NEK2_HUMAN - dbPTM
NEK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEK2_HUMAN
UniProt AC P51955
Protein Name Serine/threonine-protein kinase Nek2
Gene Name NEK2
Organism Homo sapiens (Human).
Sequence Length 445
Subcellular Localization Isoform 1: Nucleus. Nucleus, nucleolus . Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere. STK3/MST2 and SAV1 are requir
Protein Description Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly. [PubMed: 24554434 NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis]
Protein Sequence MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCEGGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPLIADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKERKFLSLASNPELLNLPSSVIKKKVHFSGESKENIMRSENSESQLTSKSKCKDLKKRLHAAQLRAQALSDIEKNYQLKSRQILGMR
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
37UbiquitinationDGKILVWKELDYGSM
CCCEEEEEECCCCCC		40.70-
63UbiquitinationVNLLRELKHPNIVRY
HHHHHHCCCCCHHHH		52.87-
143 (in isoform 1)Ubiquitination-46.5021890473
143UbiquitinationTVLHRDLKPANVFLD
EEECCCCCCCCEEEC		46.5021906983
143 (in isoform 2)Ubiquitination-46.5021906983
143 (in isoform 3)Ubiquitination-46.5021906983
152 (in isoform 1)Ubiquitination-38.0621890473
152UbiquitinationANVFLDGKQNVKLGD
CCEEECCCCCEECCC		38.0621906983
152 (in isoform 3)Ubiquitination-38.0621906983
152 (in isoform 2)Ubiquitination-38.0621906983
156 (in isoform 1)Ubiquitination-55.0621890473
156UbiquitinationLDGKQNVKLGDFGLA
ECCCCCEECCCHHHH		55.0621906983
156 (in isoform 3)Ubiquitination-55.0621906983
156 (in isoform 2)Ubiquitination-55.0621906983
170PhosphorylationARILNHDTSFAKTFV
HHHHCCCCCCCCCCC		20.4218691976
171PhosphorylationRILNHDTSFAKTFVG
HHHCCCCCCCCCCCC		29.3017197699
174UbiquitinationNHDTSFAKTFVGTPY
CCCCCCCCCCCCCCC		40.25-
175PhosphorylationHDTSFAKTFVGTPYY
CCCCCCCCCCCCCCC		21.8117197699
179PhosphorylationFAKTFVGTPYYMSPE
CCCCCCCCCCCCCHH		11.6517197699
181PhosphorylationKTFVGTPYYMSPEQM
CCCCCCCCCCCHHHH		16.1921945579
182PhosphorylationTFVGTPYYMSPEQMN
CCCCCCCCCCHHHHH		7.7221945579
184PhosphorylationVGTPYYMSPEQMNRM
CCCCCCCCHHHHHCC		14.7921945579
227UbiquitinationSQKELAGKIREGKFR
CHHHHCHHHCCCCCC		32.74-
241PhosphorylationRRIPYRYSDELNEII
CCCCCCCCHHHHHHH		18.6617197699
261PhosphorylationLKDYHRPSVEEILEN
CCCCCCCCHHHHHHC		41.9624719451
295UbiquitinationRQLGEPEKSQDSSPV
HHCCCCCCCCCCCHH		65.22-
296PhosphorylationQLGEPEKSQDSSPVL
HCCCCCCCCCCCHHH		37.2425159151
299PhosphorylationEPEKSQDSSPVLSEL
CCCCCCCCCHHHHHH		28.9818691976
300PhosphorylationPEKSQDSSPVLSELK
CCCCCCCCHHHHHHH		27.5825159151
304PhosphorylationQDSSPVLSELKLKEI
CCCCHHHHHHHHHHH		40.9129396449
307UbiquitinationSPVLSELKLKEIQLQ
CHHHHHHHHHHHHHH		54.16-
309UbiquitinationVLSELKLKEIQLQER
HHHHHHHHHHHHHHH		51.70-
330UbiquitinationREERLEQKEQELCVR
HHHHHHHHHHHHHHH		52.57-
344UbiquitinationRERLAEDKLARAENL
HHHHHHHHHHHHHHH		35.24-
353UbiquitinationARAENLLKNYSLLKE
HHHHHHHHHHHHHHH		57.94-
355PhosphorylationAENLLKNYSLLKERK
HHHHHHHHHHHHHHC		10.1024719451
356PhosphorylationENLLKNYSLLKERKF
HHHHHHHHHHHHHCH		36.3021076410
359UbiquitinationLKNYSLLKERKFLSL
HHHHHHHHHHCHHHH		61.85-
362 (in isoform 1)Ubiquitination-52.3121890473
362UbiquitinationYSLLKERKFLSLASN
HHHHHHHCHHHHCCC		52.3121890473
362UbiquitinationYSLLKERKFLSLASN
HHHHHHHCHHHHCCC		52.3121890473
365 (in isoform 2)Phosphorylation-25.64-
365 (in isoform 4)Phosphorylation-25.6424260401
365PhosphorylationLKERKFLSLASNPEL
HHHHCHHHHCCCHHH		25.6421076410
368PhosphorylationRKFLSLASNPELLNL
HCHHHHCCCHHHHCC		59.2024719451
368 (in isoform 2)Phosphorylation-59.20-
377PhosphorylationPELLNLPSSVIKKKV
HHHHCCCHHHHHCCC		40.1628122231
378PhosphorylationELLNLPSSVIKKKVH
HHHCCCHHHHHCCCC		26.3921857030
380 (in isoform 2)Phosphorylation-6.1428348404
381UbiquitinationNLPSSVIKKKVHFSG
CCCHHHHHCCCCCCC		44.37-
382UbiquitinationLPSSVIKKKVHFSGE
CCHHHHHCCCCCCCC		49.24-
383UbiquitinationPSSVIKKKVHFSGES
CHHHHHCCCCCCCCC		35.62-
387PhosphorylationIKKKVHFSGESKENI
HHCCCCCCCCCHHHH		27.1217197699
390PhosphorylationKVHFSGESKENIMRS
CCCCCCCCHHHHHCC		49.1217197699
391 (in isoform 1)Ubiquitination-50.9421890473
391UbiquitinationVHFSGESKENIMRSE
CCCCCCCHHHHHCCC		50.942190698
397PhosphorylationSKENIMRSENSESQL
CHHHHHCCCCCHHHH		24.6117197699
400PhosphorylationNIMRSENSESQLTSK
HHHCCCCCHHHHCCH		34.2823532336
402PhosphorylationMRSENSESQLTSKSK
HCCCCCHHHHCCHHH		30.2517197699
405PhosphorylationENSESQLTSKSKCKD
CCCHHHHCCHHHHHH		26.8627251275
406PhosphorylationNSESQLTSKSKCKDL
CCHHHHCCHHHHHHH		43.4521076410
407 (in isoform 1)Ubiquitination-49.0121890473
407UbiquitinationSESQLTSKSKCKDLK
CHHHHCCHHHHHHHH		49.01-
408PhosphorylationESQLTSKSKCKDLKK
HHHHCCHHHHHHHHH		42.9523532336
428PhosphorylationQLRAQALSDIEKNYQ
HHHHHHHHHHHHHHH		39.2917197699
432UbiquitinationQALSDIEKNYQLKSR
HHHHHHHHHHHCHHH		62.38-
437UbiquitinationIEKNYQLKSRQILGM
HHHHHHCHHHHHHCC		28.24-
437AcetylationIEKNYQLKSRQILGM
HHHHHHCHHHHHHCC		28.2419816813
438PhosphorylationEKNYQLKSRQILGMR
HHHHHCHHHHHHCCC		37.7021076410
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
170TPhosphorylationKinaseNEK2P51955
PSP
171SPhosphorylationKinaseNEK2P51955
PSP
175TPhosphorylationKinaseNEK2P51955
PSP
179TPhosphorylationKinaseNEK2P51955
PSP
241SPhosphorylationKinaseNEK2P51955
PSP
356SPhosphorylationKinaseNEK2P51955
PSP
356SPhosphorylationKinaseSTK3Q13188
GPS
365SPhosphorylationKinaseSTK3Q13188
GPS
397SPhosphorylationKinaseNEK2P51955
PSP
402SPhosphorylationKinaseNEK2P51955
PSP
406SPhosphorylationKinaseSTK3Q13188
GPS
428SPhosphorylationKinaseNEK2P51955
PSP
438SPhosphorylationKinaseSTK3Q13188
GPS
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:26387737
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:26387737
-KUbiquitinationE3 ubiquitin ligaseCDC20Q12834
PMID:16648845
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEK2_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 NEK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEK2_HUMANNEK2physical
10347187
CP250_HUMANCEP250physical
9647649
CLC4C_HUMANCLEC4Cphysical
12386167
NDC80_HUMANNDC80physical
12386167
MYOME_HUMANPDE4DIPphysical
21900206
TCF25_HUMANTCF25physical
21900206
MIC60_HUMANIMMTphysical
21900206
TPM3_HUMANTPM3physical
21900206
IF4A2_HUMANEIF4A2physical
21900206
CRCM_HUMANMCCphysical
21900206
NDC80_HUMANNDC80physical
21900206
IF140_HUMANIFT140physical
21900206
GIT1_HUMANGIT1physical
21900206
CC85A_HUMANCCDC85Aphysical
21900206
EDRF1_HUMANEDRF1physical
21900206
SPTN4_HUMANSPTBN4physical
21900206
CMGA_HUMANCHGAphysical
21900206
DCTN1_HUMANDCTN1physical
21900206
CASB_HUMANCSN2physical
15147269
CTNB1_HUMANCTNNB1physical
24501426
NEK2_HUMANNEK2physical
23288039
PP1G_HUMANPPP1CCphysical
24902662
CDC27_HUMANCDC27physical
25673878
CDC20_HUMANCDC20physical
25673878
MD2L1_HUMANMAD2L1physical
25673878
APC4_HUMANANAPC4physical
25673878
FZR1_HUMANFZR1physical
25673878
DTD1_HUMANDTD1physical
28514442
DPP9_HUMANDPP9physical
28514442
FANCA_HUMANFANCAphysical
23806870
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615565Retinitis pigmentosa 67 (RP67)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEK2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Structure and regulation of the human Nek2 centrosomal kinase.";
Rellos P., Ivins F.J., Baxter J.E., Pike A., Nott T.J.,Parkinson D.M., Das S., Howell S., Fedorov O., Shen Q.Y., Fry A.M.,Knapp S., Smerdon S.J.;
J. Biol. Chem. 282:6833-6842(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-271 IN COMPLEX WITHINHIBITOR SU11652, PHOSPHORYLATION AT THR-170; SER-171; THR-175;THR-179; SER-241; SER-356; SER-387; SER-390; SER-397; SER-402 ANDSER-428, MUTAGENESIS OF LYS-37; ASP-141; THR-170; SER-171; THR-175;THR-179 AND SER-241, AND MASS SPECTROMETRY.
"Components of the Hippo pathway cooperate with Nek2 kinase toregulate centrosome disjunction.";
Mardin B.R., Lange C., Baxter J.E., Hardy T., Scholz S.R., Fry A.M.,Schiebel E.;
Nat. Cell Biol. 12:1166-1176(2010).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK3/MST2 AND SAV1,AND PHOSPHORYLATION AT SER-356; SER-365; SER-406 AND SER-438.
"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 SER-296; SER-299 ANDSER-300, AND MASS SPECTROMETRY.
"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-184; SER-296 ANDSER-300, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASSSPECTROMETRY.

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