Search Results
Overview
| Uniprot ID | Q14004 |
|---|---|
| Protein Name | Cyclin-dependent kinase 13 |
| Gene Name | CDK13 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1029 | SKKRRRQKQMGMTDD |
| 1045 | STIKAPRKDLSLGLD |
| 455 | SLAAELNKNKKARAA |
| 457 | AAELNKNKKARAAEA |
| 513 | ASQTNHVKDVKKIKI |
| 519 | VKDVKKIKIEHAPSP |
| 560 | IVDKATKKAVIVGKE |
Function
Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, probably by phosphorylating SRSF1/SF2. Required during hematopoiesis. In case of infection by HIV-1 virus, interacts with HIV-1 Tat protein acetylated at 'Lys-50' and 'Lys-51', thereby increasing HIV-1 mRNA splicing and promoting the production of the doubly spliced HIV-1 protein Nef
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0002945 | cyclin K-CDK13 complex |
| Cellular Component | GO:0008024 | cyclin/CDK positive transcription elongation factor complex |
| Cellular Component | GO:0005576 | extracellular region |
| Cellular Component | GO:0005615 | extracellular space |
| Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
| Cellular Component | GO:0019908 | nuclear cyclin-dependent protein kinase holoenzyme complex |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0030332 | cyclin binding |
| Molecular Function | GO:0004693 | cyclin-dependent protein serine/threonine kinase activity |
| Molecular Function | GO:0004672 | protein kinase activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0008353 | RNA polymerase II CTD heptapeptide repeat kinase activity |
| Biological Process | GO:0000380 | alternative mRNA splicing, via spliceosome |
| Biological Process | GO:0030097 | hemopoiesis |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0032968 | positive regulation of transcription elongation by RNA polymerase II |
| Biological Process | GO:0009966 | regulation of signal transduction |
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] 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.
[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.