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Entry version 168 (03 Jul 2019)
Sequence version 2 (18 May 2010)
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Protein

Insulin-like growth factor 2 mRNA-binding protein 1

Gene

IGF2BP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. 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 prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. 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.By similarity15 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processmRNA transport, Translation regulation, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-428359 Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA
R-HSA-5687128 MAPK6/MAPK4 signaling

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Insulin-like growth factor 2 mRNA-binding protein 1
Short name:
IGF2 mRNA-binding protein 1
Short name:
IMP-1
Short name:
IMP1
Alternative name(s):
Coding region determinant-binding protein
Short name:
CRD-BP
IGF-II mRNA-binding protein 1
VICKZ family member 1
Zipcode-binding protein 1
Short name:
ZBP-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:IGF2BP1
Synonyms:CRDBP, VICKZ1, ZBP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:28866 IGF2BP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608288 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9NZI8

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi213 – 214KE → 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. 1 Publication2
Mutagenesisi294 – 295KE → 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. 1 Publication2
Mutagenesisi423 – 424KK → 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. 1 Publication2

Organism-specific databases

DisGeNET

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DisGeNETi
10642

Open Targets

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OpenTargetsi
ENSG00000159217

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA143485501

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
IGF2BP1

Domain mapping of disease mutations (DMDM)

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DMDMi
296434536

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002825331 – 577Insulin-like growth factor 2 mRNA-binding protein 1Add BLAST577

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei12PhosphoserineCombined sources1
Modified residuei73PhosphoserineCombined sources1
Modified residuei181PhosphoserineCombined sources1
Modified residuei528PhosphothreonineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated. Phosphorylation may impair association with ACTB mRNA and hence abolishes translational repression (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9NZI8

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9NZI8

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9NZI8

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9NZI8

PeptideAtlas

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PeptideAtlasi
Q9NZI8

PRoteomics IDEntifications database

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PRIDEi
Q9NZI8

ProteomicsDB human proteome resource

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ProteomicsDBi
83410

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q9NZI8-1 [Q9NZI8-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9NZI8

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9NZI8

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9NZI8

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Mainly expressed in the embryo, including in fetal liver, fetal lung, fetal kidney, fetal thymus (at protein level). Also expressed follicles of ovary, as well as in gonocytes of testis, spermatogonia, semen, oocytes and placenta (at protein level). Expressed in various cancers, including testis and lung cancers (at protein level), as well as kidney, prostate and trachea cancers.4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

May be up-regulated in response to CTNNB1/beta-catenin activation.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000159217 Expressed in 65 organ(s), highest expression level in lung

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9NZI8 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA021367
HPA062273

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Can form homodimers and heterodimers with IGF2BP1 and IGF2BP3.

Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. During HCV infection, identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon.

Interacts (via the KH domains) with HIV-1 GAG (via the second zinc finger motif of NC). Associates (via the RRM domains and KH domains) with HIV-1 particles.

Identified in a mRNP complex, composed of at least DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1.

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.

Interacts with DHX9, ELAVL2, HNRNPA2B1, HNRNPC, HNRNPH1, HNRNPU, IGF2BP2, ILF2, and YBX1.

Interacts with FMR1.

Component of a multisubunit autoregulatory RNP complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1/UNR. Directly interacts with PABPC1.

Component of a TAU mRNP complex, at least composed of IGF2BP1, ELAVL4 and G3BP.

Interacts with ELAVL4 in an RNA-dependent manner. Associates with microtubules and polysomes.

Interacts with AGO1 and AGO2.

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115886, 213 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1080 CRD-mediated mRNA stability complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9NZI8

Database of interacting proteins

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DIPi
DIP-38139N

Protein interaction database and analysis system

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IntActi
Q9NZI8, 72 interactors

Molecular INTeraction database

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MINTi
Q9NZI8

STRING: functional protein association networks

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STRINGi
9606.ENSP00000290341

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9NZI8

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9NZI8

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 75RRM 1PROSITE-ProRule annotationAdd BLAST74
Domaini81 – 156RRM 2PROSITE-ProRule annotationAdd BLAST76
Domaini195 – 260KH 1PROSITE-ProRule annotationAdd BLAST66
Domaini276 – 343KH 2PROSITE-ProRule annotationAdd BLAST68
Domaini405 – 470KH 3PROSITE-ProRule annotationAdd BLAST66
Domaini487 – 553KH 4PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni187 – 570Necessary for interaction with ELAVL4 and binding to TAU mRNABy similarityAdd BLAST384
Regioni310 – 324Sufficient for nuclear exportAdd BLAST15
Regioni485 – 495Sufficient for nuclear exportAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Domain KH3 and KH4 are the major RNA-binding modules, although KH1 and KH2 may also contribute. 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. KH3 and KH4 mediate association with the cytoskeleton. Two nuclear export signals (NES) have been identified in KH2 and KH4 domains, respectively. Only KH2 NES is XPO1-dependent. Both NES may be redundant, since individual in vitro mutations do not affect subcellular location of the full-length protein. The 4 KH domains are important to suppress HIV-1 infectivity.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RRM IMP/VICKZ family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2193 Eukaryota
ENOG410ZKB4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160427

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000000675

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NZI8

KEGG Orthology (KO)

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KOi
K17391

Identification of Orthologs from Complete Genome Data

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OMAi
EKPISIH

Database of Orthologous Groups

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OrthoDBi
286875at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9NZI8

TreeFam database of animal gene trees

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TreeFami
TF320229

Family and domain databases

Conserved Domains Database

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CDDi
cd12625 RRM1_IGF2BP1, 1 hit
cd12628 RRM2_IGF2BP1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1370.10, 2 hits
3.30.70.330, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034837 IGF2BP1_RRM1
IPR034842 IGF2BP1_RRM2
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00013 KH_1, 4 hits
PF00076 RRM_1, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00322 KH, 4 hits
SM00360 RRM, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54791 SSF54791, 4 hits
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50084 KH_TYPE_1, 4 hits
PS50102 RRM, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9NZI8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNKLYIGNLN ESVTPADLEK VFAEHKISYS GQFLVKSGYA FVDCPDEHWA
60 70 80 90 100
MKAIETFSGK VELQGKRLEI EHSVPKKQRS RKIQIRNIPP QLRWEVLDSL
110 120 130 140 150
LAQYGTVENC EQVNTESETA VVNVTYSNRE QTRQAIMKLN GHQLENHALK
160 170 180 190 200
VSYIPDEQIA QGPENGRRGG FGSRGQPRQG SPVAAGAPAK QQQVDIPLRL
210 220 230 240 250
LVPTQYVGAI IGKEGATIRN ITKQTQSKID VHRKENAGAA EKAISVHSTP
260 270 280 290 300
EGCSSACKMI LEIMHKEAKD TKTADEVPLK ILAHNNFVGR LIGKEGRNLK
310 320 330 340 350
KVEQDTETKI TISSLQDLTL YNPERTITVK GAIENCCRAE QEIMKKVREA
360 370 380 390 400
YENDVAAMSL QSHLIPGLNL AAVGLFPASS SAVPPPPSSV TGAAPYSSFM
410 420 430 440 450
QAPEQEMVQV FIPAQAVGAI IGKKGQHIKQ LSRFASASIK IAPPETPDSK
460 470 480 490 500
VRMVIITGPP EAQFKAQGRI YGKLKEENFF GPKEEVKLET HIRVPASAAG
510 520 530 540 550
RVIGKGGKTV NELQNLTAAE VVVPRDQTPD ENDQVIVKII GHFYASQMAQ
560 570
RKIRDILAQV KQQHQKGQSN QAQARRK
Length:577
Mass (Da):63,481
Last modified:May 18, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1D036AE5388D05FA
GO
Isoform 2 (identifier: Q9NZI8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-273: Missing.

Show »
Length:438
Mass (Da):48,598
Checksum:i2F615D03F5C00C1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti10Missing AA sequence (PubMed:9891060).Curated1
Sequence conflicti281I → T in AAF37203 (Ref. 1) Curated1
Sequence conflicti320Missing AA sequence (PubMed:9891060).Curated1
Sequence conflicti365I → T in AAF37203 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_045366135 – 273Missing in isoform 2. 1 PublicationAdd BLAST139

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF198254 mRNA Translation: AAF37203.1
DQ227344 mRNA Translation: ABB46294.1
AC091133 Genomic DNA No translation available.
AC105030 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS11543.1 [Q9NZI8-1]
CCDS54138.1 [Q9NZI8-2]

NCBI Reference Sequences

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RefSeqi
NP_001153895.1, NM_001160423.1 [Q9NZI8-2]
NP_006537.3, NM_006546.3 [Q9NZI8-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000290341; ENSP00000290341; ENSG00000159217 [Q9NZI8-1]
ENST00000431824; ENSP00000389135; ENSG00000159217 [Q9NZI8-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
10642

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:10642

UCSC genome browser

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UCSCi
uc002iom.4 human [Q9NZI8-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF198254 mRNA Translation: AAF37203.1
DQ227344 mRNA Translation: ABB46294.1
AC091133 Genomic DNA No translation available.
AC105030 Genomic DNA No translation available.
CCDSiCCDS11543.1 [Q9NZI8-1]
CCDS54138.1 [Q9NZI8-2]
RefSeqiNP_001153895.1, NM_001160423.1 [Q9NZI8-2]
NP_006537.3, NM_006546.3 [Q9NZI8-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3KRMX-ray2.75A/B/C404-566[»]
6QEYX-ray2.20A194-369[»]
SMRiQ9NZI8
ModBaseiSearch...

Protein-protein interaction databases

BioGridi115886, 213 interactors
ComplexPortaliCPX-1080 CRD-mediated mRNA stability complex
CORUMiQ9NZI8
DIPiDIP-38139N
IntActiQ9NZI8, 72 interactors
MINTiQ9NZI8
STRINGi9606.ENSP00000290341

PTM databases

iPTMnetiQ9NZI8
PhosphoSitePlusiQ9NZI8
SwissPalmiQ9NZI8

Polymorphism and mutation databases

BioMutaiIGF2BP1
DMDMi296434536

Proteomic databases

EPDiQ9NZI8
jPOSTiQ9NZI8
MaxQBiQ9NZI8
PaxDbiQ9NZI8
PeptideAtlasiQ9NZI8
PRIDEiQ9NZI8
ProteomicsDBi83410
TopDownProteomicsiQ9NZI8-1 [Q9NZI8-1]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
10642
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290341; ENSP00000290341; ENSG00000159217 [Q9NZI8-1]
ENST00000431824; ENSP00000389135; ENSG00000159217 [Q9NZI8-2]
GeneIDi10642
KEGGihsa:10642
UCSCiuc002iom.4 human [Q9NZI8-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
10642
DisGeNETi10642

GeneCards: human genes, protein and diseases

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GeneCardsi
IGF2BP1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0013955
HGNCiHGNC:28866 IGF2BP1
HPAiHPA021367
HPA062273
MIMi608288 gene
neXtProtiNX_Q9NZI8
OpenTargetsiENSG00000159217
PharmGKBiPA143485501

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2193 Eukaryota
ENOG410ZKB4 LUCA
GeneTreeiENSGT00940000160427
HOGENOMiHOG000000675
InParanoidiQ9NZI8
KOiK17391
OMAiEKPISIH
OrthoDBi286875at2759
PhylomeDBiQ9NZI8
TreeFamiTF320229

Enzyme and pathway databases

ReactomeiR-HSA-428359 Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA
R-HSA-5687128 MAPK6/MAPK4 signaling

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
IGF2BP1 human
EvolutionaryTraceiQ9NZI8

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
IGF2BP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
10642

Protein Ontology

More...
PROi
PR:Q9NZI8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000159217 Expressed in 65 organ(s), highest expression level in lung
GenevisibleiQ9NZI8 HS

Family and domain databases

CDDicd12625 RRM1_IGF2BP1, 1 hit
cd12628 RRM2_IGF2BP1, 1 hit
Gene3Di3.30.1370.10, 2 hits
3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR034837 IGF2BP1_RRM1
IPR034842 IGF2BP1_RRM2
IPR004087 KH_dom
IPR004088 KH_dom_type_1
IPR036612 KH_dom_type_1_sf
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
PfamiView protein in Pfam
PF00013 KH_1, 4 hits
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00322 KH, 4 hits
SM00360 RRM, 2 hits
SUPFAMiSSF54791 SSF54791, 4 hits
SSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50084 KH_TYPE_1, 4 hits
PS50102 RRM, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIF2B1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NZI8
Secondary accession number(s): C9JT33
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: May 18, 2010
Last modified: July 3, 2019
This is version 168 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
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