CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012673
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase N2 
Protein Synonyms/Alias
 PKN gamma; Protein kinase C-like 2; Protein-kinase C-related kinase 2 
Gene Name
 PKN2 
Gene Synonyms/Alias
 PRK2; PRKCL2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
272SQKLDLLKYSLEQRLacetylation[1]
565ASDSTVTKLDFDLEPubiquitination[2]
784KIVYRDLKLDNLLLDubiquitination[3]
805IADFGLCKEGMGYGDubiquitination[4]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] 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]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] 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
Functional Description
 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). Phosphorylates HCV NS5B leading to stimulation of HCV RNA replication. 
Sequence Annotation
 REPEAT 44 119 REM 1.
 REPEAT 133 213 REM 2.
 REPEAT 214 295 REM 3.
 DOMAIN 330 463 C2.
 DOMAIN 657 916 Protein kinase.
 DOMAIN 917 984 AGC-kinase C-terminal.
 NP_BIND 663 671 ATP (By similarity).
 REGION 382 463 Necessary to rescue apical junction
 REGION 917 977 Necessary for the catalytic activity.
 REGION 978 984 Negatively regulates the responsiveness
 ACT_SITE 782 782 Proton acceptor (By similarity).
 BINDING 686 686 ATP (By similarity).
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 121 121 Phosphothreonine.
 MOD_RES 124 124 Phosphothreonine.
 MOD_RES 302 302 Phosphoserine.
 MOD_RES 306 306 Phosphoserine.
 MOD_RES 360 360 Phosphoserine.
 MOD_RES 362 362 Phosphoserine.
 MOD_RES 367 367 Phosphoserine (By similarity).
 MOD_RES 535 535 Phosphoserine.
 MOD_RES 583 583 Phosphoserine.
 MOD_RES 628 628 Phosphothreonine.
 MOD_RES 631 631 Phosphoserine.
 MOD_RES 816 816 Phosphothreonine; by PDPK1.
 MOD_RES 958 958 Phosphothreonine.  
Keyword
 Alternative splicing; Apoptosis; ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell junction; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; 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
 984 AA 
Protein Sequence
MASNPERGEI LLTELQGDSR SLPFSENVSA VQKLDFSDTM VQQKLDDIKD RIKREIRKEL 60
KIKEGAENLR KVTTDKKSLA YVDNILKKSN KKLEELHHKL QELNAHIVVS DPEDITDCPR 120
TPDTPNNDPR CSTSNNRLKA LQKQLDIELK VKQGAENMIQ MYSNGSSKDR KLHGTAQQLL 180
QDSKTKIEVI RMQILQAVQT NELAFDNAKP VISPLELRME ELRHHFRIEF AVAEGAKNVM 240
KLLGSGKVTD RKALSEAQAR FNESSQKLDL LKYSLEQRLN EVPKNHPKSR IIIEELSLVA 300
ASPTLSPRQS MISTQNQYST LSKPAALTGT LEVRLMGCQD ILENVPGRSK ATSVALPGWS 360
PSETRSSFMS RTSKSKSGSS RNLLKTDDLS NDVCAVLKLD NTVVGQTSWK PISNQSWDQK 420
FTLELDRSRE LEISVYWRDW RSLCAVKFLR LEDFLDNQRH GMCLYLEPQG TLFAEVTFFN 480
PVIERRPKLQ RQKKIFSKQQ GKTFLRAPQM NINIATWGRL VRRAIPTVNH SGTFSPQAPV 540
PTTVPVVDVR IPQLAPPASD STVTKLDFDL EPEPPPAPPR ASSLGEIDES SELRVLDIPG 600
QDSETVFDIQ NDRNSILPKS QSEYKPDTPQ SGLEYSGIQE LEDRRSQQRF QFNLQDFRCC 660
AVLGRGHFGK VLLAEYKNTN EMFAIKALKK GDIVARDEVD SLMCEKRIFE TVNSVRHPFL 720
VNLFACFQTK EHVCFVMEYA AGGDLMMHIH TDVFSEPRAV FYAACVVLGL QYLHEHKIVY 780
RDLKLDNLLL DTEGFVKIAD FGLCKEGMGY GDRTSTFCGT PEFLAPEVLT ETSYTRAVDW 840
WGLGVLIYEM LVGESPFPGD DEEEVFDSIV NDEVRYPRFL STEAISIMRR LLRRNPERRL 900
GASEKDAEDV KKHPFFRLID WSALMDKKVK PPFIPTIRGR EDVSNFDDEF TSEAPILTPP 960
REPRILSEEE QEMFRDFDYI ADWC 984 
Gene Ontology
 GO:0043296; C:apical junction complex; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
 GO:0004697; F:protein kinase C activity; IEA:EC.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0043297; P:apical junction assembly; IMP:UniProtKB.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0010631; P:epithelial cell migration; IDA:UniProtKB.
 GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
 GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
 GO:2000145; P:regulation of cell motility; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 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