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O00425 (IF2B3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor 2 mRNA-binding protein 3

Short name=IGF2 mRNA-binding protein 3
Short name=IMP-3
Alternative name(s):
IGF-II mRNA-binding protein 3
KH domain-containing protein overexpressed in cancer
Short name=hKOC
VICKZ family member 3
Gene names
Name:IGF2BP3
Synonyms:IMP3, KOC1, VICKZ3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding factor that may recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Ref.13 Ref.22

Subunit structure

Can form homooligomers and heterooligomers with IGF2BP1 and IGF2BP3 in an RNA-dependent manner. Interacts with IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU. Ref.16 Ref.22

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. In response to cellular stress, such as oxidative stress, recruited to stress granules. Ref.6 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.22

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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.11 Ref.12 Ref.14 Ref.15

Domain

All KH domains contribute binding to target mRNA. They are also required for RNA-dependent homo- and heterooligomerization. The integrity of KH domains seems not to be required for localization to stress granules. Ref.19 Ref.22

Miscellaneous

Autoantibodies against IGF2BP3 are detected in sera from some patients with a variety of carcinomas.

Sequence similarities

Belongs to the RRM IMP/VICKZ family.

Contains 4 KH domains.

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA transport
Translation regulation
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.6. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from sequence or structural similarity Ref.6. Source: BHF-UCL

regulation of cytokine biosynthetic process

Inferred by curator Ref.6. Source: BHF-UCL

translation

Traceable author statement Ref.6. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay Ref.6. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement Ref.6. Source: ProtInc

mRNA 3'-UTR binding

Inferred from direct assay Ref.19. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from direct assay Ref.6. Source: BHF-UCL

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

translation regulator activity

Inferred from sequence or structural similarity Ref.6. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00425-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O00425-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-381: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Insulin-like growth factor 2 mRNA-binding protein 3
PRO_0000282538

Regions

Domain2 – 7574RRM 1
Domain81 – 15676RRM 2
Domain195 – 26066KH 1
Domain276 – 34368KH 2
Domain405 – 47066KH 3
Domain487 – 55367KH 4

Amino acid modifications

Modified residue1841Phosphoserine Ref.21
Modified residue1871Phosphoserine Ref.21
Modified residue1891Phosphoserine Ref.21
Modified residue5281Phosphothreonine Ref.18 Ref.21

Natural variations

Alternative sequence1 – 381381Missing in isoform 2.
VSP_024172

Experimental info

Mutagenesis2131K → E: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-294; 422-E-E-423 and 505-E-E-506. Ref.22
Mutagenesis2941K → E: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; 422-E-E-423 and 505-E-E-506. Ref.22
Mutagenesis423 – 4242KQ → EE: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 505-E-E-506. Ref.22
Mutagenesis505 – 5062KG → EE: Loss of homo- and heterooligomerization with IGF2BP1 and IGF2BP2, Modestly impaired binding to ACTB and MYC transcripts and almost no effect on ELAVL1-, DHX9- and HNRNPU-binding, nor on subcellular location; when associated with E-213; E-294 and 422-E-E-423. Ref.22
Sequence conflict4101L → Q in AAD09223. Ref.1
Sequence conflict4101L → Q in AAC35208. Ref.1
Sequence conflict4941V → A in CAH56186. Ref.2

Secondary structure

.............. 579
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 2.
Checksum: 78884F56A9D98CDE

FASTA57963,705
        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 EQSETETVHL 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 

« Hide

Isoform 2 [UniParc].

Checksum: 69BEB7C296373BE7
Show »

FASTA19821,630

References

« Hide 'large scale' references
[1]"Cloning of a gene highly overexpressed in cancer coding for a novel KH-domain containing protein."
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.
Oncogene 14:2729-2733(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Pancreas and Pancreatic cancer.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Endometrial tumor.
[3]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Eye.
[5]"Expression of the highly conserved RNA binding protein KOC in embryogenesis."
Mueller-Pillasch F., Pohl B., Wilda M., Lacher U., Beil M., Wallrapp C., Hameister H., Knoechel W., Adler G., Gress T.M.
Mech. Dev. 88:95-99(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"A family of insulin-like growth factor II mRNA-binding proteins represses translation in late development."
Nielsen J., Christiansen J., Lykke-Andersen J., Johnsen A.H., Wewer U.M., Nielsen F.C.
Mol. Cell. Biol. 19:1262-1270(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE NOMENCLATURE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING.
[7]"Autoimmune responses to mRNA binding proteins p62 and Koc in diverse malignancies."
Zhang J.-Y., Chan E.K., Peng X.-X., Lu M., Wang X., Mueller F., Tan E.M.
Clin. Immunol. 100:149-156(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A CARCINOMA ANTIGEN.
[8]"Characterisation of the growth regulating gene IMP3, a candidate for Silver-Russell syndrome."
Monk D., Bentley L., Beechey C., Hitchins M., Peters J., Preece M.A., Stanier P., Moore G.E.
J. Med. Genet. 39:575-581(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[9]"Nuclear transit of human zipcode-binding protein IMP1."
Nielsen J., Adolph S.K., Rajpert-De Meyts E., Lykke-Andersen J., Koch G., Christiansen J., Nielsen F.C.
Biochem. J. 376:383-391(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"VICKZ proteins: a multi-talented family of regulatory RNA-binding proteins."
Yisraeli J.K.
Biol. Cell 97:87-96(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"KOC (K homology domain containing protein overexpressed in cancer): a novel molecular marker that distinguishes between benign and malignant lesions of the pancreas."
Yantiss R.K., Woda B.A., Fanger G.R., Kalos M., Whalen G.F., Tada H., Andersen D.K., Rock K.L., Dresser K.
Diagn. Mol. Pathol. 29:188-195(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular cancer."
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.
Reproduction 130:203-212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[13]"RNA-binding IMPs promote cell adhesion and invadopodia formation."
Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., Nielsen F.C.
EMBO J. 25:1456-1468(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[14]"Analysis of RNA-binding protein IMP3 to predict metastasis and prognosis of renal-cell carcinoma: a retrospective study."
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.
Lancet Oncol. 7:556-564(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"IMP3 is a novel biomarker for adenocarcinoma in situ of the uterine cervix: an immunohistochemical study in comparison with p16(INK4a) expression."
Li C., Rock K.L., Woda B.A., Jiang Z., Fraire A.E., Dresser K.
Mod. Pathol. 20:242-247(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IGF2BP1.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"ZBP1 recognition of beta-actin zipcode induces RNA looping."
Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H.
Genes Dev. 24:148-158(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, DOMAIN.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-187; SER-189 AND THR-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-binding proteins) is modulated by distinct RNA-binding domains."
Wachter K., Kohn M., Stohr N., Huttelmaier S.
Biol. Chem. 394:1077-1090(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9 AND HNRNPU, DOMAIN, SUBCELLULAR LOCATION, MUTAGENESIS OF 213-LYS-GLU-214; 294-LYS-GLU-295; 423-LYS-LYS-424 AND 505-LYS-GLY-506.
[23]"Solution structure of RNA binding domain in insulin-like growth factor 2 mRNA-binding protein 3."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 73-161.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76705 mRNA. Translation: AAD09223.1.
U97188 mRNA. Translation: AAC35208.1.
BX640800 mRNA. Translation: CAE45883.1.
BX648488 mRNA. Translation: CAH56186.1.
AC005082 Genomic DNA. No translation available.
AC021876 Genomic DNA. No translation available.
AC079780 Genomic DNA. No translation available.
BC065269 mRNA. Translation: AAH65269.1.
CCDSCCDS5382.1. [O00425-1]
RefSeqNP_006538.2. NM_006547.2. [O00425-1]
UniGeneHs.700696.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E44NMR-A73-161[»]
ProteinModelPortalO00425.
SMRO00425. Positions 1-161, 198-349, 406-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115887. 58 interactions.
IntActO00425. 17 interactions.
MINTMINT-2997694.
STRING9606.ENSP00000258729.

PTM databases

PhosphoSiteO00425.

Proteomic databases

MaxQBO00425.
PaxDbO00425.
PRIDEO00425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258729; ENSP00000258729; ENSG00000136231. [O00425-1]
GeneID10643.
KEGGhsa:10643.
UCSCuc003swf.3. human. [O00425-2]
uc003swg.3. human. [O00425-1]

Organism-specific databases

CTD10643.
GeneCardsGC07M023316.
HGNCHGNC:28868. IGF2BP3.
HPAHPA002037.
MIM608259. gene.
neXtProtNX_O00425.
PharmGKBPA128394576.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249985.
HOGENOMHOG000000675.
HOVERGENHBG052725.
InParanoidO00425.
KOK13197.
OMANPSQQPR.
OrthoDBEOG7T7GSK.
PhylomeDBO00425.
TreeFamTF320229.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressO00425.
BgeeO00425.
CleanExHS_IGF2BP3.
HS_IMP3.
GenevestigatorO00425.

Family and domain databases

Gene3D3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 4 hits.
PROSITEPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIgf2bp3. human.
EvolutionaryTraceO00425.
GeneWikiIGF2BP3.
GenomeRNAi10643.
NextBio40451.
PROO00425.
SOURCESearch...

Entry information

Entry nameIF2B3_HUMAN
AccessionPrimary (citable) accession number: O00425
Secondary accession number(s): A0A4Z5 expand/collapse secondary AC list , Q63HM0, Q6MZZ2, Q86VB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM