Search Results
Overview
| Uniprot ID | Q9NWB6 |
|---|---|
| Protein Name | Arginine and glutamate-rich protein 1 |
| Gene Name | ARGLU1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 253 | RQQKEEQKIILGKGK |
| 258 | EQKIILGKGKSRPKL |
| 264 | GKGKSRPKLSFSLKT |
Function
Dual function regulator of gene expression; regulator of transcription and modulator of alternative splicing (PubMed:30698747). General coactivator of nuclear receptor-induced gene expression, including genes activated by the glucocorticoid receptor NR3C1 (PubMed:30698747). Binds to a subset of pre-mRNAs and to components of the spliceosome machinery to directly modulate basal alternative splicing; involved in simple and complex cassette exon splicing events (PubMed:30698747). Binds its own pre-mRNA and regulates its alternative splicing and degradation; one of the alternatively spliced products is a stable intronic sequence RNA (sisRNA) that binds the protein to regulate its ability to affect splicing (PubMed:27899669, PubMed:36533631). Binding of the sisRNA stimulates phase separation and localization to nuclear speckles, which may contribute to activation of nuclear receptor-induced gene expression (PubMed:36533631). May also indirectly modulate alternative splicing (PubMed:30698747). Regulates transcription of genes involved in heart development, neuronal cell function, protein localization and chromatin localization (By similarity). Regulates splicing of genes involved in neurogenesis and chromatin organization (By similarity). Essential for central nervous system development (By similarity). Required for the estrogen-dependent expression of ESR1 target genes (PubMed:21454576). Can act in cooperation with MED1 (PubMed:21454576)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0036002 | pre-mRNA binding |
| Molecular Function | GO:0003713 | transcription coactivator activity |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0000381 | regulation of alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0008380 | RNA splicing |
Reference
[1] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[2] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] 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.
[5] 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.