Search Results
Overview
| Uniprot ID | Q15717 |
|---|---|
| Protein Name | ELAV-like protein 1 |
| Gene Name | ELAVL1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 191 | AANPNQNKNVALLSQ |
Function
RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability (PubMed:14517288, PubMed:18285462, PubMed:31358969). Involved in embryonic stem cell (ESC) differentiation: preferentially binds mRNAs that are not methylated by N6-methyladenosine (m6A), stabilizing them, promoting ESC differentiation (By similarity). Has also been shown to be capable of binding to m6A-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). Binds to poly-U elements and AU-rich elements (AREs) in the 3'-UTR of target mRNAs (PubMed:14731398, PubMed:17632515, PubMed:18285462, PubMed:23519412, PubMed:8626503). Binds avidly to the AU-rich element in FOS and IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element, binds to a core element of 27 nucleotides that contain AUUUA, AUUUUA, and AUUUUUA motifs. Binds preferentially to the 5'-UUUU[AG]UUU-3' motif in vitro (PubMed:8626503). With ZNF385A, binds the 3'-UTR of p53/TP53 mRNA to control their nuclear export induced by CDKN2A. Hence, may regulate p53/TP53 expression and mediate in part the CDKN2A anti-proliferative activity. May also bind with ZNF385A the CCNB1 mRNA (By similarity). Increases the stability of the leptin mRNA harboring an AU-rich element (ARE) in its 3' UTR (PubMed:29180010)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0031410 | cytoplasmic vesicle |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000932 | P-body |
| Cellular Component | GO:0098794 | postsynapse |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0003725 | double-stranded RNA binding |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:0035198 | miRNA binding |
| Molecular Function | GO:0035925 | mRNA 3'-UTR AU-rich region binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0140517 | protein-RNA adaptor activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0070935 | 3'-UTR-mediated mRNA stabilization |
| Biological Process | GO:0008283 | cell population proliferation |
| Biological Process | GO:0000512 | lncRNA-mediated post-transcriptional gene silencing |
| Biological Process | GO:0061157 | mRNA destabilization |
| Biological Process | GO:0048255 | mRNA stabilization |
| Biological Process | GO:0060965 | negative regulation of miRNA-mediated gene silencing |
| Biological Process | GO:0045772 | positive regulation of autophagosome size |
| Biological Process | GO:0010508 | positive regulation of autophagy |
| Biological Process | GO:0032930 | positive regulation of superoxide anion generation |
| Biological Process | GO:0045727 | positive regulation of translation |
| Biological Process | GO:0051260 | protein homooligomerization |
| Biological Process | GO:0006606 | protein import into nucleus |
| Biological Process | GO:2000036 | regulation of stem cell population maintenance |
| Biological Process | GO:0009749 | response to glucose |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.