CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018015
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase Nek9 
Protein Synonyms/Alias
 Nercc1 kinase; Never in mitosis A-related kinase 9; NimA-related protein kinase 9; NimA-related kinase 8; Nek8 
Gene Name
 NEK9 
Gene Synonyms/Alias
 KIAA1995; NEK8; NERCC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
81DDSLVVWKEVDLTRLubiquitination[1]
186TLNIFLTKANLIKLGubiquitination[2]
199LGDYGLAKKLNSEYSubiquitination[2]
327TLLNAPTKRPRSSTVubiquitination[3, 4]
499VVVLTRNKEVYSWGCubiquitination[1, 5]
525EDYYTPQKVDVPKALubiquitination[1, 2, 5, 6]
606IRTIAPGKTHTAAIDubiquitination[1, 5]
625LLTFGCNKCGQLGVGubiquitination[1]
650LGGPLGGKQVIRVSCubiquitination[1, 5, 6]
731VEKVLNSKTIRSNSSacetylation[7]
731VEKVLNSKTIRSNSSubiquitination[1]
929QIFTQLQKLNKKLEGubiquitination[3, 4]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] 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]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively. 
Sequence Annotation
 DOMAIN 52 308 Protein kinase.
 REPEAT 388 444 RCC1 1.
 REPEAT 445 498 RCC1 2.
 REPEAT 499 550 RCC1 3.
 REPEAT 551 615 RCC1 4.
 REPEAT 616 668 RCC1 5.
 REPEAT 669 726 RCC1 6.
 NP_BIND 58 66 ATP (By similarity).
 REGION 732 891 Interaction with NEK6.
 ACT_SITE 176 176 Proton acceptor (By similarity).
 BINDING 81 81 ATP.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 52 52 Phosphotyrosine.
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 210 210 Phosphothreonine; by autocatalysis
 MOD_RES 254 254 Phosphothreonine.
 MOD_RES 333 333 Phosphothreonine.
 MOD_RES 741 741 Phosphoserine.
 MOD_RES 801 801 Phosphoserine.
 MOD_RES 832 832 Phosphoserine.
 MOD_RES 886 886 Phosphothreonine.
 MOD_RES 944 944 Phosphoserine.
 MOD_RES 978 978 Phosphoserine.  
Keyword
 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Kinase; Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 979 AA 
Protein Sequence
MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL HYIPIRVLGR 60
GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD 120
NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL 180
NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV 240
IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD 300
ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ 360
KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV 420
EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN 480
PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG 540
CDGTFLLTQS GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR 600
TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK QVIRVSCGDE 660
FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP RPIFGSLHHV PDLSCRGWHT 720
ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS PGGGGGGGGG EEEDSQQESE TPDPSGGFRG 780
TMEADRGMEG LISPTEAMGN SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK 840
DTLPYEELQG LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE 900
RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA KEEMEMDPKP 960
DLDSDSWCLL GTDSCRPSL 979 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; 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; EXP:Reactome.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR009091; RCC1/BLIP-II.
 IPR000408; Reg_chr_condens.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase
 PF00415; RCC1 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00625; RCC1_1
 PS00626; RCC1_2
 PS50012; RCC1_3 
PRINTS