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Insulin-like growth factor 2 mRNA-binding protein 1 (IGF2 mRNA-binding protein 1) (IMP-1) (Coding region determinant-binding protein) (CRD-BP) (IGF-II mRNA-binding protein 1) (VICKZ family member 1) (Zipcode-binding protein 1) (ZBP-1)

 IF2B1_MOUSE             Reviewed;         577 AA.
O88477; Q80US9; Q8BRH1;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
10-OCT-2018, entry version 152.
RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 1;
Short=IGF2 mRNA-binding protein 1;
Short=IMP-1;
AltName: Full=Coding region determinant-binding protein;
Short=CRD-BP;
AltName: Full=IGF-II mRNA-binding protein 1;
AltName: Full=VICKZ family member 1;
AltName: Full=Zipcode-binding protein 1;
Short=ZBP-1;
Name=Igf2bp1; Synonyms=Vickz1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND RNA-BINDING.
PubMed=1559612; DOI=10.1101/gad.6.4.642;
Bernstein P.L., Herrick D.J., Prokipcak R.D., Ross J.;
"Control of c-myc mRNA half-life in vitro by a protein capable of
binding to a coding region stability determinant.";
Genes Dev. 6:642-654(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND RNA-BINDING.
PubMed=8132663;
Prokipcak R.D., Herrick D.J., Ross J.;
"Purification and properties of a protein that binds to the C-terminal
coding region of human c-myc mRNA.";
J. Biol. Chem. 269:9261-9269(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8114742; DOI=10.1128/MCB.14.3.2119;
Herrick D.J., Ross J.;
"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.";
Mol. Cell. Biol. 14:2119-2128(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9178888; DOI=10.1038/sj.onc.1201093;
Leeds P., Kren B.T., Boylan J.M., Betz N.A., Steer C.J.,
Gruppuso P.A., Ross J.;
"Developmental regulation of CRD-BP, an RNA-binding protein that
stabilizes c-myc mRNA in vitro.";
Oncogene 14:1279-1286(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9801297; DOI=10.1093/nar/26.22.5036;
Doyle G.A., Betz N.A., Leeds P.F., Fleisig A.J., Prokipcak R.D.,
Ross J.;
"The c-myc coding region determinant-binding protein: a member of a
family of KH domain RNA-binding proteins.";
Nucleic Acids Res. 26:5036-5044(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
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., 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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[9]
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, AND ASSOCIATION WITH
POLYSOMES.
PubMed=15086518; DOI=10.1111/j.1471-4159.2004.02371.x;
Atlas R., Behar L., Elliott E., Ginzburg I.;
"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.";
J. Neurochem. 89:613-626(2004).
[10]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=9891060; DOI=10.1128/MCB.19.2.1262;
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).
[11]
DEVELOPMENTAL STAGE.
PubMed=10875929; DOI=10.1074/jbc.M001156200;
Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M.,
Christiansen J.;
"H19 RNA binds four molecules of insulin-like growth factor II mRNA-
binding protein.";
J. Biol. Chem. 275:29562-29569(2000).
[12]
ASSOCIATION WITH MICROTUBULES, RNA-BINDING, AND SUBCELLULAR LOCATION.
PubMed=11973350;
Nielsen F.C., Nielsen J., Kristensen M.A., Koch G., Christiansen J.;
"Cytoplasmic trafficking of IGF-II mRNA-binding protein by conserved
KH domains.";
J. Cell Sci. 115:2087-2097(2002).
[13]
SUBCELLULAR LOCATION.
PubMed=12921532; DOI=10.1042/BJ20030943;
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).
[14]
FUNCTION.
PubMed=15355996; DOI=10.1074/jbc.M405853200;
Liao B., Patel M., Hu Y., Charles S., Herrick D.J., Brewer G.;
"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.";
J. Biol. Chem. 279:48716-48724(2004).
[15]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=15121863; DOI=10.1128/MCB.24.10.4448-4464.2004;
Hansen T.V., Hammer N.A., Nielsen J., Madsen M., Dalbaeck C.,
Wewer U.M., Christiansen J., Nielsen F.C.;
"Dwarfism and impaired gut development in insulin-like growth factor
II mRNA-binding protein 1-deficient mice.";
Mol. Cell. Biol. 24:4448-4464(2004).
[16]
DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
PubMed=16049158; DOI=10.1530/rep.1.00664;
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).
[17]
FUNCTION, AND RNA-BINDING.
PubMed=17264115; DOI=10.1093/nar/gkl1148;
Sparanese D., Lee C.H.;
"CRD-BP shields c-myc and MDR-1 RNA from endonucleolytic attack by a
mammalian endoribonuclease.";
Nucleic Acids Res. 35:1209-1221(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[20]
FUNCTION IN AXONAL REGENERATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=21964071; DOI=10.1038/emboj.2011.347;
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.;
"Limited availability of ZBP1 restricts axonal mRNA localization and
nerve regeneration capacity.";
EMBO J. 30:4665-4677(2011).
[21]
FUNCTION IN INTESTINAL WOUND REPAIR, RNA-BINDING, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=22465430; DOI=10.1053/j.gastro.2012.03.037;
Manieri N.A., Drylewicz M.R., Miyoshi H., Stappenbeck T.S.;
"Igf2bp1 is required for full induction of Ptgs2 mRNA in colonic
mesenchymal stem cells in mice.";
Gastroenterology 143:110-121(2012).
[22]
REVIEW.
PubMed=23069990; DOI=10.1007/s00018-012-1186-z;
Bell J.L., Wachter K., Muhleck B., Pazaitis N., Kohn M., Lederer M.,
Huttelmaier S.;
"Insulin-like growth factor 2 mRNA-binding proteins (IGF2BPs): post-
transcriptional drivers of cancer progression?";
Cell. Mol. Life Sci. 70:2657-2675(2013).
-!- 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.
{ECO:0000250, ECO:0000269|PubMed:15355996,
ECO:0000269|PubMed:17264115, ECO:0000269|PubMed:21964071,
ECO:0000269|PubMed:22465430}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:15086518}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear
region {ECO:0000250}. Cell projection, lamellipodium
{ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
projection, dendritic spine {ECO:0000250}. Cell projection, growth
cone {ECO:0000250}. Cell projection, filopodium {ECO:0000250}.
Cell projection, axon {ECO:0000250}. 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). {ECO:0000250}.
-!- 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).
{ECO:0000269|PubMed:16049158, ECO:0000269|PubMed:21964071,
ECO:0000269|PubMed:22465430, ECO:0000269|PubMed:9891060}.
-!- 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. {ECO:0000269|PubMed:10875929,
ECO:0000269|PubMed:15121863, ECO:0000269|PubMed:16049158,
ECO:0000269|PubMed:21964071, ECO:0000269|PubMed:22465430,
ECO:0000269|PubMed:9891060}.
-!- 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.
-!- PTM: Phosphorylated. Phosphorylation may impair association with
ACTB mRNA and hence abolishes translational repression (By
similarity). {ECO:0000250}.
-!- 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. {ECO:0000269|PubMed:15121863}.
-!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF061569; AAC72743.1; -; mRNA.
EMBL; AK044850; BAC32119.1; -; mRNA.
EMBL; AK013940; BAB29071.1; -; mRNA.
EMBL; AL603682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL606704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051679; AAH51679.1; -; mRNA.
CCDS; CCDS25286.1; -.
RefSeq; NP_034081.1; NM_009951.4.
UniGene; Mm.294769; -.
UniGene; Mm.491157; -.
ProteinModelPortal; O88477; -.
SMR; O88477; -.
BioGrid; 228260; 7.
ComplexPortal; CPX-1089; CRD-mediated mRNA stability complex.
DIP; DIP-48578N; -.
IntAct; O88477; 5.
MINT; O88477; -.
STRING; 10090.ENSMUSP00000013559; -.
iPTMnet; O88477; -.
PhosphoSitePlus; O88477; -.
MaxQB; O88477; -.
PaxDb; O88477; -.
PeptideAtlas; O88477; -.
PRIDE; O88477; -.
Ensembl; ENSMUST00000013559; ENSMUSP00000013559; ENSMUSG00000013415.
GeneID; 140486; -.
KEGG; mmu:140486; -.
UCSC; uc007lay.2; mouse.
CTD; 10642; -.
MGI; MGI:1890357; Igf2bp1.
eggNOG; KOG2193; Eukaryota.
eggNOG; ENOG410ZKB4; LUCA.
GeneTree; ENSGT00530000063171; -.
HOGENOM; HOG000000675; -.
HOVERGEN; HBG052725; -.
InParanoid; O88477; -.
KO; K17391; -.
OMA; EKPISIH; -.
OrthoDB; EOG091G17T1; -.
PhylomeDB; O88477; -.
TreeFam; TF320229; -.
PRO; PR:O88477; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000013415; Expressed in 145 organ(s), highest expression level in brain.
Genevisible; O88477; MM.
GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:MGI.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0045182; F:translation regulator activity; ISO:MGI.
GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISO:MGI.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
GO; GO:0022013; P:pallium cell proliferation in forebrain; IMP:MGI.
GO; GO:0010610; P:regulation of mRNA stability involved in response to stress; ISS:UniProtKB.
GO; GO:0006403; P:RNA localization; ISO:MGI.
CDD; cd12625; RRM1_IGF2BP1; 1.
CDD; cd12628; RRM2_IGF2BP1; 1.
Gene3D; 3.30.1370.10; -; 2.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR034837; IGF2BP1_RRM1.
InterPro; IPR034842; IGF2BP1_RRM2.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00013; KH_1; 4.
Pfam; PF00076; RRM_1; 2.
SMART; SM00322; KH; 4.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54791; SSF54791; 4.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50084; KH_TYPE_1; 4.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
Cell projection; Complete proteome; Cytoplasm;
Direct protein sequencing; mRNA transport; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Translation regulation;
Transport.
CHAIN 1 577 Insulin-like growth factor 2 mRNA-binding
protein 1.
/FTId=PRO_0000282534.
DOMAIN 2 75 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 81 156 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 195 260 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 276 343 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 405 470 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 487 553 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
REGION 187 570 Necessary for interaction with IGF2BP1
and binding to TAU mRNA.
REGION 312 323 Sufficient for nuclear export.
{ECO:0000250}.
REGION 485 495 Sufficient for nuclear export.
{ECO:0000250}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NZI8}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NZI8}.
MOD_RES 181 181 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 528 528 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9NZI8}.
CONFLICT 276 276 E -> G (in Ref. 8; AAH51679).
{ECO:0000305}.
CONFLICT 406 406 E -> G (in Ref. 6; BAC32119).
{ECO:0000305}.
SEQUENCE 577 AA; 63451 MW; EFBB1AF2FF9F0344 CRC64;
MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA MKAIETFSGK
VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL LAQYGTVENC EQVNTESETA
VVNVTYSNRE QTRQAIMKLN GHQLENHALK VSYIPDEQIT QGPENGRRGG FGSRGQPRQG
SPVAAGAPAK QQPVDIPLRL LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA
EKAISVHSTP EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK
KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA YENDVAAMSL
QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM QAPEQEMVQV FIPAQAVGAI
IGKKGQHIKQ LSRFASASIK IAPPETPDSK VRMVVITGPP EAQFKAQGRI YGKLKEENFF
GPKEEVKLET HIRVPASAAG RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII
GHFYASQMAQ RKIRDILAQV KQQHQKGQSN LAQARRK


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