Search Results
Overview
| Uniprot ID | Q6PKG0 |
|---|---|
| Protein Name | La-related protein 1 |
| Gene Name | LARP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 160 | VVRAAVPKQRKGSKV |
| 251 | KKKGNKHKWVPLQID |
| 367 | DYQFGYRKFDGVEGP |
| 543 | SNLKTLPKGLSASLP |
Function
RNA-binding protein that regulates the translation of specific target mRNA species downstream of the mTORC1 complex, in function of growth signals and nutrient availability (PubMed:20430826, PubMed:23711370, PubMed:24532714, PubMed:25940091, PubMed:28650797, PubMed:28673543, PubMed:29244122). Interacts on the one hand with the 3' poly-A tails that are present in all mRNA molecules, and on the other hand with the 7-methylguanosine cap structure of mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding ribosomal proteins and several components of the translation machinery (PubMed:23711370, PubMed:25940091, PubMed:26206669, PubMed:28379136, PubMed:28650797, PubMed:29244122). The interaction with the 5' end of mRNAs containing a 5'TOP motif leads to translational repression by preventing the binding of EIF4G1 (PubMed:25940091, PubMed:28379136, PubMed:28650797, PubMed:29244122). When mTORC1 is activated, LARP1 is phosphorylated and dissociates from the 5' untranslated region (UTR) of mRNA (PubMed:25940091, PubMed:28650797). Does not prevent binding of EIF4G1 to mRNAs that lack a 5'TOP motif (PubMed:28379136). Interacts with the free 40S ribosome subunit and with ribosomes, both monosomes and polysomes (PubMed:20430826, PubMed:24532714, PubMed:25940091, PubMed:28673543). Under normal nutrient availability, interacts primarily with the 3' untranslated region (UTR) of mRNAs encoding ribosomal proteins and increases protein synthesis (PubMed:23711370, PubMed:28650797). Associates with actively translating ribosomes and stimulates translation of mRNAs containing a 5'TOP motif, thereby regulating protein synthesis, and as a consequence, cell growth and proliferation (PubMed:20430826, PubMed:24532714). Stabilizes mRNAs species with a 5'TOP motif, which is required to prevent apoptosis (PubMed:20430826, PubMed:23711370, PubMed:25940091, PubMed:28673543)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016020 | membrane |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0008190 | eukaryotic initiation factor 4E binding |
| Molecular Function | GO:0003730 | mRNA 3'-UTR binding |
| Molecular Function | GO:0048027 | mRNA 5'-UTR binding |
| Molecular Function | GO:0043024 | ribosomal small subunit binding |
| Molecular Function | GO:0000340 | RNA 7-methylguanosine cap binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0000339 | RNA cap binding |
| Molecular Function | GO:0008494 | translation activator activity |
| Molecular Function | GO:0031369 | translation initiation factor binding |
| Biological Process | GO:0008283 | cell population proliferation |
| Biological Process | GO:0072752 | cellular response to rapamycin |
| Biological Process | GO:0048255 | mRNA stabilization |
| Biological Process | GO:0017148 | negative regulation of translation |
| Biological Process | GO:0045947 | negative regulation of translational initiation |
| Biological Process | GO:0016239 | positive regulation of macroautophagy |
| Biological Process | GO:0045727 | positive regulation of translation |
| Biological Process | GO:0045948 | positive regulation of translational initiation |
| Biological Process | GO:0045070 | positive regulation of viral genome replication |
| Biological Process | GO:0010608 | post-transcriptional regulation of gene expression |
| Biological Process | GO:1990928 | response to amino acid starvation |
| Biological Process | GO:0031929 | TOR signaling |
| Biological Process | GO:0038202 | TORC1 signaling |
| Biological Process | GO:0006413 | translational initiation |
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] 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.
[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.