CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008453
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase Nek2 
Protein Synonyms/Alias
 HSPK 21; Never in mitosis A-related kinase 2; NimA-related protein kinase 2; NimA-like protein kinase 1 
Gene Name
 NEK2 
Gene Synonyms/Alias
 NEK2A; NLK1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
37DGKILVWKELDYGSMubiquitination[1]
63VNLLRELKHPNIVRYubiquitination[1]
143TVLHRDLKPANVFLDubiquitination[1, 2]
152ANVFLDGKQNVKLGDubiquitination[1, 2]
156LDGKQNVKLGDFGLAubiquitination[1, 2]
174NHDTSFAKTFVGTPYubiquitination[1]
227SQKELAGKIREGKFRubiquitination[1]
295RQLGEPEKSQDSSPVubiquitination[1]
309VLSELKLKEIQLQERubiquitination[1]
330REERLEQKEQELCVRubiquitination[1]
344RERLAEDKLARAENLubiquitination[1]
353ARAENLLKNYSLLKEubiquitination[1]
359LKNYSLLKERKFLSLubiquitination[1]
362YSLLKERKFLSLASNubiquitination[1, 3, 4]
381NLPSSVIKKKVHFSGubiquitination[5]
382LPSSVIKKKVHFSGEubiquitination[1]
391VHFSGESKENIMRSEubiquitination[1, 2, 5]
407SESQLTSKSKCKDLKubiquitination[1, 2, 5]
437IEKNYQLKSRQILGMubiquitination[1]
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] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] 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
 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; SGOL1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Isoform 1 phosphorylates and activates NEK11 in G1/S- arrested cells. Isoform 2, which is not present in the nucleolus, does not. 
Sequence Annotation
 DOMAIN 8 271 Protein kinase.
 NP_BIND 14 22 ATP (By similarity).
 REGION 264 445 Interaction with PCNT.
 REGION 306 334 Leucine-zipper.
 REGION 329 445 Necessary for interaction with MAD1L1.
 REGION 333 370 Required for microtubule binding and for
 REGION 403 439 Interaction with SAV1 and STK3/MST2.
 ACT_SITE 141 141 Proton acceptor (By similarity).
 BINDING 37 37 ATP.
 MOD_RES 170 170 Phosphothreonine; by autocatalysis
 MOD_RES 171 171 Phosphoserine; by autocatalysis
 MOD_RES 175 175 Phosphothreonine; by autocatalysis.
 MOD_RES 179 179 Phosphothreonine; by autocatalysis.
 MOD_RES 241 241 Phosphoserine; by autocatalysis.
 MOD_RES 296 296 Phosphoserine.
 MOD_RES 356 356 Phosphoserine; by STK3/MST2.
 MOD_RES 365 365 Phosphoserine; by STK3/MST2.
 MOD_RES 387 387 Phosphoserine.
 MOD_RES 390 390 Phosphoserine.
 MOD_RES 397 397 Phosphoserine.
 MOD_RES 402 402 Phosphoserine.
 MOD_RES 406 406 Phosphoserine; by STK3/MST2.
 MOD_RES 428 428 Phosphoserine.
 MOD_RES 438 438 Phosphoserine; by STK3/MST2.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinase; Kinetochore; Magnesium; Meiosis; Metal-binding; Microtubule; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 445 AA 
Protein Sequence
MPSRAEDYEV LYTIGTGSYG RCQKIRRKSD GKILVWKELD YGSMTEAEKQ MLVSEVNLLR 60
ELKHPNIVRY YDRIIDRTNT TLYIVMEYCE GGDLASVITK GTKERQYLDE EFVLRVMTQL 120
TLALKECHRR SDGGHTVLHR DLKPANVFLD GKQNVKLGDF GLARILNHDT SFAKTFVGTP 180
YYMSPEQMNR MSYNEKSDIW SLGCLLYELC ALMPPFTAFS QKELAGKIRE GKFRRIPYRY 240
SDELNEIITR MLNLKDYHRP SVEEILENPL IADLVADEQR RNLERRGRQL GEPEKSQDSS 300
PVLSELKLKE IQLQERERAL KAREERLEQK EQELCVRERL AEDKLARAEN LLKNYSLLKE 360
RKFLSLASNP ELLNLPSSVI KKKVHFSGES KENIMRSENS ESQLTSKSKC KDLKKRLHAA 420
QLRAQALSDI EKNYQLKSRQ ILGMR 445 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
 GO:0000794; C:condensed nuclear chromosome; IEA:Compara.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
 GO:0001824; P:blastocyst development; IEA:Compara.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0051299; P:centrosome separation; IDA:UniProtKB.
 GO:0007059; P:chromosome segregation; IDA:UniProtKB.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007126; P:meiosis; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0000070; P:mitotic sister chromatid segregation; IEA:Compara.
 GO:0043392; P:negative regulation of DNA binding; IEA:Compara.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
 GO:0046602; P:regulation of mitotic centrosome separation; TAS:UniProtKB.
 GO:0051225; P:spindle assembly; TAS:UniProtKB.
 GO:0090307; P:spindle assembly involved in mitosis; IEA:Compara. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS