CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022408
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase PLK2 
Protein Synonyms/Alias
 Polo-like kinase 2; PLK-2; hPlk2; Serine/threonine-protein kinase SNK; hSNK; Serum-inducible kinase 
Gene Name
 PLK2 
Gene Synonyms/Alias
 SNK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
24MCEQALGKGCGADSKubiquitination[1]
80IVDPTTGKRYCRGKVubiquitination[1, 2]
194RQIVSGLKYLHEQEIubiquitination[1]
207EILHRDLKLGNFFINubiquitination[1, 2, 3]
317LIASMLSKNPEDRPSubiquitination[1, 2, 3]
375AAALFGGKKDKARYIubiquitination[1, 2, 3]
376AALFGGKKDKARYIDubiquitination[1]
378LFGGKKDKARYIDTHubiquitination[1]
390DTHNRVSKEDEDIYKubiquitination[2, 3]
438GTPAVENKQQIGDAIubiquitination[1, 2, 3]
670SGCSSELKNRMEYALubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 
Functional Description
 Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress. 
Sequence Annotation
 DOMAIN 82 334 Protein kinase.
 DOMAIN 510 573 POLO box 1.
 DOMAIN 606 677 POLO box 2.
 NP_BIND 88 96 ATP (By similarity).
 ACT_SITE 205 205 Proton acceptor (By similarity).
 BINDING 111 111 ATP (By similarity).
 MOD_RES 239 239 Phosphothreonine (By similarity).  
Keyword
 ATP-binding; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Tumor suppressor. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 685 AA 
Protein Sequence
MELLRTITYQ PAASTKMCEQ ALGKGCGADS KKKRPPQPPE ESQPPQSQAQ VPPAAPHHHH 60
HHSHSGPEIS RIIVDPTTGK RYCRGKVLGK GGFAKCYEMT DLTNNKVYAA KIIPHSRVAK 120
PHQREKIDKE IELHRILHHK HVVQFYHYFE DKENIYILLE YCSRRSMAHI LKARKVLTEP 180
EVRYYLRQIV SGLKYLHEQE ILHRDLKLGN FFINEAMELK VGDFGLAARL EPLEHRRRTI 240
CGTPNYLSPE VLNKQGHGCE SDIWALGCVM YTMLLGRPPF ETTNLKETYR CIREARYTMP 300
SSLLAPAKHL IASMLSKNPE DRPSLDDIIR HDFFLQGFTP DRLSSSCCHT VPDFHLSSPA 360
KNFFKKAAAA LFGGKKDKAR YIDTHNRVSK EDEDIYKLRH DLKKTSITQQ PSKHRTDEEL 420
QPPTTTVARS GTPAVENKQQ IGDAIRMIVR GTLGSCSSSS ECLEDSTMGS VADTVARVLR 480
GCLENMPEAD CIPKEQLSTS FQWVTKWVDY SNKYGFGYQL SDHTVGVLFN NGAHMSLLPD 540
KKTVHYYAEL GQCSVFPATD APEQFISQVT VLKYFSHYME ENLMDGGDLP SVTDIRRPRL 600
YLLQWLKSDK ALMMLFNDGT FQVNFYHDHT KIIICSQNEE YLLTYINEDR ISTTFRLTTL 660
LMSGCSSELK NRMEYALNML LQRCN 685 
Gene Ontology
 GO:0005814; C:centriole; IDA:UniProtKB.
 GO:0030425; C:dendrite; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0060292; P:long term synaptic depression; ISS:UniProtKB.
 GO:0060291; P:long-term synaptic potentiation; ISS:UniProtKB.
 GO:0007613; P:memory; ISS:UniProtKB.
 GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
 GO:0007052; P:mitotic spindle organization; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
 GO:0046599; P:regulation of centriole replication; IDA:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000959; POLO_box_duplicated_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase
 PF00659; POLO_box 
SMART
 SM00220; S_TKc 
PROSITE
 PS50078; POLO_BOX
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS