PLK2_HUMAN - dbPTM
PLK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLK2_HUMAN
UniProt AC Q9NYY3
Protein Name Serine/threonine-protein kinase PLK2
Gene Name PLK2
Organism Homo sapiens (Human).
Sequence Length 685
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Cell projection, dendrite. Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and
Protein 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..
Protein Sequence MELLRTITYQPAASTKMCEQALGKGCGADSKKKRPPQPPEESQPPQSQAQVPPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYIDTHNRVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPTTTVARSGTPAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICSQNEEYLLTYINEDRISTTFRLTTLLMSGCSSELKNRMEYALNMLLQRCN
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
6Phosphorylation--MELLRTITYQPAA
--CCCEEEEECCCCC		20.0324719451
8PhosphorylationMELLRTITYQPAAST
CCCEEEEECCCCCCH		18.5824719451
24UbiquitinationMCEQALGKGCGADSK
HHHHHHCCCCCCCCC		52.45-
26S-nitrosylationEQALGKGCGADSKKK
HHHHCCCCCCCCCCC		4.6519483679
26S-nitrosocysteineEQALGKGCGADSKKK
HHHHCCCCCCCCCCC		4.65-
80UbiquitinationIVDPTTGKRYCRGKV
EECCCCCCCCCCCEE		37.79-
90UbiquitinationCRGKVLGKGGFAKCY
CCCEEECCCCCCCEE		52.26-
95UbiquitinationLGKGGFAKCYEMTDL
ECCCCCCCEEEEECC		34.78-
100PhosphorylationFAKCYEMTDLTNNKV
CCCEEEEECCCCCEE		18.86-
106UbiquitinationMTDLTNNKVYAAKII
EECCCCCEEEEEEEC		38.40-
108PhosphorylationDLTNNKVYAAKIIPH
CCCCCEEEEEEECCC		11.49-
129UbiquitinationHQREKIDKEIELHRI
HHHHHHHHHHHHHHH		65.15-
156PhosphorylationFEDKENIYILLEYCS
ECCCCCEEHHHHHHC		9.3329978859
161PhosphorylationNIYILLEYCSRRSMA
CEEHHHHHHCHHHHH		8.8329978859
163PhosphorylationYILLEYCSRRSMAHI
EHHHHHHCHHHHHHH		29.8129978859
184PhosphorylationLTEPEVRYYLRQIVS
CCCHHHHHHHHHHHH		16.4218083107
185PhosphorylationTEPEVRYYLRQIVSG
CCHHHHHHHHHHHHH		5.7122817900
194UbiquitinationRQIVSGLKYLHEQEI
HHHHHHHHHHHHHHH		49.65-
207UbiquitinationEILHRDLKLGNFFIN
HHHCCCHHHHCHHHH		59.6521906983
239PhosphorylationPLEHRRRTICGTPNY
CCHHHCCCCCCCCCC		20.8628348404
243PhosphorylationRRRTICGTPNYLSPE
HCCCCCCCCCCCCHH		12.1625954137
246PhosphorylationTICGTPNYLSPEVLN
CCCCCCCCCCHHHHH		15.1221945579
271PhosphorylationWALGCVMYTMLLGRP
HHHHHHHHHHHHCCC		2.91-
297PhosphorylationRCIREARYTMPSSLL
HHHHHHHCCCCHHHH		17.9029978859
298PhosphorylationCIREARYTMPSSLLA
HHHHHHCCCCHHHHH		19.6329978859
301PhosphorylationEARYTMPSSLLAPAK
HHHCCCCHHHHHHHH		23.8524719451
302PhosphorylationARYTMPSSLLAPAKH
HHCCCCHHHHHHHHH		22.8724719451
313PhosphorylationPAKHLIASMLSKNPE
HHHHHHHHHHCCCCC		17.1729978859
316PhosphorylationHLIASMLSKNPEDRP
HHHHHHHCCCCCCCC		23.0322210691
317UbiquitinationLIASMLSKNPEDRPS
HHHHHHCCCCCCCCC		72.9821906983
358PhosphorylationVPDFHLSSPAKNFFK
CCCCCCCCHHHHHHH		34.9325627689
366MethylationPAKNFFKKAAAALFG
HHHHHHHHHHHHHHC		37.79-
366UbiquitinationPAKNFFKKAAAALFG
HHHHHHHHHHHHHHC		37.79-
375UbiquitinationAAALFGGKKDKARYI
HHHHHCCCCCCCCEE		59.1721906983
376UbiquitinationAALFGGKKDKARYID
HHHHCCCCCCCCEEC		68.67-
378UbiquitinationLFGGKKDKARYIDTH
HHCCCCCCCCEECCC		43.58-
390UbiquitinationDTHNRVSKEDEDIYK
CCCCCCCCCHHHHHH		67.3421906983
396PhosphorylationSKEDEDIYKLRHDLK
CCCHHHHHHHHHHHH		19.1128674419
397UbiquitinationKEDEDIYKLRHDLKK
CCHHHHHHHHHHHHH		39.10-
404UbiquitinationKLRHDLKKTSITQQP
HHHHHHHHCCCCCCC		55.60-
412PhosphorylationTSITQQPSKHRTDEE
CCCCCCCCCCCCCCC		36.4328348404
413UbiquitinationSITQQPSKHRTDEEL
CCCCCCCCCCCCCCC		43.73-
438UbiquitinationGTPAVENKQQIGDAI
CCCCCCCHHHHHHHH		30.0321906983
457PhosphorylationRGTLGSCSSSSECLE
HCCCCCCCCCHHHHC		34.6522210691
460PhosphorylationLGSCSSSSECLEDST
CCCCCCCHHHHCCCC		33.9928985074
470PhosphorylationLEDSTMGSVADTVAR
HCCCCHHHHHHHHHH		11.8722210691
574PhosphorylationSQVTVLKYFSHYMEE
HHHHHHHHHHHHHHH		13.2229083192
576PhosphorylationVTVLKYFSHYMEENL
HHHHHHHHHHHHHHC		15.6029083192
578PhosphorylationVLKYFSHYMEENLMD
HHHHHHHHHHHHCCC		12.6729083192
591PhosphorylationMDGGDLPSVTDIRRP
CCCCCCCCHHCCCCH		44.9724719451
593PhosphorylationGGDLPSVTDIRRPRL
CCCCCCHHCCCCHHH		30.0024719451
670UbiquitinationSGCSSELKNRMEYAL
CCCCHHHHHHHHHHH		38.16-
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
-KUbiquitinationE3 ubiquitin ligaseVPS18Q9P253
PMID:16203730
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
239TPhosphorylation

-
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 PLK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CIB1_HUMANCIB1physical
12651910
SYUA_HUMANSNCAphysical
19889641
A4_HUMANAPPphysical
21832049
SYUA_HUMANSNCAphysical
22988096
CENPU_HUMANCENPUphysical
19597481
CD20B_HUMANCDC20Bphysical
25416956
KLK7_HUMANKLK7physical
26186194
CATL2_HUMANCTSVphysical
26186194
RNAS7_HUMANRNASE7physical
26186194
POF1B_HUMANPOF1Bphysical
26186194
IF2P_HUMANEIF5Bphysical
26186194
SUGP1_HUMANSUGP1physical
26186194
TAF8_HUMANTAF8physical
26186194
CCD12_HUMANCCDC12physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
RABL6_HUMANRABL6physical
26186194
ANR44_HUMANANKRD44physical
26186194
ANR28_HUMANANKRD28physical
26186194
PAK2_HUMANPAK2physical
26186194
SPA12_HUMANSERPINA12physical
26186194
SAR1B_HUMANSAR1Bphysical
26186194
CBPA4_HUMANCPA4physical
26186194
CSTF1_HUMANCSTF1physical
26186194
DR9C7_HUMANSDR9C7physical
26186194
A1AT_HUMANSERPINA1physical
26186194
SPB7_HUMANSERPINB7physical
26186194
CATZ_HUMANCTSZphysical
26496610
ITPR1_HUMANITPR1physical
26496610
FXR1_HUMANFXR1physical
26496610
TR150_HUMANTHRAP3physical
26496610
MFN1_HUMANMFN1physical
26496610
FGD6_HUMANFGD6physical
26496610
LENG1_HUMANLENG1physical
26496610
PCGF5_HUMANPCGF5physical
26496610
RT4I1_HUMANRTN4IP1physical
26496610
TDIF1_HUMANDNTTIP1physical
26496610
IRGQ_HUMANIRGQphysical
26496610
MY18A_HUMANMYO18Aphysical
26496610
CA226_HUMANC1orf226physical
26496610
ANR44_HUMANANKRD44physical
28514442
SUGP1_HUMANSUGP1physical
28514442
SPB7_HUMANSERPINB7physical
28514442
A1AT_HUMANSERPINA1physical
28514442
RABL6_HUMANRABL6physical
28514442
DR9C7_HUMANSDR9C7physical
28514442
HEM2_HUMANALADphysical
28514442
RNAS7_HUMANRNASE7physical
28514442
CBPA4_HUMANCPA4physical
28514442
CATL2_HUMANCTSVphysical
28514442
TAF8_HUMANTAF8physical
28514442
PAK2_HUMANPAK2physical
28514442
SPA12_HUMANSERPINA12physical
28514442
ANR28_HUMANANKRD28physical
28514442
POF1B_HUMANPOF1Bphysical
28514442
FBXW7_HUMANFBXW7physical
27423313
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLK2_HUMAN

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