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P78344

- IF4G2_HUMAN

UniProt

P78344 - IF4G2_HUMAN

Protein

Eukaryotic translation initiation factor 4 gamma 2

Gene

EIF4G2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    Functioni

    Appears to play a role in the switch from cap-dependent to IRES-mediated translation during mitosis, apoptosis and viral infection. Cleaved by some caspases and viral proteases.4 Publications

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle arrest Source: ProtInc
    2. cell death Source: ProtInc
    3. cytokine-mediated signaling pathway Source: Reactome
    4. regulation of translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor, Repressor

    Keywords - Biological processi

    Protein biosynthesis, Translation regulation

    Enzyme and pathway databases

    ReactomeiREACT_115831. ISG15 antiviral mechanism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic translation initiation factor 4 gamma 2
    Short name:
    eIF-4-gamma 2
    Short name:
    eIF-4G 2
    Short name:
    eIF4G 2
    Alternative name(s):
    Death-associated protein 5
    Short name:
    DAP-5
    p97
    Gene namesi
    Name:EIF4G2Imported
    Synonyms:DAP51 Publication
    ORF Names:OK/SW-cl.75
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:3297. EIF4G2.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27723.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 907907Eukaryotic translation initiation factor 4 gamma 2PRO_0000213325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Modified residuei395 – 3951Phosphoserine2 Publications
    Modified residuei508 – 5081Phosphothreonine2 Publications
    Modified residuei514 – 5141Phosphothreonine2 Publications
    Modified residuei902 – 9021Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation; hyperphosphorylated during mitosis.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP78344.
    PaxDbiP78344.
    PRIDEiP78344.

    PTM databases

    PhosphoSiteiP78344.

    Miscellaneous databases

    PMAP-CutDBP78344.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all adult tissues examined, with high levels in skeletal muscle and heart. Also expressed in fetal brain, lung, liver and kidney.3 Publications

    Gene expression databases

    ArrayExpressiP78344.
    BgeeiP78344.
    CleanExiHS_EIF4G2.
    GenevestigatoriP78344.

    Organism-specific databases

    HPAiCAB005163.
    HPA006773.
    HPA016965.

    Interactioni

    Subunit structurei

    Interacts with the serine/threonine protein kinases MKNK1 and MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P299914EBI-296519,EBI-8826747From a different organism.
    EIF2S2P200424EBI-296519,EBI-711977
    EIF4A1P608423EBI-296519,EBI-73449

    Protein-protein interaction databases

    BioGridi108297. 21 interactions.
    DIPiDIP-31366N.
    IntActiP78344. 17 interactions.
    MINTiMINT-1182471.
    STRINGi9606.ENSP00000340281.

    Structurei

    Secondary structure

    1
    907
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi68 – 8619
    Turni90 – 923
    Helixi93 – 10311
    Helixi108 – 12417
    Helixi126 – 1283
    Helixi129 – 14214
    Helixi162 – 18221
    Helixi196 – 21823
    Turni219 – 2213
    Helixi225 – 23612
    Beta strandi240 – 2423
    Helixi244 – 2463
    Helixi248 – 26518
    Helixi268 – 2703
    Helixi271 – 28212
    Turni283 – 2864
    Helixi292 – 30615
    Turni307 – 3093
    Helixi541 – 55818
    Helixi561 – 57111
    Helixi575 – 5773
    Helixi578 – 59013
    Helixi594 – 60916
    Helixi615 – 62713
    Helixi629 – 6357
    Helixi639 – 65214
    Helixi658 – 6658
    Helixi666 – 6683
    Turni669 – 6724
    Helixi673 – 68412
    Helixi687 – 69711
    Helixi702 – 7043
    Helixi707 – 7093
    Helixi712 – 72211
    Helixi725 – 7273
    Helixi731 – 74313
    Helixi747 – 75711
    Helixi760 – 7645
    Helixi766 – 78419
    Helixi799 – 82022
    Helixi824 – 84017
    Helixi847 – 85711
    Helixi863 – 8719
    Helixi880 – 89516

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3D3MX-ray1.90A/B730-897[»]
    3L6AX-ray2.00A540-897[»]
    4IULX-ray2.30A/B61-323[»]
    ProteinModelPortaliP78344.
    SMRiP78344. Positions 78-311, 540-897.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78344.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini78 – 308231MIF4GPROSITE-ProRule annotationAdd
    BLAST
    Domaini543 – 666124MIPROSITE-ProRule annotationAdd
    BLAST
    Domaini720 – 904185W2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG301289.
    HOVERGENiHBG052084.
    InParanoidiP78344.
    KOiK03260.
    OrthoDBiEOG73FQMQ.
    PhylomeDBiP78344.

    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78344-1) [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

    MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW    50
    IPARSTRRDD NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL 100
    LNVGVESKLI LKGVILLIVD KALEEPKYSS LYAQLCLRLA EDAPNFDGPA 150
    AEGQPGQKQS TTFRRLLISK LQDEFENRTR NVDVYDKREN PLLPEEEEQR 200
    AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK RVQLKDMGED 250
    LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD 300
    TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGMRSDF 350
    FLEGPFMPPR MKMDRDPLGG LADMFGQMPG SGIGTGPGVI QDRFSPTMGR 400
    HRSNQLFNGH GGHIMPPTQS QFGEMGGKFM KSQGLSQLYH NQSQGLLSQL 450
    QGQSKDMPPR FSKKGQLNAD EISLRPAQSF LMNKNQVPKL QPQITMIPPS 500
    AQPPRTQTPP LGQTPQLGLK TNPPLIQEKP AKTSKKPPPS KEELLKLTET 550
    VVTEYLNSGN ANEAVNGVRE MRAPKHFLPE MLSKVIILSL DRSDEDKEKA 600
    SSLISLLKQE GIATSDNFMQ AFLNVLDQCP KLEVDIPLVK SYLAQFAARA 650
    IISELVSISE LAQPLESGTH FPLFLLCLQQ LAKLQDREWL TELFQQSKVN 700
    MQKMLPEIDQ NKDRMLEILE GKGLSFLFPL LKLEKELLKQ IKLDPSPQTI 750
    YKWIKDNISP KLHVDKGFVN ILMTSFLQYI SSEVNPPSDE TDSSSAPSKE 800
    QLEQEKQLLL SFKPVMQKFL HDHVDLQVSA LYALQVHCYN SNFPKGMLLR 850
    FFVHFYDMEI IEEEAFLAWK EDITQEFPGK GKALFQVNQW LTWLETAEEE 900
    ESEEEAD 907
    Length:907
    Mass (Da):102,362
    Last modified:May 1, 1997 - v1
    Checksum:i4EF050B5EEA4DF91
    GO
    Isoform 2 (identifier: P78344-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         434-471: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:869
    Mass (Da):98,150
    Checksum:iF400E1E28654A2E4
    GO

    Sequence cautioni

    The sequence BAD97268.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.
    The sequence CAA61857.1 differs from that shown. Reason: Unusual initiator. The initiator methionine is coded by a non-canonical GTG valine codon.
    The sequence BAB93515.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691S → P in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti233 – 2331K → Q in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti245 – 2451K → Q in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti351 – 3511F → L in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti441 – 4411N → S in AAH18746. (PubMed:15489334)Curated
    Sequence conflicti531 – 5311A → G in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti534 – 5341S → N in AAH43149. (PubMed:15489334)Curated
    Sequence conflicti613 – 6131A → G in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti861 – 8611I → S in AAC51166. (PubMed:9030685)Curated
    Sequence conflicti899 – 8991E → G in AAC51166. (PubMed:9030685)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti236 – 2361L → M.
    Corresponds to variant rs34885591 [ dbSNP | Ensembl ].
    VAR_048923

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei434 – 47138Missing in isoform 2. 1 PublicationVSP_038726Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73824 mRNA. Translation: AAB49973.1.
    U76111 mRNA. Translation: AAC51166.1.
    X89713 mRNA. Translation: CAA61857.1. Sequence problems.
    AK223548 mRNA. Translation: BAD97268.1. Sequence problems.
    AC116535 Genomic DNA. No translation available.
    BC014930 mRNA. Translation: AAH14930.2.
    BC018746 mRNA. Translation: AAH18746.1.
    BC018975 mRNA. Translation: AAH18975.1.
    BC039851 mRNA. Translation: AAH39851.1.
    BC043149 mRNA. Translation: AAH43149.2.
    BC111415 mRNA. Translation: AAI11416.1.
    BC111548 mRNA. Translation: AAI11549.2.
    AB063323 mRNA. Translation: BAB93515.1. Different initiation.
    CCDSiCCDS31428.1. [P78344-1]
    CCDS41618.1. [P78344-2]
    RefSeqiNP_001036024.3. NM_001042559.2. [P78344-2]
    NP_001166176.1. NM_001172705.1. [P78344-1]
    NP_001409.3. NM_001418.3. [P78344-1]
    UniGeneiHs.183684.

    Genome annotation databases

    EnsembliENST00000339995; ENSP00000340281; ENSG00000110321.
    GeneIDi1982.
    KEGGihsa:1982.
    UCSCiuc001mjb.3. human. [P78344-1]
    uc001mjd.3. human. [P78344-2]

    Polymorphism databases

    DMDMi30315906.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U73824 mRNA. Translation: AAB49973.1 .
    U76111 mRNA. Translation: AAC51166.1 .
    X89713 mRNA. Translation: CAA61857.1 . Sequence problems.
    AK223548 mRNA. Translation: BAD97268.1 . Sequence problems.
    AC116535 Genomic DNA. No translation available.
    BC014930 mRNA. Translation: AAH14930.2 .
    BC018746 mRNA. Translation: AAH18746.1 .
    BC018975 mRNA. Translation: AAH18975.1 .
    BC039851 mRNA. Translation: AAH39851.1 .
    BC043149 mRNA. Translation: AAH43149.2 .
    BC111415 mRNA. Translation: AAI11416.1 .
    BC111548 mRNA. Translation: AAI11549.2 .
    AB063323 mRNA. Translation: BAB93515.1 . Different initiation.
    CCDSi CCDS31428.1. [P78344-1 ]
    CCDS41618.1. [P78344-2 ]
    RefSeqi NP_001036024.3. NM_001042559.2. [P78344-2 ]
    NP_001166176.1. NM_001172705.1. [P78344-1 ]
    NP_001409.3. NM_001418.3. [P78344-1 ]
    UniGenei Hs.183684.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3D3M X-ray 1.90 A/B 730-897 [» ]
    3L6A X-ray 2.00 A 540-897 [» ]
    4IUL X-ray 2.30 A/B 61-323 [» ]
    ProteinModelPortali P78344.
    SMRi P78344. Positions 78-311, 540-897.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108297. 21 interactions.
    DIPi DIP-31366N.
    IntActi P78344. 17 interactions.
    MINTi MINT-1182471.
    STRINGi 9606.ENSP00000340281.

    PTM databases

    PhosphoSitei P78344.

    Polymorphism databases

    DMDMi 30315906.

    Proteomic databases

    MaxQBi P78344.
    PaxDbi P78344.
    PRIDEi P78344.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339995 ; ENSP00000340281 ; ENSG00000110321 .
    GeneIDi 1982.
    KEGGi hsa:1982.
    UCSCi uc001mjb.3. human. [P78344-1 ]
    uc001mjd.3. human. [P78344-2 ]

    Organism-specific databases

    CTDi 1982.
    GeneCardsi GC11M010775.
    HGNCi HGNC:3297. EIF4G2.
    HPAi CAB005163.
    HPA006773.
    HPA016965.
    MIMi 602325. gene.
    neXtProti NX_P78344.
    PharmGKBi PA27723.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG301289.
    HOVERGENi HBG052084.
    InParanoidi P78344.
    KOi K03260.
    OrthoDBi EOG73FQMQ.
    PhylomeDBi P78344.

    Enzyme and pathway databases

    Reactomei REACT_115831. ISG15 antiviral mechanism.

    Miscellaneous databases

    ChiTaRSi EIF4G2. human.
    EvolutionaryTracei P78344.
    GeneWikii EIF4G2.
    GenomeRNAii 1982.
    NextBioi 8025.
    PMAP-CutDB P78344.
    PROi P78344.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78344.
    Bgeei P78344.
    CleanExi HS_EIF4G2.
    Genevestigatori P78344.

    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 new translational regulator with homology to eukaryotic translation initiation factor 4G."
      Imataka H., Olsen H.S., Sonenberg N.
      EMBO J. 16:817-825(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION OF A NON-AUG INITIATOR START CODON, INTERACTION WITH EIF4A AND EIF3.
      Tissue: Placenta1 Publication.
    2. "A novel translational repressor mRNA is edited extensively in livers containing tumors caused by the transgene expression of the apoB mRNA-editing enzyme."
      Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.
      Genes Dev. 11:321-333(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH EIF4A.
      Tissue: Liver1 Publication.
    3. "DAP-5, a novel homolog of eukaryotic translation initiation factor 4G isolated as a putative modulator of gamma interferon-induced programmed cell death."
      Levy-Strumpf N., Deiss L.P., Berissi H., Kimchi A.
      Mol. Cell. Biol. 17:1615-1625(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Kidney1 Publication.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1 AND 2).
      Tissue: Retinal pigment epithelium, Skin1 Publication and Testis1 Publication.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12, ACETYLATION AT MET-1.
      Tissue: Platelet1 Publication.
    8. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-907.
      Tissue: Colon adenocarcinoma1 Publication.
    9. "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.
    10. "Suppression of cap-dependent translation in mitosis."
      Pyronnet S., Dostie J., Sonenberg N.
      Genes Dev. 15:2083-2093(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    11. "The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins."
      Henis-Korenblit S., Shani G., Sines T., Marash L., Shohat G., Kimchi A.
      Proc. Natl. Acad. Sci. U.S.A. 99:5400-5405(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    14. "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.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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-508, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395 AND SER-902, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIF4G2_HUMAN
    AccessioniPrimary (citable) accession number: P78344
    Secondary accession number(s): O60877
    , P78404, Q0VH00, Q0VH01, Q2NKW9, Q49A79, Q53EU1, Q58EZ2, Q8NI71, Q96C16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 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

    Miscellaneous

    This gene has been shown to be extensively edited in the liver of APOBEC1 transgenic animal model. Its aberrant editing could contribute to the potent oncogenesis induced by overexpression of APOBEC1. The aberrant edited sequence, called NAT1, is likely to be a fundamental translational repressor.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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