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Database: UniProt
Entry: Q9Y6M1
LinkDB: Q9Y6M1
Original site: Q9Y6M1 
ID   IF2B2_HUMAN             Reviewed;         599 AA.
AC   Q9Y6M1; A0A4Z0; B3FTN2; B3FTN3; B3FTN4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   02-DEC-2020, entry version 178.
DE   RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 2;
DE            Short=IGF2 mRNA-binding protein 2;
DE            Short=IMP-2;
DE   AltName: Full=Hepatocellular carcinoma autoantigen p62;
DE   AltName: Full=IGF-II mRNA-binding protein 2;
DE   AltName: Full=VICKZ family member 2;
GN   Name=IGF2BP2; Synonyms=IMP2, VICKZ2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION AS A HEPATOCELLULAR
RP   CARCINOMA ANTIGEN, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Colon adenocarcinoma;
RX   PubMed=10190901; DOI=10.1084/jem.189.7.1101;
RA   Zhang J.-Y., Chan E.K.L., Peng X.-X., Tan E.M.;
RT   "A novel cytoplasmic protein with RNA-binding motifs is an autoantigen in
RT   human hepatocellular carcinoma.";
RL   J. Exp. Med. 189:1101-1110(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
RC   TISSUE=Pancreatic islet;
RA   Prokunina-Olsson L., Hanisch J.J., Jackson A., Chines P.S., Erdos M.R.,
RA   Bonnycastle L.L., Swift A., Narisu N., Scott L.J., Morken M., Mohlke K.,
RA   Bergman R., Tuomilehto J., Boehnke M., Rotimi C.N., Watanabe R.N.,
RA   Collins F.S.;
RT   "A novel type 2 diabetes-associated variant of IGF2BP2 gene affects
RT   expression of a functional alternative splicing form.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9891060; DOI=10.1128/mcb.19.2.1262;
RA   Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M.,
RA   Nielsen F.C.;
RT   "A family of insulin-like growth factor II mRNA-binding proteins represses
RT   translation in late development.";
RL   Mol. Cell. Biol. 19:1262-1270(1999).
RN   [6]
RP   INTERACTION WITH HNRPD.
RX   PubMed=12674497; DOI=10.1515/bc.2003.004;
RA   Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.;
RT   "Identification and characterization of proteins that selectively interact
RT   with isoforms of the mRNA binding protein AUF1 (hnRNP D).";
RL   Biol. Chem. 384:25-37(2003).
RN   [7]
RP   REVIEW.
RX   PubMed=15601260; DOI=10.1042/bc20040151;
RA   Yisraeli J.K.;
RT   "VICKZ proteins: a multi-talented family of regulatory RNA-binding
RT   proteins.";
RL   Biol. Cell 97:87-96(2005).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16049158; DOI=10.1530/rep.1.00664;
RA   Hammer N.A., Hansen T.O., Byskov A.G., Rajpert-De Meyts E., Groendahl M.L.,
RA   Bredkjaer H.E., Wewer U.M., Christiansen J., Nielsen F.C.;
RT   "Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular
RT   cancer.";
RL   Reproduction 130:203-212(2005).
RN   [9]
RP   INTERACTION WITH IGF2BP1, AND SUBCELLULAR LOCATION.
RX   PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA   Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA   Johnsen A.H., Christiansen J., Nielsen F.C.;
RT   "Molecular composition of IMP1 ribonucleoprotein granules.";
RL   Mol. Cell. Proteomics 6:798-811(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   RNA-BINDING, AND DOMAIN.
RX   PubMed=20080952; DOI=10.1101/gad.1862910;
RA   Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H.;
RT   "ZBP1 recognition of beta-actin zipcode induces RNA looping.";
RL   Genes Dev. 24:148-158(2010).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 6), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [17]
RP   ALTERNATIVE INITIATION (ISOFORM 6).
RX   PubMed=22427968; DOI=10.1371/journal.pone.0033140;
RA   Le H.T., Sorrell A.M., Siddle K.;
RT   "Two isoforms of the mRNA binding protein IGF2BP2 are generated by
RT   alternative translational initiation.";
RL   PLoS ONE 7:E33140-E33140(2012).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 6), AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [19]
RP   FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9 AND
RP   HNRNPU, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-211; LYS-292;
RP   445-LYS-LYS-446 AND 527-LYS-GLY-528.
RX   PubMed=23640942; DOI=10.1515/hsz-2013-0111;
RA   Wachter K., Kohn M., Stohr N., Huttelmaier S.;
RT   "Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding
RT   proteins) is modulated by distinct RNA-binding domains.";
RL   Biol. Chem. 394:1077-1090(2013).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-164, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [21]
RP   STRUCTURE BY NMR OF 2-81.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA binding domain of IGF-II mRNA-binding
RT   protein 2.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: RNA-binding factor that recruits target transcripts to
CC       cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging'
CC       into mRNPs allows mRNA transport and transient storage. It also
CC       modulates the rate and location at which target transcripts encounter
CC       the translational apparatus and shields them from endonuclease attacks
CC       or microRNA-mediated degradation (By similarity). Binds to the 5'-UTR
CC       of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-
CC       specific. Binds to beta-actin/ACTB and MYC transcripts. {ECO:0000250,
CC       ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9891060}.
CC   -!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and
CC       IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD and IGF2BP1.
CC       Interacts with ELAVL1, DHX9 and HNRNPU. {ECO:0000269|PubMed:12674497,
CC       ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23640942}.
CC   -!- INTERACTION:
CC       Q9Y6M1; Q14103-4: HNRNPD; NbExp=4; IntAct=EBI-1024419, EBI-432545;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in cytoplasmic
CC       mRNP granules containing untranslated mRNAs. Localizes at the
CC       connecting piece and the tail of the spermatozoa. In response to
CC       cellular stress, such as oxidative stress, recruited to stress
CC       granules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q9Y6M1-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y6M1-1; Sequence=VSP_036553;
CC       Name=3;
CC         IsoId=Q9Y6M1-3; Sequence=VSP_036550;
CC       Name=4;
CC         IsoId=Q9Y6M1-4; Sequence=VSP_036550, VSP_036552;
CC       Name=5;
CC         IsoId=Q9Y6M1-5; Sequence=VSP_036550, VSP_036553;
CC       Name=6;
CC         IsoId=Q9Y6M1-6; Sequence=VSP_043699;
CC   -!- TISSUE SPECIFICITY: Expressed in oocytes, granulosa cells of small and
CC       growing follicles, Leydig cells, spermatogonia and semen (at protein
CC       level). Expressed in testicular cancer (at protein level). Expressed
CC       weakly in heart, placenta, skeletal muscle, bone marrow, colon, kidney,
CC       salivary glands, testis and pancreas. Detected in fetal liver, fetal
CC       ovary, gonocytes and interstitial cells of the testis.
CC       {ECO:0000269|PubMed:10190901, ECO:0000269|PubMed:16049158}.
CC   -!- DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules, although
CC       KH1 and KH2 may also contribute. The contribution to RNA-binding of
CC       individual KH domains may be target-specific. KH1 and KH2, and possibly
CC       KH3 and KH4, promote the formation of higher ordered protein-RNA
CC       complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH
CC       domains are required for RNA-dependent homo- and heterooligomerization
CC       and for localization to stress granules. {ECO:0000269|PubMed:20080952,
CC       ECO:0000269|PubMed:23640942}.
CC   -!- MISCELLANEOUS: Autoantibodies against IGF2BP2 are detected in sera from
CC       some patients with hepatocellular carcinoma.
CC   -!- MISCELLANEOUS: [Isoform 6]: Generated by alternative initiation at Met-
CC       69. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF057352; AAD31596.1; -; mRNA.
DR   EMBL; EU408701; ACB86625.1; -; mRNA.
DR   EMBL; EU408702; ACB86626.1; -; mRNA.
DR   EMBL; EU408703; ACB86627.1; -; mRNA.
DR   EMBL; AC016961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021290; AAH21290.1; ALT_INIT; mRNA.
DR   CCDS; CCDS3273.2; -. [Q9Y6M1-2]
DR   CCDS; CCDS33903.1; -. [Q9Y6M1-1]
DR   CCDS; CCDS77869.1; -. [Q9Y6M1-3]
DR   RefSeq; NP_001007226.1; NM_001007225.2. [Q9Y6M1-1]
DR   RefSeq; NP_001278801.1; NM_001291872.2. [Q9Y6M1-4]
DR   RefSeq; NP_001278802.1; NM_001291873.2. [Q9Y6M1-3]
DR   RefSeq; NP_001278803.1; NM_001291874.2. [Q9Y6M1-5]
DR   RefSeq; NP_001278804.1; NM_001291875.2.
DR   RefSeq; NP_006539.3; NM_006548.5. [Q9Y6M1-2]
DR   PDB; 2CQH; NMR; -; A=2-81.
DR   PDB; 6ROL; X-ray; 2.10 A; A/B/C/D=426-588.
DR   PDBsum; 2CQH; -.
DR   PDBsum; 6ROL; -.
DR   SMR; Q9Y6M1; -.
DR   BioGRID; 115888; 149.
DR   DIP; DIP-35539N; -.
DR   IntAct; Q9Y6M1; 48.
DR   MINT; Q9Y6M1; -.
DR   STRING; 9606.ENSP00000371634; -.
DR   iPTMnet; Q9Y6M1; -.
DR   PhosphoSitePlus; Q9Y6M1; -.
DR   SwissPalm; Q9Y6M1; -.
DR   BioMuta; IGF2BP2; -.
DR   DMDM; 224471831; -.
DR   EPD; Q9Y6M1; -.
DR   jPOST; Q9Y6M1; -.
DR   MassIVE; Q9Y6M1; -.
DR   MaxQB; Q9Y6M1; -.
DR   PaxDb; Q9Y6M1; -.
DR   PeptideAtlas; Q9Y6M1; -.
DR   PRIDE; Q9Y6M1; -.
DR   ProteomicsDB; 86724; -. [Q9Y6M1-2]
DR   ProteomicsDB; 86725; -. [Q9Y6M1-1]
DR   ProteomicsDB; 86726; -. [Q9Y6M1-3]
DR   ProteomicsDB; 86727; -. [Q9Y6M1-4]
DR   ProteomicsDB; 86728; -. [Q9Y6M1-5]
DR   ProteomicsDB; 86729; -. [Q9Y6M1-6]
DR   Antibodypedia; 33841; 585 antibodies.
DR   DNASU; 10644; -.
DR   Ensembl; ENST00000346192; ENSP00000320204; ENSG00000073792. [Q9Y6M1-1]
DR   Ensembl; ENST00000382199; ENSP00000371634; ENSG00000073792. [Q9Y6M1-2]
DR   Ensembl; ENST00000421047; ENSP00000413787; ENSG00000073792. [Q9Y6M1-3]
DR   GeneID; 10644; -.
DR   KEGG; hsa:10644; -.
DR   UCSC; uc003fpo.4; human. [Q9Y6M1-2]
DR   CTD; 10644; -.
DR   DisGeNET; 10644; -.
DR   EuPathDB; HostDB:ENSG00000073792.15; -.
DR   GeneCards; IGF2BP2; -.
DR   HGNC; HGNC:28867; IGF2BP2.
DR   HPA; ENSG00000073792; Tissue enhanced (placenta).
DR   MalaCards; IGF2BP2; -.
DR   MIM; 608289; gene.
DR   neXtProt; NX_Q9Y6M1; -.
DR   OpenTargets; ENSG00000073792; -.
DR   PharmGKB; PA128394577; -.
DR   eggNOG; KOG2193; Eukaryota.
DR   GeneTree; ENSGT00940000154913; -.
DR   HOGENOM; CLU_020744_1_0_1; -.
DR   InParanoid; Q9Y6M1; -.
DR   PhylomeDB; Q9Y6M1; -.
DR   TreeFam; TF320229; -.
DR   PathwayCommons; Q9Y6M1; -.
DR   Reactome; R-HSA-428359; Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
DR   BioGRID-ORCS; 10644; 14 hits in 843 CRISPR screens.
DR   ChiTaRS; IGF2BP2; human.
DR   EvolutionaryTrace; Q9Y6M1; -.
DR   GeneWiki; IGF2BP2; -.
DR   GenomeRNAi; 10644; -.
DR   Pharos; Q9Y6M1; Tbio.
DR   PRO; PR:Q9Y6M1; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9Y6M1; protein.
DR   Bgee; ENSG00000073792; Expressed in kidney and 216 other tissues.
DR   ExpressionAtlas; Q9Y6M1; baseline and differential.
DR   Genevisible; Q9Y6M1; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:BHF-UCL.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0045182; F:translation regulator activity; ISS:BHF-UCL.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; ISS:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0042035; P:regulation of cytokine biosynthetic process; IC:BHF-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR   CDD; cd12626; RRM1_IGF2BP2; 1.
DR   Gene3D; 3.30.1370.10; -; 2.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR028743; IGF2BP2.
DR   InterPro; IPR034843; IGF2BP2_RRM1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR10288:SF93; PTHR10288:SF93; 1.
DR   Pfam; PF00013; KH_1; 4.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00322; KH; 4.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54791; SSF54791; 4.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW   Cytoplasm; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; RNA-binding; Translation regulation; Transport.
FT   CHAIN           1..599
FT                   /note="Insulin-like growth factor 2 mRNA-binding protein 2"
FT                   /id="PRO_0000244496"
FT   DOMAIN          3..76
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          82..157
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          193..258
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          274..341
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          427..492
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          509..575
FT                   /note="KH 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         162
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:21406692"
FT   MOD_RES         164
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         550
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5SF07"
FT   VAR_SEQ         1..80
FT                   /note="MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAI
FT                   RAIETLSGKVELHGKIMEVDYSVSKKLR -> MFSCPGHYHVDGFLNPG (in
FT                   isoform 3, isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_036550"
FT   VAR_SEQ         1..68
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_043699"
FT   VAR_SEQ         113
FT                   /note="Q -> QVFAFSL (in isoform 4)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_036552"
FT   VAR_SEQ         358..400
FT                   /note="Missing (in isoform 2 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:10190901, ECO:0000303|Ref.2"
FT                   /id="VSP_036553"
FT   MUTAGEN         211
FT                   /note="K->E: Significantly impaired binding to ACTB
FT                   transcript, but little effect on MYC transcript binding,
FT                   accumulation in the nucleus; when associated with E-292.
FT                   Loss of homo- and heterooligomerization with IGF2BP1 and
FT                   IGF2BP2, almost complete loss of ACTB and MYC transcript
FT                   binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-
FT                   binding and perturbed subcellular location, including
FT                   accumulation in the nucleus and loss of localization to
FT                   stress granules; when associated with E-292; 445-E-E-446
FT                   and 526-E-E-527."
FT                   /evidence="ECO:0000269|PubMed:23640942"
FT   MUTAGEN         292
FT                   /note="K->E: Significantly impaired binding to ACTB
FT                   transcript, but little effect on MYC transcript binding,
FT                   accumulation in the nucleus; when associated with E-211.
FT                   Loss of homo- and heterooligomerization with IGF2BP1 and
FT                   IGF2BP2, almost complete loss of ACTB and MYC transcript
FT                   binding, almost complete loss of ELAVL1-, DHX9- and HNRNPU-
FT                   binding and perturbed subcellular location, including
FT                   accumulation in the nucleus and loss of localization to
FT                   stress granules; when associated with E-211; 445-E-E-445
FT                   and 526-E-E-527."
FT                   /evidence="ECO:0000269|PubMed:23640942"
FT   MUTAGEN         445..446
FT                   /note="KK->EE: Significantly impaired binding to ACTB and
FT                   MYC transcripts; when associated with 527-E-E-528. Loss of
FT                   homo- and heterooligomerization with IGF2BP1 and IGF2BP2,
FT                   almost complete loss of ACTB and MYC transcript binding,
FT                   almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding
FT                   and perturbed subcellular location, including accumulation
FT                   in the nucleus and loss of localization to stress granules;
FT                   when associated with E-211; E-292 and 527-E-E-528."
FT                   /evidence="ECO:0000269|PubMed:23640942"
FT   MUTAGEN         527..528
FT                   /note="KG->EE: Significantly impaired binding to ACTB and
FT                   MYC transcripts; when associated with 445-E-E-446. Loss of
FT                   homo- and heterooligomerization with IGF2BP1 and IGF2BP2,
FT                   almost complete loss of ACTB and MYC transcript binding,
FT                   almost complete loss of ELAVL1-, DHX9- and HNRNPU-binding
FT                   and perturbed subcellular location, including accumulation
FT                   in the nucleus and loss of localization to stress granules;
FT                   when associated with E-211; E-292 and 445-E-E-446."
FT                   /evidence="ECO:0000269|PubMed:23640942"
FT   STRAND          5..8
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   HELIX           16..25
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   STRAND          34..37
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   STRAND          40..43
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   HELIX           48..58
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   TURN            59..61
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   STRAND          70..73
FT                   /evidence="ECO:0000244|PDB:2CQH"
FT   STRAND          428..435
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           436..438
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           439..443
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           445..447
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           448..457
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   STRAND          459..463
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   STRAND          472..480
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           482..498
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   STRAND          510..517
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           518..520
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           521..525
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           527..529
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           530..539
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   STRAND          542..544
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   STRAND          555..563
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   HELIX           565..584
FT                   /evidence="ECO:0000244|PDB:6ROL"
FT   MOD_RES         Q9Y6M1-6:1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000244|PubMed:22223895,
FT                   ECO:0000244|PubMed:22814378"
SQ   SEQUENCE   599 AA;  66121 MW;  EA656F8733BBB39A CRC64;
     MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW AIRAIETLSG
     KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG LLAQYGTVEN VEQVNTDTET
     AVVNVTYATR EEAKIAMEKL SGHQFENYSF KISYIPDEEV SSPSPPQRAQ RGDHSSREQG
     HAPGGTSQAR QIDFPLRILV PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK
     PVTIHATPEG TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI
     EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE NDMLAVNQQA
     NLIPGLNLSA LGIFSTGLSV LSPPAGPRGA PPAAPYHPFT THSGYFSSLY PHHQFGPFPH
     HHSYPEQEIV NLFIPTQAVG AIIGKKGAHI KQLARFAGAS IKIAPAEGPD VSERMVIITG
     PPEAQFKAQG RIFGKLKEEN FFNPKEEVKL EAHIRVPSST AGRVIGKGGK TVNELQNLTS
     AEVIVPRDQT PDENEEVIVR IIGHFFASQT AQRKIREIVQ QVKQQEQKYP QGVASQRSK
//
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