Search Results

Overview

Uniprot ID	Q16513
Protein Name	Serine/threonine-protein kinase N2
Gene Name	PKN2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
247	MKLLGSGKVTDRKAL
252	SGKVTDRKALSEAQA
385	GSSRNLLKTDDLSND
77	RKVTTDKKSLAYVDN

Function

PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (PubMed:27104747)

Protein Sequence

10 MASNPERGEI 20 LLTELQGDSR 30 SLPFSENVSA 40 VQKLDFSDTM 50 VQQKLDDIKD 60 RIKREIRKEL 70 KIKEGAENLR 80 KVTTDKKSLA 90 YVDNILKKSN 100 KKLEELHHKL 110 QELNAHIVVS 120 DPEDITDCPR 130 TPDTPNNDPR 140 CSTSNNRLKA 150 LQKQLDIELK 160 VKQGAENMIQ 170 MYSNGSSKDR 180 KLHGTAQQLL 190 QDSKTKIEVI 200 RMQILQAVQT 210 NELAFDNAKP 220 VISPLELRME 230 ELRHHFRIEF 240 AVAEGAKNVM 250 KLLGSGKVTD 260 RKALSEAQAR 270 FNESSQKLDL 280 LKYSLEQRLN 290 EVPKNHPKSR 300 IIIEELSLVA 310 ASPTLSPRQS 320 MISTQNQYST 330 LSKPAALTGT 340 LEVRLMGCQD 350 ILENVPGRSK 360 ATSVALPGWS 370 PSETRSSFMS 380 RTSKSKSGSS 390 RNLLKTDDLS 400 NDVCAVLKLD 410 NTVVGQTSWK 420 PISNQSWDQK 430 FTLELDRSRE 440 LEISVYWRDW 450 RSLCAVKFLR 460 LEDFLDNQRH 470 GMCLYLEPQG 480 TLFAEVTFFN 490 PVIERRPKLQ 500 RQKKIFSKQQ 510 GKTFLRAPQM 520 NINIATWGRL 530 VRRAIPTVNH 540 SGTFSPQAPV 550 PTTVPVVDVR 560 IPQLAPPASD 570 STVTKLDFDL 580 EPEPPPAPPR 590 ASSLGEIDES 600 SELRVLDIPG 610 QDSETVFDIQ 620 NDRNSILPKS 630 QSEYKPDTPQ 640 SGLEYSGIQE 650 LEDRRSQQRF 660 QFNLQDFRCC 670 AVLGRGHFGK 680 VLLAEYKNTN 690 EMFAIKALKK 700 GDIVARDEVD 710 SLMCEKRIFE 720 TVNSVRHPFL 730 VNLFACFQTK 740 EHVCFVMEYA 750 AGGDLMMHIH 760 TDVFSEPRAV 770 FYAACVVLGL 780 QYLHEHKIVY 790 RDLKLDNLLL 800 DTEGFVKIAD 810 FGLCKEGMGY 820 GDRTSTFCGT 830 PEFLAPEVLT 840 ETSYTRAVDW 850 WGLGVLIYEM 860 LVGESPFPGD 870 DEEEVFDSIV 880 NDEVRYPRFL 890 STEAISIMRR 900 LLRRNPERRL 910 GASEKDAEDV 920 KKHPFFRLID 930 WSALMDKKVK 940 PPFIPTIRGR 950 EDVSNFDDEF 960 TSEAPILTPP 970 REPRILSEEE 980 QEMFRDFDYI ADWC

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0043296	apical junction complex
Cellular Component	GO:0032154	cleavage furrow
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0045111	intermediate filament cytoskeleton
Cellular Component	GO:0030027	lamellipodium
Cellular Component	GO:0030496	midbody
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
Cellular Component	GO:0048471	perinuclear region of cytoplasm
Cellular Component	GO:0032991	protein-containing complex
Molecular Function	GO:0005524	ATP binding
Molecular Function	GO:0045296	cadherin binding
Molecular Function	GO:0004697	diacylglycerol-dependent serine/threonine kinase activity
Molecular Function	GO:0042826	histone deacetylase binding
Molecular Function	GO:0016301	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:0004713	protein tyrosine kinase activity
Molecular Function	GO:0003723	RNA binding
Molecular Function	GO:0070063	RNA polymerase binding
Molecular Function	GO:0031267	small GTPase binding
Biological Process	GO:0043297	apical junction assembly
Biological Process	GO:0006915	apoptotic process
Biological Process	GO:0007155	cell adhesion
Biological Process	GO:0051301	cell division
Biological Process	GO:0030030	cell projection organization
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0010631	epithelial cell migration
Biological Process	GO:0035556	intracellular signal transduction
Biological Process	GO:0032467	positive regulation of cytokinesis
Biological Process	GO:0045931	positive regulation of mitotic cell cycle
Biological Process	GO:0045070	positive regulation of viral genome replication
Biological Process	GO:0006468	protein phosphorylation
Biological Process	GO:2000145	regulation of cell motility
Biological Process	GO:0007165	signal transduction
Biological Process	GO:0097700	vascular endothelial cell response to laminar fluid shear stress

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] 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] 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.

[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.