Search Results
Overview
| Uniprot ID | O60563 |
|---|---|
| Protein Name | Cyclin-T1 |
| Gene Name | CCNT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 380 | ISQKQNSKSVPSAKV |
| 390 | PSAKVSLKEYRAKHA |
| 471 | IPVAGGDKAASSKPE |
| 481 | SSKPEEIKMRIKVHA |
| 540 | LPVGTGNKRPGDPKH |
| 590 | AVFDHPAKIAKSTKS |
| 593 | DHPAKIAKSTKSSSL |
| 638 | KTRVPHSKLDKGPTG |
Function
Regulatory subunit of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor B (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNA Pol II) (PubMed:16109376, PubMed:16109377, PubMed:30134174, PubMed:35393539). Required to activate the protein kinase activity of CDK9: acts by mediating formation of liquid-liquid phase separation (LLPS) that enhances binding of P-TEFb to the CTD of RNA Pol II (PubMed:29849146, PubMed:35393539)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0008024 | cyclin/CDK positive transcription elongation factor complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0070691 | P-TEFb complex |
| Molecular Function | GO:0097322 | 7SK snRNA binding |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0061575 | cyclin-dependent protein serine/threonine kinase activator activity |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0140297 | DNA-binding transcription factor binding |
| Molecular Function | GO:0140693 | molecular condensate scaffold activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0070063 | RNA polymerase binding |
| Molecular Function | GO:0000976 | transcription cis-regulatory region binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0043923 | host-mediated activation of viral transcription |
| Biological Process | GO:0032786 | positive regulation of DNA-templated transcription, elongation |
| 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:0000079 | regulation of cyclin-dependent protein serine/threonine kinase activity |
| Biological Process | GO:0006366 | transcription by RNA polymerase II |
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] 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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[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.