Search Results
Overview
| Uniprot ID | P61978 |
|---|---|
| Protein Name | Heterogeneous nuclear ribonucleoprotein K |
| Gene Name | HNRNPK |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 163 | AGGIIGVKGAKIKEL |
| 198 | RVVLIGGKPDRVVEC |
| 219 | LISESPIKGRAQPYD |
| 34 | MEEEQAFKRSRNTDE |
| 405 | LAGSIIGKGGQRIKQ |
| 422 | HESGASIKIDEPLEG |
| 461 | SVKQYSGKFF***** |
| 52 | LRILLQSKNAGAVIG |
| 60 | NAGAVIGKGGKNIKA |
| 63 | AVIGKGGKNIKALRT |
Function
One of the major pre-mRNA-binding proteins. Binds tenaciously to poly(C) sequences. Likely to play a role in the nuclear metabolism of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich sequences. Can also bind poly(C) single-stranded DNA. Plays an important role in p53/TP53 response to DNA damage, acting at the level of both transcription activation and repression. When sumoylated, acts as a transcriptional coactivator of p53/TP53, playing a role in p21/CDKN1A and 14-3-3 sigma/SFN induction. As far as transcription repression is concerned, acts by interacting with long intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53. This interaction is necessary for the induction of apoptosis, but not cell cycle arrest. As part of a ribonucleoprotein complex composed at least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates the complex on chromatin, may negatively regulate the transcription of genes involved in neuronal differentiation (PubMed:33174841)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0010494 | cytoplasmic stress granule |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0002102 | podosome |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:0003729 | mRNA binding |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0045892 | negative regulation of DNA-templated transcription |
| Biological Process | GO:1905581 | positive regulation of low-density lipoprotein particle clearance |
| Biological Process | GO:0060816 | random inactivation of X chromosome |
| Biological Process | GO:0048024 | regulation of mRNA splicing, via spliceosome |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0031048 | regulatory ncRNA-mediated heterochromatin formation |
| Biological Process | GO:0006396 | RNA processing |
| Biological Process | GO:0007165 | signal transduction |
Reference
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[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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[6] 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.
[7] 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.
[8] 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.
[9] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[10] 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.
[11] 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.
[12] 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.