CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010766
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-dependent kinase 17 
Protein Synonyms/Alias
 Cell division protein kinase 17; PCTAIRE-motif protein kinase 2; Serine/threonine-protein kinase PCTAIRE-2 
Gene Name
 CDK17 
Gene Synonyms/Alias
 PCTAIRE2; PCTK2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
143ISMEDLNKRLSLPADubiquitination[1]
160IPDGYLEKLQINSPPubiquitination[1, 2]
188LSEIGFGKMETYIKLubiquitination[1]
194GKMETYIKLEKLGEGubiquitination[2]
197ETYIKLEKLGEGTYAubiquitination[2]
208GTYATVYKGRSKLTEubiquitination[1]
212TVYKGRSKLTENLVAubiquitination[1]
221TENLVALKEIRLEHEubiquitination[1, 2]
243IREVSLLKDLKHANIubiquitination[1]
315KVLHRDLKPQNLLINubiquitination[1]
324QNLLINEKGELKLADubiquitination[1]
328INEKGELKLADFGLAubiquitination[1, 2]
423ISSNEEFKNYNFPKYubiquitination[1]
431NYNFPKYKPQPLINHubiquitination[1]
452EGIELITKFLQYESKubiquitination[1, 3]
459KFLQYESKKRVSAEEubiquitination[1]
469VSAEEAMKHVYFRSLubiquitination[1]
493SVSIFSLKEIQLQKDubiquitination[1, 4, 5]
499LKEIQLQKDPGFRNSubiquitination[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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [4] 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]
 [5] 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
Functional Description
 May play a role in terminally differentiated neurons. Has a Ser/Thr-phosphorylating activity for histone H1 (By similarity). 
Sequence Annotation
 DOMAIN 192 473 Protein kinase.
 NP_BIND 198 206 ATP (By similarity).
 ACT_SITE 313 313 Proton acceptor (By similarity).
 BINDING 221 221 ATP (By similarity).
 MOD_RES 9 9 Phosphoserine (By similarity).
 MOD_RES 80 80 Phosphoserine.
 MOD_RES 105 105 Phosphoserine.
 MOD_RES 137 137 Phosphoserine.
 MOD_RES 146 146 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 180 180 Phosphoserine.
 MOD_RES 203 203 Phosphotyrosine (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 523 AA 
Protein Sequence
MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEENSSKDNE PIVKNGRPPT SHSMHSFLHQ 60
YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV 120
QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQINSPPFDQ PMSRRSRRAS 180
LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS 240
LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG 300
LAYCHRRKVL HRDLKPQNLL INEKGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL 360
LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGISSNE 420
EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RVSAEEAMKH VYFRSLGPRI 480
HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGHGKNRRQS MLF 523 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:EC.
 GO:0004672; F:protein kinase activity; TAS:ProtInc. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 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