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Q9NZI8 (IF2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor 2 mRNA-binding protein 1

Short name=IGF2 mRNA-binding protein 1
Short name=IMP-1
Short name=IMP1
Alternative name(s):
Coding region determinant-binding protein
Short name=CRD-BP
IGF-II mRNA-binding protein 1
VICKZ family member 1
Zipcode-binding protein 1
Short name=ZBP-1
Gene names
Name:IGF2BP1
Synonyms:CRDBP, VICKZ1, ZBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length577 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

RNA-binding factor that 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. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons By similarity. Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton By similarity. During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB By similarity. May regulate mRNA transport to activated synapses By similarity. Binds to and stabilizes ABCB1/MDR-1 mRNA By similarity. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing By similarity. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts. Ref.4 Ref.5 Ref.7 Ref.8 Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.23 Ref.26 Ref.27 Ref.28 Ref.32 Ref.35

Subunit structure

Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. During HCV infection, identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon. Interacts (via the KH domains) with HIV-1 GAG (via the second zinc finger motif of NC). Associates (via the RRM domains and KH domains) with HIV-1 particles. Identified in a mRNP complex, composed of at least DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with DHX9, ELAVL2, HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, ILF2, and YBX1. Interacts with FMR1. Component of a multisubunit autoregulatory RNP complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1/UNR. Directly interacts with PABPC1. Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP. Interacts with ELAVL4 in an RNA-dependent manner. Associates with microtubules and polysomes. Interacts with AGO1 and AGO2. Ref.5 Ref.10 Ref.11 Ref.15 Ref.20 Ref.22 Ref.23 Ref.27 Ref.28 Ref.33

Subcellular location

Nucleus. Cytoplasm. Cytoplasmperinuclear region. Cell projectionlamellipodium. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Cell projectiongrowth cone. Cell projectionfilopodium By similarity. Cell projectionaxon By similarity. Note: In the nucleus, located in discrete foci, coinciding with the sites of ACTB transcription By similarity. In the cytoplasm, localizes in cytoplasmic mRNP granules. Colocalizes with microtubules in growth cone filopodia and along neurites in neuronal cells By similarity. Cytoplasmic colocalization with ACTB mRNA is partially lost at the cell periphery, suggesting release of the transcript. In neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited By similarity. In hippocampal neurons, predominantly located within dendrites, particularly at dendritic branching points in young cells, compared to axons By similarity. In axons, predominantly found in axonal branches and their growth cones By similarity. In motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails By similarity. Dendritic levels are regulated by neuronal activity and glutaminergic signals: they are increased by KCl-induced depolarization, which induces rapid efflux from the cell body into dendrites, and decreased by the NMDA receptor agonist By similarity. In motile cells, transported towards the leading edge into the cortical region of the lamellipodia where it is connected to microfilaments By similarity. In response to cellular stress, such as oxidative stress or heat shock, recruited to stress granules, but not to processing bodies. Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 Ref.14 Ref.16 Ref.22 Ref.23 Ref.27

Tissue specificity

Mainly expressed in the embryo, including in fetal liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also expressed follicles of ovary, as well as in gonocytes of testis, spermatogonia, semen, oocytes and placenta (at protein level). Expressed in various cancers, including testis and lung cancers (at protein level), as well as kidney, prostate and trachea cancers. Ref.4 Ref.9 Ref.12 Ref.19

Induction

May be up-regulated in response to CTNNB1/beta-catenin activation (Ref.18). Ref.18

Domain

Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. KH1 and KH2, and possibly KH3 and KH4, promote the formation of higher ordered protein-RNA complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH domains are required for RNA-dependent homo- and heterooligomerization and for localization to stress granules. KH3 and KH4 mediate association with the cytoskeleton. Two nuclear export signals (NES) have been identified in KH2 and KH4 domains, respectively. Only KH2 NES is XPO1-dependent. Both NES may be redundant, since individual in vitro mutations do not affect subcellular location of the full length protein. The 4 KH domains are important to suppress HIV-1 infectivity. Ref.35

Post-translational modification

Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression By similarity.

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 componentCell projection
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCRD-mediated mRNA stabilization

Inferred from direct assay Ref.27. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from direct assay Ref.4. Source: BHF-UCL

regulation of cytokine biosynthetic process

Inferred by curator Ref.4. Source: BHF-UCL

regulation of mRNA stability involved in response to stress

Inferred from mutant phenotype Ref.16. Source: UniProtKB

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from direct assay Ref.27. Source: UniProtKB

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.22. Source: UniProtKB

cytoplasmic stress granule

Inferred from direct assay Ref.16. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

filopodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionmRNA 3'-UTR binding

Inferred from direct assay Ref.35. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from direct assay Ref.4. Source: BHF-UCL

mRNA binding

Inferred from direct assay Ref.16Ref.22. Source: UniProtKB

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.22Ref.20. Source: UniProtKB

translation regulator activity

Inferred from direct assay Ref.4. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZI8-1)

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: Q9NZI8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-273: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Insulin-like growth factor 2 mRNA-binding protein 1
PRO_0000282533

Regions

Domain2 – 7574RRM 1
Domain81 – 15676RRM 2
Domain195 – 26066KH 1
Domain276 – 34368KH 2
Domain405 – 47066KH 3
Domain487 – 55367KH 4
Region187 – 570384Necessary for interaction with ELAVL4 and binding to TAU mRNA By similarity
Region310 – 32415Sufficient for nuclear export
Region485 – 49511Sufficient for nuclear export

Amino acid modifications

Modified residue1811Phosphoserine Ref.13 Ref.17 Ref.29 Ref.31

Natural variations

Alternative sequence135 – 273139Missing in isoform 2.
VSP_045366

Experimental info

Mutagenesis213 – 2142KE → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 294-E-L-295 and 423-E-L-424. Ref.9
Mutagenesis294 – 2952KE → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 423-E-L-424. Ref.9
Mutagenesis423 – 4242KK → EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 294-E-L-295. Ref.9
Sequence conflict101Missing AA sequence Ref.4
Sequence conflict2811I → T in AAF37203. Ref.1
Sequence conflict3201Missing AA sequence Ref.4
Sequence conflict3651I → T in AAF37203. Ref.1

Secondary structure

........................... 577
Helix Strand Turn

Details...

Sequences

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

Last modified May 18, 2010. Version 2.
Checksum: 1D036AE5388D05FA

FASTA57763,481
        10         20         30         40         50         60 
MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA MKAIETFSGK 

        70         80         90        100        110        120 
VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL LAQYGTVENC EQVNTESETA 

       130        140        150        160        170        180 
VVNVTYSNRE QTRQAIMKLN GHQLENHALK VSYIPDEQIA QGPENGRRGG FGSRGQPRQG 

       190        200        210        220        230        240 
SPVAAGAPAK QQQVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA 

       250        260        270        280        290        300 
EKAISVHSTP EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK 

       310        320        330        340        350        360 
KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL 

       370        380        390        400        410        420 
QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM QAPEQEMVQV FIPAQAVGAI 

       430        440        450        460        470        480 
IGKKGQHIKQ LSRFASASIK IAPPETPDSK VRMVIITGPP EAQFKAQGRI YGKLKEENFF 

       490        500        510        520        530        540 
GPKEEVKLET HIRVPASAAG RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII 

       550        560        570 
GHFYASQMAQ RKIRDILAQV KQQHQKGQSN QAQARRK 

« Hide

Isoform 2 [UniParc].

Checksum: 2F615D03F5C00C1E
Show »

FASTA43848,598

References

« Hide 'large scale' references
[1]"Ectopic expression of a KH-domain containing protein, highly homologous to both human IMP-1 and mouse CRD-BP, in benign and malignant mesenchymal tumors."
Ioannidis P., Trangas T., Dimitriadis E., Samiotaki M., Panoutsakopoulos G., Kyriazoglou I., Voutzoulias S., Tsiapalis C.M., Kittas C., Agnantis N., Pandis N.
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A novel splice variant of the human IGF2 mRNA-binding protein 1 (IMP1/CRD-BP) isolated from human Hep3B hepatoma cells."
Gong H.Y., Hu M.C., Wu J.L.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: PROTEIN SEQUENCE OF 4-19; 26-35; 309-324 AND 508-525, FUNCTION, RNA-BINDING, ASSOCIATION WITH A MRNP COMPLEX, TISSUE SPECIFICITY, GENE NOMENCLATURE, SUBCELLULAR LOCATION.
[5]"The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex."
Patel G.P., Ma S., Bag J.
Nucleic Acids Res. 33:7074-7089(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-35; 66-75 AND 510-524, FUNCTION, IDENTIFICATION IN A MRNP COMPLEX WITH PABPC1 AND CSDE1, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING.
[6]"The c-myc coding region determinant-binding protein: a member of a family of KH domain RNA-binding proteins."
Doyle G.A., Betz N.A., Leeds P.F., Fleisig A.J., Prokipcak R.D., Ross J.
Nucleic Acids Res. 26:5036-5044(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 413-429 AND 510-524, SUBCELLULAR LOCATION, RNA-BINDING.
[7]"Purification and properties of a protein that binds to the C-terminal coding region of human c-myc mRNA."
Prokipcak R.D., Herrick D.J., Ross J.
J. Biol. Chem. 269:9261-9269(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[8]"H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding protein."
Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M., Christiansen J.
J. Biol. Chem. 275:29562-29569(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING.
[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, TISSUE SPECIFICITY, MUTAGENESIS OF 213-LYS-GLU-214; 294-LYS-GLU-295 AND 423-LYS-LYS-424.
[10]"Visualization of RNA-protein interactions in living cells: FMRP and IMP1 interact on mRNAs."
Rackham O., Brown C.M.
EMBO J. 23:3346-3355(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FMR1, RNA-BINDING, SUBCELLULAR LOCATION.
[11]"Sequential dimerization of human zipcode-binding protein IMP1 on RNA: a cooperative mechanism providing RNP stability."
Nielsen J., Kristensen M.A., Willemoes M., Nielsen F.C., Christiansen J.
Nucleic Acids Res. 32:4368-4376(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, RNA-BINDING.
[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: TISSUE SPECIFICITY.
[13]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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.
[15]"IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain."
Patel G.P., Bag J.
FEBS J. 273:5678-5690(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, INTERACTION WITH PABPC1, RNA-BINDING.
[16]"ZBP1 regulates mRNA stability during cellular stress."
Stoehr N., Lederer M., Reinke C., Meyer S., Hatzfeld M., Singer R.H., Huettelmaier S.
J. Cell Biol. 175:527-534(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[17]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"CRD-BP mediates stabilization of betaTrCP1 and c-myc mRNA in response to beta-catenin signaling."
Noubissi F.K., Elcheva I., Bhatia N., Shakoori A., Ougolkov A., Liu J., Minamoto T., Ross J., Fuchs S.Y., Spiegelman V.S.
Nature 441:898-901(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, INDUCTION.
[19]"Increased expression of insulin-like growth factor-II messenger RNA-binding protein 1 is associated with tumor progression in patients with lung cancer."
Kato T., Hayama S., Yamabuki T., Ishikawa N., Miyamoto M., Ito T., Tsuchiya E., Kondo S., Nakamura Y., Daigo Y.
Clin. Cancer Res. 13:434-442(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]"Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AGO1 AND AGO2.
[21]"ZBP2 facilitates binding of ZBP1 to beta-actin mRNA during transcription."
Pan F., Huettelmaier S., Singer R.H., Gu W.
Mol. Cell. Biol. 27:8340-8351(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]"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: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH DHX9; ELAVL2; HNRNPA2B1; HNRNPC; HNRNPH1; HNRNPU; IGF2BP2; IGF2BP3; ILF2; PABPC1 AND YBX1, RNA-BINDING, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[23]"Insulin-like growth factor II mRNA binding protein 1 associates with Gag protein of human immunodeficiency virus type 1, and its overexpression affects virus assembly."
Zhou Y., Rong L., Lu J., Pan Q., Liang C.
J. Virol. 82:5683-5692(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIV-1 GAG, SUBCELLULAR LOCATION.
[24]"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.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"CRD-BP protects the coding region of betaTrCP1 mRNA from miR-183-mediated degradation."
Elcheva I., Goswami S., Noubissi F.K., Spiegelman V.S.
Mol. Cell 35:240-246(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[27]"Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[28]"IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR."
Weinlich S., Huettelmaier S., Schierhorn A., Behrens S.-E., Ostareck-Lederer A., Ostareck D.H.
RNA 15:1528-1542(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, IDENTIFICATION IN A HCV IRES-MEDIATED TRANSLATION COMPLEX.
[29]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[30]"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].
[31]"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-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling."
Stohr N., Kohn M., Lederer M., Glass M., Reinke C., Singer R.H., Huttelmaier S.
Genes Dev. 26:176-189(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION.
[33]"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: INTERACTION WITH ELAVL1; DHX9 AND HNRNPU.
[34]"Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-transcriptional drivers of cancer progression?"
Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M., Huttelmaier S.
Cell. Mol. Life Sci. 70:2657-2675(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[35]"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: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 404-566, FUNCTION, RNA-BINDING, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF198254 mRNA. Translation: AAF37203.1.
DQ227344 mRNA. Translation: ABB46294.1.
AC091133 Genomic DNA. No translation available.
AC105030 Genomic DNA. No translation available.
CCDSCCDS11543.1. [Q9NZI8-1]
CCDS54138.1. [Q9NZI8-2]
RefSeqNP_001153895.1. NM_001160423.1. [Q9NZI8-2]
NP_006537.3. NM_006546.3. [Q9NZI8-1]
UniGeneHs.144936.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3KRMX-ray2.75A/B/C404-566[»]
ProteinModelPortalQ9NZI8.
SMRQ9NZI8. Positions 1-161, 198-349, 405-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115886. 50 interactions.
DIPDIP-38139N.
IntActQ9NZI8. 25 interactions.
MINTMINT-4998820.
STRING9606.ENSP00000290341.

PTM databases

PhosphoSiteQ9NZI8.

Polymorphism databases

DMDM296434536.

Proteomic databases

MaxQBQ9NZI8.
PaxDbQ9NZI8.
PeptideAtlasQ9NZI8.
PRIDEQ9NZI8.

Protocols and materials databases

DNASU10642.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290341; ENSP00000290341; ENSG00000159217. [Q9NZI8-1]
ENST00000431824; ENSP00000389135; ENSG00000159217. [Q9NZI8-2]
GeneID10642.
KEGGhsa:10642.
UCSCuc002iom.3. human. [Q9NZI8-1]

Organism-specific databases

CTD10642.
GeneCardsGC17P047074.
H-InvDBHIX0013955.
HGNCHGNC:28866. IGF2BP1.
HPAHPA021367.
MIM608288. gene.
neXtProtNX_Q9NZI8.
PharmGKBPA143485501.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249985.
HOGENOMHOG000000675.
HOVERGENHBG052725.
InParanoidQ9NZI8.
KOK17391.
OMAGSIENCC.
OrthoDBEOG7T7GSK.
PhylomeDBQ9NZI8.
TreeFamTF320229.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9NZI8.
BgeeQ9NZI8.
CleanExHS_IGF2BP1.
HS_ZBP1.
GenevestigatorQ9NZI8.

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

EvolutionaryTraceQ9NZI8.
GeneWikiIGF2BP1.
GenomeRNAi10642.
NextBio40447.
PROQ9NZI8.
SOURCESearch...

Entry information

Entry nameIF2B1_HUMAN
AccessionPrimary (citable) accession number: Q9NZI8
Secondary accession number(s): C9JT33
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 121 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 17

Human chromosome 17: entries, gene names and cross-references to MIM