CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016155
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase Nek8 
Protein Synonyms/Alias
 Never in mitosis A-related kinase 8; NimA-related protein kinase 8; Nima-related protein kinase 12a 
Gene Name
 NEK8 
Gene Synonyms/Alias
 JCK; NEK12A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
152IGDFGISKILSSKSKubiquitination[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
Functional Description
 Required for renal tubular integrity. May regulate local cytoskeletal structure in kidney tubule epithelial cells. May regulate ciliary biogenesis through targeting of proteins to the cilia (By similarity). 
Sequence Annotation
 DOMAIN 4 258 Protein kinase.
 REPEAT 312 350 RCC1 1.
 REPEAT 410 461 RCC1 2.
 REPEAT 462 513 RCC1 3.
 REPEAT 580 631 RCC1 4.
 REPEAT 632 684 RCC1 5.
 NP_BIND 10 18 ATP (By similarity).
 ACT_SITE 128 128 Proton acceptor (By similarity).
 BINDING 33 33 ATP (By similarity).
 MOD_RES 162 162 Phosphothreonine; by autocatalysis (By  
Keyword
 ATP-binding; Cell projection; Ciliopathy; Cilium; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Kinase; Magnesium; Metal-binding; Nephronophthisis; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MEKYERIRVV GRGAFGIVHL CLRKADQKLV IIKQIPVEQM TKEERQAAQN ECQVLKLLNH 60
PNVIEYYENF LEDKALMIAM EYAPGGTLAE FIQKRCNSLL EEETILHFFV QILLALHHVH 120
THLILHRDLK TQNILLDKHR MVVKIGDFGI SKILSSKSKA YTVVGTPCYI SPELCEGKPY 180
NQKSDIWALG CVLYELASLK RAFEAANLPA LVLKIMSGTF APISDRYSPE LRQLVLSLLS 240
LEPAQRPPLS HIMAQPLCIR ALLNLHTDVG SVRMRRAEKS VAPSNTGSRT TSVRCRGIPR 300
GPVRPAIPPP LSSVYAWGGG LGTPLRLPML NTEVVQVAAG RTQKAGVTRS GRLILWEAPP 360
LGAGGGSLLP GAVEQPQPQF ISRFLEGQSG VTIKHVACGD FFTACLTDRG IIMTFGSGSN 420
GCLGHGSLTD ISQPTIVEAL LGYEMVQVAC GASHVLALST ERELFAWGRG DSGRLGLGTR 480
ESHSCPQQVP MPPGQEAQRV VCGIDSSMIL TVPGQALACG SNRFNKLGLD HLSLGEEPVP 540
HQQVEEALSF TLLGSAPLDQ EPLLSIDLGT AHSAAVTASG DCYTFGSNQH GQLGTNTRRG 600
SRAPCKVQGL EGIKMAMVAC GDAFTVAIGA ESEVYSWGKG ARGRLGRRDE DAGLPRPVQL 660
DETHPYTVTS VSCCHGNTLL AVRSVTDEPV PP 692 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0072372; C:primary cilium; ISS:UniProtKB.
 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; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 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
 PR00633; RCCNDNSATION.