CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015190
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase N3 
Protein Synonyms/Alias
 Protein kinase PKN-beta; Protein-kinase C-related kinase 3 
Gene Name
 PKN3 
Gene Synonyms/Alias
 PKNBETA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
273QPSGTPVKPTALTGTubiquitination[1]
500PSNFLPKKTPLGEEMubiquitination[1]
592YAIKALKKQEVLSRDubiquitination[2]
686KIIYRDLKLDNLLLDubiquitination[1]
707IADFGLCKEGIGFGDubiquitination[3, 4]
813EQDAEEIKVQPFFRTubiquitination[2]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Contributes to invasiveness in malignant prostate cancer. 
Sequence Annotation
 REPEAT 18 90 REM 1.
 REPEAT 105 181 REM 2.
 REPEAT 182 255 REM 3.
 DOMAIN 559 818 Protein kinase.
 DOMAIN 819 889 AGC-kinase C-terminal.
 NP_BIND 565 573 ATP (By similarity).
 ACT_SITE 684 684 Proton acceptor (By similarity).
 BINDING 588 588 ATP (By similarity).
 MOD_RES 544 544 Phosphoserine.
 MOD_RES 548 548 Phosphoserine.
 MOD_RES 718 718 Phosphothreonine.
 MOD_RES 722 722 Phosphothreonine.
 MOD_RES 860 860 Phosphothreonine.  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 889 AA 
Protein Sequence
MEEGAPRQPG PSQWPPEDEK EVIRRAIQKE LKIKEGVENL RRVATDRRHL GHVQQLLRSS 60
NRRLEQLHGE LRELHARILL PGPGPGPAEP VASGPRPWAE QLRARHLEAL RRQLHVELKV 120
KQGAENMTHT CASGTPKERK LLAAAQQMLR DSQLKVALLR MKISSLEASG SPEPGPELLA 180
EELQHRLHVE AAVAEGAKNV VKLLSSRRTQ DRKALAEAQA QLQESSQKLD LLRLALEQLL 240
EQLPPAHPLR SRVTRELRAA VPGYPQPSGT PVKPTALTGT LQVRLLGCEQ LLTAVPGRSP 300
AAALASSPSE GWLRTKAKHQ RGRGELASEV LAVLKVDNRV VGQTGWGQVA EQSWDQTFVI 360
PLERARELEI GVHWRDWRQL CGVAFLRLED FLDNACHQLS LSLVPQGLLF AQVTFCDPVI 420
ERRPRLQRQE RIFSKRRGQD FLRASQMNLG MAAWGRLVMN LLPPCSSPST ISPPKGCPRT 480
PTTLREASDP ATPSNFLPKK TPLGEEMTPP PKPPRLYLPQ EPTSEETPRT KRPHMEPRTR 540
RGPSPPASPT RKPPRLQDFR CLAVLGRGHF GKVLLVQFKG TGKYYAIKAL KKQEVLSRDE 600
IESLYCEKRI LEAVGCTGHP FLLSLLACFQ TSSHACFVTE FVPGGDLMMQ IHEDVFPEPQ 660
ARFYVACVVL GLQFLHEKKI IYRDLKLDNL LLDAQGFLKI ADFGLCKEGI GFGDRTSTFC 720
GTPEFLAPEV LTQEAYTRAV DWWGLGVLLY EMLVGECPFP GDTEEEVFDC IVNMDAPYPG 780
FLSVQGLEFI QKLLQKCPEK RLGAGEQDAE EIKVQPFFRT TNWQALLART IQPPFVPTLC 840
GPADLRYFEG EFTGLPPALT PPAPHSLLTA RQQAAFRDFD FVSERFLEP 889 
Gene Ontology
 GO:0005794; C:Golgi apparatus; TAS:ProtInc.
 GO:0005634; C:nucleus; TAS:ProtInc.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004672; F:protein kinase activity; TAS:ProtInc.
 GO:0004697; F:protein kinase C activity; IEA:EC.
 GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
 GO:0007165; P:signal transduction; TAS:ProtInc. 
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
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS