IF2B2_MOUSE
ID IF2B2_MOUSE Reviewed; 592 AA.
AC Q5SF07; A6X8Z4; Q3TCU4; Q7TQF9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 2;
DE Short=IGF2 mRNA-binding protein 2;
DE Short=IMP-2;
DE AltName: Full=IGF-II mRNA-binding protein 2;
DE AltName: Full=VICKZ family member 2;
GN Name=Igf2bp2; Synonyms=Imp2, Vickz2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15225648; DOI=10.1016/j.febslet.2004.05.075;
RA Brants J.R., Ayoubi T.A.Y., Chada K., Marchal K., Van de Ven W.J.M.,
RA Petit M.M.R.;
RT "Differential regulation of the insulin-like growth factor II mRNA-binding
RT protein genes by architectural transcription factor HMGA2.";
RL FEBS Lett. 569:277-283(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Dendritic cell;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=10875929; DOI=10.1074/jbc.m001156200;
RA Runge S., Nielsen F.C., Nielsen J., Lykke-Andersen J., Wewer U.M.,
RA Christiansen J.;
RT "H19 RNA binds four molecules of insulin-like growth factor II mRNA-binding
RT protein.";
RL J. Biol. Chem. 275:29562-29569(2000).
RN [5]
RP REVIEW.
RX PubMed=15601260; DOI=10.1042/bc20040151;
RA Yisraeli J.K.;
RT "VICKZ proteins: a multi-talented family of regulatory RNA-binding
RT proteins.";
RL Biol. Cell 97:87-96(2005).
RN [6]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16049158; DOI=10.1530/rep.1.00664;
RA Hammer N.A., Hansen T.O., Byskov A.G., Rajpert-De Meyts E., Groendahl M.L.,
RA Bredkjaer H.E., Wewer U.M., Christiansen J., Nielsen F.C.;
RT "Expression of IGF-II mRNA-binding proteins (IMPs) in gonads and testicular
RT cancer.";
RL Reproduction 130:203-212(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-164 AND THR-543, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: RNA-binding factor that recruits target transcripts to
CC cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging'
CC into mRNPs allows mRNA transport and transient storage. It also
CC modulates the rate and location at which target transcripts encounter
CC the translational apparatus and shields them from endonuclease attacks
CC or microRNA-mediated degradation (By similarity). Preferentially binds
CC to N6-methyladenosine (m6A)-containing mRNAs and increases their
CC stability (By similarity). Binds to the 5'-UTR of the insulin-like
CC growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to
CC beta-actin/ACTB and MYC transcripts (By similarity). Increases MYC mRNA
CC stability by binding to the coding region instability determinant (CRD)
CC and binding is enhanced by m6A-modification of the CRD (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1 and
CC IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD. Interacts
CC with IGF2BP1. Interacts with ELAVL1, DHX9, HNRNPU, MATR3 and PABPC1.
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasm, P-body {ECO:0000250|UniProtKB:Q9Y6M1}. Cytoplasm, Stress
CC granule {ECO:0000250|UniProtKB:Q9Y6M1}. Note=Localized in cytoplasmic
CC mRNP granules containing untranslated mRNAs. Localizes at the
CC connecting piece and the tail of the spermatozoa. In response to
CC cellular stress, such as oxidative stress, recruited to stress granules
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SF07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SF07-2; Sequence=VSP_019576;
CC -!- TISSUE SPECIFICITY: Expressed in oocytes, granulosa cells of small and
CC growing follicles and Leydig cells of the testis (at protein level).
CC Expressed in testis and ovary. {ECO:0000269|PubMed:16049158}.
CC -!- DEVELOPMENTAL STAGE: Expressed in zygotes and blastocysts (at protein
CC level). Expressed in gonads at 12.5, 14.5 and 16.5 dpc (at protein
CC level). Expressed during fetal development at 12.5, 14.5 and 17.5 dpc
CC and declining towards birth. {ECO:0000269|PubMed:10875929,
CC ECO:0000269|PubMed:16049158}.
CC -!- DOMAIN: Domains KH3 and KH4 are the major RNA-binding modules, although
CC KH1 and KH2 may also contribute. The contribution to RNA-binding of
CC individual KH domains may be target-specific. KH1 and KH2, and possibly
CC KH3 and KH4, promote the formation of higher ordered protein-RNA
CC complexes, which may be essential for IGF2BP1 cytoplasmic retention. KH
CC domains are required for RNA-dependent homo- and heterooligomerization
CC and for localization to stress granules.
CC {ECO:0000250|UniProtKB:Q9Y6M1}.
CC -!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
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DR EMBL; AY531659; AAT01428.1; -; mRNA.
DR EMBL; AK170531; BAE41861.1; -; mRNA.
DR EMBL; CT009567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49797.1; -. [Q5SF07-1]
DR RefSeq; NP_898850.2; NM_183029.2. [Q5SF07-1]
DR AlphaFoldDB; Q5SF07; -.
DR SMR; Q5SF07; -.
DR BioGRID; 235510; 13.
DR IntAct; Q5SF07; 1.
DR STRING; 10090.ENSMUSP00000097629; -.
DR iPTMnet; Q5SF07; -.
DR PhosphoSitePlus; Q5SF07; -.
DR REPRODUCTION-2DPAGE; Q5SF07; -.
DR jPOST; Q5SF07; -.
DR MaxQB; Q5SF07; -.
DR PaxDb; Q5SF07; -.
DR PeptideAtlas; Q5SF07; -.
DR PRIDE; Q5SF07; -.
DR ProteomicsDB; 267092; -. [Q5SF07-1]
DR ProteomicsDB; 267093; -. [Q5SF07-2]
DR Antibodypedia; 33841; 634 antibodies from 41 providers.
DR DNASU; 319765; -.
DR Ensembl; ENSMUST00000100052; ENSMUSP00000097629; ENSMUSG00000033581. [Q5SF07-1]
DR GeneID; 319765; -.
DR KEGG; mmu:319765; -.
DR UCSC; uc007yrz.1; mouse. [Q5SF07-2]
DR UCSC; uc007ysa.1; mouse. [Q5SF07-1]
DR CTD; 10644; -.
DR MGI; MGI:1890358; Igf2bp2.
DR VEuPathDB; HostDB:ENSMUSG00000033581; -.
DR eggNOG; KOG2193; Eukaryota.
DR GeneTree; ENSGT00940000154913; -.
DR InParanoid; Q5SF07; -.
DR OMA; SYETQEQ; -.
DR OrthoDB; 286875at2759; -.
DR PhylomeDB; Q5SF07; -.
DR TreeFam; TF320229; -.
DR BioGRID-ORCS; 319765; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Igf2bp2; mouse.
DR PRO; PR:Q5SF07; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q5SF07; protein.
DR Bgee; ENSMUSG00000033581; Expressed in metanephric ureteric bud and 189 other tissues.
DR ExpressionAtlas; Q5SF07; baseline and differential.
DR Genevisible; Q5SF07; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; ISS:UniProtKB.
DR GO; GO:0070934; P:CRD-mediated mRNA stabilization; ISS:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12626; RRM1_IGF2BP2; 1.
DR Gene3D; 3.30.1370.10; -; 2.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR028743; IGF2BP2.
DR InterPro; IPR034843; IGF2BP2_RRM1.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10288:SF93; PTHR10288:SF93; 1.
DR Pfam; PF00013; KH_1; 4.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00322; KH; 4.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54791; SSF54791; 4.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50084; KH_TYPE_1; 4.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..592
FT /note="Insulin-like growth factor 2 mRNA-binding protein 2"
FT /id="PRO_0000244497"
FT DOMAIN 3..76
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 82..157
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 186..251
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 267..334
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 420..485
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 502..568
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 157..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6M1"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..79
FT /note="MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAI
FT RAIETLSGKVELHGKIMEVDYSVSKKL -> MHPSQWPRYGAAGKPFS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019576"
FT CONFLICT 568
FT /note="I -> V (in Ref. 2; BAE41861)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 65584 MW; 9D0E420758F5D1BE CRC64;
MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW AIRAIETLSG
KVELHGKIME VDYSVSKKLR SRRIQIRNIP PHLQWEVLDG LLAEYGTVEN VEQVNTDTET
AVVNVTYMTR EEAKLAIEKL SGHQFEDYSF KISYIPDEEV SSPSPPHRAR EQGHGPGSSS
QARQIDFPLR ILVPTQFVGA IIGKEGLTIK NITKQTQSRV DIHRKENSGA AEKPVTIHAT
PEGTSEACRM ILEIMQKEAD ETKLAEEVPL KILAHNGFVG RLIGKEGRNL KKIEHETGTK
ITISSLQDLS IYNPERTITV RGTIEACANA EIEIMKKLRE AFENDMLAVN QQANLIPGLN
LSALGIFSTG LSVLPPPAGP RGVPPSPPYH PFATHSGYFS SLYPHHHFGP FPHHHSYPEQ
ETVSLFIPTQ AVGAIIGKKG AHIKQLARFA GASIKIAPAE GPDVSERMVI ITGPPEAQFK
AQGRIFGKLK EENFFNPKEE VKLEAHIRVP SSTAGRVIGK GGKTVNELQN LTSAEVIVPR
DQTPDENEEV IVRIIGHFFA SQTAQRKIRE IVQQVKQQEQ RYPQGVAPQR SK
