IF2B3_HUMAN
ID IF2B3_HUMAN Reviewed; 579 AA.
AC O00425; A0A4Z5; Q63HM0; Q6MZZ2; Q86VB1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 3;
DE Short=IGF2 mRNA-binding protein 3;
DE Short=IMP-3;
DE AltName: Full=IGF-II mRNA-binding protein 3;
DE AltName: Full=KH domain-containing protein overexpressed in cancer;
DE Short=hKOC;
DE AltName: Full=VICKZ family member 3;
GN Name=IGF2BP3; Synonyms=IMP3, KOC1, VICKZ3;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas, and Pancreatic cancer;
RX PubMed=9178771; DOI=10.1038/sj.onc.1201110;
RA Mueller-Pillasch F., Lacher U., Wallrapp C., Micha A., Zimmerhackl F.,
RA Hameister H., Varga G., Friess H., Buechler M., Beger H.G., Vila M.R.,
RA Adler G., Gress T.M.;
RT "Cloning of a gene highly overexpressed in cancer coding for a novel KH-
RT domain containing protein.";
RL Oncogene 14:2729-2733(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Endometrial tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 TISSUE SPECIFICITY.
RX PubMed=10525192; DOI=10.1016/s0925-4773(99)00160-4;
RA Mueller-Pillasch F., Pohl B., Wilda M., Lacher U., Beil M., Wallrapp C.,
RA Hameister H., Knoechel W., Adler G., Gress T.M.;
RT "Expression of the highly conserved RNA binding protein KOC in
RT embryogenesis.";
RL Mech. Dev. 88:95-99(1999).
RN [6]
RP GENE NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP RNA-BINDING.
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 [7]
RP IDENTIFICATION AS A CARCINOMA ANTIGEN.
RX PubMed=11465943; DOI=10.1006/clim.2001.5048;
RA Zhang J.-Y., Chan E.K., Peng X.-X., Lu M., Wang X., Mueller F., Tan E.M.;
RT "Autoimmune responses to mRNA binding proteins p62 and Koc in diverse
RT malignancies.";
RL Clin. Immunol. 100:149-156(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=12161597; DOI=10.1136/jmg.39.8.575;
RA Monk D., Bentley L., Beechey C., Hitchins M., Peters J., Preece M.A.,
RA Stanier P., Moore G.E.;
RT "Characterisation of the growth regulating gene IMP3, a candidate for
RT Silver-Russell syndrome.";
RL J. Med. Genet. 39:575-581(2002).
RN [9]
RP SUBCELLULAR LOCATION.
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 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 [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15644775; DOI=10.1097/01.pas.0000149688.98333.54;
RA Yantiss R.K., Woda B.A., Fanger G.R., Kalos M., Whalen G.F., Tada H.,
RA Andersen D.K., Rock K.L., Dresser K.;
RT "KOC (K homology domain containing protein overexpressed in cancer): a
RT novel molecular marker that distinguishes between benign and malignant
RT lesions of the pancreas.";
RL Diagn. Mol. Pathol. 29:188-195(2005).
RN [12]
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 [13]
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 [14]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16814207; DOI=10.1016/s1470-2045(06)70732-x;
RA Jiang Z., Chu P.G., Woda B.A., Rock K.L., Liu Q., Hsieh C.-C., Li C.,
RA Chen W., Duan H.O., McDougal S., Wu C.-L.;
RT "Analysis of RNA-binding protein IMP3 to predict metastasis and prognosis
RT of renal-cell carcinoma: a retrospective study.";
RL Lancet Oncol. 7:556-564(2006).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17192788; DOI=10.1038/modpathol.3800735;
RA Li C., Rock K.L., Woda B.A., Jiang Z., Fraire A.E., Dresser K.;
RT "IMP3 is a novel biomarker for adenocarcinoma in situ of the uterine
RT cervix: an immunohistochemical study in comparison with p16(INK4a)
RT expression.";
RL Mod. Pathol. 20:242-247(2007).
RN [16]
RP INTERACTION WITH IGF2BP1.
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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528, 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 [19]
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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND THR-528, 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 [22]
RP FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9 AND
RP HNRNPU, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-213; LYS-294;
RP 423-LYS-LYS-424 AND 505-LYS-GLY-506.
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528, AND IDENTIFICATION BY
RP 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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-475, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-450 AND LYS-475, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
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 [28]
RP STRUCTURE BY NMR OF 73-161.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in insulin-like growth factor 2
RT mRNA-binding protein 3.";
RL Submitted (JUN-2007) to the PDB data bank.
CC -!- FUNCTION: RNA-binding factor that may recruit 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). Binds to the 3'-UTR of CD44 mRNA and stabilizes it,
CC hence promotes cell adhesion and invadopodia formation in cancer cells.
CC Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA
CC stability by binding to the coding region instability determinant (CRD)
CC and binding is enhanced by m6A-modification of the CRD
CC (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth
CC factor 2 (IGF2) mRNAs. {ECO:0000269|PubMed:16541107,
CC ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152}.
CC -!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and
CC IGF2BP3 in an RNA-dependent manner (PubMed:23640942). Interacts with
CC IGF2BP1 (PubMed:17289661). Interacts with ELAVL1, DHX9, HNRNPU, MATR3
CC and PABPC1 (PubMed:23640942, PubMed:29476152).
CC {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:23640942,
CC ECO:0000269|PubMed:29476152}.
CC -!- INTERACTION:
CC O00425; Q15365: PCBP1; NbExp=3; IntAct=EBI-1058566, EBI-946095;
CC O00425; Q13148: TARDBP; NbExp=6; IntAct=EBI-1058566, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body
CC {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:29476152}. Note=Found in lamellipodia of the
CC leading edge, in the perinuclear region, and beneath the plasma
CC membrane. The subcytoplasmic localization is cell specific and
CC regulated by cell contact and growth. Localized at the connecting piece
CC and the tail of the spermatozoa. Colocalized with CD44 mRNA in RNP
CC granules. In response to cellular stress, such as oxidative stress,
CC recruited to stress granules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00425-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00425-2; Sequence=VSP_024172;
CC -!- TISSUE SPECIFICITY: Expressed in fetal liver, fetal lung, fetal kidney,
CC fetal thymus, fetal placenta, fetal follicles of ovary and gonocytes of
CC testis, growing oocytes, spermatogonia and semen (at protein level).
CC Expressed in cervix adenocarcinoma, in testicular, pancreatic and
CC renal-cell carcinomas (at protein level). Expressed ubiquitously during
CC fetal development at 8 and 14 weeks of gestation. Expressed in ovary,
CC testis, brain, placenta, pancreatic cancer tissues and pancreatic
CC cancer cell lines. {ECO:0000269|PubMed:10525192,
CC ECO:0000269|PubMed:12161597, ECO:0000269|PubMed:15644775,
CC ECO:0000269|PubMed:16049158, ECO:0000269|PubMed:16814207,
CC ECO:0000269|PubMed:17192788, ECO:0000269|PubMed:9178771,
CC ECO:0000269|PubMed:9891060}.
CC -!- DOMAIN: All KH domains contribute to binding to target mRNA. Domains
CC KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2
CC also contribute (PubMed:29476152). The KH domains are also required for
CC RNA-dependent homo- and heterooligomerization. The integrity of KH
CC domains seems not to be required for localization to stress granules.
CC {ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:23640942,
CC ECO:0000269|PubMed:29476152}.
CC -!- MISCELLANEOUS: Autoantibodies against IGF2BP3 are detected in sera from
CC some patients with a variety of carcinomas.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; U76705; AAD09223.1; -; mRNA.
DR EMBL; U97188; AAC35208.1; -; mRNA.
DR EMBL; BX640800; CAE45883.1; -; mRNA.
DR EMBL; BX648488; CAH56186.1; -; mRNA.
DR EMBL; AC005082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC021876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065269; AAH65269.1; -; mRNA.
DR CCDS; CCDS5382.1; -. [O00425-1]
DR RefSeq; NP_006538.2; NM_006547.2. [O00425-1]
DR PDB; 2E44; NMR; -; A=73-161.
DR PDB; 6FQ1; X-ray; 1.31 A; A/B=1-161.
DR PDB; 6FQR; X-ray; 2.10 A; A/B=1-161.
DR PDB; 6GQE; X-ray; 2.15 A; A=192-355.
DR PDB; 6GX6; X-ray; 2.00 A; A=1-161.
DR PDBsum; 2E44; -.
DR PDBsum; 6FQ1; -.
DR PDBsum; 6FQR; -.
DR PDBsum; 6GQE; -.
DR PDBsum; 6GX6; -.
DR AlphaFoldDB; O00425; -.
DR SMR; O00425; -.
DR BioGRID; 115887; 340.
DR CORUM; O00425; -.
DR DIP; DIP-44171N; -.
DR IntAct; O00425; 82.
DR MINT; O00425; -.
DR STRING; 9606.ENSP00000258729; -.
DR GlyGen; O00425; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00425; -.
DR MetOSite; O00425; -.
DR PhosphoSitePlus; O00425; -.
DR SwissPalm; O00425; -.
DR BioMuta; IGF2BP3; -.
DR EPD; O00425; -.
DR jPOST; O00425; -.
DR MassIVE; O00425; -.
DR MaxQB; O00425; -.
DR PaxDb; O00425; -.
DR PeptideAtlas; O00425; -.
DR PRIDE; O00425; -.
DR ProteomicsDB; 47882; -. [O00425-1]
DR ProteomicsDB; 47883; -. [O00425-2]
DR Antibodypedia; 1056; 423 antibodies from 39 providers.
DR DNASU; 10643; -.
DR Ensembl; ENST00000258729.8; ENSP00000258729.3; ENSG00000136231.14. [O00425-1]
DR Ensembl; ENST00000619562.4; ENSP00000480267.1; ENSG00000136231.14. [O00425-2]
DR GeneID; 10643; -.
DR KEGG; hsa:10643; -.
DR MANE-Select; ENST00000258729.8; ENSP00000258729.3; NM_006547.3; NP_006538.2.
DR UCSC; uc003swf.4; human. [O00425-1]
DR CTD; 10643; -.
DR DisGeNET; 10643; -.
DR GeneCards; IGF2BP3; -.
DR HGNC; HGNC:28868; IGF2BP3.
DR HPA; ENSG00000136231; Tissue enhanced (lymphoid tissue, placenta).
DR MIM; 608259; gene.
DR neXtProt; NX_O00425; -.
DR OpenTargets; ENSG00000136231; -.
DR PharmGKB; PA128394576; -.
DR VEuPathDB; HostDB:ENSG00000136231; -.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000154957; -.
DR HOGENOM; CLU_020744_1_0_1; -.
DR InParanoid; O00425; -.
DR OMA; CPDEGWA; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; O00425; -.
DR TreeFam; TF320229; -.
DR PathwayCommons; O00425; -.
DR Reactome; R-HSA-428359; Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
DR SignaLink; O00425; -.
DR BioGRID-ORCS; 10643; 21 hits in 1089 CRISPR screens.
DR ChiTaRS; IGF2BP3; human.
DR EvolutionaryTrace; O00425; -.
DR GeneWiki; IGF2BP3; -.
DR GenomeRNAi; 10643; -.
DR Pharos; O00425; Tbio.
DR PRO; PR:O00425; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O00425; protein.
DR Bgee; ENSG00000136231; Expressed in secondary oocyte and 133 other tissues.
DR ExpressionAtlas; O00425; baseline and differential.
DR Genevisible; O00425; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; 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; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
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:0070934; P:CRD-mediated mRNA stabilization; IDA:UniProtKB.
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:0001817; P:regulation of cytokine production; IC:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR CDD; cd12630; RRM2_IGF2BP3; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034844; IGF2BP3_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 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; Alternative splicing; Cytoplasm; Isopeptide bond;
KW mRNA transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Translation regulation; Transport; Ubl conjugation.
FT CHAIN 1..579
FT /note="Insulin-like growth factor 2 mRNA-binding protein 3"
FT /id="PRO_0000282538"
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..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 528
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..381
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_024172"
FT MUTAGEN 213
FT /note="K->E: Partial reduction in interaction with m6A-
FT modified mRNA; when associated with E-294. Loss of
FT homo- and heterooligomerization with IGF2BP1 and IGF2BP2,
FT modestly impaired binding to ACTB and MYC transcripts and
FT almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor
FT on subcellular location; when associated with E-294; 422-E-
FT E-423 and 505-E-E-506."
FT /evidence="ECO:0000269|PubMed:23640942,
FT ECO:0000269|PubMed:29476152"
FT MUTAGEN 294
FT /note="K->E: Partial reduction in interaction with m6A-
FT modified mRNA; when associated with E-213. Loss of
FT homo- and heterooligomerization with IGF2BP1 and IGF2BP2,
FT modestly impaired binding to ACTB and MYC transcripts and
FT almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor
FT on subcellular location; when associated with E-213; 422-E-
FT E-423 and 505-E-E-506."
FT /evidence="ECO:0000269|PubMed:23640942,
FT ECO:0000269|PubMed:29476152"
FT MUTAGEN 423..424
FT /note="KQ->EE: Loss of interaction with m6A-modified mRNA;
FT when associated with 505-E-E-506. Loss of homo- and
FT heterooligomerization with IGF2BP1 and IGF2BP2, modestly
FT impaired binding to ACTB and MYC transcripts and almost no
FT effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on
FT subcellular location; when associated with E-213; E-294 and
FT 505-E-E-506."
FT /evidence="ECO:0000269|PubMed:23640942,
FT ECO:0000269|PubMed:29476152"
FT MUTAGEN 505..506
FT /note="KG->EE: Loss of interaction with m6A-modified mRNA;
FT when associated with 422-E-E-423. Loss of homo- and
FT heterooligomerization with IGF2BP1 and IGF2BP2, modestly
FT impaired binding to ACTB and MYC transcripts and almost no
FT effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on
FT subcellular location; when associated with E-213; E-294 and
FT 422-E-E-423."
FT /evidence="ECO:0000269|PubMed:23640942,
FT ECO:0000269|PubMed:29476152"
FT CONFLICT 410
FT /note="L -> Q (in Ref. 1; AAD09223/AAC35208)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="V -> A (in Ref. 2; CAH56186)"
FT /evidence="ECO:0000305"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:6FQ1"
FT HELIX 15..24
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:6FQ1"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:6FQ1"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6GX6"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6FQ1"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2E44"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 116..128
FT /evidence="ECO:0007829|PDB:6FQ1"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:6FQ1"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:6FQ1"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6FQ1"
SQ SEQUENCE 579 AA; 63705 MW; 78884F56A9D98CDE CRC64;
MNKLYIGNLS ENAAPSDLES IFKDAKIPVS GPFLVKTGYA FVDCPDESWA LKAIEALSGK
IELHGKPIEV EHSVPKRQRI RKLQIRNIPP HLQWEVLDSL LVQYGVVESC EQVNTDSETA
VVNVTYSSKD QARQALDKLN GFQLENFTLK VAYIPDEMAA QQNPLQQPRG RRGLGQRGSS
RQGSPGSVSK QKPCDLPLRL LVPTQFVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA
EKSITILSTP EGTSAACKSI LEIMHKEAQD IKFTEEIPLK ILAHNNFVGR LIGKEGRNLK
KIEQDTDTKI TISPLQELTL YNPERTITVK GNVETCAKAE EEIMKKIRES YENDIASMNL
QAHLIPGLNL NALGLFPPTS GMPPPTSGPP SAMTPPYPQF EQSETETVHL FIPALSVGAI
IGKQGQHIKQ LSRFAGASIK IAPAEAPDAK VRMVIITGPP EAQFKAQGRI YGKIKEENFV
SPKEEVKLEA HIRVPSFAAG RVIGKGGKTV NELQNLSSAE VVVPRDQTPD ENDQVVVKIT
GHFYACQVAQ RKIQEILTQV KQHQQQKALQ SGPPQSRRK
