CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021371
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase PLK3 
Protein Synonyms/Alias
 Cytokine-inducible serine/threonine-protein kinase; FGF-inducible kinase; Polo-like kinase 3; PLK-3; Proliferation-related kinase 
Gene Name
 PLK3 
Gene Synonyms/Alias
 CNK; FNK; PRK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
187GILHRDLKLGNFFITubiquitination[1]
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] 
Functional Description
 Serine/threonine-protein kinase involved in cell cycle regulation, response to stress and Golgi disassembly. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates ATF2, BCL2L1, CDC25A, CDC25C, CHEK2, HIF1A, JUN, p53/TP53, p73/TP73, PTEN, TOP2A and VRK1. Involved in cell cycle regulation: required for entry into S phase and cytokinesis. Phosphorylates BCL2L1, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Plays a key role in response to stress: rapidly activated upon stress stimulation, such as ionizing radiation, reactive oxygen species (ROS), hyperosmotic stress, UV irradiation and hypoxia. Involved in DNA damage response and G1/S transition checkpoint by phosphorylating CDC25A, p53/TP53 and p73/TP73. Phosphorylates p53/TP53 in response to reactive oxygen species (ROS), thereby promoting p53/TP53-mediated apoptosis. Phosphorylates CHEK2 in response to DNA damage, promoting the G2/M transition checkpoint. Phosphorylates the transcription factor p73/TP73 in response to DNA damage, leading to inhibit p73/TP73-mediated transcriptional activation and pro-apoptotic functions. Phosphorylates HIF1A and JUN is response to hypoxia. Phosphorylates ATF2 following hyperosmotic stress in corneal epithelium. Also involved in Golgi disassembly during the cell cycle: part of a MEK1/MAP2K1-dependent pathway that induces Golgi fragmentation during mitosis by mediating phosphorylation of VRK1. May participate in endomitotic cell cycle, a form of mitosis in which both karyokinesis and cytokinesis are interrupted and is a hallmark of megakaryocyte differentiation, via its interaction with CIB1. 
Sequence Annotation
 DOMAIN 62 314 Protein kinase.
 DOMAIN 470 537 POLO box 1.
 DOMAIN 567 637 POLO box 2.
 NP_BIND 68 76 ATP (By similarity).
 ACT_SITE 185 185 Proton acceptor (By similarity).
 BINDING 91 91 ATP (By similarity).  
Keyword
 Apoptosis; ATP-binding; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; Golgi apparatus; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 646 AA 
Protein Sequence
MEPAAGFLSP RPFQRAAAAP APPAGPGPPP SALRGPELEM LAGLPTSDPG RLITDPRSGR 60
TYLKGRLLGK GGFARCYEAT DTETGSAYAV KVIPQSRVAK PHQREKILNE IELHRDLQHR 120
HIVRFSHHFE DADNIYIFLE LCSRKSLAHI WKARHTLLEP EVRYYLRQIL SGLKYLHQRG 180
ILHRDLKLGN FFITENMELK VGDFGLAARL EPPEQRKKTI CGTPNYVAPE VLLRQGHGPE 240
ADVWSLGCVM YTLLCGSPPF ETADLKETYR CIKQVHYTLP ASLSLPARQL LAAILRASPR 300
DRPSIDQILR HDFFTKGYTP DRLPISSCVT VPDLTPPNPA RSLFAKVTKS LFGRKKKSKN 360
HAQERDEVSG LVSGLMRTSV GHQDARPEAP AASGPAPVSL VETAPEDSSP RGTLASSGDG 420
FEEGLTVATV VESALCALRN CIAFMPPAEQ NPAPLAQPEP LVWVSKWVDY SNKFGFGYQL 480
SSRRVAVLFN DGTHMALSAN RKTVHYNPTS TKHFSFSVGA VPRALQPQLG ILRYFASYME 540
QHLMKGGDLP SVEEVEVPAP PLLLQWVKTD QALLMLFSDG TVQVNFYGDH TKLILSGWEP 600
LLVTFVARNR SACTYLASHL RQLGCSPDLR QRLRYALRLL RDRSPA 646 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0005795; C:Golgi stack; IDA:UniProtKB.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0002039; F:p53 binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; TAS:UniProtKB.
 GO:0000910; P:cytokinesis; TAS:UniProtKB.
 GO:0007113; P:endomitotic cell cycle; TAS:UniProtKB.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
 GO:0090166; P:Golgi disassembly; IDA:UniProtKB.
 GO:0007093; P:mitotic cell cycle checkpoint; TAS:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; IDA:UniProtKB.
 GO:0043491; P:protein kinase B signaling cascade; ISS:UniProtKB.
 GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB.
 GO:0006970; P:response to osmotic stress; IDA:UniProtKB.
 GO:0009314; P:response to radiation; IDA:UniProtKB.
 GO:0000302; P:response to reactive oxygen species; IDA:UniProtKB.
 GO:0000084; P:S phase of mitotic cell cycle; IMP: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.
 IPR020658; Ser/Thr_kinase_Plk3. 
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