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UniProtKB/Swiss-Prot entry O00425


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name IF2B3_HUMAN
Primary accession number O00425
Secondary accession numbers A0A4Z5 Q63HM0 Q6MZZ2 Q86VB1
Integrated into Swiss-Prot on April 3, 2007
Sequence was last modified on July 1, 1997 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 70)
Name and origin of the protein
Protein name Insulin-like growth factor 2 mRNA-binding protein 3
Synonyms IGF2 mRNA-binding protein 3
IMP-3
IGF-II mRNA-binding protein 3
KH domain-containing protein overexpressed in cancer
hKOC
VICKZ family member 3
Gene name
Name: IGF2BP3
Synonyms: IMP3, KOC1, VICKZ3
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Pancreas, and Pancreatic cancer;
DOI=10.1038/sj.onc.1201110; PubMed=9178771 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller-Pillasch F., Lacher U., Wallrapp C., Micha A., Zimmerhackl F., Hameister H., Varga G., Friess H., Buechler M., Beger H.G., Vila M.R., Adler G., Gress T.M.;
"Cloning of a gene highly overexpressed in cancer coding for a novel KH-domain containing protein.";
Oncogene 14:2729-2733(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Endometrial tumor;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Eye, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
DOI=10.1016/S0925-4773(99)00160-4; PubMed=10525192 [NCBI, ExPASy, EBI, Israel, Japan]
Mueller-Pillasch F., Pohl B., Wilda M., Lacher U., Beil M., Wallrapp C., Hameister H., Knoechel W., Adler G., Gress T.M.;
"Expression of the highly conserved RNA binding protein KOC in embryogenesis.";
Mech. Dev. 88:95-99(1999).
[5]
GENE FAMILY NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RNA-BINDING.
PubMed=9891060 [NCBI, ExPASy, EBI, Israel, Japan]
Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M., Nielsen F.C.;
"A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development.";
Mol. Cell. Biol. 19:1262-1270(1999).
[6]
IDENTIFICATION AS A CARCINOMA ANTIGEN.
DOI=10.1006/clim.2001.5048; PubMed=11465943 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J.-Y., Chan E.K., Peng X.-X., Lu M., Wang X., Mueller F., Tan E.M.;
"Autoimmune responses to mRNA binding proteins p62 and Koc in diverse malignancies.";
Clin. Immunol. 100:149-156(2001).
[7]
TISSUE SPECIFICITY.
DOI=10.1136/jmg.39.8.575; PubMed=12161597 [NCBI, ExPASy, EBI, Israel, Japan]
Monk D., Bentley L., Beechey C., Hitchins M., Peters J., Preece M.A., Stanier P., Moore G.E.;
"Characterisation of the growth regulating gene IMP3, a candidate for Silver-Russell syndrome.";
J. Med. Genet. 39:575-581(2002).
[8]
SUBCELLULAR LOCATION.
DOI=10.1042/BJ20030943; PubMed=12921532 [NCBI, ExPASy, EBI, Israel, Japan]
Nielsen J., Adolph S.K., Rajpert-De Meyts E., Lykke-Andersen J., Koch G., Christiansen J., Nielsen F.C.;
"Nuclear transit of human zipcode-binding protein IMP1.";
Biochem. J. 376:383-391(2003).
[9]
REVIEW.
DOI=10.1042/BC20040151; PubMed=15601260 [NCBI, ExPASy, EBI, Israel, Japan]
Yisraeli J.K.;
"VICKZ proteins: a multi-talented family of regulatory RNA-binding proteins.";
Biol. Cell 97:87-96(2005).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1097/01.pas.0000149688.98333.54; PubMed=15644775 [NCBI, ExPASy, EBI, Israel, Japan]
Yantiss R.K., Woda B.A., Fanger G.R., Kalos M., Whalen G.F., Tada H., Andersen D.K., Rock K.L., Dresser K.;
"KOC (K homology domain containing protein overexpressed in cancer): a novel molecular marker that distinguishes between benign and malignant lesions of the pancreas.";
Diagn. Mol. Pathol. 29:188-195(2005).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1530/rep.1.00664; PubMed=16049158 [NCBI, ExPASy, EBI, Israel, Japan]
Hammer N.A., Hansen T.O., Byskov A.G., Rajpert-De Meyts E., Groendahl M.L., Bredkjaer H.E., Wewer U.M., Christiansen J., Nielsen F.C.;
"Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular cancer.";
Reproduction 130:203-212(2005).
[12]
FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
DOI=10.1038/sj.emboj.7601039; PubMed=16541107 [NCBI, ExPASy, EBI, Israel, Japan]
Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., Nielsen F.C.;
"RNA-binding IMPs promote cell adhesion and invadopodia formation.";
EMBO J. 25:1456-1468(2006).
[13]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S1470-2045(06)70732-X; PubMed=16814207 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang Z., Chu P.G., Woda B.A., Rock K.L., Liu Q., Hsieh C.-C., Li C., Chen W., Duan H.O., McDougal S., Wu C.-L.;
"Analysis of RNA-binding protein IMP3 to predict metastasis and prognosis of renal-cell carcinoma: a retrospective study.";
Lancet Oncol. 7:556-564(2006).
[14]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1038/modpathol.3800735; PubMed=17192788 [NCBI, ExPASy, EBI, Israel, Japan]
Li C., Rock K.L., Woda B.A., Jiang Z., Fraire A.E., Dresser K.;
"IMP3 is a novel biomarker for adenocarcinoma in situ of the uterine cervix: an immunohistochemical study in comparison with p16(INK4a) expression.";
Mod. Pathol. 20:242-247(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[17]
STRUCTURE BY NMR OF 73-161.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain in insulin-like growth factor 2 mRNA-binding protein 3.";
Submitted (JUN-2007) to the PDB data bank.
Comments
  • FUNCTION: RNA-binding protein that act as a regulator of mRNA translation and stability. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binds to sequences in the 3'-UTR of CD44 mRNA.
  • SUBUNIT: Homodimer and multimer (By similarity).
  • SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece and the tail of the spermatozoa. Colocalized with CD44 mRNA in RNP granules.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO00425-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO00425-2
    Features which should be applied to build the isoform sequence: VSP_024172.
    Name3
    Isoform IDO00425-3
    Features which should be applied to build the isoform sequence: VSP_024173, VSP_024174.
  • TISSUE SPECIFICITY: Expressed in fetal liver, fetal lung, fetal kidney, fetal thymus, fetal placenta, fetal follicles of ovary and gonocytes of testis, growing oocytes, spermatogonia and semen (at protein level). Expressed in cervix adenocarcinoma, in testicular, pancreatic and renal-cell carcinomas (at protein level). Expressed ubiquitously during fetal development at 8 and 14 weeks of gestation. Expressed in ovary, testis, brain, placenta, pancreatic cancer tissues and pancreatic cancer cell lines.
  • DISEASE: Autoantibodies against IGF2BP3 are detected in sera from some patients with a variety of carcinomas.
  • SIMILARITY: Belongs to the RRM IMP/VICKZ family.
  • SIMILARITY: Contains 4 KH domains.
  • SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U76705; AAD09223.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U97188; AAC35208.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX640800; CAE45883.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX648488; CAH56186.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051296; AAH51296.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065269; AAH65269.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00165467; -.
IPI00658000; -.
IPI00843931; -.
UniGene Hs.700696
3D structure databases
PDB
2E44; NMR; -; A=73-161.[ExPASy / RCSB / EBI]
PDBsum 2E44; -.
ModBase O00425.
PTM databases
PhosphoSite O00425; -.
Organism-specific databases
GeneCards GC07M023316; -.
HGNC HGNC:28868; IGF2BP3.
GenAtlas IGF2BP3.
HPA HPA002037; -.
MIM 608259; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress O00425; -.
Bgee O00425; -.
CleanEx HS_IGF2BP3; -.
HS_IMP3; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0048027; Molecular function: mRNA 5'-UTR binding (inferred from direct assay from UniProtKB).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0045182; Molecular function: translation regulator activity (inferred from sequence or structural similarity from UniProtKB).
GO:0009653; Biological process: anatomical structure morphogenesis (traceable author statement from ProtInc).
GO:0017148; Biological process: negative regulation of translation (inferred from sequence or structural similarity from UniProtKB).
GO:0042035; Biological process: regulation of cytokine biosynthetic process (inferred by curator from UniProtKB).
GO:0006412; Biological process: translation (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR004087; KH.
IPR004088; KH_type_1.
IPR018111; KH_type_1_subgr.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
Pfam PF00013; KH_1; 4.
PF00076; RRM_1; 2.
Pfam graphical view of domain structure.
SMART SM00322; KH; 4.
SM00360; RRM; 2.
SMART graphical view of domain structure.
PROSITE PS50084; KH_TYPE_1; 4.
PS50102; RRM; 2.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl ENSG00000136231; Homo sapiens. [Contig view]
Phylogenomic databases
HOVERGEN O00425; -.
Other
SOURCE IGF2BP3; Homo sapiens.
ProtoNet O00425.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; Repeat; RNA-binding; Translation regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   579  579     Insulin-like growth factor 2 mRNA-binding protein 3. PRO_0000282538
DOMAIN   2    75  74     RRM 1. 
DOMAIN   81   156  76     RRM 2. 
DOMAIN   195   260  66     KH 1. 
DOMAIN   276   343  68     KH 2. 
DOMAIN   405   470  66     KH 3. 
DOMAIN   487   553  67     KH 4. 
MOD_RES   528   528        Phosphothreonine. 
VAR_SEQ   1   381        Missing (in isoform 2). VSP_024172
VAR_SEQ   96   100        VLDSL -> EMGQP (in isoform 3). VSP_024173
VAR_SEQ   101   579        Missing (in isoform 3). VSP_024174
CONFLICT   410   410        Q -> L (in Ref. 2; CAH56186/CAE45883 and 3; AAH65269). 
CONFLICT   494   494        V -> A (in Ref. 2; CAH56186). 
STRAND   83    88  6      
STRAND   90    92  3      
HELIX   94   104  11      
STRAND   107   113  7      
STRAND   116   128  13      
HELIX   129   139  11      
STRAND   150   153  4      
Sequence information
Length: 579 AA [This is the length of the unprocessed precursor] Molecular weight: 63720 Da [This is the MW of the unprocessed precursor] CRC64: AE5C3A8EE3C135C5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNKLYIGNLS ENAAPSDLES IFKDAKIPVS GPFLVKTGYA FVDCPDESWA LKAIEALSGK 

        70         80         90        100        110        120 
IELHGKPIEV EHSVPKRQRI RKLQIRNIPP HLQWEVLDSL LVQYGVVESC EQVNTDSETA 

       130        140        150        160        170        180 
VVNVTYSSKD QARQALDKLN GFQLENFTLK VAYIPDEMAA QQNPLQQPRG RRGLGQRGSS 

       190        200        210        220        230        240 
RQGSPGSVSK QKPCDLPLRL LVPTQFVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA 

       250        260        270        280        290        300 
EKSITILSTP EGTSAACKSI LEIMHKEAQD IKFTEEIPLK ILAHNNFVGR LIGKEGRNLK 

       310        320        330        340        350        360 
KIEQDTDTKI TISPLQELTL YNPERTITVK GNVETCAKAE EEIMKKIRES YENDIASMNL 

       370        380        390        400        410        420 
QAHLIPGLNL NALGLFPPTS GMPPPTSGPP SAMTPPYPQF EQSETETVHQ FIPALSVGAI 

       430        440        450        460        470        480 
IGKQGQHIKQ LSRFAGASIK IAPAEAPDAK VRMVIITGPP EAQFKAQGRI YGKIKEENFV 

       490        500        510        520        530        540 
SPKEEVKLEA HIRVPSFAAG RVIGKGGKTV NELQNLSSAE VVVPRDQTPD ENDQVVVKIT 

       550        560        570 
GHFYACQVAQ RKIQEILTQV KQHQQQKALQ SGPPQSRRK 

O00425 in FASTA format

View entry in raw text format (no links)
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