Search Results
Overview
| Uniprot ID | P50613 |
|---|---|
| Protein Name | Cyclin-dependent kinase 7 |
| Gene Name | CDK7 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 328 | SNPALAIKRKRTEAL |
| 342 | LEQGGLPKKLIF*** |
| 343 | EQGGLPKKLIF**** |
Function
Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription (PubMed:9852112, PubMed:19136461, PubMed:26257281, PubMed:28768201). As a cyclin-dependent kinase, CDK7 is activated by the binding to cyclin-H/CCNH and the CDK-activating kinase assembly factor MAT1 (PubMed:41100585). Catalytic subunit of the CDK-activating kinase (CAK) complex, a master regulator of CDK activity by catalyzing the activating threonine phosphorylation of CDKs (PubMed:41100585). CAK activates major mediators of cell cycle control, including CDK1, CDK2, CDK4 and CDK6, and plays a key role in regulating cell cycle progression (PubMed:41100585). CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the CTD of POLR2A, allowing its escape from the promoter and elongation of the transcripts (PubMed:9852112). Initiates transcription by RNA polymerase II by mediating phosphorylation of POLR2A at 'Ser-5' of the repetitive C-terminal domain (CTD) when POLR2A is in complex with DNA, promoting dissociation from DNA and initiation (PubMed:19136461, PubMed:26257281, PubMed:28768201). Phosphorylates SPT5/SUPT5H, SF1/NR5A1, POLR2A, p53/TP53, CDK1, CDK2, CDK4, CDK6 and CDK11B/CDK11 (PubMed:9372954, PubMed:9840937, PubMed:19136461, PubMed:26257281, PubMed:28768201, PubMed:41100585, PubMed:41100585). Its expression and activity are constant throughout the cell cycle. Upon DNA damage, triggers p53/TP53 activation by phosphorylation, but is inactivated in turn by p53/TP53; this feedback loop may lead to an arrest of the cell cycle and of the transcription, helping in cell recovery, or to apoptosis. Required for DNA-bound peptides-mediated transcription and cellular growth inhibition
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0070516 | CAK-ERCC2 complex |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0001650 | fibrillar center |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0000439 | transcription factor TFIIH core complex |
| Cellular Component | GO:0005675 | transcription factor TFIIH holo complex |
| Cellular Component | GO:0070985 | transcription factor TFIIK complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0008094 | ATP-dependent activity, acting on DNA |
| Molecular Function | GO:0004693 | cyclin-dependent protein serine/threonine kinase activity |
| Molecular Function | GO:0004672 | protein kinase activity |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Molecular Function | GO:0004674 | protein serine/threonine kinase activity |
| Molecular Function | GO:0008353 | RNA polymerase II CTD heptapeptide repeat kinase activity |
| Molecular Function | GO:0140836 | RNA polymerase II CTD heptapeptide repeat S5 kinase activity |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0006289 | nucleotide-excision repair |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:2000045 | regulation of G1/S transition of mitotic cell cycle |
| Biological Process | GO:0042795 | snRNA transcription by RNA polymerase II |
| Biological Process | GO:0006366 | transcription by RNA polymerase II |
| Biological Process | GO:0006367 | transcription initiation at RNA polymerase II promoter |
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] 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.
[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.