ID IF2B1_HUMAN Reviewed; 577 AA. AC Q9NZI8; C9JT33; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 195. DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 1; DE Short=IGF2 mRNA-binding protein 1; DE Short=IMP-1; DE Short=IMP1; DE AltName: Full=Coding region determinant-binding protein; DE Short=CRD-BP; DE AltName: Full=IGF-II mRNA-binding protein 1; DE AltName: Full=VICKZ family member 1; DE AltName: Full=Zipcode-binding protein 1; DE Short=ZBP-1; GN Name=IGF2BP1; Synonyms=CRDBP, VICKZ1, ZBP1; 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 1). RA Ioannidis P., Trangas T., Dimitriadis E., Samiotaki M., RA Panoutsakopoulos G., Kyriazoglou I., Voutzoulias S., Tsiapalis C.M., RA Kittas C., Agnantis N., Pandis N.; RT "Ectopic expression of a KH-domain containing protein, highly homologous to RT both human IMP-1 and mouse CRD-BP, in benign and malignant mesenchymal RT tumors."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RA Gong H.Y., Hu M.C., Wu J.L.; RT "A novel splice variant of the human IGF2 mRNA-binding protein 1 (IMP1/CRD- RT BP) isolated from human Hep3B hepatoma cells."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [4] RP PROTEIN SEQUENCE OF 4-19; 26-35; 309-324 AND 508-525, FUNCTION, RP RNA-BINDING, ASSOCIATION WITH A MRNP COMPLEX, TISSUE SPECIFICITY, GENE RP NOMENCLATURE, 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 [5] RP PROTEIN SEQUENCE OF 27-35; 66-75 AND 510-524, FUNCTION, IDENTIFICATION IN A RP MRNP COMPLEX WITH PABPC1 AND CSDE1, IDENTIFICATION BY MASS SPECTROMETRY, RP AND RNA-BINDING. RX PubMed=16356927; DOI=10.1093/nar/gki1014; RA Patel G.P., Ma S., Bag J.; RT "The autoregulatory translational control element of poly(A)-binding RT protein mRNA forms a heteromeric ribonucleoprotein complex."; RL Nucleic Acids Res. 33:7074-7089(2005). RN [6] RP PROTEIN SEQUENCE OF 413-429 AND 510-524, SUBCELLULAR LOCATION, AND RP RNA-BINDING. RX PubMed=9801297; DOI=10.1093/nar/26.22.5036; RA Doyle G.A., Betz N.A., Leeds P.F., Fleisig A.J., Prokipcak R.D., Ross J.; RT "The c-myc coding region determinant-binding protein: a member of a family RT of KH domain RNA-binding proteins."; RL Nucleic Acids Res. 26:5036-5044(1998). RN [7] RP FUNCTION, AND RNA-BINDING. RX PubMed=8132663; DOI=10.1016/s0021-9258(17)37102-8; RA Prokipcak R.D., Herrick D.J., Ross J.; RT "Purification and properties of a protein that binds to the C-terminal RT coding region of human c-myc mRNA."; RL J. Biol. Chem. 269:9261-9269(1994). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING. RX PubMed=10875929; DOI=10.1074/jbc.m001156200; RA Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M., RA Christiansen J.; RT "H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding RT protein."; RL J. Biol. Chem. 275:29562-29569(2000). RN [9] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF RP 213-LYS-GLU-214; 294-LYS-GLU-295 AND 423-LYS-LYS-424. RX PubMed=12921532; DOI=10.1042/bj20030943; RA Nielsen J., Adolph S.K., Rajpert-De Meyts E., Lykke-Andersen J., Koch G., RA Christiansen J., Nielsen F.C.; RT "Nuclear transit of human zipcode-binding protein IMP1."; RL Biochem. J. 376:383-391(2003). RN [10] RP INTERACTION WITH FMR1, RNA-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=15282548; DOI=10.1038/sj.emboj.7600341; RA Rackham O., Brown C.M.; RT "Visualization of RNA-protein interactions in living cells: FMRP and IMP1 RT interact on mRNAs."; RL EMBO J. 23:3346-3355(2004). RN [11] RP SUBUNIT, AND RNA-BINDING. RX PubMed=15314207; DOI=10.1093/nar/gkh754; RA Nielsen J., Kristensen M.A., Willemoes M., Nielsen F.C., Christiansen J.; RT "Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a RT cooperative mechanism providing RNP stability."; RL Nucleic Acids Res. 32:4368-4376(2004). RN [12] RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [14] RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=16541107; DOI=10.1038/sj.emboj.7601039; RA Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., RA Nielsen F.C.; RT "RNA-binding IMPs promote cell adhesion and invadopodia formation."; RL EMBO J. 25:1456-1468(2006). RN [15] RP HOMODIMERIZATION, INTERACTION WITH PABPC1, AND RNA-BINDING. RX PubMed=17212783; DOI=10.1111/j.1742-4658.2006.05556.x; RA Patel G.P., Bag J.; RT "IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory RT translational control element of PABP-mRNA through the KH III-IV domain."; RL FEBS J. 273:5678-5690(2006). RN [16] RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=17101699; DOI=10.1083/jcb.200608071; RA Stoehr N., Lederer M., Reinke C., Meyer S., Hatzfeld M., Singer R.H., RA Huettelmaier S.; RT "ZBP1 regulates mRNA stability during cellular stress."; RL J. Cell Biol. 175:527-534(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [18] RP FUNCTION, RNA-BINDING, AND INDUCTION. RX PubMed=16778892; DOI=10.1038/nature04839; RA Noubissi F.K., Elcheva I., Bhatia N., Shakoori A., Ougolkov A., Liu J., RA Minamoto T., Ross J., Fuchs S.Y., Spiegelman V.S.; RT "CRD-BP mediates stabilization of betaTrCP1 and c-myc mRNA in response to RT beta-catenin signaling."; RL Nature 441:898-901(2006). RN [19] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17255263; DOI=10.1158/1078-0432.ccr-06-1297; RA Kato T., Hayama S., Yamabuki T., Ishikawa N., Miyamoto M., Ito T., RA Tsuchiya E., Kondo S., Nakamura Y., Daigo Y.; RT "Increased expression of insulin-like growth factor-II messenger RNA- RT binding protein 1 is associated with tumor progression in patients with RT lung cancer."; RL Clin. Cancer Res. 13:434-442(2007). RN [20] RP INTERACTION WITH AGO1 AND AGO2. RX PubMed=17932509; DOI=10.1038/sj.embor.7401088; RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., RA Urlaub H., Meister G.; RT "Proteomic and functional analysis of Argonaute-containing mRNA-protein RT complexes in human cells."; RL EMBO Rep. 8:1052-1060(2007). RN [21] RP FUNCTION. RX PubMed=17893325; DOI=10.1128/mcb.00972-07; RA Pan F., Huettelmaier S., Singer R.H., Gu W.; RT "ZBP2 facilitates binding of ZBP1 to beta-actin mRNA during RT transcription."; RL Mol. Cell. Biol. 27:8340-8351(2007). RN [22] RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH DHX9; ELAVL2; RP HNRNPA2B1; HNRNPC; HNRNPH1; HNRNPU; IGF2BP2; IGF2BP3; ILF2; PABPC1 AND RP YBX1, RNA-BINDING, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. 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 [23] RP FUNCTION, INTERACTION WITH HIV-1 GAG, AND SUBCELLULAR LOCATION. RX PubMed=18385235; DOI=10.1128/jvi.00189-08; RA Zhou Y., Rong L., Lu J., Pan Q., Liang C.; RT "Insulin-like growth factor II mRNA binding protein 1 associates with Gag RT protein of human immunodeficiency virus type 1, and its overexpression RT affects virus assembly."; RL J. Virol. 82:5683-5692(2008). RN [24] 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 [25] 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 [26] RP FUNCTION, AND RNA-BINDING. RX PubMed=19647520; DOI=10.1016/j.molcel.2009.06.007; RA Elcheva I., Goswami S., Noubissi F.K., Spiegelman V.S.; RT "CRD-BP protects the coding region of betaTrCP1 mRNA from miR-183-mediated RT degradation."; RL Mol. Cell 35:240-246(2009). RN [27] RP FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, RP IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RX PubMed=19029303; DOI=10.1261/rna.1175909; RA Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., RA Buchmeier S., Wahle E., Huettelmaiery S.; RT "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."; RL RNA 15:104-115(2009). RN [28] RP FUNCTION, RNA-BINDING, AND IDENTIFICATION IN A HCV IRES-MEDIATED RP TRANSLATION COMPLEX. RX PubMed=19541769; DOI=10.1261/rna.1578409; RA Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., RA Ostareck-Lederer A., Ostareck D.H.; RT "IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."; RL RNA 15:1528-1542(2009). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [30] 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 [31] RP FUNCTION IN CELL MIGRATION. RX PubMed=22279049; DOI=10.1101/gad.177642.111; RA Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H., RA Huttelmaier S.; RT "IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling."; RL Genes Dev. 26:176-189(2012). RN [32] RP INTERACTION WITH ELAVL1; DHX9 AND HNRNPU. 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 [33] RP REVIEW. RX PubMed=23069990; DOI=10.1007/s00018-012-1186-z; RA Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M., RA Huttelmaier S.; RT "Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post- RT transcriptional drivers of cancer progression?"; RL Cell. Mol. Life Sci. 70:2657-2675(2013). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-73; SER-181 AND RP THR-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [35] RP FUNCTION, INTERACTION WITH ELAVL1; MATR3 AND PABPC1, SUBCELLULAR LOCATION, RP ROLE OF KH DOMAINS, MUTAGENESIS OF LYS-213; LYS-294; 423-LYS-LYS-424 AND RP 505-LYS-GLY-506, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=29476152; DOI=10.1038/s41556-018-0045-z; RA Huang H., Weng H., Sun W., Qin X., Shi H., Wu H., Zhao B.S., Mesquita A., RA Liu C., Yuan C.L., Hu Y.C., Huettelmaier S., Skibbe J.R., Su R., Deng X., RA Dong L., Sun M., Li C., Nachtergaele S., Wang Y., Hu C., Ferchen K., RA Greis K.D., Jiang X., Wei M., Qu L., Guan J.L., He C., Yang J., Chen J.; RT "Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA RT stability and translation."; RL Nat. Cell Biol. 20:285-295(2018). RN [36] RP FUNCTION, INTERACTION WITH RBRP; ELAVL1; MATR3 AND PABPC1, AND MUTAGENESIS RP OF 423-LYS-LYS-424 AND 505-LYS-GLY-506. RX PubMed=32245947; DOI=10.1038/s41467-020-15403-9; RA Zhu S., Wang J.Z., Chen D., He Y.T., Meng N., Chen M., Lu R.X., Chen X.H., RA Zhang X.L., Yan G.R.; RT "An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and RT tumorigenesis."; RL Nat. Commun. 11:1685-1685(2020). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 404-566, FUNCTION, RNA-BINDING, RP 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). 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. Preferentially binds to N6- CC methyladenosine (m6A)-containing mRNAs and increases their stability CC (PubMed:29476152, PubMed:32245947). Plays a direct role in the CC transport and translation of transcripts required for axonal CC regeneration in adult sensory neurons (By similarity). Regulates CC localized beta-actin/ACTB mRNA translation, a crucial process for cell CC polarity, cell migration and neurite outgrowth. Co-transcriptionally CC associates with the ACTB mRNA in the nucleus. This binding involves a CC conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the CC 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a CC motor protein and is transported along the cytoskeleton to the cell CC periphery. During transport, prevents ACTB mRNA from being translated CC into protein. When the RNP complex reaches its destination near the CC plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, CC allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB CC protein synthesis. Monomeric ACTB then assembles into the subcortical CC actin cytoskeleton (By similarity). During neuronal development, key CC regulator of neurite outgrowth, growth cone guidance and neuronal cell CC migration, presumably through the spatiotemporal fine tuning of protein CC synthesis, such as that of ACTB (By similarity). May regulate mRNA CC transport to activated synapses (By similarity). Binds to and CC stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound CC repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA CC stabilization may be crucial for colonic mucosal wound healing (By CC similarity). Binds to the 3'-UTR of IGF2 mRNA by a mechanism of CC cooperative and sequential dimerization and regulates IGF2 mRNA CC subcellular localization and translation. Binds to MYC mRNA, in the CC coding region instability determinant (CRD) of the open reading frame CC (ORF), hence preventing MYC cleavage by endonucleases and possibly CC microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is CC enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the CC 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and CC invadopodia formation in cancer cells. Binds to the oncofetal H19 CC transcript and to the neuron-specific TAU mRNA and regulates their CC localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the CC adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and CC represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 CC protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA- CC dependent interaction with AGO2. Promotes the directed movement of CC tumor-derived cells by fine-tuning intracellular signaling networks. CC Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN CC transcript open reading frame (ORF) and prevents mRNA decay. This CC combined action on MAPK4 (down-regulation) and PTEN (up-regulation) CC antagonizes HSPB1 phosphorylation, consequently it prevents G-actin CC sequestration by phosphorylated HSPB1, allowing F-actin polymerization. CC Hence enhances the velocity of cell migration and stimulates directed CC cell migration by PTEN-modulated polarization. Interacts with Hepatitis CC C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation CC at the HCV IRES, but not 5'-cap-dependent translation, possibly by CC recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the CC formation of infectious HIV-1 particles. Reduces HIV-1 assembly by CC inhibiting viral RNA packaging, as well as assembly and processing of CC GAG protein on cellular membranes. During cellular stress, such as CC oxidative stress or heat shock, stabilizes target mRNAs that are CC recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, CC RAPGEF2 and RPS6KA5 transcripts. {ECO:0000250, CC ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, CC ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, CC ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, CC ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, CC ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, CC ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, CC ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:29476152, CC ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8132663, CC ECO:0000269|PubMed:9891060}. CC -!- SUBUNIT: Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. CC Component of the coding region determinant (CRD)-mediated complex, CC composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. During HCV CC infection, identified in a HCV IRES-mediated translation complex, at CC least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts CC (via the KH domains) with HIV-1 GAG (via the second zinc finger motif CC of NC). Associates (via the RRM domains and KH domains) with HIV-1 CC particles. Identified in a mRNP complex, composed of at least DHX9, CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, CC STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule CC complex containing untranslated mRNAs. Interacts with DHX9, ELAVL2, CC HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, ILF2, and YBX1. Interacts CC with FMR1. Component of a multisubunit autoregulatory RNP complex CC (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1/UNR. Directly CC interacts with PABPC1 (PubMed:17212783, PubMed:29476152, CC PubMed:32245947). Component of a TAU mRNP complex, at least composed of CC IGF2BP1, ELAVL4 and G3BP. Interacts with ELAVL4 in an RNA-dependent CC manner. Associates with microtubules and polysomes. Interacts with AGO1 CC and AGO2. Interacts with ELAVL1 and MATR3 (PubMed:29476152, CC PubMed:32245947). Interacts (via KH3 and KH4 domains) with SEPIN14P20 CC peptide RBRP; the interaction results in increased binding of IGF2BP1 CC to N6-methyladenosine (m6A)-containing mRNAs (PubMed:32245947). CC {ECO:0000269|PubMed:15282548, ECO:0000269|PubMed:15314207, CC ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:17212783, CC ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:17932509, CC ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, CC ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:23640942, CC ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947}. CC -!- INTERACTION: CC Q9NZI8; O95793: STAU1; NbExp=6; IntAct=EBI-1053892, EBI-358174; CC Q9NZI8; Q8VDS3: Cbx7; Xeno; NbExp=2; IntAct=EBI-1053892, EBI-1216533; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear CC region. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, CC Stress granule {ECO:0000269|PubMed:29476152}. Cell projection, CC lamellipodium. Cell projection, dendrite {ECO:0000250}. Cell CC projection, dendritic spine {ECO:0000250}. Cell projection, growth CC cone. Cell projection, filopodium {ECO:0000250}. Cell projection, axon CC {ECO:0000250}. Note=In the nucleus, located in discrete foci, CC coinciding with the sites of ACTB transcription (By similarity). In the CC cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with CC microtubules in growth cone filopodia and along neurites in neuronal CC cells (By similarity). Cytoplasmic colocalization with ACTB mRNA is CC partially lost at the cell periphery, suggesting release of the CC transcript. In neuronal processes, exhibits fast retrograde and CC anterograde movements, when associated with ACTB mRNA; this motility is CC lost when the association is inhibited (By similarity). In hippocampal CC neurons, predominantly located within dendrites, particularly at CC dendritic branching points in young cells, compared to axons (By CC similarity). In axons, predominantly found in axonal branches and their CC growth cones (By similarity). In motile cells, such as migrating CC fibroblasts, localizes to leading edges where it colocalizes with CC microtubules and microfilaments and to retracting tails (By CC similarity). Dendritic levels are regulated by neuronal activity and CC glutaminergic signals: they are increased by KCl-induced CC depolarization, which induces rapid efflux from the cell body into CC dendrites, and decreased by the NMDA receptor agonist (By similarity). CC In motile cells, transported towards the leading edge into the cortical CC region of the lamellipodia where it is connected to microfilaments (By CC similarity). In response to cellular stress, such as oxidative stress CC or heat shock, recruited to stress granules, but not to processing CC bodies. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NZI8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZI8-2; Sequence=VSP_045366; CC -!- TISSUE SPECIFICITY: Mainly expressed in the embryo, including in fetal CC liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also CC expressed follicles of ovary, as well as in gonocytes of testis, CC spermatogonia, semen, oocytes and placenta (at protein level). CC Expressed in various cancers, including testis and lung cancers (at CC protein level), as well as kidney, prostate and trachea cancers. CC {ECO:0000269|PubMed:12921532, ECO:0000269|PubMed:16049158, CC ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:9891060}. CC -!- INDUCTION: May be up-regulated in response to CTNNB1/beta-catenin CC activation. {ECO:0000269|PubMed:16778892}. CC -!- DOMAIN: Domains KH3 and KH4 are the major RNA-binding modules, although CC KH1 and KH2 may also contribute (PubMed:29476152). KH1 and KH2, and CC possibly KH3 and KH4, promote the formation of higher ordered protein- CC RNA complexes, which may be essential for IGF2BP1 cytoplasmic CC retention. KH domains are required for RNA-dependent homo- and CC heterooligomerization and for localization to stress granules. KH3 and CC KH4 mediate association with the cytoskeleton. Two nuclear export CC signals (NES) have been identified in KH2 and KH4 domains, CC respectively. Only KH2 NES is XPO1-dependent. Both NES may be CC redundant, since individual in vitro mutations do not affect CC subcellular location of the full-length protein. The 4 KH domains are CC important to suppress HIV-1 infectivity. {ECO:0000269|PubMed:20080952, CC ECO:0000269|PubMed:29476152}. CC -!- PTM: Phosphorylated. Phosphorylation may impair association with ACTB CC mRNA and hence abolishes translational repression (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40969/IGF2BP1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF198254; AAF37203.1; -; mRNA. DR EMBL; DQ227344; ABB46294.1; -; mRNA. DR EMBL; AC091133; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105030; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS11543.1; -. [Q9NZI8-1] DR CCDS; CCDS54138.1; -. [Q9NZI8-2] DR RefSeq; NP_001153895.1; NM_001160423.1. [Q9NZI8-2] DR RefSeq; NP_006537.3; NM_006546.3. [Q9NZI8-1] DR PDB; 3KRM; X-ray; 2.75 A; A/B/C=404-566. DR PDB; 6QEY; X-ray; 2.20 A; A=194-369. DR PDBsum; 3KRM; -. DR PDBsum; 6QEY; -. DR AlphaFoldDB; Q9NZI8; -. DR SMR; Q9NZI8; -. DR BioGRID; 115886; 487. DR ComplexPortal; CPX-1080; CRD-mediated mRNA stability complex. DR CORUM; Q9NZI8; -. DR DIP; DIP-38139N; -. DR IntAct; Q9NZI8; 120. DR MINT; Q9NZI8; -. DR STRING; 9606.ENSP00000290341; -. DR GlyGen; Q9NZI8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZI8; -. DR PhosphoSitePlus; Q9NZI8; -. DR SwissPalm; Q9NZI8; -. DR BioMuta; IGF2BP1; -. DR DMDM; 296434536; -. DR EPD; Q9NZI8; -. DR jPOST; Q9NZI8; -. DR MassIVE; Q9NZI8; -. DR MaxQB; Q9NZI8; -. DR PaxDb; 9606-ENSP00000290341; -. DR PeptideAtlas; Q9NZI8; -. DR ProteomicsDB; 11549; -. DR ProteomicsDB; 83410; -. [Q9NZI8-1] DR Pumba; Q9NZI8; -. DR TopDownProteomics; Q9NZI8-1; -. [Q9NZI8-1] DR Antibodypedia; 17915; 364 antibodies from 37 providers. DR DNASU; 10642; -. DR Ensembl; ENST00000290341.8; ENSP00000290341.3; ENSG00000159217.10. [Q9NZI8-1] DR Ensembl; ENST00000431824.2; ENSP00000389135.2; ENSG00000159217.10. [Q9NZI8-2] DR GeneID; 10642; -. DR KEGG; hsa:10642; -. DR MANE-Select; ENST00000290341.8; ENSP00000290341.3; NM_006546.4; NP_006537.3. DR UCSC; uc002iom.4; human. [Q9NZI8-1] DR AGR; HGNC:28866; -. DR CTD; 10642; -. DR DisGeNET; 10642; -. DR GeneCards; IGF2BP1; -. DR HGNC; HGNC:28866; IGF2BP1. DR HPA; ENSG00000159217; Group enriched (placenta, testis). DR MIM; 608288; gene. DR neXtProt; NX_Q9NZI8; -. DR OpenTargets; ENSG00000159217; -. DR PharmGKB; PA143485501; -. DR VEuPathDB; HostDB:ENSG00000159217; -. DR eggNOG; KOG2193; Eukaryota. DR GeneTree; ENSGT00940000160427; -. DR HOGENOM; CLU_020744_1_0_1; -. DR InParanoid; Q9NZI8; -. DR OMA; YIPDEQT; -. DR OrthoDB; 3035007at2759; -. DR PhylomeDB; Q9NZI8; -. DR TreeFam; TF320229; -. DR PathwayCommons; Q9NZI8; -. DR Reactome; R-HSA-428359; Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA. DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling. DR SignaLink; Q9NZI8; -. DR SIGNOR; Q9NZI8; -. DR BioGRID-ORCS; 10642; 35 hits in 1167 CRISPR screens. DR ChiTaRS; IGF2BP1; human. DR EvolutionaryTrace; Q9NZI8; -. DR GeneWiki; IGF2BP1; -. DR GenomeRNAi; 10642; -. DR Pharos; Q9NZI8; Tbio. DR PRO; PR:Q9NZI8; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9NZI8; Protein. DR Bgee; ENSG00000159217; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 127 other cell types or tissues. DR GO; GO:0070937; C:CRD-mediated mRNA stability complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000932; C:P-body; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0045182; F:translation regulator activity; IDA:BHF-UCL. DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; IDA:UniProtKB. DR GO; GO:0140059; P:dendrite arborization; IEA:Ensembl. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:ComplexPortal. DR GO; GO:0017148; P:negative regulation of translation; IDA:BHF-UCL. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl. DR GO; GO:0022013; P:pallium cell proliferation in forebrain; IEA:Ensembl. DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; IDA:ComplexPortal. DR GO; GO:0001817; P:regulation of cytokine production; IC:BHF-UCL. DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central. DR GO; GO:0010610; P:regulation of mRNA stability involved in response to stress; IMP:UniProtKB. DR CDD; cd22490; KH-I_IGF2BP1_rpt1; 1. DR CDD; cd22493; KH-I_IGF2BP1_rpt2; 1. DR CDD; cd22496; KH-I_IGF2BP1_rpt3; 1. DR CDD; cd22499; KH-I_IGF2BP1_rpt4; 1. DR CDD; cd12625; RRM1_IGF2BP1; 1. DR CDD; cd12628; RRM2_IGF2BP1; 1. DR Gene3D; 3.30.310.210; -; 1. DR Gene3D; 3.30.70.330; -; 2. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 2. DR InterPro; IPR034837; IGF2BP1_RRM1. DR InterPro; IPR034842; IGF2BP1_RRM2. 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:SF92; INSULIN-LIKE GROWTH FACTOR 2 MRNA-BINDING PROTEIN 1; 1. DR PANTHER; PTHR10288; KH DOMAIN CONTAINING RNA BINDING PROTEIN; 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; Eukaryotic type KH-domain (KH-domain type I); 4. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50084; KH_TYPE_1; 4. DR PROSITE; PS50102; RRM; 2. DR Genevisible; Q9NZI8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell projection; Cytoplasm; KW Direct protein sequencing; mRNA transport; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Synapse; Translation regulation; KW Transport. FT CHAIN 1..577 FT /note="Insulin-like growth factor 2 mRNA-binding protein 1" FT /id="PRO_0000282533" FT DOMAIN 2..75 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 81..156 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 195..260 FT /note="KH 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 276..343 FT /note="KH 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 405..470 FT /note="KH 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT DOMAIN 487..553 FT /note="KH 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 160..190 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..570 FT /note="Necessary for interaction with ELAVL4 and binding to FT TAU mRNA" FT /evidence="ECO:0000250" FT REGION 310..324 FT /note="Sufficient for nuclear export" FT REGION 485..495 FT /note="Sufficient for nuclear export" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 73 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 181 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 528 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 135..273 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_045366" FT MUTAGEN 213..214 FT /note="KE->EL: 50-fold decrease in RNA-binding affinity, FT decreased location in cytoplasmic RNP, increased nuclear FT location; when associated with 294-E-L-295 and FT 423-E-L-424." FT /evidence="ECO:0000269|PubMed:12921532" FT MUTAGEN 213 FT /note="K->E: Partial reduction in interaction with FT m6A-modified mRNA; when associated with E-294." FT /evidence="ECO:0000269|PubMed:29476152" FT MUTAGEN 294..295 FT /note="KE->EL: 50-fold decrease in RNA-binding affinity, FT decreased location in cytoplasmic RNP, increased nuclear FT location; when associated with 213-E-L-214 and FT 423-E-L-424." FT /evidence="ECO:0000269|PubMed:12921532" FT MUTAGEN 294 FT /note="K->E: Partial reduction in interaction with FT m6A-modified mRNA; when associated with E-213." FT /evidence="ECO:0000269|PubMed:29476152" FT MUTAGEN 423..424 FT /note="KK->EE: Loss of binding to RBPR and loss of FT interaction with m6A-modified mRNA; when associated with FT 505-E-E-506." FT /evidence="ECO:0000269|PubMed:29476152, FT ECO:0000269|PubMed:32245947" FT MUTAGEN 423..424 FT /note="KK->EL: 50-fold decrease in RNA-binding affinity, FT decreased location in cytoplasmic RNP, increased nuclear FT location; when associated with 213-E-L-214 and FT 294-E-L-295." FT /evidence="ECO:0000269|PubMed:12921532" FT MUTAGEN 505..506 FT /note="KG->EE: Loss of binding to RBPR and loss of FT interaction with m6A-modified mRNA; when associated with FT 423-E-E-424." FT /evidence="ECO:0000269|PubMed:29476152, FT ECO:0000269|PubMed:32245947" FT CONFLICT 10 FT /note="Missing (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="I -> T (in Ref. 1; AAF37203)" FT /evidence="ECO:0000305" FT CONFLICT 320 FT /note="Missing (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="I -> T (in Ref. 1; AAF37203)" FT /evidence="ECO:0000305" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 207..211 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 216..225 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 228..232 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 241..248 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 250..270 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 279..284 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 285..292 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 297..306 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 309..312 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 315..317 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 324..331 FT /evidence="ECO:0007829|PDB:6QEY" FT HELIX 333..361 FT /evidence="ECO:0007829|PDB:6QEY" FT STRAND 406..413 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 414..416 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 417..421 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 423..425 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 426..435 FT /evidence="ECO:0007829|PDB:3KRM" FT STRAND 438..441 FT /evidence="ECO:0007829|PDB:3KRM" FT STRAND 450..458 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 460..476 FT /evidence="ECO:0007829|PDB:3KRM" FT STRAND 488..495 FT /evidence="ECO:0007829|PDB:3KRM" FT TURN 496..498 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 499..503 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 505..507 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 508..517 FT /evidence="ECO:0007829|PDB:3KRM" FT STRAND 520..522 FT /evidence="ECO:0007829|PDB:3KRM" FT STRAND 533..541 FT /evidence="ECO:0007829|PDB:3KRM" FT HELIX 543..560 FT /evidence="ECO:0007829|PDB:3KRM" SQ SEQUENCE 577 AA; 63481 MW; 1D036AE5388D05FA CRC64; MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA MKAIETFSGK VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL LAQYGTVENC EQVNTESETA VVNVTYSNRE QTRQAIMKLN GHQLENHALK VSYIPDEQIA QGPENGRRGG FGSRGQPRQG SPVAAGAPAK QQQVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA EKAISVHSTP EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM QAPEQEMVQV FIPAQAVGAI IGKKGQHIKQ LSRFASASIK IAPPETPDSK VRMVIITGPP EAQFKAQGRI YGKLKEENFF GPKEEVKLET HIRVPASAAG RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII GHFYASQMAQ RKIRDILAQV KQQHQKGQSN QAQARRK //