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O00425

- IF2B3_HUMAN

UniProt

O00425 - IF2B3_HUMAN

Protein

Insulin-like growth factor 2 mRNA-binding protein 3

Gene

IGF2BP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    RNA-binding factor that may recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs.2 Publications

    GO - Molecular functioni

    1. mRNA 3'-UTR binding Source: UniProtKB
    2. mRNA 5'-UTR binding Source: BHF-UCL
    3. nucleotide binding Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. RNA binding Source: ProtInc
    7. translation regulator activity Source: BHF-UCL

    GO - Biological processi

    1. anatomical structure morphogenesis Source: ProtInc
    2. gene expression Source: Reactome
    3. mRNA transport Source: UniProtKB-KW
    4. negative regulation of translation Source: BHF-UCL
    5. regulation of cytokine biosynthetic process Source: BHF-UCL
    6. translation Source: ProtInc

    Keywords - Biological processi

    mRNA transport, Translation regulation, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_22166. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin-like growth factor 2 mRNA-binding protein 3
    Short name:
    IGF2 mRNA-binding protein 3
    Short name:
    IMP-3
    Alternative name(s):
    IGF-II mRNA-binding protein 3
    KH domain-containing protein overexpressed in cancer
    Short name:
    hKOC
    VICKZ family member 3
    Gene namesi
    Name:IGF2BP3
    Synonyms:IMP3, KOC1, VICKZ3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:28868. IGF2BP3.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. Colocalized with CD44 mRNA in RNP granules. In response to cellular stress, such as oxidative stress, recruited to stress granules.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131K → E: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-294; 422-E-E-423 and 505-E-E-506. 1 Publication
    Mutagenesisi294 – 2941K → E: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; 422-E-E-423 and 505-E-E-506. 1 Publication
    Mutagenesisi423 – 4242KQ → EE: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 505-E-E-506. 1 Publication
    Mutagenesisi505 – 5062KG → EE: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 422-E-E-423. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394576.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 579579Insulin-like growth factor 2 mRNA-binding protein 3PRO_0000282538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei184 – 1841Phosphoserine1 Publication
    Modified residuei187 – 1871Phosphoserine1 Publication
    Modified residuei189 – 1891Phosphoserine1 Publication
    Modified residuei528 – 5281Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00425.
    PaxDbiO00425.
    PRIDEiO00425.

    PTM databases

    PhosphoSiteiO00425.

    Expressioni

    Tissue specificityi

    Expressed in fetal liver, fetal lung, fetal kidney, fetal thymus, fetal placenta, fetal follicles of ovary and gonocytes of testis, growing oocytes, spermatogonia and semen (at protein level). Expressed in cervix adenocarcinoma, in testicular, pancreatic and renal-cell carcinomas (at protein level). Expressed ubiquitously during fetal development at 8 and 14 weeks of gestation. Expressed in ovary, testis, brain, placenta, pancreatic cancer tissues and pancreatic cancer cell lines.8 Publications

    Gene expression databases

    ArrayExpressiO00425.
    BgeeiO00425.
    CleanExiHS_IGF2BP3.
    HS_IMP3.
    GenevestigatoriO00425.

    Organism-specific databases

    HPAiHPA002037.

    Interactioni

    Subunit structurei

    Can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. Interacts with IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU.2 Publications

    Protein-protein interaction databases

    BioGridi115887. 59 interactions.
    IntActiO00425. 17 interactions.
    MINTiMINT-2997694.
    STRINGi9606.ENSP00000258729.

    Structurei

    Secondary structure

    1
    579
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi83 – 886
    Beta strandi90 – 923
    Helixi94 – 10411
    Beta strandi107 – 1137
    Beta strandi116 – 12813
    Helixi129 – 13911
    Beta strandi150 – 1534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E44NMR-A73-161[»]
    ProteinModelPortaliO00425.
    SMRiO00425. Positions 1-161, 198-349, 406-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00425.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 7574RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini81 – 15676RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini195 – 26066KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini276 – 34368KH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 47066KH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini487 – 55367KH 4PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    All KH domains contribute binding to target mRNA. They are also required for RNA-dependent homo- and heterooligomerization. The integrity of KH domains seems not to be required for localization to stress granules.2 Publications

    Sequence similaritiesi

    Belongs to the RRM IMP/VICKZ family.Curated
    Contains 4 KH domains.PROSITE-ProRule annotation
    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG249985.
    HOGENOMiHOG000000675.
    HOVERGENiHBG052725.
    InParanoidiO00425.
    KOiK13197.
    OMAiNPSQQPR.
    OrthoDBiEOG7T7GSK.
    PhylomeDBiO00425.
    TreeFamiTF320229.

    Family and domain databases

    Gene3Di3.30.1370.10. 4 hits.
    3.30.70.330. 2 hits.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00013. KH_1. 4 hits.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 4 hits.
    SM00360. RRM. 2 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 4 hits.
    PROSITEiPS50084. KH_TYPE_1. 4 hits.
    PS50102. RRM. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00425-1) [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

    MNKLYIGNLS ENAAPSDLES IFKDAKIPVS GPFLVKTGYA FVDCPDESWA    50
    LKAIEALSGK IELHGKPIEV EHSVPKRQRI RKLQIRNIPP HLQWEVLDSL 100
    LVQYGVVESC EQVNTDSETA VVNVTYSSKD QARQALDKLN GFQLENFTLK 150
    VAYIPDEMAA QQNPLQQPRG RRGLGQRGSS RQGSPGSVSK QKPCDLPLRL 200
    LVPTQFVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA EKSITILSTP 250
    EGTSAACKSI LEIMHKEAQD IKFTEEIPLK ILAHNNFVGR LIGKEGRNLK 300
    KIEQDTDTKI TISPLQELTL YNPERTITVK GNVETCAKAE EEIMKKIRES 350
    YENDIASMNL QAHLIPGLNL NALGLFPPTS GMPPPTSGPP SAMTPPYPQF 400
    EQSETETVHL FIPALSVGAI IGKQGQHIKQ LSRFAGASIK IAPAEAPDAK 450
    VRMVIITGPP EAQFKAQGRI YGKIKEENFV SPKEEVKLEA HIRVPSFAAG 500
    RVIGKGGKTV NELQNLSSAE VVVPRDQTPD ENDQVVVKIT GHFYACQVAQ 550
    RKIQEILTQV KQHQQQKALQ SGPPQSRRK 579
    Length:579
    Mass (Da):63,705
    Last modified:July 28, 2009 - v2
    Checksum:i78884F56A9D98CDE
    GO
    Isoform 2 (identifier: O00425-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-381: Missing.

    Show »
    Length:198
    Mass (Da):21,630
    Checksum:i69BEB7C296373BE7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101L → Q in AAD09223. (PubMed:9178771)Curated
    Sequence conflicti410 – 4101L → Q in AAC35208. (PubMed:9178771)Curated
    Sequence conflicti494 – 4941V → A in CAH56186. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 381381Missing in isoform 2. 1 PublicationVSP_024172Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76705 mRNA. Translation: AAD09223.1.
    U97188 mRNA. Translation: AAC35208.1.
    BX640800 mRNA. Translation: CAE45883.1.
    BX648488 mRNA. Translation: CAH56186.1.
    AC005082 Genomic DNA. No translation available.
    AC021876 Genomic DNA. No translation available.
    AC079780 Genomic DNA. No translation available.
    BC065269 mRNA. Translation: AAH65269.1.
    CCDSiCCDS5382.1. [O00425-1]
    RefSeqiNP_006538.2. NM_006547.2. [O00425-1]
    UniGeneiHs.700696.

    Genome annotation databases

    EnsembliENST00000258729; ENSP00000258729; ENSG00000136231. [O00425-1]
    GeneIDi10643.
    KEGGihsa:10643.
    UCSCiuc003swf.3. human. [O00425-2]
    uc003swg.3. human. [O00425-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U76705 mRNA. Translation: AAD09223.1 .
    U97188 mRNA. Translation: AAC35208.1 .
    BX640800 mRNA. Translation: CAE45883.1 .
    BX648488 mRNA. Translation: CAH56186.1 .
    AC005082 Genomic DNA. No translation available.
    AC021876 Genomic DNA. No translation available.
    AC079780 Genomic DNA. No translation available.
    BC065269 mRNA. Translation: AAH65269.1 .
    CCDSi CCDS5382.1. [O00425-1 ]
    RefSeqi NP_006538.2. NM_006547.2. [O00425-1 ]
    UniGenei Hs.700696.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E44 NMR - A 73-161 [» ]
    ProteinModelPortali O00425.
    SMRi O00425. Positions 1-161, 198-349, 406-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115887. 59 interactions.
    IntActi O00425. 17 interactions.
    MINTi MINT-2997694.
    STRINGi 9606.ENSP00000258729.

    PTM databases

    PhosphoSitei O00425.

    Proteomic databases

    MaxQBi O00425.
    PaxDbi O00425.
    PRIDEi O00425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258729 ; ENSP00000258729 ; ENSG00000136231 . [O00425-1 ]
    GeneIDi 10643.
    KEGGi hsa:10643.
    UCSCi uc003swf.3. human. [O00425-2 ]
    uc003swg.3. human. [O00425-1 ]

    Organism-specific databases

    CTDi 10643.
    GeneCardsi GC07M023316.
    HGNCi HGNC:28868. IGF2BP3.
    HPAi HPA002037.
    MIMi 608259. gene.
    neXtProti NX_O00425.
    PharmGKBi PA128394576.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249985.
    HOGENOMi HOG000000675.
    HOVERGENi HBG052725.
    InParanoidi O00425.
    KOi K13197.
    OMAi NPSQQPR.
    OrthoDBi EOG7T7GSK.
    PhylomeDBi O00425.
    TreeFami TF320229.

    Enzyme and pathway databases

    Reactomei REACT_22166. Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.

    Miscellaneous databases

    ChiTaRSi Igf2bp3. human.
    EvolutionaryTracei O00425.
    GeneWikii IGF2BP3.
    GenomeRNAii 10643.
    NextBioi 40451.
    PROi O00425.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00425.
    Bgeei O00425.
    CleanExi HS_IGF2BP3.
    HS_IMP3.
    Genevestigatori O00425.

    Family and domain databases

    Gene3Di 3.30.1370.10. 4 hits.
    3.30.70.330. 2 hits.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00013. KH_1. 4 hits.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 4 hits.
    SM00360. RRM. 2 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 4 hits.
    PROSITEi PS50084. KH_TYPE_1. 4 hits.
    PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a gene highly overexpressed in cancer coding for a novel KH-domain containing protein."
      Mueller-Pillasch F., Lacher U., Wallrapp C., Micha A., Zimmerhackl F., Hameister H., Varga G., Friess H., Buechler M., Beger H.G., Vila M.R., Adler G., Gress T.M.
      Oncogene 14:2729-2733(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Pancreas and Pancreatic cancer.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Endometrial tumor.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Eye.
    5. "Expression of the highly conserved RNA binding protein KOC in embryogenesis."
      Mueller-Pillasch F., Pohl B., Wilda M., Lacher U., Beil M., Wallrapp C., Hameister H., Knoechel W., Adler G., Gress T.M.
      Mech. Dev. 88:95-99(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development."
      Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M., Nielsen F.C.
      Mol. Cell. Biol. 19:1262-1270(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING.
    7. "Autoimmune responses to mRNA binding proteins p62 and Koc in diverse malignancies."
      Zhang J.-Y., Chan E.K., Peng X.-X., Lu M., Wang X., Mueller F., Tan E.M.
      Clin. Immunol. 100:149-156(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION AS A CARCINOMA ANTIGEN.
    8. "Characterisation of the growth regulating gene IMP3, a candidate for Silver-Russell syndrome."
      Monk D., Bentley L., Beechey C., Hitchins M., Peters J., Preece M.A., Stanier P., Moore G.E.
      J. Med. Genet. 39:575-581(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    9. Cited for: SUBCELLULAR LOCATION.
    10. "VICKZ proteins: a multi-talented family of regulatory RNA-binding proteins."
      Yisraeli J.K.
      Biol. Cell 97:87-96(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "KOC (K homology domain containing protein overexpressed in cancer): a novel molecular marker that distinguishes between benign and malignant lesions of the pancreas."
      Yantiss R.K., Woda B.A., Fanger G.R., Kalos M., Whalen G.F., Tada H., Andersen D.K., Rock K.L., Dresser K.
      Diagn. Mol. Pathol. 29:188-195(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    12. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "RNA-binding IMPs promote cell adhesion and invadopodia formation."
      Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., Nielsen F.C.
      EMBO J. 25:1456-1468(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
    14. "Analysis of RNA-binding protein IMP3 to predict metastasis and prognosis of renal-cell carcinoma: a retrospective study."
      Jiang Z., Chu P.G., Woda B.A., Rock K.L., Liu Q., Hsieh C.-C., Li C., Chen W., Duan H.O., McDougal S., Wu C.-L.
      Lancet Oncol. 7:556-564(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    15. "IMP3 is a novel biomarker for adenocarcinoma in situ of the uterine cervix: an immunohistochemical study in comparison with p16(INK4a) expression."
      Li C., Rock K.L., Woda B.A., Jiang Z., Fraire A.E., Dresser K.
      Mod. Pathol. 20:242-247(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. Cited for: INTERACTION WITH IGF2BP1.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "ZBP1 recognition of beta-actin zipcode induces RNA looping."
      Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H.
      Genes Dev. 24:148-158(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, DOMAIN.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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-184; SER-187; SER-189 AND THR-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
      Wachter K., Kohn M., Stohr N., Huttelmaier S.
      Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9 AND HNRNPU, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF 213-LYS-GLU-214; 294-LYS-GLU-295; 423-LYS-LYS-424 AND 505-LYS-GLY-506.
    23. "Solution structure of RNA binding domain in insulin-like growth factor 2 mRNA-binding protein 3."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUN-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 73-161.

    Entry informationi

    Entry nameiIF2B3_HUMAN
    AccessioniPrimary (citable) accession number: O00425
    Secondary accession number(s): A0A4Z5
    , Q63HM0, Q6MZZ2, Q86VB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 124 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

    Miscellaneous

    Autoantibodies against IGF2BP3 are detected in sera from some patients with a variety of carcinomas.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3