PLK4_HUMAN - dbPTM
PLK4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLK4_HUMAN
UniProt AC O00444
Protein Name Serine/threonine-protein kinase PLK4
Gene Name PLK4
Organism Homo sapiens (Human).
Sequence Length 970
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Nucleus, nucleolus. Cleavage furrow. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more
Protein 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 deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification. [PubMed: 22020124]
Protein Sequence MATCIGEKIEDFKVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMNRYLKNRVKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPSFLSIEAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSTKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDKRRLLIGQPLPNKMTVFPKNKSSTDFSSSGDGNSFYTQWGNQETSNSGRGRVIQDAEERPHSRYLRRAYSSDRSGTSNSQSQAKTYTMERCHSAEMLSVSKRSGGGENEERYSPTDNNANIFNFFKEKTSSSSGSFERPDNNQALSNHLCPGKTPFPFADPTPQTETVQQWFGNLQINAHLRKTTEYDSISPNRDFQGHPDLQKDTSKNAWTDTKVKKNSDASDNAHSVKQQNTMKYMTALHSKPEIIQQECVFGSDPLSEQSKTRGMEPPWGYQNRTLRSITSPLVAHRLKPIRQKTKKAVVSILDSEEVCVELVKEYASQEYVKEVLQISSDGNTITIYYPNGGRGFPLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCILMENSPGADFEVWFYDGVKIHKTEDFIQVIEKTGKSYTLKSESEVNSLKEEIKMYMDHANEGHRICLALESIISEEERKTRSAPFFPIIIGRKPGSTSSPKALSPPPSVDSNYPTRERASFNRMVMHSAASPTQAPILNPSMVTNEGLGLTTTASGTDISSNSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
8UbiquitinationMATCIGEKIEDFKVG
CCCCCCCCCCCCCCC		46.30-
13UbiquitinationGEKIEDFKVGNLLGK
CCCCCCCCCCCCCCC		62.6529967540
22PhosphorylationGNLLGKGSFAGVYRA
CCCCCCCCCCEEEEH		18.5321985771
45AcetylationVAIKMIDKKAMYKAG
HHHHHCCHHHHHHHC		31.3527796307
46AcetylationAIKMIDKKAMYKAGM
HHHHCCHHHHHHHCC		34.3427796307
50UbiquitinationIDKKAMYKAGMVQRV
CCHHHHHHHCCHHHH		25.9429967540
121UbiquitinationRHFMHQIITGMLYLH
HHHHHHHHHHHHHHH		1.8829967540
130UbiquitinationGMLYLHSHGILHRDL
HHHHHHHCCCCCCCC		19.3029967540
151UbiquitinationLTRNMNIKIADFGLA
HHCCCCCEECCCCHH		27.17-
159PhosphorylationIADFGLATQLKMPHE
ECCCCHHHHCCCCCH		39.2024732914
162UbiquitinationFGLATQLKMPHEKHY
CCHHHHCCCCCHHCC		40.3429967540
167UbiquitinationQLKMPHEKHYTLCGT
HCCCCCHHCCEECCC		38.59-
170PhosphorylationMPHEKHYTLCGTPNY
CCCHHCCEECCCCCC		18.4521985771
174PhosphorylationKHYTLCGTPNYISPE
HCCEECCCCCCCCHH		13.83-
177PhosphorylationTLCGTPNYISPEIAT
EECCCCCCCCHHHHH		12.1821985771
255PhosphorylationRNPADRLSLSSVLDH
CCHHHCCCHHHHHCC		27.4023090842
257PhosphorylationPADRLSLSSVLDHPF
HHHCCCHHHHHCCCC		18.2823090842
258PhosphorylationADRLSLSSVLDHPFM
HHCCCHHHHHCCCCC		31.8023090842
266PhosphorylationVLDHPFMSRNSSTKS
HHCCCCCCCCCCCCC		28.7923090842
269PhosphorylationHPFMSRNSSTKSKDL
CCCCCCCCCCCCCCC		37.9723090842
270PhosphorylationPFMSRNSSTKSKDLG
CCCCCCCCCCCCCCC		43.3223090842
271PhosphorylationFMSRNSSTKSKDLGT
CCCCCCCCCCCCCCC		38.8823090842
286UbiquitinationVEDSIDSGHATISTA
HHHHHHCCCEEEEEE		15.6529967540
295UbiquitinationATISTAITASSSTSI
EEEEEEEEECCCCCC		20.3029967540
298PhosphorylationSTAITASSSTSISGS
EEEEEECCCCCCCCC		34.8630576142
305PhosphorylationSSTSISGSLFDKRRL
CCCCCCCCCCCCCEE		21.0520032307
321UbiquitinationIGQPLPNKMTVFPKN
CCCCCCCCCEEECCC		33.73-
323PhosphorylationQPLPNKMTVFPKNKS
CCCCCCCEEECCCCC		22.17-
327UbiquitinationNKMTVFPKNKSSTDF
CCCEEECCCCCCCCC		66.5929967540
329UbiquitinationMTVFPKNKSSTDFSS
CEEECCCCCCCCCCC		52.49-
330PhosphorylationTVFPKNKSSTDFSSS
EEECCCCCCCCCCCC		48.1123917254
331PhosphorylationVFPKNKSSTDFSSSG
EECCCCCCCCCCCCC		33.3423186163
332PhosphorylationFPKNKSSTDFSSSGD
ECCCCCCCCCCCCCC		48.4223186163
345PhosphorylationGDGNSFYTQWGNQET
CCCCCCEEECCCCCC		18.81-
357MethylationQETSNSGRGRVIQDA
CCCCCCCCCCCCCCH		29.57115383317
370PhosphorylationDAEERPHSRYLRRAY
CHHHCCCHHHHHHHH		25.8827282143
372PhosphorylationEERPHSRYLRRAYSS
HHCCCHHHHHHHHCC		13.9427282143
377PhosphorylationSRYLRRAYSSDRSGT
HHHHHHHHCCCCCCC		13.5930576142
378PhosphorylationRYLRRAYSSDRSGTS
HHHHHHHCCCCCCCC		25.4428450419
379PhosphorylationYLRRAYSSDRSGTSN
HHHHHHCCCCCCCCC		25.1128450419
382PhosphorylationRAYSSDRSGTSNSQS
HHHCCCCCCCCCCHH		51.9528102081
384PhosphorylationYSSDRSGTSNSQSQA
HCCCCCCCCCCHHHH		26.4428102081
385PhosphorylationSSDRSGTSNSQSQAK
CCCCCCCCCCHHHHH		37.7028102081
387PhosphorylationDRSGTSNSQSQAKTY
CCCCCCCCHHHHHEE		30.8628102081
392UbiquitinationSNSQSQAKTYTMERC
CCCHHHHHEEEHHHH		34.13-
393UbiquitinationNSQSQAKTYTMERCH
CCHHHHHEEEHHHHC		27.5229967540
394PhosphorylationSQSQAKTYTMERCHS
CHHHHHEEEHHHHCC		11.90-
401PhosphorylationYTMERCHSAEMLSVS
EEHHHHCCCEEEEEE		29.5619369195
402UbiquitinationTMERCHSAEMLSVSK
EHHHHCCCEEEEEEC		5.2029967540
406PhosphorylationCHSAEMLSVSKRSGG
HCCCEEEEEECCCCC		24.0429496963
408PhosphorylationSAEMLSVSKRSGGGE
CCEEEEEECCCCCCC		20.9822210691
411PhosphorylationMLSVSKRSGGGENEE
EEEEECCCCCCCCCC		45.5923186163
420PhosphorylationGGENEERYSPTDNNA
CCCCCCCCCCCCCCC		23.4525850435
421PhosphorylationGENEERYSPTDNNAN
CCCCCCCCCCCCCCC		27.7821712546
423PhosphorylationNEERYSPTDNNANIF
CCCCCCCCCCCCCHH		45.4825850435
434UbiquitinationANIFNFFKEKTSSSS
CCHHHHHHHHCCCCC		54.9129967540
436UbiquitinationIFNFFKEKTSSSSGS
HHHHHHHHCCCCCCC		55.06-
439PhosphorylationFFKEKTSSSSGSFER
HHHHHCCCCCCCCCC		33.48-
471UbiquitinationFPFADPTPQTETVQQ
CCCCCCCCCCHHHHH		44.4729967540
480UbiquitinationTETVQQWFGNLQINA
CHHHHHHHHCCEEHH		3.9529967540
495PhosphorylationHLRKTTEYDSISPNR
EEECCCCCCCCCCCC		16.9527642862
499PhosphorylationTTEYDSISPNRDFQG
CCCCCCCCCCCCCCC		21.7717192257
512UbiquitinationQGHPDLQKDTSKNAW
CCCCCCCCCCCCCCC		70.9829967540
528PhosphorylationDTKVKKNSDASDNAH
CCCCCCCCCCCCCCH		43.3529978859
531PhosphorylationVKKNSDASDNAHSVK
CCCCCCCCCCCHHHH		36.0729978859
536PhosphorylationDASDNAHSVKQQNTM
CCCCCCHHHHHHHHH		28.7120860994
538AcetylationSDNAHSVKQQNTMKY
CCCCHHHHHHHHHHH		49.5420167786
542PhosphorylationHSVKQQNTMKYMTAL
HHHHHHHHHHHHHHH		15.6529978859
547PhosphorylationQNTMKYMTALHSKPE
HHHHHHHHHHHCCCH		23.99-
551PhosphorylationKYMTALHSKPEIIQQ
HHHHHHHCCCHHHHC		51.24-
582PhosphorylationGMEPPWGYQNRTLRS
CCCCCCCCCCCCHHH		9.95-
589PhosphorylationYQNRTLRSITSPLVA
CCCCCHHHCCCHHHH		33.0728985074
591PhosphorylationNRTLRSITSPLVAHR
CCCHHHCCCHHHHHC		26.0720860994
592PhosphorylationRTLRSITSPLVAHRL
CCHHHCCCHHHHHCC		17.9917192257
665PhosphorylationPLADRPPSPTDNISR
CCCCCCCCCCCCCHH		43.0125159151
667PhosphorylationADRPPSPTDNISRYS
CCCCCCCCCCCHHCC		46.1223186163
671PhosphorylationPSPTDNISRYSFDNL
CCCCCCCHHCCCCCC		31.2717192257
712UbiquitinationYFTRYAKCILMENSP
EEEEEEEEEEECCCC		1.8929967540
721UbiquitinationLMENSPGADFEVWFY
EECCCCCCCEEEEEE		23.0029967540
736PhosphorylationDGVKIHKTEDFIQVI
CCEEEEECHHHHHHH		26.9929083192
746PhosphorylationFIQVIEKTGKSYTLK
HHHHHHHHCCCEECC		36.7329083192
749PhosphorylationVIEKTGKSYTLKSES
HHHHHCCCEECCCHH		25.3729083192
750PhosphorylationIEKTGKSYTLKSESE
HHHHCCCEECCCHHH		21.4129083192
751PhosphorylationEKTGKSYTLKSESEV
HHHCCCEECCCHHHH		34.5029083192
753UbiquitinationTGKSYTLKSESEVNS
HCCCEECCCHHHHHH		44.3629967540
809PhosphorylationIIGRKPGSTSSPKAL
EECCCCCCCCCCCCC		33.3724732914
810PhosphorylationIGRKPGSTSSPKALS
ECCCCCCCCCCCCCC		38.8624732914
817PhosphorylationTSSPKALSPPPSVDS
CCCCCCCCCCCCCCC		39.9719369195
821PhosphorylationKALSPPPSVDSNYPT
CCCCCCCCCCCCCCC		44.31-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
22SPhosphorylationKinasePLK4O00444
PSP
170TPhosphorylationKinasePLK4O00444
PSP
177YPhosphorylationKinasePLK4O00444
PSP
305SPhosphorylationKinasePLK4O00444
PSP
-KUbiquitinationE3 ubiquitin ligaseBTRCQ9Y297
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseFBXW11Q9UKB1
PMID:19084407
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLK4_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PLK4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FA46C_HUMANFAM46Cphysical
16189514
MTUS2_HUMANMTUS2physical
16189514
PLK4_HUMANPLK4physical
16189514
FBXW5_HUMANFBXW5physical
21725316
CHD3_HUMANCHD3physical
21900206
FBW1A_HUMANBTRCphysical
20516151
TX1B3_HUMANTAX1BP3physical
21988832
PLK4_HUMANPLK4physical
25416956
CA109_HUMANC1orf109physical
25416956
MIB1_HUMANMIB1physical
25795303
SDCG3_HUMANSDCCAG3physical
24613305
CE152_HUMANCEP152physical
24613305
CEP85_HUMANCEP85physical
24613305
PCNT_HUMANPCNTphysical
24613305
K1671_HUMANKIAA1671physical
24613305
NEDD1_HUMANNEDD1physical
24613305
MAGD1_HUMANMAGED1physical
24613305
TTK_HUMANTTKphysical
24613305
LZTS2_HUMANLZTS2physical
24613305
PLK1_HUMANPLK1physical
24613305
ALMS1_HUMANALMS1physical
24613305
UBP54_HUMANUSP54physical
24613305
STIL_HUMANSTILphysical
24613305
CE128_HUMANCEP128physical
24613305
FA83H_HUMANFAM83Hphysical
24613305
OFD1_HUMANOFD1physical
24613305
CSPP1_HUMANCSPP1physical
24613305
DOCK7_HUMANDOCK7physical
24613305
KIF2A_HUMANKIF2Aphysical
24613305
SPICE_HUMANSPICE1physical
24613305
CE350_HUMANCEP350physical
24613305
MYCB2_HUMANMYCBP2physical
24613305
CP131_HUMANCEP131physical
24613305
CEP63_HUMANCEP63physical
24613305
CK5P2_HUMANCDK5RAP2physical
24613305
FBW1B_HUMANFBXW11physical
24613305
CCD15_HUMANCCDC15physical
24613305
SAS6_HUMANSASS6physical
24613305
CP250_HUMANCEP250physical
24613305
TCPZ_HUMANCCT6Aphysical
26496610
PTSS1_HUMANPTDSS1physical
26496610
ATP9A_HUMANATP9Aphysical
26496610
TCPB_HUMANCCT2physical
26496610
CE152_HUMANCEP152physical
26496610
PLPL8_HUMANPNPLA8physical
26496610
CAB45_HUMANSDF4physical
26496610
RFOX1_HUMANRBFOX1physical
26496610
SYNP2_HUMANSYNPO2physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616171Microcephaly and chorioretinopathy, autosomal recessive, 2 (MCCRP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLK4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377; SER-378; SER-401;TYR-420; SER-421; THR-591; SER-592; SER-665 AND SER-817, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-421; SER-499;SER-592; SER-671 AND SER-817, AND MASS SPECTROMETRY.

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