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Protein

Insulin-like growth factor 2 mRNA-binding protein 3

Gene

Igf2bp3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity). Binds to beta-actin/ACTB and MYC transcripts (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA transport, Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor 2 mRNA-binding protein 3
Short name:
IGF2 mRNA-binding protein 3
Short name:
IMP-3
Short name:
mIMP-3
Alternative name(s):
IGF-II mRNA-binding protein 3
VICKZ family member 3
Gene namesi
Name:Igf2bp3
Synonyms:Vickz3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1890359. Igf2bp3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Insulin-like growth factor 2 mRNA-binding protein 3PRO_0000282539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei184 – 1841PhosphoserineBy similarity
Cross-linki475 – 475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei528 – 5281PhosphothreonineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9CPN8.
MaxQBiQ9CPN8.
PaxDbiQ9CPN8.
PRIDEiQ9CPN8.

PTM databases

iPTMnetiQ9CPN8.
PhosphoSiteiQ9CPN8.

Expressioni

Tissue specificityi

Expressed in oocytes, spermatogonia and spermatocytes (at protein level).3 Publications

Developmental stagei

Expressed in zygotes and blastocysts (at protein level). Expressed in gonads at 12.5 and 14.5 dpc (at protein level). Expressed in germ cells at 16.5 dpc (at protein level). Expressed in brain at 10.5 dpc and declining towards birth (at protein level). Expressed during fetal development at 7, 9.5, 10.5, 12.5, 14.5 and 17.5 dpc and declining towards birth.4 Publications

Gene expression databases

BgeeiQ9CPN8.
GenevisibleiQ9CPN8. MM.

Interactioni

Subunit structurei

Homodimer and multimer. Interacts with IGF2BP1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi228262. 2 interactions.
IntActiQ9CPN8. 3 interactions.
MINTiMINT-1848725.
STRINGi10090.ENSMUSP00000031838.

Structurei

3D structure databases

ProteinModelPortaliQ9CPN8.
SMRiQ9CPN8. Positions 1-161, 198-349, 406-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7574RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 15676RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 26066KH 1PROSITE-ProRule annotationAdd
BLAST
Domaini276 – 34368KH 2PROSITE-ProRule annotationAdd
BLAST
Domaini405 – 47066KH 3PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 55367KH 4PROSITE-ProRule annotationAdd
BLAST

Domaini

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the RRM IMP/VICKZ family.Curated
Contains 4 KH domains.PROSITE-ProRule annotation
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2193. Eukaryota.
ENOG410ZKB4. LUCA.
GeneTreeiENSGT00530000063171.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
InParanoidiQ9CPN8.
KOiK13197.
OMAiNPSQQPR.
OrthoDBiEOG7T7GSK.
PhylomeDBiQ9CPN8.
TreeFamiTF320229.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CPN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKLYIGNLS DHAGPADLES VFKDAKIPVA GPFLVKTGYA FVDCPDEGWA
60 70 80 90 100
LKAIEALSGK MELHGKPMEV EHSVPKRQRI RKLQIRNIPP HLQWEVLDSL
110 120 130 140 150
LVQYGVVESC EQVNTDSETA VVNVTYSSKD QARQALDKLN GFQLENFTLK
160 170 180 190 200
VAYIPDETAA QQNPSPQLRG RRGPGQRGSS RQASPGSVSK QKPCDLPLRL
210 220 230 240 250
LVPTQFVGAI IGKEGATIRN ITKQTQSKID VHRKENTGAA EKSITILSTP
260 270 280 290 300
EGTSAACKSI LEIMHKEAQD IKFTEEIPLK ILAHNNFVGR LIGKEGRNLK
310 320 330 340 350
KIEQDTDTKI TISPLQELTL YNPERTITVK GSVETCAKAE EEIMKKIRES
360 370 380 390 400
YENDIASMNL QAHLIPGLNL NALGLFPPTS GMPPPTSGPP STLTPPYPQF
410 420 430 440 450
EQSETETVHL FIPALSVGAI IGKQGQHIKQ LSRFAGASIK IAPAEAPDAK
460 470 480 490 500
VRMVIITGPP EAQFKAQGRI YGKIKEENFV SPKEEVKLEA HIRVPSFAAG
510 520 530 540 550
RVIGKGGKTV NELQSLSSAE VVVPRDQTPD ENDQVVVKIT GHFYACQVAQ
560 570
RKIQEILTQV KQHQQQKALQ SGPPQSRRK
Length:579
Mass (Da):63,575
Last modified:June 1, 2001 - v1
Checksum:iCABD9A4355B392B7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Q → R in BAE27710 (PubMed:16141072).Curated
Sequence conflicti363 – 3631H → N in BAC40370 (PubMed:16141072).Curated
Sequence conflicti574 – 5741P → H in BAE27710 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088465 mRNA. Translation: BAC40370.1.
AK011689 mRNA. Translation: BAB27779.1.
AK147140 mRNA. Translation: BAE27710.1.
BC045138 mRNA. Translation: AAH45138.1.
BC049082 mRNA. Translation: AAH49082.1.
CCDSiCCDS39485.1.
RefSeqiNP_076159.3. NM_023670.3.
UniGeneiMm.281018.

Genome annotation databases

EnsembliENSMUST00000031838; ENSMUSP00000031838; ENSMUSG00000029814.
GeneIDi140488.
KEGGimmu:140488.
UCSCiuc009bwi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088465 mRNA. Translation: BAC40370.1.
AK011689 mRNA. Translation: BAB27779.1.
AK147140 mRNA. Translation: BAE27710.1.
BC045138 mRNA. Translation: AAH45138.1.
BC049082 mRNA. Translation: AAH49082.1.
CCDSiCCDS39485.1.
RefSeqiNP_076159.3. NM_023670.3.
UniGeneiMm.281018.

3D structure databases

ProteinModelPortaliQ9CPN8.
SMRiQ9CPN8. Positions 1-161, 198-349, 406-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228262. 2 interactions.
IntActiQ9CPN8. 3 interactions.
MINTiMINT-1848725.
STRINGi10090.ENSMUSP00000031838.

PTM databases

iPTMnetiQ9CPN8.
PhosphoSiteiQ9CPN8.

Proteomic databases

EPDiQ9CPN8.
MaxQBiQ9CPN8.
PaxDbiQ9CPN8.
PRIDEiQ9CPN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031838; ENSMUSP00000031838; ENSMUSG00000029814.
GeneIDi140488.
KEGGimmu:140488.
UCSCiuc009bwi.2. mouse.

Organism-specific databases

CTDi10643.
MGIiMGI:1890359. Igf2bp3.

Phylogenomic databases

eggNOGiKOG2193. Eukaryota.
ENOG410ZKB4. LUCA.
GeneTreeiENSGT00530000063171.
HOGENOMiHOG000000675.
HOVERGENiHBG052725.
InParanoidiQ9CPN8.
KOiK13197.
OMAiNPSQQPR.
OrthoDBiEOG7T7GSK.
PhylomeDBiQ9CPN8.
TreeFamiTF320229.

Miscellaneous databases

ChiTaRSiIgf2bp3. mouse.
PROiQ9CPN8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CPN8.
GenevisibleiQ9CPN8. MM.

Family and domain databases

Gene3Di3.30.1370.10. 4 hits.
3.30.70.330. 2 hits.
InterProiIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00013. KH_1. 4 hits.
PF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00322. KH. 4 hits.
SM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54791. SSF54791. 4 hits.
SSF54928. SSF54928. 1 hit.
PROSITEiPS50084. KH_TYPE_1. 4 hits.
PS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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 and NOD.
    Tissue: Kidney and Thymus.
  2. "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: C57BL/6J.
    Tissue: Brain and Olfactory epithelium.
  3. "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.
  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: DEVELOPMENTAL STAGE.
  5. "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.
  6. "Expression of mouse igf2 mRNA-binding protein 3 and its implications for the developing central nervous system."
    Mori H., Sakakibara S., Imai T., Nakamura Y., Iijima T., Suzuki A., Yuasa Y., Takeda M., Okano H.
    J. Neurosci. Res. 64:132-143(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, RNA-BINDING.
  7. "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.
  8. Cited for: SUBCELLULAR LOCATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  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. "The RNA-binding protein IMP-3 is a translational activator of insulin-like growth factor II leader-3 mRNA during proliferation of human K562 leukemia cells."
    Liao B., Hu Y., Herrick D.J., Brewer G.
    J. Biol. Chem. 280:18517-18524(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  12. Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  13. "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-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND THR-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Pancreas and Testis.

Entry informationi

Entry nameiIF2B3_MOUSE
AccessioniPrimary (citable) accession number: Q9CPN8
Secondary accession number(s): Q3UHZ6, Q8C2J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.