IGF2BP2

Also known as IMP-2, IMP2, VICKZ2, insulin like growth factor 2 mRNA binding protein 2

Insulin-like growth factor 2 mRNA-binding protein 2 is a protein that in humans is encoded by the IGF2BP2 gene.

Gene data

IGF2BP2

Name: insulin like growth factor 2 mRNA binding protein 2
Type: protein-coding
Position: 185,643,130–185,825,061 (−)
Aliases: IMP-2, IMP2, VICKZ2
Ensembl: ENSG00000073792
RefSeq RNA: NM_001007225.3, NM_001291869.3, NM_001291872.3, NM_001291873.3, NM_001291874.3
RefSeq protein: NP_001007226.1, NP_001278798.1, NP_001278801.1, NP_001278802.1, NP_001278803.1

This gene encodes a protein that binds the 5' UTR of insulin-like growth factor 2 (IGF2) mRNA and regulates its translation. It plays an important role in metabolism and variation in this gene is associated with susceptibility to diabetes. Alternative splicing and promoter usage results in multiple transcript variants. Related pseudogenes are found on several chromosomes. [provided by RefSeq, Sep 2016].

Pathways

Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs) bind RNA Metabolism of RNA

via MyGene.info

Gene · Ensembl

insulin like growth factor 2 mRNA binding protein 2

Symbol: IGF2BP2
Biotype: Protein coding
Organism: Homo sapiens
Location: 3:185,643,130-185,825,309
Strand: Reverse (−)
Assembly: GRCh38

View on Ensembl →

via Ensembl · EMBL-EBI

Wikidata facts

Image: Protein IGF2BP2 PDB 2cqh.png

Show 5 more facts

HomoloGene ID: 4774
exact match: identifiers.org/ncbigene/10644
genomic end: 185825042
genomic start: 185643130
cytogenetic location: 3q27.2

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Further reading

Insulin-like growth factor 2 mRNA-binding protein 2 is a protein that in humans is encoded by the IGF2BP2 gene.

This gene encodes a member of the IGF-II mRNA-binding protein (IMP) family. The protein encoded by this gene contains four KH domains and two RRM domains. It functions by binding to the 5' UTR of the insulin-like growth factor 2 (IGF2) mRNA and regulating IGF2 translation. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.