Search Results
Overview
| Uniprot ID | Q92879 |
|---|---|
| Protein Name | CUGBP Elav-like family member 1 |
| Gene Name | CELF1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 436 | SAKVFIDKQTNLSKC |
| 480 | KVQLKRSKNDSKPY* |
Function
RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts both as an activator and as a repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity). Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (PubMed:28431233)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0097356 | perinucleolar compartment |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0042835 | BRE binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0000900 | mRNA regulatory element binding translation repressor activity |
| Molecular Function | GO:0036002 | pre-mRNA binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0009792 | embryo development ending in birth or egg hatching |
| Biological Process | GO:0007281 | germ cell development |
| Biological Process | GO:0061157 | mRNA destabilization |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0006376 | mRNA splice site recognition |
| Biological Process | GO:0010629 | negative regulation of gene expression |
| Biological Process | GO:0010628 | positive regulation of gene expression |
| Biological Process | GO:0016441 | post-transcriptional gene silencing |
| Biological Process | GO:0000381 | regulation of alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0050727 | regulation of inflammatory response |
| Biological Process | GO:0043484 | regulation of RNA splicing |
| Biological Process | GO:0035194 | regulatory ncRNA-mediated post-transcriptional gene silencing |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[3] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.