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Overview

Uniprot ID	Q16512
Protein Name	Serine/threonine-protein kinase N1
Gene Name	PKN1
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
243	LRLLSAAKAPDRKAV

Function

PKC-related serine/threonine-protein kinase involved in various processes such as regulation of the intermediate filaments of the actin cytoskeleton, cell migration, tumor cell invasion and transcription regulation. Part of a signaling cascade that begins with the activation of the adrenergic receptor ADRA1B and leads to the activation of MAPK14. Regulates the cytoskeletal network by phosphorylating proteins such as VIM and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and 'Ser-669' of MAPT/Tau, lowering its ability to bind to microtubules, resulting in disruption of tubulin assembly. Acts as a key coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-11' of histone H3 (H3T11ph), a specific tag for epigenetic transcriptional activation that promotes demethylation of histone H3 'Lys-9' (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9, leading to impair their import in the nucleus. Phosphorylates 'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170' of MARCKS, and GFAP. Able to phosphorylate RPS6 in vitro

Protein Sequence

10 MASDAVQSEP 20 RSWSLLEQLG 30 LAGADLAAPG 40 VQQQLELERE 50 RLRREIRKEL 60 KLKEGAENLR 70 RATTDLGRSL 80 GPVELLLRGS 90 SRRLDLLHQQ 100 LQELHAHVVL 110 PDPAATHDGP 120 QSPGAGGPTC 130 SATNLSRVAG 140 LEKQLAIELK 150 VKQGAENMIQ 160 TYSNGSTKDR 170 KLLLTAQQML 180 QDSKTKIDII 190 RMQLRRALQA 200 GQLENQAAPD 210 DTQGSPDLGA 220 VELRIEELRH 230 HFRVEHAVAE 240 GAKNVLRLLS 250 AAKAPDRKAV 260 SEAQEKLTES 270 NQKLGLLREA 280 LERRLGELPA 290 DHPKGRLLRE 300 ELAAASSAAF 310 STRLAGPFPA 320 THYSTLCKPA 330 PLTGTLEVRV 340 VGCRDLPETI 350 PWNPTPSMGG 360 PGTPDSRPPF 370 LSRPARGLYS 380 RSGSLSGRSS 390 LKAEAENTSE 400 VSTVLKLDNT 410 VVGQTSWKPC 420 GPNAWDQSFT 430 LELERARELE 440 LAVFWRDQRG 450 LCALKFLKLE 460 DFLDNERHEV 470 QLDMEPQGCL 480 VAEVTFRNPV 490 IERIPRLRRQ 500 KKIFSKQQGK 510 AFQRARQMNI 520 DVATWVRLLR 530 RLIPNATGTG 540 TFSPGASPGS 550 EARTTGDISV 560 EKLNLGTDSD 570 SSPQKSSRDP 580 PSSPSSLSSP 590 IQESTAPELP 600 SETQETPGPA 610 LCSPLRKSPL 620 TLEDFKFLAV 630 LGRGHFGKVL 640 LSEFRPSGEL 650 FAIKALKKGD 660 IVARDEVESL 670 MCEKRILAAV 680 TSAGHPFLVN 690 LFGCFQTPEH 700 VCFVMEYSAG 710 GDLMLHIHSD 720 VFSEPRAIFY 730 SACVVLGLQF 740 LHEHKIVYRD 750 LKLDNLLLDT 760 EGYVKIADFG 770 LCKEGMGYGD 780 RTSTFCGTPE 790 FLAPEVLTDT 800 SYTRAVDWWG 810 LGVLLYEMLV 820 GESPFPGDDE 830 EEVFDSIVND 840 EVRYPRFLSA 850 EAIGIMRRLL 860 RRNPERRLGS 870 SERDAEDVKK 880 QPFFRTLGWE 890 ALLARRLPPP 900 FVPTLSGRTD 910 VSNFDEEFTG 920 EAPTLSPPRD 930 ARPLTAAEQA 940 AFLDFDFVAG GC

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0032154	cleavage furrow
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005768	endosome
Cellular Component	GO:0030496	midbody
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:0003682	chromatin binding
Molecular Function	GO:0004697	diacylglycerol-dependent serine/threonine kinase activity
Molecular Function	GO:0042393	histone binding
Molecular Function	GO:0042826	histone deacetylase binding
Molecular Function	GO:0035402	histone H3T11 kinase activity
Molecular Function	GO:0050681	nuclear androgen receptor binding
Molecular Function	GO:0004672	protein kinase activity
Molecular Function	GO:0005080	protein kinase C binding
Molecular Function	GO:0106310	protein serine kinase activity
Molecular Function	GO:0004674	protein serine/threonine kinase activity
Molecular Function	GO:0031267	small GTPase binding
Molecular Function	GO:0003713	transcription coactivator activity
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0010631	epithelial cell migration
Biological Process	GO:0035556	intracellular signal transduction
Biological Process	GO:0043687	post-translational protein modification
Biological Process	GO:0006468	protein phosphorylation
Biological Process	GO:0060765	regulation of androgen receptor signaling pathway
Biological Process	GO:2000145	regulation of cell motility
Biological Process	GO:0006357	regulation of transcription by RNA polymerase II
Biological Process	GO:0007165	signal transduction

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] 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.