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Q9Y6M1

- IF2B2_HUMAN

UniProt

Q9Y6M1 - IF2B2_HUMAN

Protein

Insulin-like growth factor 2 mRNA-binding protein 2

Gene

IGF2BP2

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 (03 Mar 2009)
      Previous versions | rss
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    Functioni

    RNA-binding factor that 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 By similarity. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts.By similarity2 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. 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

    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 2
    Short name:
    IGF2 mRNA-binding protein 2
    Short name:
    IMP-2
    Alternative name(s):
    Hepatocellular carcinoma autoantigen p62
    IGF-II mRNA-binding protein 2
    VICKZ family member 2
    Gene namesi
    Name:IGF2BP2
    Synonyms:IMP2, VICKZ2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:28867. IGF2BP2.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytoskeleton Source: BHF-UCL
    3. cytosol Source: Reactome
    4. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi211 – 2111K → E: Significantly impaired binding to ACTB transcript, but little effect on MYC transcript binding, accumulation in the nucleus; when associated with E-292. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-292; 445-E-E-446 and 526-E-E-527. 1 Publication
    Mutagenesisi292 – 2921K → E: Significantly impaired binding to ACTB transcript, but little effect on MYC transcript binding, accumulation in the nucleus; when associated with E-211. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; 445-E-E-445 and 526-E-E-527. 1 Publication
    Mutagenesisi445 – 4462KK → EE: Significantly impaired binding to ACTB and MYC transcripts; when associated with 527-E-E-528. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 527-E-E-528.
    Mutagenesisi527 – 5282KG → EE: Significantly impaired binding to ACTB and MYC transcripts; when associated with 445-E-E-446. Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, almost complete loss of ACTB and MYC transcript binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding and perturbed subcellular location, including accumulation in the nucleus and loss of localization to stress granules; when associated with E-211; E-292 and 445-E-E-446.

    Organism-specific databases

    PharmGKBiPA128394577.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 599599Insulin-like growth factor 2 mRNA-binding protein 2PRO_0000244496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei162 – 1621Phosphoserine2 Publications
    Modified residuei164 – 1641Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6M1.
    PaxDbiQ9Y6M1.
    PRIDEiQ9Y6M1.

    PTM databases

    PhosphoSiteiQ9Y6M1.

    Expressioni

    Tissue specificityi

    Expressed in oocytes, granulosa cells of small and growing follicles, Leydig cells, spermatogonia and semen (at protein level). Expressed in testicular cancer (at protein level). Expressed weakly in heart, placenta, skeletal muscle, bone marrow, colon, kidney, salivary glands, testis and pancreas. Detected in fetal liver, fetal ovary, gonocytes and interstitial cells of the testis.2 Publications

    Gene expression databases

    ArrayExpressiQ9Y6M1.
    BgeeiQ9Y6M1.
    CleanExiHS_IGF2BP2.
    GenevestigatoriQ9Y6M1.

    Organism-specific databases

    HPAiCAB017126.
    HPA035145.

    Interactioni

    Subunit structurei

    Can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD and IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HNRNPDQ14103-44EBI-1024419,EBI-432545

    Protein-protein interaction databases

    BioGridi115888. 25 interactions.
    IntActiQ9Y6M1. 21 interactions.
    MINTiMINT-6946387.
    STRINGi9606.ENSP00000371634.

    Structurei

    Secondary structure

    1
    599
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Helixi16 – 2510
    Beta strandi34 – 374
    Beta strandi40 – 434
    Helixi48 – 5811
    Turni59 – 613
    Beta strandi70 – 734

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQHNMR-A2-81[»]
    ProteinModelPortaliQ9Y6M1.
    SMRiQ9Y6M1. Positions 2-158, 198-337, 427-584.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6M1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7674RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini82 – 15776RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 25866KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini274 – 34168KH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini427 – 49266KH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini509 – 57567KH 4PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. The contribution to RNA-binding of individual KH domains may be target-specific. KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and 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.
    KOiK17392.
    OrthoDBiEOG7T7GSK.
    PhylomeDBiQ9Y6M1.
    TreeFamiTF320229.

    Family and domain databases

    Gene3Di3.30.1370.10. 4 hits.
    3.30.70.330. 2 hits.
    InterProiIPR028743. IGF2BP2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PANTHERiPTHR10288:SF93. PTHR10288:SF93. 1 hit.
    PfamiPF00013. KH_1. 4 hits.
    PF00076. RRM_1. 2 hits.
    [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 (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing and alternative initiation. Align

    Isoform 1 (identifier: Q9Y6M1-2) [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

    MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW    50
    AIRAIETLSG KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG 100
    LLAQYGTVEN VEQVNTDTET AVVNVTYATR EEAKIAMEKL SGHQFENYSF 150
    KISYIPDEEV SSPSPPQRAQ RGDHSSREQG HAPGGTSQAR QIDFPLRILV 200
    PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK PVTIHATPEG 250
    TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI 300
    EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE 350
    NDMLAVNQQA NLIPGLNLSA LGIFSTGLSV LSPPAGPRGA PPAAPYHPFT 400
    THSGYFSSLY PHHQFGPFPH HHSYPEQEIV NLFIPTQAVG AIIGKKGAHI 450
    KQLARFAGAS IKIAPAEGPD VSERMVIITG PPEAQFKAQG RIFGKLKEEN 500
    FFNPKEEVKL EAHIRVPSST AGRVIGKGGK TVNELQNLTS AEVIVPRDQT 550
    PDENEEVIVR IIGHFFASQT AQRKIREIVQ QVKQQEQKYP QGVASQRSK 599
    Length:599
    Mass (Da):66,121
    Last modified:March 3, 2009 - v2
    Checksum:iEA656F8733BBB39A
    GO
    Isoform 2 (identifier: Q9Y6M1-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         358-400: Missing.

    Show »
    Length:556
    Mass (Da):61,842
    Checksum:i1EDEFB100443DDC4
    GO
    Isoform 3 (identifier: Q9Y6M1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG

    Show »
    Length:536
    Mass (Da):59,001
    Checksum:i733536C7BDAD8AF5
    GO
    Isoform 4 (identifier: Q9Y6M1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
         113-113: Q → QVFAFSL

    Show »
    Length:542
    Mass (Da):59,666
    Checksum:iF1D98409DD8AE45D
    GO
    Isoform 5 (identifier: Q9Y6M1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MMNKLYIGNL...VDYSVSKKLR → MFSCPGHYHVDGFLNPG
         358-400: Missing.

    Show »
    Length:493
    Mass (Da):54,722
    Checksum:i36BF971E2C4296F7
    GO
    Isoform 6 (identifier: Q9Y6M1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: Missing.

    Note: Generated by alternative initiation at Met-69.

    Show »
    Length:531
    Mass (Da):58,578
    Checksum:i1F5FD1AC97743530
    GO

    Sequence cautioni

    The sequence AAH21290.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080MMNKL…SKKLR → MFSCPGHYHVDGFLNPG in isoform 3, isoform 4 and isoform 5. 1 PublicationVSP_036550Add
    BLAST
    Alternative sequencei1 – 6868Missing in isoform 6. CuratedVSP_043699Add
    BLAST
    Alternative sequencei113 – 1131Q → QVFAFSL in isoform 4. 1 PublicationVSP_036552
    Alternative sequencei358 – 40043Missing in isoform 2 and isoform 5. 2 PublicationsVSP_036553Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF057352 mRNA. Translation: AAD31596.1.
    EU408701 mRNA. Translation: ACB86625.1.
    EU408702 mRNA. Translation: ACB86626.1.
    EU408703 mRNA. Translation: ACB86627.1.
    AC016961 Genomic DNA. No translation available.
    AC108670 Genomic DNA. No translation available.
    BC021290 mRNA. Translation: AAH21290.1. Different initiation.
    CCDSiCCDS3273.2. [Q9Y6M1-2]
    CCDS33903.1. [Q9Y6M1-1]
    RefSeqiNP_001007226.1. NM_001007225.1. [Q9Y6M1-1]
    NP_001278798.1. NM_001291869.1.
    NP_001278801.1. NM_001291872.1. [Q9Y6M1-4]
    NP_001278802.1. NM_001291873.1. [Q9Y6M1-3]
    NP_001278803.1. NM_001291874.1. [Q9Y6M1-5]
    NP_001278804.1. NM_001291875.1.
    NP_006539.3. NM_006548.4. [Q9Y6M1-2]
    UniGeneiHs.35354.

    Genome annotation databases

    EnsembliENST00000346192; ENSP00000320204; ENSG00000073792. [Q9Y6M1-1]
    ENST00000382199; ENSP00000371634; ENSG00000073792. [Q9Y6M1-2]
    ENST00000421047; ENSP00000413787; ENSG00000073792. [Q9Y6M1-4]
    GeneIDi10644.
    KEGGihsa:10644.
    UCSCiuc003fpo.3. human. [Q9Y6M1-2]
    uc003fpp.3. human. [Q9Y6M1-1]
    uc010hyi.3. human. [Q9Y6M1-4]
    uc010hyj.3. human. [Q9Y6M1-3]
    uc010hyl.3. human. [Q9Y6M1-5]

    Polymorphism databases

    DMDMi224471831.

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF057352 mRNA. Translation: AAD31596.1 .
    EU408701 mRNA. Translation: ACB86625.1 .
    EU408702 mRNA. Translation: ACB86626.1 .
    EU408703 mRNA. Translation: ACB86627.1 .
    AC016961 Genomic DNA. No translation available.
    AC108670 Genomic DNA. No translation available.
    BC021290 mRNA. Translation: AAH21290.1 . Different initiation.
    CCDSi CCDS3273.2. [Q9Y6M1-2 ]
    CCDS33903.1. [Q9Y6M1-1 ]
    RefSeqi NP_001007226.1. NM_001007225.1. [Q9Y6M1-1 ]
    NP_001278798.1. NM_001291869.1.
    NP_001278801.1. NM_001291872.1. [Q9Y6M1-4 ]
    NP_001278802.1. NM_001291873.1. [Q9Y6M1-3 ]
    NP_001278803.1. NM_001291874.1. [Q9Y6M1-5 ]
    NP_001278804.1. NM_001291875.1.
    NP_006539.3. NM_006548.4. [Q9Y6M1-2 ]
    UniGenei Hs.35354.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQH NMR - A 2-81 [» ]
    ProteinModelPortali Q9Y6M1.
    SMRi Q9Y6M1. Positions 2-158, 198-337, 427-584.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115888. 25 interactions.
    IntActi Q9Y6M1. 21 interactions.
    MINTi MINT-6946387.
    STRINGi 9606.ENSP00000371634.

    PTM databases

    PhosphoSitei Q9Y6M1.

    Polymorphism databases

    DMDMi 224471831.

    Proteomic databases

    MaxQBi Q9Y6M1.
    PaxDbi Q9Y6M1.
    PRIDEi Q9Y6M1.

    Protocols and materials databases

    DNASUi 10644.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346192 ; ENSP00000320204 ; ENSG00000073792 . [Q9Y6M1-1 ]
    ENST00000382199 ; ENSP00000371634 ; ENSG00000073792 . [Q9Y6M1-2 ]
    ENST00000421047 ; ENSP00000413787 ; ENSG00000073792 . [Q9Y6M1-4 ]
    GeneIDi 10644.
    KEGGi hsa:10644.
    UCSCi uc003fpo.3. human. [Q9Y6M1-2 ]
    uc003fpp.3. human. [Q9Y6M1-1 ]
    uc010hyi.3. human. [Q9Y6M1-4 ]
    uc010hyj.3. human. [Q9Y6M1-3 ]
    uc010hyl.3. human. [Q9Y6M1-5 ]

    Organism-specific databases

    CTDi 10644.
    GeneCardsi GC03M185361.
    HGNCi HGNC:28867. IGF2BP2.
    HPAi CAB017126.
    HPA035145.
    MIMi 608289. gene.
    neXtProti NX_Q9Y6M1.
    PharmGKBi PA128394577.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249985.
    HOGENOMi HOG000000675.
    HOVERGENi HBG052725.
    KOi K17392.
    OrthoDBi EOG7T7GSK.
    PhylomeDBi Q9Y6M1.
    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 IGF2BP2. human.
    EvolutionaryTracei Q9Y6M1.
    GeneWikii IGF2BP2.
    GenomeRNAii 10644.
    NextBioi 40455.
    PROi Q9Y6M1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6M1.
    Bgeei Q9Y6M1.
    CleanExi HS_IGF2BP2.
    Genevestigatori Q9Y6M1.

    Family and domain databases

    Gene3Di 3.30.1370.10. 4 hits.
    3.30.70.330. 2 hits.
    InterProi IPR028743. IGF2BP2.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    PANTHERi PTHR10288:SF93. PTHR10288:SF93. 1 hit.
    Pfami PF00013. KH_1. 4 hits.
    PF00076. RRM_1. 2 hits.
    [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. "A novel cytoplasmic protein with RNA-binding motifs is an autoantigen in human hepatocellular carcinoma."
      Zhang J.-Y., Chan E.K.L., Peng X.-X., Tan E.M.
      J. Exp. Med. 189:1101-1110(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION AS A HEPATOCELLULAR CARCINOMA ANTIGEN, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Colon adenocarcinoma.
    2. "A novel type 2 diabetes-associated variant of IGF2BP2 gene affects expression of a functional alternative splicing form."
      Prokunina-Olsson L., Hanisch J.J., Jackson A., Chines P.S., Erdos M.R., Bonnycastle L.L., Swift A., Narisu N., Scott L.J., Morken M., Mohlke K., Bergman R., Tuomilehto J., Boehnke M., Rotimi C.N., Watanabe R.N., Collins F.S.
      Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
      Tissue: Pancreatic islet.
    3. "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].
    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: Pancreas.
    5. "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: FUNCTION, SUBCELLULAR LOCATION.
    6. "Identification and characterization of proteins that selectively interact with isoforms of the mRNA binding protein AUF1 (hnRNP D)."
      Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.
      Biol. Chem. 384:25-37(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRPD.
    7. "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.
    8. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    9. Cited for: INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "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.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-162 AND SER-164, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Two isoforms of the mRNA binding protein IGF2BP2 are generated by alternative translational initiation."
      Le H.T., Sorrell A.M., Siddle K.
      PLoS ONE 7:E33140-E33140(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE INITIATION (ISOFORM 6).
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-211; LYS-292; 445-LYS-LYS-446 AND 527-LYS-GLY-528.
    19. "Solution structure of the RNA binding domain of IGF-II mRNA-binding protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 2-81.

    Entry informationi

    Entry nameiIF2B2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6M1
    Secondary accession number(s): A0A4Z0
    , B3FTN2, B3FTN3, B3FTN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: March 3, 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 IGF2BP2 are detected in sera from some patients with hepatocellular carcinoma.

    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. 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