CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012672
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase N1 
Protein Synonyms/Alias
 Protease-activated kinase 1; PAK-1; Protein kinase C-like 1; Protein kinase C-like PKN; Protein kinase PKN-alpha; Protein-kinase C-related kinase 1; Serine-threonine protein kinase N 
Gene Name
 PKN1 
Gene Synonyms/Alias
 PAK1; PKN; PRK1; PRKCL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59IRKELKLKEGAENLRubiquitination[1]
167NGSTKDRKLLLTAQQubiquitination[1]
269KLTESNQKLGLLREAubiquitination[2]
451QRGLCALKFLKLEDFubiquitination[1]
613ALCSPLRKSPLTLEDubiquitination[1]
650SGELFAIKALKKGDIubiquitination[1]
670VESLMCEKRILAAVTubiquitination[1]
875ERDAEDVKKQPFFRTubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 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. 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 (ANDR)-dependent transcription, by being recruited to ANDR 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. 
Sequence Annotation
 REPEAT 34 110 REM 1.
 REPEAT 123 209 REM 2.
 REPEAT 210 291 REM 3.
 DOMAIN 325 461 C2.
 DOMAIN 615 874 Protein kinase.
 DOMAIN 875 942 AGC-kinase C-terminal.
 NP_BIND 621 629 ATP (By similarity).
 ACT_SITE 740 740 Proton acceptor (By similarity).
 BINDING 644 644 ATP (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 205 205 Phosphoserine.
 MOD_RES 374 374 Phosphoserine (By similarity).
 MOD_RES 448 448 N6-acetyllysine.
 MOD_RES 533 533 Phosphoserine.
 MOD_RES 537 537 Phosphoserine.
 MOD_RES 559 559 Phosphoserine.
 MOD_RES 562 562 Phosphoserine.
 MOD_RES 774 774 Phosphothreonine; by PDPK1.
 MOD_RES 778 778 Phosphothreonine.
 MOD_RES 914 914 Phosphothreonine.
 MOD_RES 916 916 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell membrane; Chromatin regulator; Complete proteome; Cytoplasm; Endosome; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 942 AA 
Protein Sequence
MAEANNPSEQ ELESEPRSWS LLEQLGLAGA DLAAPGVQQQ LELERERLRR EIRKELKLKE 60
GAENLRRATT DLGRSLGPVE LLLRGSSRRL DLLHQQLQEL HAHVVLPDPA ATHDGPQSPG 120
AGGPTCSATN LSRVAGLEKQ LAIELKVKQG AENMIQTYSN GSTKDRKLLL TAQQMLQDSK 180
TKIDIIRMQL RRALQAGQLE NQAAPDDTQG SPDLGAVELR IEELRHHFRV EHAVAEGAKN 240
VLRLLSAAKA PDRKAVSEAQ EKLTESNQKL GLLREALERR LGELPADHPK GRLLREELAA 300
ASSAAFSTRL AGPFPATHYS TLCKPAPLTG TLEVRVVGCR DLPETIPWNP TPSMGGPGTP 360
DSRPPFLSRP ARGLYSRSGS LSGRSSLKAE AENTSEVSTV LKLDNTVVGQ TSWKPCGPNA 420
WDQSFTLELE RARELELAVF WRDQRGLCAL KFLKLEDFLD NERHEVQLDM EPQGCLVAEV 480
TFRNPVIERI PRLRRQKKIF SKQQGKAFQR ARQMNIDVAT WVRLLRRLIP NATGTGTFSP 540
GASPGSEART TGDISVEKLN LGTDSDSSPQ KSSRDPPSSP SSLSSPIQES TAPELPSETQ 600
ETPGPALCSP LRKSPLTLED FKFLAVLGRG HFGKVLLSEF RPSGELFAIK ALKKGDIVAR 660
DEVESLMCEK RILAAVTSAG HPFLVNLFGC FQTPEHVCFV MEYSAGGDLM LHIHSDVFSE 720
PRAIFYSACV VLGLQFLHEH KIVYRDLKLD NLLLDTEGYV KIADFGLCKE GMGYGDRTST 780
FCGTPEFLAP EVLTDTSYTR AVDWWGLGVL LYEMLVGESP FPGDDEEEVF DSIVNDEVRY 840
PRFLSAEAIG IMRRLLRRNP ERRLGSSERD AEDVKKQPFF RTLGWEALLA RRLPPPFVPT 900
LSGRTDVSNF DEEFTGEAPT LSPPRDARPL TAAEQAAFLD FDFVAGGC 948 
Gene Ontology
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Compara.
 GO:0005768; C:endosome; IDA:UniProtKB.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IDA:UniProtKB.
 GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
 GO:0035402; F:histone kinase activity (H3-T11 specific); IDA:UniProtKB.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
 GO:0004697; F:protein kinase C activity; IEA:EC.
 GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
 GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
 GO:0010631; P:epithelial cell migration; IMP:UniProtKB.
 GO:0006972; P:hyperosmotic response; IEA:Compara.
 GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR011072; HR1_rho-bd.
 IPR011009; Kinase-like_dom.
 IPR017892; Pkinase_C.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF02185; HR1
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00239; C2
 SM00742; Hr1
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS50004; C2
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS