CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001286
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-K 
Protein Synonyms/Alias
  
Gene Name
 CCNK 
Gene Synonyms/Alias
 CPR4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
166HPYQFLLKYAKQLKGubiquitination[1, 2, 3]
Reference
 [1] 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]
 [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] 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 transcriptional regulation. In vitro, is associated with a kinase activity toward both RNA polymerase II C-terminal domain and CDK2 (CAK). 
Sequence Annotation
 MOD_RES 324 324 Phosphoserine.
 MOD_RES 328 328 Phosphoserine (By similarity).
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 340 340 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cyclin; Mitosis; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 580 AA 
Protein Sequence
MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR REGARFIFDV 60
GTRLGLHYDT LATGIIYFHR FYMFHSFKQF PRYVTGACCL FLAGKVEETP KKCKDIIKTA 120
RSLLNDVQFG QFGDDPKEEV MVLERILLQT IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK 180
LVQMAWTFVN DSLCTTLSLQ WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ 240
DVPVDVLEDI CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQVQQ SQPSQSSEPS 300
QPQQKDPQQP AQQQQPAQQP KKPSPQPSSP RQVKRAVVVS PKEENKAAEP PPPKIPKIET 360
THPPLPPAHP PPDRKPPLAA ALGEAEPPGP VDATDLPKVQ IPPPAHPAPV HQPPPLPHRP 420
PPPPPSSYMT GMSTTSSYMS GEGYQSLQSM MKTEGPSYGA LPPAYGPPAH LPYHPHVYPP 480
NPPPPPVPPP PASFPPPAIP PPTPGYPPPP PTYNPNFPPP PPRLPPTHAV PPHPPPGLGL 540
PPASYPPPAV PPGGQPPVPP PIPPPGMPPV GGLGRAAWMR 580 
Gene Ontology
 GO:0002944; C:cyclin K-CDK12 complex; IPI:MGI.
 GO:0002945; C:cyclin K-CDK13 complex; IPI:MGI.
 GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:MGI.
 GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:MGI.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0071157; P:negative regulation of cell cycle arrest; IGI:MGI.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006974; P:response to DNA damage stimulus; IMP:MGI.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR013763; Cyclin-like.
 IPR015429; Cyclin_C/H/T/L.
 IPR006671; Cyclin_N. 
Pfam
 PF00134; Cyclin_N 
SMART
 SM00385; CYCLIN 
PROSITE
 PS00292; CYCLINS 
PRINTS