CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012714
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cyclin-dependent kinase inhibitor 3 
Protein Synonyms/Alias
 CDK2-associated dual-specificity phosphatase; Cyclin-dependent kinase interactor 1; Cyclin-dependent kinase-interacting protein 2; Kinase-associated phosphatase 
Gene Name
 CDKN3 
Gene Synonyms/Alias
 CDI1; CIP2; KAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52LCALPGCKFKDVRRNubiquitination[1]
54ALPGCKFKDVRRNVQubiquitination[1]
86CTRGELSKYRVPNLLubiquitination[1, 2, 3]
135TCLKNYRKTLIHCYGubiquitination[1]
184SGAIQTIKQYNYLHEubiquitination[1, 2, 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] 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]
 [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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 May play a role in cell cycle regulation. Dual specificity phosphatase active toward substrates containing either phosphotyrosine or phosphoserine residues. Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner. 
Sequence Annotation
 REGION 1 34 Interaction with CDK2.
 ACT_SITE 140 140 By similarity.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Complete proteome; Cytoplasm; Disease mutation; Hydrolase; Polymorphism; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 212 AA 
Protein Sequence
MKPPSSIQTS EFDSSDEEPI EDEQTPIHIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV 60
QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC 120
EIMEELTTCL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI 180
QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR 212 
Gene Ontology
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
 GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
 GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:ProtInc.
 GO:0007050; P:cell cycle arrest; IDA:MGI.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
 GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. 
Interpro
 IPR008425; CDK_inhib_3.
 IPR022778; CDKN3.
 IPR000387; Tyr/Dual-sp_Pase. 
Pfam
 PF05706; CDKN3 
SMART
  
PROSITE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2 
PRINTS