IGF2BP2
entrez
10644
canonical
uniprot
Q9Y6M1
canonical
ensembl
ENSG00000073792
resolver
ensp
ENSP00000320204
resolver
ensp
ENSP00000371634
resolver
ensp
ENSP00000410242
resolver
ensp
ENSP00000413787
resolver
ensp
ENSP00000551647
resolver
ensp
ENSP00000591384
resolver
ensp
ENSP00000591385
resolver
ensp
ENSP00000591396
resolver
ensp
ENSP00000660590
resolver
enst
ENST00000457616
resolver
genesymbol
IGF2BP2
resolver
genesymbol_syn
IMP2
resolver
genesymbol_syn
VICKZ2
resolver
hgnc
HGNC:28867
resolver
uniprot
A0A4Z0
resolver
uniprot
B3FTN2
resolver
uniprot
B3FTN3
resolver
uniprot
B3FTN4
resolver
uniprot
B3FTN5
resolver
uniprot
B4DKT5
resolver
uniprot
F8W930
resolver
uniprot_entry
B3FTN5_HUMAN
resolver
uniprot_entry
B4DKT5_HUMAN
resolver
uniprot_entry
F8W930_HUMAN
resolver
uniprot_entry
IF2B2_HUMAN
resolver
uniprot_sec
A0A4Z0
resolver
uniprot_sec
B3FTN2
resolver
uniprot_sec
B3FTN3
resolver
uniprot_sec
B3FTN4
resolver
amino_acid_sequence
MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLRSRKIQIRNIPPHLQWEVLDGLLAQYGTVENVEQVNTDTETAVVNVTYATREEAKIAMEKLSGHQFENYSFKISYIPDEEVSSPSPPQRAQRGDHSSREQGHAPGGTSQARQIDFPLRILVPTQFVGAIIGKEGLTIKNITKQTQSRVDIHRKENSGAAEKPVTIHATPEGTSEACRMILEIMQKEADETKLAEEIPLKILAHNGLVGRLIGKEGRNLKKIEHETGTKITISSLQDLSIYNPERTITVKGTVEACASAEIEIMKKLREAFENDMLAVNQQANLIPGLNLSALGIFSTGLSVLSPPAGPRGAPPAAPYHPFTTHSGYFSSLYPHHQFGPFPHHHSYPEQEIVNLFIPTQAVGAIIGKKGAHIKQLARFAGASIKIAPAEGPDVSERMVIITGPPEAQFKAQGRIFGKLKEENFFNPKEEVKLEAHIRVPSSTAGRVIGKGGKTVNELQNLTSAEVIVPRDQTPDENEEVIVRIIGHFFASQTAQRKIREIVQQVKQQEQKYPQGVASQRSK
uniprot
proteins
function
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). Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs (PubMed:9891060). Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts. Increases MYC mRNA stability by binding to the coding region instability determinant (CRD) and binding is enhanced by m6A-modification of the CRD (PubMed:29476152). {ECO:0000250, ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:9891060}.
uniprot
proteins
mass_dalton
66121
uniprot
proteins
mutagenesis
MUTAGEN 211; /note="K->E: Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding, accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA; 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."; /evidence="ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152"; MUTAGEN 292; /note="K->E: Significantly impaired binding to ACTB transcript but little effect on MYC transcript binding, accumulation in the nucleus and partial reduction in interaction with m6A-modified mRNA; 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."; /evidence="ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152"; MUTAGEN 445..446; /note="KK->EE: Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA; 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."; /evidence="ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152"; MUTAGEN 527..528; /note="KG->EE: Significantly impaired binding to ACTB and MYC transcripts and loss of interaction with m6A-modified mRNA; 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."; /evidence="ECO:0000269|PubMed:23640942, ECO:0000269|PubMed:29476152
uniprot
proteins
protein_family
RRM IMP/VICKZ family
uniprot
proteins
pubmed
10190901
uniprot
proteins
pubmed
12674497
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15601260
uniprot
proteins
pubmed
16049158
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20080952
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22427968
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23640942
uniprot
proteins
pubmed
29476152
uniprot
proteins
pubmed
34457052
uniprot
proteins
pubmed
9891060
uniprot
proteins
sequence_length
599
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:29476152}. 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.
uniprot
proteins