Search Results
Overview
| Uniprot ID | Q13043 |
|---|---|
| Protein Name | Serine/threonine-protein kinase 4 |
| Gene Name | STK4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 16 | PPRRQLKKLDEDSLT |
| 413 | NQINSFGKSVPGPLK |
Function
Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation (By similarity). Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016604 | nuclear body |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0000287 | magnesium ion binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0004672 | protein kinase activity |
| Molecular Function | GO:0106310 | protein serine kinase activity |
| Molecular Function | GO:0043539 | protein serine/threonine kinase activator activity |
| Molecular Function | GO:0004674 | protein serine/threonine kinase activity |
| Molecular Function | GO:0061629 | RNA polymerase II-specific DNA-binding transcription factor binding |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0000902 | cell morphogenesis |
| Biological Process | GO:0035329 | hippo signaling |
| Biological Process | GO:0035556 | intracellular signal transduction |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0018105 | peptidyl-serine phosphorylation |
| Biological Process | GO:0043065 | positive regulation of apoptotic process |
| Biological Process | GO:0035332 | positive regulation of hippo signaling |
| Biological Process | GO:0033138 | positive regulation of peptidyl-serine phosphorylation |
| Biological Process | GO:0001934 | positive regulation of protein phosphorylation |
| Biological Process | GO:1904237 | positive regulation of substrate-dependent cell migration, cell attachment to substrate |
| Biological Process | GO:0046777 | protein autophosphorylation |
| Biological Process | GO:0006606 | protein import into nucleus |
| Biological Process | GO:0006468 | protein phosphorylation |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0051262 | protein tetramerization |
| Biological Process | GO:0043408 | regulation of MAPK cascade |
| Biological Process | GO:0007165 | signal transduction |
Reference
[1] 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.
[2] 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.