Search Results
Overview
| Uniprot ID | Q07666 |
|---|---|
| Protein Name | KH domain-containing, RNA-binding, signal transduction-associated protein 1 |
| Gene Name | KHDRBS1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 165 | ERVLIPVKQYPKFNF |
| 169 | IPVKQYPKFNFVGKI |
| 185 | GPQGNTIKRLQEETG |
| 208 | GSMRDKAKEEELRKG |
| 424 | NGTRPSLKAPPARPV |
| 432 | APPARPVKGAYREHP |
Function
Recruited and tyrosine phosphorylated by several receptor systems, for example the T-cell, leptin and insulin receptors. Once phosphorylated, functions as an adapter protein in signal transduction cascades by binding to SH2 and SH3 domain-containing proteins. Role in G2-M progression in the cell cycle. Represses CBP-dependent transcriptional activation apparently by competing with other nuclear factors for binding to CBP. Also acts as a putative regulator of mRNA stability and/or translation rates and mediates mRNA nuclear export. Positively regulates the association of constitutive transport element (CTE)-containing mRNA with large polyribosomes and translation initiation. According to some authors, is not involved in the nucleocytoplasmic export of unspliced (CTE)-containing RNA species according to (PubMed:22253824). RNA-binding protein that plays a role in the regulation of alternative splicing and influences mRNA splice site selection and exon inclusion. Binds to RNA containing 5'-[AU]UAA-3' as a bipartite motif spaced by more than 15 nucleotides. Binds poly(A). Can regulate CD44 alternative splicing in a Ras pathway-dependent manner (PubMed:26080397). In cooperation with HNRNPA1 modulates alternative splicing of BCL2L1 by promoting splicing toward isoform Bcl-X(S), and of SMN1 (PubMed:17371836, PubMed:20186123). Can regulate alternative splicing of NRXN1 and NRXN3 in the laminin G-like domain 6 containing the evolutionary conserved neurexin alternative spliced segment 4 (AS4) involved in neurexin selective targeting to postsynaptic partners. In a neuronal activity-dependent manner cooperates synergistically with KHDRBS2/SLIM-1 in regulation of NRXN1 exon skipping at AS4. The cooperation with KHDRBS2/SLIM-1 is antagonistic for regulation of NXRN3 alternative splicing at AS4 (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0070618 | Grb2-Sos complex |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0140678 | molecular function inhibitor activity |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0008143 | poly(A) binding |
| Molecular Function | GO:0008266 | poly(U) RNA binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:1990782 | protein tyrosine kinase binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0042169 | SH2 domain binding |
| Molecular Function | GO:0017124 | SH3 domain binding |
| Molecular Function | GO:0035591 | signaling adaptor activity |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0000082 | G1/S transition of mitotic cell cycle |
| Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
| Biological Process | GO:0006397 | mRNA processing |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:0046833 | positive regulation of RNA export from nucleus |
| Biological Process | GO:0045948 | positive regulation of translational initiation |
| Biological Process | GO:0000381 | regulation of alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0046831 | regulation of RNA export from nucleus |
| Biological Process | GO:0043484 | regulation of RNA splicing |
| Biological Process | GO:0007283 | spermatogenesis |
| Biological Process | GO:0050852 | T cell receptor signaling pathway |
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] 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.
[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] 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.
[6] 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.
[7] 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.