Cugbp elav-like family member 6

CELF6
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2DGQ
Identifiers
Aliases	CELF6, BRUNOL6, CUGBP, Elav-like family member 6, CUGBP Elav-like family member 6
External IDs	OMIM: 612681 GeneCards: CELF6
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right uterine tube hypothalamus pituitary gland anterior pituitary prefrontal cortex superior frontal gyrus sural nerve Brodmann area 9 right lobe of thyroid gland left lobe of thyroid gland n/a More reference expression data BioGPS n/a
Gene ontology Molecular function nucleic acid binding RNA binding mRNA binding Cellular component nucleus cytoplasm cytosol ribonucleoprotein complex Biological process mRNA processing regulation of alternative mRNA splicing, via spliceosome mRNA splice site selection Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 60677 n/a Ensembl n/a n/a UniProt Q96J87 n/a RefSeq (mRNA) NM_052840 NM_001172684 NM_001172685 n/a RefSeq (protein) NP_001166155 NP_001166156 NP_443072 n/a Location (UCSC) n/a n/a PubMed search n/a
Wikidata
View/Edit Human

CUGBP Elav-like family member 6 is a protein that in humans is encoded by the CELF6 gene.

Function

Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Multiple alternatively spliced transcript variants encoding different isoforms have been identified in this gene. [provided by RefSeq, Feb 2010].

Further reading

• Ladd AN, Nguyen NH, Malhotra K, Cooper TA (April 2004). "CELF6, a member of the CELF family of RNA-binding proteins, regulates muscle-specific splicing enhancer-dependent alternative splicing". J. Biol. Chem. 279 (17): 17756–64. doi:10.1074/jbc.M310687200. PMID 14761971.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.