol. Cell. Biol. 17:6940-6947(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-1599 (ISOFORM 8), INTERACTION WITH EIF4A, VARIANTS ALA-161 AND VAL-432, MUTAGENESIS OF LEU-768; LEU-771; PHE-776; 842-LEU-LEU-843; 851-PHE-GLU-852; LEU-896; ILE-902; LEU-905; ARG-974; PHE-977; LEU-985 AND TRP-990.
    11. "The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 gamma and the translational repressors 4E-binding proteins."
      Mader S., Lee H., Pause A., Sonenberg N.
      Mol. Cell. Biol. 15:4990-4997(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 605-721, INTERACTION WITH EIF4E, MUTAGENESIS OF TYR-612 AND 617-LEU-LEU-618.
    12. De Gregorio E.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 682-912 (ISOFORM 8).
    13. "Mapping the cleavage site in protein synthesis initiation factor eIF-4 gamma of the 2A proteases from human Coxsackievirus and rhinovirus."
      Lamphear B.J., Yan R., Yang F., Waters D., Liebig H.-D., Klump H., Kuechler E., Skern T., Rhoads R.E.
      J. Biol. Chem. 268:19200-19203(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY RHINOVIRUS AND COXSACKIEVIRUS PROTEASE.
    14. "Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function."
      Pause A., Belsham G.J., Gingras A.-C., Donze O., Lin T.-A., Lawrence J.C. Jr., Sonenberg N.
      Nature 371:762-767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4E.
      Tissue: Placenta.
    15. "Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E."
      Haghighat A., Mader S., Pause A., Sonenberg N.
      EMBO J. 14:5701-5709(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF4E AND EIF4EBP1.
    16. "A single amino acid change in protein synthesis initiation factor 4G renders cap-dependent translation resistant to picornaviral 2A proteases."
      Lamphear B.J., Rhoads R.E.
      Biochemistry 35:15726-15733(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLY-682.
    17. "Poliovirus 2A proteinase cleaves directly the eIF-4G subunit of eIF-4F complex."
      Ventoso I., MacMillan S.E., Hershey J.W., Carrasco L.
      FEBS Lett. 435:79-83(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY POLIOVIRUS.
    18. "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.
    19. "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
      Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
      EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKNK1.
    20. "Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation."
      Wakiyama M., Imataka H., Sonenberg N.
      Curr. Biol. 10:1147-1150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PABPC1, MUTAGENESIS OF 174-LYS--LYS-178 AND 184-ASP--GLN-197.
    21. "Multiple portions of poly(A)-binding protein stimulate translation in vivo."
      Gray N.K., Coller J.M., Dickson K.S., Wickens M.
      EMBO J. 19:4723-4733(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PABPC1.
    22. "Extremely efficient cleavage of eIF4G by picornaviral proteinases L and 2A in vitro."
      Glaser W., Skern T.
      FEBS Lett. 480:151-155(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY FMDV AND HRV-2.
    23. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
      Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
      Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MKNK2.
    24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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-1231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "Post-transcriptional regulation of thioredoxin by the stress inducible heterogeneous ribonucleoprotein A18."
      Yang R., Weber D.J., Carrier F.
      Nucleic Acids Res. 34:1224-1236(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CIRBP.
    27. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "Cell stress modulates the function of splicing regulatory protein RBM4 in translation control."
      Lin J.C., Hsu M., Tarn W.Y.
      Proc. Natl. Acad. Sci. U.S.A. 104:2235-2240(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM4.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    30. "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
      Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
      J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROTAVIRUS A NSP3.
    31. "SLIP1, a factor required for activation of histone mRNA translation by the stem-loop binding protein."
      Cakmakci N.G., Lerner R.S., Wagner E.J., Zheng L., Marzluff W.F.
      Mol. Cell. Biol. 28:1182-1194(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MIF4GD.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-223; THR-647; SER-1092 AND SER-1209, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "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].
    34. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1095, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "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-1028; SER-1092; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    39. "Phosphorylation of eukaryotic translation initiation factor 4G1 (eIF4G1) by protein kinase C{alpha} regulates eIF4G1 binding to Mnk1."
      Dobrikov M., Dobrikova E., Shveygert M., Gromeier M.
      Mol. Cell. Biol. 31:2947-2959(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1185.
    40. "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-1028; SER-1092; SER-1145; SER-1147; SER-1185; SER-1187; SER-1209; THR-1211; SER-1231 AND SER-1596, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    41. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    42. "AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation."
      Lee K.H., Kim S.H., Kim H.J., Kim W., Lee H.R., Jung Y., Choi J.H., Hong K.Y., Jang S.K., Kim K.T.
      Nucleic Acids Res. 42:3590-3606(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRPD, RNA-BINDING.
    43. "Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."
      Groft C.M., Burley S.K.
      Mol. Cell 9:1273-1283(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 172-199 IN COMPLEX WITH ROTAVIRAL NSP3, INTERACTION WITH PABPC1, MUTAGENESIS OF ILE-180; ILE-182; ILE-192 AND ILE-196.
    44. "Two structurally atypical HEAT domains in the C-terminal portion of human eIF4G support binding to eIF4A and Mnk1."
      Bellsolell L., Cho-Park P.F., Poulin F., Sonenberg N., Burley S.K.
      Structure 14:913-923(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 1234-1571.
    45. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-696.
    46. "Translation initiator EIF4G1 mutations in familial Parkinson disease."
      Chartier-Harlin M.C., Dachsel J.C., Vilarino-Guell C., Lincoln S.J., Lepretre F., Hulihan M.M., Kachergus J., Milnerwood A.J., Tapia L., Song M.S., Le Rhun E., Mutez E., Larvor L., Duflot A., Vanbesien-Mailliot C., Kreisler A., Ross O.A., Nishioka K.
      , Soto-Ortolaza A.I., Cobb S.A., Melrose H.L., Behrouz B., Keeling B.H., Bacon J.A., Hentati E., Williams L., Yanagiya A., Sonenberg N., Lockhart P.J., Zubair A.C., Uitti R.J., Aasly J.O., Krygowska-Wajs A., Opala G., Wszolek Z.K., Frigerio R., Maraganore D.M., Gosal D., Lynch T., Hutchinson M., Bentivoglio A.R., Valente E.M., Nichols W.C., Pankratz N., Foroud T., Gibson R.A., Hentati F., Dickson D.W., Destee A., Farrer M.J.
      Am. J. Hum. Genet. 89:398-406(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PARK18 VAL-502 AND HIS-1205, VARIANTS SER-71; ALA-161; CYS-311; VAL-432; 466-GLY--ALA-468 DEL; CYS-686; VAL-806; SER-829; ARG-1164; TRP-1197; ALA-1229; PRO-1233 AND SER-1257.

    Entry informationi

    Entry nameiIF4G1_HUMAN
    AccessioniPrimary (citable) accession number: Q04637
    Secondary accession number(s): D3DNT2
    , D3DNT4, D3DNT5, E9PFM1, G5E9S1, O43177, O95066, Q5HYG0, Q6ZN21, Q8N102
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 165 of the entry and version 4 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 3
      Human chromosome 3: 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