Search Results
Overview
| Uniprot ID | Q13177 |
|---|---|
| Protein Name | Serine/threonine-protein kinase PAK 2 |
| Gene Name | PAK2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 191 | APRPDHTKSIYTRSV |
| 216 | SHVDGAAKSLDKQKK |
| 220 | GAAKSLDKQKKKTKM |
| 399 | QITPEQSKRSTMVGT |
| 52 | EEKKPRHKIISIFSG |
| 62 | SIFSGTEKGSKKKEK |
| 65 | SGTEKGSKKKEKERP |
Function
Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation (PubMed:12853446, PubMed:16617111, PubMed:19273597, PubMed:19923322, PubMed:33693784, PubMed:7744004, PubMed:9171063). Acts as a downstream effector of the small GTPases CDC42 and RAC1 (PubMed:7744004). Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues (PubMed:7744004). Full-length PAK2 stimulates cell survival and cell growth (PubMed:7744004). Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration (PubMed:21317288). Phosphorylates JUN and plays an important role in EGF-induced cell proliferation (PubMed:21177766). Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP (PubMed:21724829). Phosphorylates CASP7, thereby preventing its activity (PubMed:21555521, PubMed:27889207). Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis (PubMed:19273597, PubMed:19923322). On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway (PubMed:12853446, PubMed:16617111, PubMed:9171063). Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation (PubMed:15234964)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005911 | cell-cell junction |
| Biological Process | GO:0034333 | adherens junction assembly |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0070830 | bicellular tight junction assembly |
| Biological Process | GO:0003300 | cardiac muscle hypertrophy |
| Biological Process | GO:0016477 | cell migration |
| Biological Process | GO:0009267 | cellular response to starvation |
| Biological Process | GO:0071560 | cellular response to transforming growth factor beta stimulus |
| Biological Process | GO:0035556 | intracellular signal transduction |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0006469 | negative regulation of protein kinase activity |
| Biological Process | GO:0051497 | negative regulation of stress fiber assembly |
| Biological Process | GO:2001238 | positive regulation of extrinsic apoptotic signaling pathway |
| Biological Process | GO:0046777 | protein autophosphorylation |
| Biological Process | GO:0150105 | protein localization to cell-cell junction |
| Biological Process | GO:0006468 | protein phosphorylation |
| Biological Process | GO:0050770 | regulation of axonogenesis |
| Biological Process | GO:0051493 | regulation of cytoskeleton organization |
| Biological Process | GO:0043408 | regulation of MAPK cascade |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0002223 | stimulatory C-type lectin receptor signaling pathway |
| Biological Process | GO:0048010 | vascular endothelial growth factor receptor signaling pathway |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0014069 | postsynaptic density |
| Cellular Component | GO:0030141 | secretory granule |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0042802 | identical protein binding |
| 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:0004674 | protein serine/threonine kinase activity |
| Molecular Function | GO:0030296 | protein tyrosine kinase activator activity |
| Molecular Function | GO:0031267 | small GTPase binding |
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] 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.
[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] 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.
[6] 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.
[7] 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.
[8] 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.
[9] 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.