IGF2BP1
entrez
10642
canonical
uniprot
Q9NZI8
canonical
ensembl
ENSG00000159217
resolver
ensp
ENSP00000290341
resolver
ensp
ENSP00000389135
resolver
ensp
ENSP00000595748
resolver
genesymbol
IGF2BP1
resolver
genesymbol_syn
CRDBP
resolver
genesymbol_syn
VICKZ1
resolver
genesymbol_syn
ZBP1
resolver
hgnc
HGNC:28866
resolver
uniprot
C9JT33
resolver
uniprot
D3DTW3
resolver
uniprot_entry
D3DTW3_HUMAN
resolver
uniprot_entry
IF2B1_HUMAN
resolver
uniprot_sec
C9JT33
resolver
amino_acid_sequence
MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNQAQARRK
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. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (PubMed:29476152, PubMed:32245947). Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons (By similarity). 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 and stabilizes ABCB1/MDR-1 mRNA (By similarity). During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing (By similarity). 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 preventing MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD (PubMed:29476152). Binding to MYC mRNA is enhanced by m6A-modification of the CRD (PubMed:29476152). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to the oncofetal H19 transcript and to the neuron-specific TAU mRNA and regulates their localizations. Binds to and stabilizes BTRC/FBW1A mRNA. 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. Promotes the directed movement of tumor-derived cells by fine-tuning intracellular signaling networks. Binds to MAPK4 3'-UTR and inhibits its translation. Interacts with PTEN transcript open reading frame (ORF) and prevents mRNA decay. This combined action on MAPK4 (down-regulation) and PTEN (up-regulation) antagonizes HSPB1 phosphorylation, consequently it prevents G-actin sequestration by phosphorylated HSPB1, allowing F-actin polymerization. Hence enhances the velocity of cell migration and stimulates directed cell migration by PTEN-modulated polarization. Interacts with Hepatitis C virus (HCV) 5'-UTR and 3'-UTR and specifically enhances translation at the HCV IRES, but not 5'-cap-dependent translation, possibly by recruiting eIF3. Interacts with HIV-1 GAG protein and blocks the formation of infectious HIV-1 particles. Reduces HIV-1 assembly by inhibiting viral RNA packaging, as well as assembly and processing of GAG protein on cellular membranes. 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. {ECO:0000250, ECO:0000269|PubMed:10875929, ECO:0000269|PubMed:16356927, ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:16778892, ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:17255263, ECO:0000269|PubMed:17893325, ECO:0000269|PubMed:18385235, ECO:0000269|PubMed:19029303, ECO:0000269|PubMed:19541769, ECO:0000269|PubMed:19647520, ECO:0000269|PubMed:20080952, ECO:0000269|PubMed:22279049, ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947, ECO:0000269|PubMed:8132663, ECO:0000269|PubMed:9891060}.
uniprot
proteins
mass_dalton
63481
uniprot
proteins
mutagenesis
MUTAGEN 213..214; /note="KE->EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 294-E-L-295 and 423-E-L-424."; /evidence="ECO:0000269|PubMed:12921532"; MUTAGEN 213; /note="K->E: Partial reduction in interaction with m6A-modified mRNA; when associated with E-294."; /evidence="ECO:0000269|PubMed:29476152"; MUTAGEN 294..295; /note="KE->EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 423-E-L-424."; /evidence="ECO:0000269|PubMed:12921532"; MUTAGEN 294; /note="K->E: Partial reduction in interaction with m6A-modified mRNA; when associated with E-213."; /evidence="ECO:0000269|PubMed:29476152"; MUTAGEN 423..424; /note="KK->EE: Loss of binding to RBPR and loss of interaction with m6A-modified mRNA; when associated with 505-E-E-506."; /evidence="ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947"; MUTAGEN 423..424; /note="KK->EL: 50-fold decrease in RNA-binding affinity, decreased location in cytoplasmic RNP, increased nuclear location; when associated with 213-E-L-214 and 294-E-L-295."; /evidence="ECO:0000269|PubMed:12921532"; MUTAGEN 505..506; /note="KG->EE: Loss of binding to RBPR and loss of interaction with m6A-modified mRNA; when associated with 423-E-E-424."; /evidence="ECO:0000269|PubMed:29476152, ECO:0000269|PubMed:32245947
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-181 by mTORC2 cotranslationally, promoting binding to the 3'-UTR of IGF2 mRNA. {ECO:0000250|UniProtKB:O88477}.
uniprot
proteins
protein_family
RRM IMP/VICKZ family
uniprot
proteins
pubmed
10875929
uniprot
proteins
pubmed
12921532
uniprot
proteins
pubmed
15282548
uniprot
proteins
pubmed
15314207
uniprot
proteins
pubmed
16049158
uniprot
proteins
pubmed
16356927
uniprot
proteins
pubmed
16541107
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16778892
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17101699
uniprot
proteins
pubmed
17212783
uniprot
proteins
pubmed
17255263
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
17893325
uniprot
proteins
pubmed
17932509
uniprot
proteins
pubmed
18385235
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19029303
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19541769
uniprot
proteins
pubmed
19647520
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20080952
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22279049
uniprot
proteins
pubmed
23069990
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23640942
uniprot
proteins
pubmed
29476152
uniprot
proteins
pubmed
32245947
uniprot
proteins
pubmed
8132663
uniprot
proteins
pubmed
9801297
uniprot
proteins
pubmed
9891060
uniprot
proteins
sequence_length
577
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000269|PubMed:17289661}. Cytoplasm, perinuclear region. Cytoplasm, P-body {ECO:0000269|PubMed:29476152}. Cytoplasm, Stress granule {ECO:0000269|PubMed:17101699, ECO:0000269|PubMed:29476152}. Cell projection, lamellipodium. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Cell projection, growth cone. 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. 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). 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 motile cells, such as migrating fibroblasts, localizes to leading edges where it colocalizes with microtubules and microfilaments and to retracting tails (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 the NMDA receptor agonist (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. {ECO:0000250}.
uniprot
proteins