Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Insulin-like growth factor 2 mRNA-binding protein 2 (IGF2 mRNA-binding protein 2) (IMP-2) (Hepatocellular carcinoma autoantigen p62) (IGF-II mRNA-binding protein 2) (VICKZ family member 2)

 IF2B2_HUMAN             Reviewed;         599 AA.
Q9Y6M1; A0A4Z0; B3FTN2; B3FTN3; B3FTN4;
27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
03-MAR-2009, sequence version 2.
10-OCT-2018, entry version 161.
RecName: Full=Insulin-like growth factor 2 mRNA-binding protein 2;
Short=IGF2 mRNA-binding protein 2;
Short=IMP-2;
AltName: Full=Hepatocellular carcinoma autoantigen p62;
AltName: Full=IGF-II mRNA-binding protein 2;
AltName: Full=VICKZ family member 2;
Name=IGF2BP2; Synonyms=IMP2, VICKZ2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION AS A
HEPATOCELLULAR CARCINOMA ANTIGEN, TISSUE SPECIFICITY, AND SUBCELLULAR
LOCATION.
TISSUE=Colon adenocarcinoma;
PubMed=10190901; DOI=10.1084/jem.189.7.1101;
Zhang J.-Y., Chan E.K.L., Peng X.-X., Tan E.M.;
"A novel cytoplasmic protein with RNA-binding motifs is an autoantigen
in human hepatocellular carcinoma.";
J. Exp. Med. 189:1101-1110(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5).
TISSUE=Pancreatic islet;
Prokunina-Olsson L., Hanisch J.J., Jackson A., Chines P.S.,
Erdos M.R., Bonnycastle L.L., Swift A., Narisu N., Scott L.J.,
Morken M., Mohlke K., Bergman R., Tuomilehto J., Boehnke M.,
Rotimi C.N., Watanabe R.N., Collins F.S.;
"A novel type 2 diabetes-associated variant of IGF2BP2 gene affects
expression of a functional alternative splicing form.";
Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
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).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[6]
INTERACTION WITH HNRPD.
PubMed=12674497; DOI=10.1515/BC.2003.004;
Moraes K.C., Quaresma A.J., Maehnss K., Kobarg J.;
"Identification and characterization of proteins that selectively
interact with isoforms of the mRNA binding protein AUF1 (hnRNP D).";
Biol. Chem. 384:25-37(2003).
[7]
REVIEW.
PubMed=15601260; DOI=10.1042/BC20040151;
Yisraeli J.K.;
"VICKZ proteins: a multi-talented family of regulatory RNA-binding
proteins.";
Biol. Cell 97:87-96(2005).
[8]
SUBCELLULAR LOCATION, 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).
[9]
INTERACTION WITH IGF2BP1, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
RNA-BINDING, AND DOMAIN.
PubMed=20080952; DOI=10.1101/gad.1862910;
Chao J.A., Patskovsky Y., Patel V., Levy M., Almo S.C., Singer R.H.;
"ZBP1 recognition of beta-actin zipcode induces RNA looping.";
Genes Dev. 24:148-158(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ALTERNATIVE INITIATION (ISOFORM 6).
PubMed=22427968; DOI=10.1371/journal.pone.0033140;
Le H.T., Sorrell A.M., Siddle K.;
"Two isoforms of the mRNA binding protein IGF2BP2 are generated by
alternative translational initiation.";
PLoS ONE 7:E33140-E33140(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
FUNCTION, RNA-BINDING, OLIGOMERIZATION, INTERACTION WITH ELAVL1; DHX9
AND HNRNPU, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-211;
LYS-292; 445-LYS-LYS-446 AND 527-LYS-GLY-528.
PubMed=23640942; DOI=10.1515/hsz-2013-0111;
Wachter K., Kohn M., Stohr N., Huttelmaier S.;
"Subcellular localization and RNP formation of IGF2BPs (IGF2 mRNA-
binding proteins) is modulated by distinct RNA-binding domains.";
Biol. Chem. 394:1077-1090(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-164, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
STRUCTURE BY NMR OF 2-81.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RNA binding domain of IGF-II mRNA-binding
protein 2.";
Submitted (NOV-2005) to the PDB data bank.
-!- 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 (By
similarity). Binds to the 5'-UTR of the insulin-like growth factor
2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-
actin/ACTB and MYC transcripts. {ECO:0000250,
ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:9891060}.
-!- SUBUNIT: Can form homooligomers and heterooligomers with IGF2BP1
and IGF2BP3 in an RNA-dependent manner. Interacts with HNRPD and
IGF2BP1. Interacts with ELAVL1, DHX9 and HNRNPU.
{ECO:0000269|PubMed:12674497, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:23640942}.
-!- INTERACTION:
Q14103-4:HNRNPD; NbExp=4; IntAct=EBI-1024419, EBI-432545;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
cytoplasmic mRNP granules containing untranslated mRNAs. Localizes
at the connecting piece and the tail of the spermatozoa. In
response to cellular stress, such as oxidative stress, recruited
to stress granules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=6;
Name=1;
IsoId=Q9Y6M1-2; Sequence=Displayed;
Name=2;
IsoId=Q9Y6M1-1; Sequence=VSP_036553;
Name=3;
IsoId=Q9Y6M1-3; Sequence=VSP_036550;
Name=4;
IsoId=Q9Y6M1-4; Sequence=VSP_036550, VSP_036552;
Name=5;
IsoId=Q9Y6M1-5; Sequence=VSP_036550, VSP_036553;
Name=6;
IsoId=Q9Y6M1-6; Sequence=VSP_043699;
Note=Generated by alternative initiation at Met-69. Contains a
N-acetylmethionine at position 1. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: Expressed in oocytes, granulosa cells of small
and growing follicles, Leydig cells, spermatogonia and semen (at
protein level). Expressed in testicular cancer (at protein level).
Expressed weakly in heart, placenta, skeletal muscle, bone marrow,
colon, kidney, salivary glands, testis and pancreas. Detected in
fetal liver, fetal ovary, gonocytes and interstitial cells of the
testis. {ECO:0000269|PubMed:10190901,
ECO:0000269|PubMed:16049158}.
-!- DOMAIN: Domain KH3 and KH4 are the major RNA-binding modules,
although KH1 and KH2 may also contribute. The contribution to RNA-
binding of individual KH domains may be target-specific. 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. {ECO:0000269|PubMed:20080952,
ECO:0000269|PubMed:23640942}.
-!- MISCELLANEOUS: Autoantibodies against IGF2BP2 are detected in sera
from some patients with hepatocellular carcinoma.
-!- SIMILARITY: Belongs to the RRM IMP/VICKZ family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH21290.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF057352; AAD31596.1; -; mRNA.
EMBL; EU408701; ACB86625.1; -; mRNA.
EMBL; EU408702; ACB86626.1; -; mRNA.
EMBL; EU408703; ACB86627.1; -; mRNA.
EMBL; AC016961; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021290; AAH21290.1; ALT_INIT; mRNA.
CCDS; CCDS3273.2; -. [Q9Y6M1-2]
CCDS; CCDS33903.1; -. [Q9Y6M1-1]
CCDS; CCDS77869.1; -. [Q9Y6M1-3]
RefSeq; NP_001007226.1; NM_001007225.2. [Q9Y6M1-1]
RefSeq; NP_001278801.1; NM_001291872.2. [Q9Y6M1-4]
RefSeq; NP_001278802.1; NM_001291873.2. [Q9Y6M1-3]
RefSeq; NP_001278803.1; NM_001291874.2. [Q9Y6M1-5]
RefSeq; NP_001278804.1; NM_001291875.2.
RefSeq; NP_006539.3; NM_006548.5. [Q9Y6M1-2]
UniGene; Hs.293396; -.
UniGene; Hs.35354; -.
PDB; 2CQH; NMR; -; A=2-81.
PDBsum; 2CQH; -.
ProteinModelPortal; Q9Y6M1; -.
SMR; Q9Y6M1; -.
BioGrid; 115888; 122.
DIP; DIP-35539N; -.
IntAct; Q9Y6M1; 36.
MINT; Q9Y6M1; -.
STRING; 9606.ENSP00000371634; -.
iPTMnet; Q9Y6M1; -.
PhosphoSitePlus; Q9Y6M1; -.
SwissPalm; Q9Y6M1; -.
BioMuta; IGF2BP2; -.
DMDM; 224471831; -.
EPD; Q9Y6M1; -.
MaxQB; Q9Y6M1; -.
PaxDb; Q9Y6M1; -.
PeptideAtlas; Q9Y6M1; -.
PRIDE; Q9Y6M1; -.
ProteomicsDB; 86724; -.
ProteomicsDB; 86725; -. [Q9Y6M1-1]
ProteomicsDB; 86726; -. [Q9Y6M1-3]
ProteomicsDB; 86727; -. [Q9Y6M1-4]
ProteomicsDB; 86728; -. [Q9Y6M1-5]
ProteomicsDB; 86729; -. [Q9Y6M1-6]
DNASU; 10644; -.
Ensembl; ENST00000346192; ENSP00000320204; ENSG00000073792. [Q9Y6M1-1]
Ensembl; ENST00000382199; ENSP00000371634; ENSG00000073792. [Q9Y6M1-2]
Ensembl; ENST00000421047; ENSP00000413787; ENSG00000073792. [Q9Y6M1-3]
GeneID; 10644; -.
KEGG; hsa:10644; -.
UCSC; uc003fpo.4; human. [Q9Y6M1-2]
CTD; 10644; -.
DisGeNET; 10644; -.
EuPathDB; HostDB:ENSG00000073792.15; -.
GeneCards; IGF2BP2; -.
HGNC; HGNC:28867; IGF2BP2.
HPA; CAB017126; -.
HPA; HPA035145; -.
MalaCards; IGF2BP2; -.
MIM; 608289; gene.
neXtProt; NX_Q9Y6M1; -.
OpenTargets; ENSG00000073792; -.
PharmGKB; PA128394577; -.
eggNOG; KOG2193; Eukaryota.
eggNOG; ENOG410ZKB4; LUCA.
GeneTree; ENSGT00530000063171; -.
HOGENOM; HOG000000675; -.
HOVERGEN; HBG052725; -.
InParanoid; Q9Y6M1; -.
KO; K17392; -.
PhylomeDB; Q9Y6M1; -.
TreeFam; TF320229; -.
Reactome; R-HSA-428359; Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA.
ChiTaRS; IGF2BP2; human.
EvolutionaryTrace; Q9Y6M1; -.
GeneWiki; IGF2BP2; -.
GenomeRNAi; 10644; -.
PRO; PR:Q9Y6M1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000073792; Expressed in 204 organ(s), highest expression level in kidney.
CleanEx; HS_IGF2BP2; -.
ExpressionAtlas; Q9Y6M1; baseline and differential.
Genevisible; Q9Y6M1; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0045182; F:translation regulator activity; ISS:BHF-UCL.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0017148; P:negative regulation of translation; ISS:BHF-UCL.
GO; GO:0042035; P:regulation of cytokine biosynthetic process; IC:BHF-UCL.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
CDD; cd12626; RRM1_IGF2BP2; 1.
Gene3D; 3.30.1370.10; -; 2.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR028743; IGF2BP2.
InterPro; IPR034843; IGF2BP2_RRM1.
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.
PANTHER; PTHR10288:SF93; PTHR10288:SF93; 1.
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;
3D-structure; Acetylation; Alternative initiation;
Alternative splicing; Complete proteome; Cytoplasm; mRNA transport;
Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
Translation regulation; Transport.
CHAIN 1 599 Insulin-like growth factor 2 mRNA-binding
protein 2.
/FTId=PRO_0000244496.
DOMAIN 3 76 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 82 157 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 193 258 KH 1. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 274 341 KH 2. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 427 492 KH 3. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
DOMAIN 509 575 KH 4. {ECO:0000255|PROSITE-
ProRule:PRU00117}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 164 164 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 550 550 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5SF07}.
VAR_SEQ 1 80 MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYA
FVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLR
-> MFSCPGHYHVDGFLNPG (in isoform 3,
isoform 4 and isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_036550.
VAR_SEQ 1 68 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_043699.
VAR_SEQ 113 113 Q -> QVFAFSL (in isoform 4).
{ECO:0000303|Ref.2}.
/FTId=VSP_036552.
VAR_SEQ 358 400 Missing (in isoform 2 and isoform 5).
{ECO:0000303|PubMed:10190901,
ECO:0000303|Ref.2}.
/FTId=VSP_036553.
MUTAGEN 211 211 K->E: Significantly impaired binding to
ACTB transcript, but little effect on MYC
transcript binding, accumulation in the
nucleus; when associated with E-292. Loss
of homo- and heterooligomerization with
IGF2BP1 and IGF2BP2, almost complete loss
of ACTB and MYC transcript binding,
almost complete loss of ELAVL1-,
DHX9- and HNRNPU-binding and perturbed
subcellular location, including
accumulation in the nucleus and loss of
localization to stress granules; when
associated with E-292; 445-E-E-446 and
526-E-E-527.
{ECO:0000269|PubMed:23640942}.
MUTAGEN 292 292 K->E: Significantly impaired binding to
ACTB transcript, but little effect on MYC
transcript binding, accumulation in the
nucleus; when associated with E-211. Loss
of homo- and heterooligomerization with
IGF2BP1 and IGF2BP2, almost complete loss
of ACTB and MYC transcript binding,
almost complete loss of ELAVL1-,
DHX9- and HNRNPU-binding and perturbed
subcellular location, including
accumulation in the nucleus and loss of
localization to stress granules; when
associated with E-211; 445-E-E-445 and
526-E-E-527.
{ECO:0000269|PubMed:23640942}.
MUTAGEN 445 446 KK->EE: Significantly impaired binding to
ACTB and MYC transcripts; when associated
with 527-E-E-528. Loss of homo- and
heterooligomerization with IGF2BP1 and
IGF2BP2, almost complete loss of ACTB and
MYC transcript binding, almost complete
loss of ELAVL1-, DHX9- and HNRNPU-binding
and perturbed subcellular location,
including accumulation in the nucleus and
loss of localization to stress granules;
when associated with E-211; E-292 and
527-E-E-528.
{ECO:0000269|PubMed:23640942}.
MUTAGEN 527 528 KG->EE: Significantly impaired binding to
ACTB and MYC transcripts; when associated
with 445-E-E-446. Loss of homo- and
heterooligomerization with IGF2BP1 and
IGF2BP2, almost complete loss of ACTB and
MYC transcript binding, almost complete
loss of ELAVL1-, DHX9- and HNRNPU-binding
and perturbed subcellular location,
including accumulation in the nucleus and
loss of localization to stress granules;
when associated with E-211; E-292 and
445-E-E-446.
{ECO:0000269|PubMed:23640942}.
STRAND 5 8 {ECO:0000244|PDB:2CQH}.
HELIX 16 25 {ECO:0000244|PDB:2CQH}.
STRAND 34 37 {ECO:0000244|PDB:2CQH}.
STRAND 40 43 {ECO:0000244|PDB:2CQH}.
HELIX 48 58 {ECO:0000244|PDB:2CQH}.
TURN 59 61 {ECO:0000244|PDB:2CQH}.
STRAND 70 73 {ECO:0000244|PDB:2CQH}.
SEQUENCE 599 AA; 66121 MW; EA656F8733BBB39A CRC64;
MMNKLYIGNL SPAVTADDLR QLFGDRKLPL AGQVLLKSGY AFVDYPDQNW AIRAIETLSG
KVELHGKIME VDYSVSKKLR SRKIQIRNIP PHLQWEVLDG LLAQYGTVEN VEQVNTDTET
AVVNVTYATR EEAKIAMEKL SGHQFENYSF KISYIPDEEV SSPSPPQRAQ RGDHSSREQG
HAPGGTSQAR QIDFPLRILV PTQFVGAIIG KEGLTIKNIT KQTQSRVDIH RKENSGAAEK
PVTIHATPEG TSEACRMILE IMQKEADETK LAEEIPLKIL AHNGLVGRLI GKEGRNLKKI
EHETGTKITI SSLQDLSIYN PERTITVKGT VEACASAEIE IMKKLREAFE NDMLAVNQQA
NLIPGLNLSA LGIFSTGLSV LSPPAGPRGA PPAAPYHPFT THSGYFSSLY PHHQFGPFPH
HHSYPEQEIV NLFIPTQAVG AIIGKKGAHI KQLARFAGAS IKIAPAEGPD VSERMVIITG
PPEAQFKAQG RIFGKLKEEN FFNPKEEVKL EAHIRVPSST AGRVIGKGGK TVNELQNLTS
AEVIVPRDQT PDENEEVIVR IIGHFFASQT AQRKIREIVQ QVKQQEQKYP QGVASQRSK


Related products :

Catalog number Product name Quantity
18-003-44208 Insulin-like growth factor 2 mRNA-binding protein 1 - IGF2 mRNA-binding protein 1; IGF-II mRNA-binding protein 1; IMP-1; Coding region determinant-binding protein; CRD-BP; VICKZ family member 1 Polycl 0.05 mg Aff Pur
27-158 IGF2BP1 is a member of the IGF-II mRNA-binding protein (IMP) family. The protein contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-l 0.05 mg
29-384 IGF2BP1 is a member of the IGF-II mRNA-binding protein (IMP) family. The protein contains four K homology domains and two RNA recognition motifs. It functions by binding to the 5' UTR of the insulin-l 0.05 mg
29-520 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.05 mg
29-521 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.1 mg
29-519 CPEB2 is highly similar to cytoplasmic polyadenylation element binding protein (CPEB), an mRNA-binding protein that regulates cytoplasmic polyadenylation of mRNA as a trans factor in oogenesis and spe 0.05 mg
29-424 PUM2 is a sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of mRNA targets. Its interactions and tissue specificity suggest that it may be requ 0.1 mg
EH3257 Insulin Like Growth Factor 2 mRNA Binding Protein 3 Elisa Kit 96T
CE98 Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 IGF2BP2 lmg
CE98 Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 IGF2BP2 500
CSB-EL011090RA Rat Insulin-like growth factor 2 mRNA-binding protein 1(IGF2BP1) ELISA kit 96T
E80617Hu ELISA Kit for Insulin Like Growth Factor 2 mRNA Binding Protein 3 (IGF2BP3) 96T/Kit
E1388h Chicken ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 1 96T
CN128_HUMAN Human ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 1 96T
E0674h Human ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 2 96T
CF61 Human Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 IGF2BP2 50
IGFALS IGF2BP3 Gene insulin-like growth factor 2 mRNA binding protein 3
RGC32_RAT Human ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 2 96T
IGF2R IGF2BP2 Gene insulin-like growth factor 2 mRNA binding protein 2
IF2B3_MOUSE Mouse ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 3 96T
IGF2BP3 IGF2BP1 Gene insulin-like growth factor 2 mRNA binding protein 1
TMC8_HUMAN Human ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 1 96T
E0131h Human ELISA Kit FOR Insulin-like growth factor 2 mRNA-binding protein 1 96T
201-20-2725 IGF2BP2{insulin-like growth factor 2 mRNA binding protein }rabbit.pAb 0.2ml
C031 Human Insulin-Like Growth Factor 2 mRNA-Binding Protein 2 IGF2BP2 l0


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur