CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000078
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase PLK4 
Protein Synonyms/Alias
 Polo-like kinase 4; PLK-4; Serine/threonine-protein kinase 18; Serine/threonine-protein kinase Sak 
Gene Name
 PLK4 
Gene Synonyms/Alias
 SAK; STK18 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MATCIGEKIEDFKVGubiquitination[1]
13GEKIEDFKVGNLLGKubiquitination[1]
151LTRNMNIKIADFGLAubiquitination[1]
162FGLATQLKMPHEKHYubiquitination[1]
167QLKMPHEKHYTLCGTubiquitination[1]
321IGQPLPNKMTVFPKNubiquitination[1]
327NKMTVFPKNKSSTDFubiquitination[1]
329MTVFPKNKSSTDFSSubiquitination[1]
392SNSQSQAKTYTMERCubiquitination[1]
436IFNFFKEKTSSSSGSubiquitination[1]
512QGHPDLQKDTSKNAWubiquitination[1]
538SDNAHSVKQQNTMKYacetylation[2]
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] 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] 
Functional Description
 Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. 
Sequence Annotation
 DOMAIN 12 265 Protein kinase.
 DOMAIN 892 956 POLO box.
 NP_BIND 18 26 ATP (By similarity).
 ACT_SITE 136 136 Proton acceptor (By similarity).
 BINDING 41 41 ATP (Probable).
 MOD_RES 401 401 Phosphoserine.
 MOD_RES 817 817 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 970 AA 
Protein Sequence
MATCIGEKIE DFKVGNLLGK GSFAGVYRAE SIHTGLEVAI KMIDKKAMYK AGMVQRVQNE 60
VKIHCQLKHP SILELYNYFE DSNYVYLVLE MCHNGEMNRY LKNRVKPFSE NEARHFMHQI 120
ITGMLYLHSH GILHRDLTLS NLLLTRNMNI KIADFGLATQ LKMPHEKHYT LCGTPNYISP 180
EIATRSAHGL ESDVWSLGCM FYTLLIGRPP FDTDTVKNTL NKVVLADYEM PSFLSIEAKD 240
LIHQLLRRNP ADRLSLSSVL DHPFMSRNSS TKSKDLGTVE DSIDSGHATI STAITASSST 300
SISGSLFDKR RLLIGQPLPN KMTVFPKNKS STDFSSSGDG NSFYTQWGNQ ETSNSGRGRV 360
IQDAEERPHS RYLRRAYSSD RSGTSNSQSQ AKTYTMERCH SAEMLSVSKR SGGGENEERY 420
SPTDNNANIF NFFKEKTSSS SGSFERPDNN QALSNHLCPG KTPFPFADPT PQTETVQQWF 480
GNLQINAHLR KTTEYDSISP NRDFQGHPDL QKDTSKNAWT DTKVKKNSDA SDNAHSVKQQ 540
NTMKYMTALH SKPEIIQQEC VFGSDPLSEQ SKTRGMEPPW GYQNRTLRSI TSPLVAHRLK 600
PIRQKTKKAV VSILDSEEVC VELVKEYASQ EYVKEVLQIS SDGNTITIYY PNGGRGFPLA 660
DRPPSPTDNI SRYSFDNLPE KYWRKYQYAS RFVQLVRSKS PKITYFTRYA KCILMENSPG 720
ADFEVWFYDG VKIHKTEDFI QVIEKTGKSY TLKSESEVNS LKEEIKMYMD HANEGHRICL 780
ALESIISEEE RKTRSAPFFP IIIGRKPGST SSPKALSPPP SVDSNYPTRE RASFNRMVMH 840
SAASPTQAPI LNPSMVTNEG LGLTTTASGT DISSNSLKDC LPKSAQLLKS VFVKNVGWAT 900
QLTSGAVWVQ FNDGSQLVVQ AGVSSISYTS PNGQTTRYGE NEKLPDYIKQ KLQCLSSILL 960
MFSNPTPNFH 970 
Gene Ontology
 GO:0005814; C:centriole; IDA:UniProtKB.
 GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005730; C:nucleolus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
 GO:0007099; P:centriole replication; IMP:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0046601; P:positive regulation of centriole replication; IMP:UniProtKB.
 GO:0060707; P:trophoblast giant cell differentiation; ISS: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.
 IPR008266; Tyr_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