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O88477 (IF2B1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
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:Vickz1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. 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 the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells By similarity. Binds to the oncofetal H19 transcript and regulates its localization By similarity. Binds to and stabilizes BTRC/FBW1A mRNA By similarity. 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 By similarity. 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 By similarity. Interacts with GAP43 transcript and transports it to axons. 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 and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing. Ref.14 Ref.17 Ref.19 Ref.20

Subunit structure

Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3 By similarity. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1 By similarity. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1 By similarity. Associates with mRNP complex By similarity. Interacts with FMR1 By similarity. Component of a multisubunit autoregulatory RNP complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Interacts with AGO1 and AGO2 By similarity. Interacts, through domains KH3 and KH4, with PABPC1 in an RNA-independent manner By similarity. 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. Ref.9

Subcellular location

Nucleus. Cytoplasm. Cytoplasmperinuclear region By similarity. Cell projectionlamellipodium By similarity. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Cell projectiongrowth cone By similarity. 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 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 neuronal processes, exhibits fast retrograde and anterograde movements, when associated with ACTB mRNA; this motility is lost when the association is inhibited 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 NMDA receptor agonists 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. 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 By similarity. Ref.12 Ref.13

Tissue specificity

Expressed in zygotes and blastocysts (at protein level). Expressed in brain, skeletal muscle, trophoblasts of placenta, oocytes and spermatogonia (at protein level). Expressed in testis and ovary. Following colon injury, expressed in the wound bed mesenchyme during the first phase of repair, probably by colonic mesenchymal stem cells (at protein level). Ref.10 Ref.16 Ref.19 Ref.20

Developmental stage

Expressed during embryonic development and expression declines towards birth (at protein level). At 10.5 dpc, mainly expressed in the fore- and hindbrain, the snout, the branchial arches, the developing limb buds, and the tail. At 12.5 dpc, expression increased in the expanding fore- and hindbrain, as well as in the neural tract. Marked expression also observed in the snout, the interdigital mesenchyme of the limb buds, the tail, the branchial arches and somites, and the developing eye, tongue, heart and liver. Expressed in myoblasts and myotubes at 12.5 dpc (at protein level). From 12.5 to 15.5 dpc, expressed at the basal plasma cell membrane in the basal layer of the epidermis of the skin, lung and intestine (at protein level). Expressed in gonads at 12.5 and 14.5 dpc (at protein level). At 14.5 dpc in limb buds, becomes restricted to the future tendons. Expressed in germ cells at 16.5 dpc (at protein level). At 17.5 dpc, expression generally decreases, but remains high in the intestine, in the developing tubules of the kidney, and in the liver. Expressed until P12, although very low levels may remain in some tissues, such as intestines, kidney and brain, throughout adulthood. Following colonic injury, up-regulated in the wound mucosa at days 2 and 4 post-injury and down-regulated at day 6 post-injury, as compared with uninjured mucosa. Ref.10 Ref.11 Ref.15 Ref.16 Ref.19 Ref.20

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.

Post-translational modification

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

Disruption phenotype

Mutant mice exhibit high perinatal mortality and only 50% are alive 3 days after birth. Early death may be due to intestinal dysfunction. Animals are on average 40% smaller than wild-type and heterozygous sex-matched littermates. Growth retardation, probably due to hypoplasia, appears from 17.5 dpc and remains permanent into adult life. Mutant animals exhibit other stricking features, including impaired development of the intestine, with small and misshapen villi and twisted colon crypts, abnormal kidney architecture and loss of cartilage in the lower extremities. Some animals show signs of neurological damage, including aggressive behavior, restlessness and circular movements. Ref.15

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
   DomainRepeat
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCRD-mediated mRNA stabilization

Inferred from electronic annotation. Source: Ensembl

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of translation

Inferred from electronic annotation. Source: Ensembl

regulation of mRNA stability involved in response to stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentCRD-mediated mRNA stability complex

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic stress granule

Inferred from sequence or structural similarity. Source: UniProtKB

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

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmRNA 3'-UTR binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from electronic annotation. Source: Ensembl

mRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

translation regulator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 577577Insulin-like growth factor 2 mRNA-binding protein 1
PRO_0000282534

Regions

Domain2 – 7574RRM 1
Domain81 – 15676RRM 2
Domain195 – 26066KH 1
Domain276 – 34368KH 2
Domain405 – 47066KH 3
Domain487 – 55367KH 4
Region187 – 570384Necessary for interaction with IGF2BP1 and binding to TAU mRNA
Region312 – 32312Sufficient for nuclear export By similarity
Region485 – 49511Sufficient for nuclear export By similarity

Amino acid modifications

Modified residue1811Phosphoserine Ref.18

Experimental info

Sequence conflict2761E → G in AAH51679. Ref.8
Sequence conflict4061E → G in BAC32119. Ref.6

Sequences

Sequence LengthMass (Da)Tools
O88477 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: EFBB1AF2FF9F0344

FASTA57763,451
        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 VSYIPDEQIT QGPENGRRGG FGSRGQPRQG 

       190        200        210        220        230        240 
SPVAAGAPAK QQPVDIPLRL 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 VRMVVITGPP EAQFKAQGRI YGKLKEENFF 

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

       550        560        570 
GHFYASQMAQ RKIRDILAQV KQQHQKGQSN LAQARRK 

« Hide

References

« Hide 'large scale' references
[1]"Control of c-myc mRNA half-life in vitro by a protein capable of binding to a coding region stability determinant."
Bernstein P.L., Herrick D.J., Prokipcak R.D., Ross J.
Genes Dev. 6:642-654(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING.
[3]"The half-life of c-myc mRNA in growing and serum-stimulated cells: influence of the coding and 3' untranslated regions and role of ribosome translocation."
Herrick D.J., Ross J.
Mol. Cell. Biol. 14:2119-2128(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Developmental regulation of CRD-BP, an RNA-binding protein that stabilizes c-myc mRNA in vitro."
Leeds P., Kren B.T., Boylan J.M., Betz N.A., Steer C.J., Gruppuso P.A., Ross J.
Oncogene 14:1279-1286(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"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: NUCLEOTIDE SEQUENCE [MRNA].
[6]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Head.
[7]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[8]"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].
Strain: 129/Sv X 129SvCp.
Tissue: Embryonic stem cell.
[9]"The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in differentiated P19 neuronal cells."
Atlas R., Behar L., Elliott E., Ginzburg I.
J. Neurochem. 89:613-626(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-20; 27-52; 302-325; 509-525 AND 555-561, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A MRNP COMPLEX WITH ELAVL4 AND G3BP, INTERACTION WITH ELAVL4, ASSOCIATION WITH POLYSOMES.
[10]"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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[11]"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: DEVELOPMENTAL STAGE.
[12]"Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved KH domains."
Nielsen F.C., Nielsen J., Kristensen M.A., Koch G., Christiansen J.
J. Cell Sci. 115:2087-2097(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH MICROTUBULES, RNA-BINDING, SUBCELLULAR LOCATION.
[13]"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.
[14]"Targeted knockdown of the RNA-binding protein CRD-BP promotes cell proliferation via an insulin-like growth factor II-dependent pathway in human K562 leukemia cells."
Liao B., Patel M., Hu Y., Charles S., Herrick D.J., Brewer G.
J. Biol. Chem. 279:48716-48724(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Dwarfism and impaired gut development in insulin-like growth factor II mRNA-binding protein 1-deficient mice."
Hansen T.V., Hammer N.A., Nielsen J., Madsen M., Dalbaeck C., Wewer U.M., Christiansen J., Nielsen F.C.
Mol. Cell. Biol. 24:4448-4464(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[16]"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: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[17]"CRD-BP shields c-myc and MDR-1 RNA from endonucleolytic attack by a mammalian endoribonuclease."
Sparanese D., Lee C.H.
Nucleic Acids Res. 35:1209-1221(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[18]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[19]"Limited availability of ZBP1 restricts axonal mRNA localization and nerve regeneration capacity."
Donnelly C.J., Willis D.E., Xu M., Tep C., Jiang C., Yoo S., Schanen N.C., Kirn-Safran C.B., van Minnen J., English A., Yoon S.O., Bassell G.J., Twiss J.L.
EMBO J. 30:4665-4677(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN AXONAL REGENERATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[20]"Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic mesenchymal stem cells in mice."
Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.
Gastroenterology 143:110-121(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INTESTINAL WOUND REPAIR, RNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[21]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF061569 mRNA. Translation: AAC72743.1.
AK044850 mRNA. Translation: BAC32119.1.
AK013940 mRNA. Translation: BAB29071.1.
AL603682 Genomic DNA. Translation: CAM18266.1.
AL606704 Genomic DNA. Translation: CAM22496.1.
BC051679 mRNA. Translation: AAH51679.1.
CCDSCCDS25286.1.
RefSeqNP_034081.1. NM_009951.4.
UniGeneMm.294769.
Mm.491157.

3D structure databases

ProteinModelPortalO88477.
SMRO88477. Positions 1-161, 198-349, 405-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid228260. 3 interactions.
DIPDIP-48578N.
IntActO88477. 2 interactions.
MINTMINT-4112066.

PTM databases

PhosphoSiteO88477.

Proteomic databases

MaxQBO88477.
PaxDbO88477.
PRIDEO88477.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000013559; ENSMUSP00000013559; ENSMUSG00000013415.
GeneID140486.
KEGGmmu:140486.
UCSCuc007lay.2. mouse.

Organism-specific databases

CTD10642.
MGIMGI:1890357. Igf2bp1.

Phylogenomic databases

eggNOGNOG249985.
GeneTreeENSGT00530000063171.
HOGENOMHOG000000675.
HOVERGENHBG052725.
InParanoidO88477.
KOK17391.
OMAGSIENCC.
OrthoDBEOG7T7GSK.
PhylomeDBO88477.
TreeFamTF320229.

Gene expression databases

BgeeO88477.
GenevestigatorO88477.

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

NextBio369796.
PROO88477.
SOURCESearch...

Entry information

Entry nameIF2B1_MOUSE
AccessionPrimary (citable) accession number: O88477
Secondary accession number(s): Q80US9, Q8BRH1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: November 1, 1998
Last modified: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot