CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005862
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 M-phase inducer phosphatase 3 
Protein Synonyms/Alias
 Dual specificity phosphatase Cdc25C 
Gene Name
 CDC25C 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52VPRTPVGKFLGDSANubiquitination[1]
251KYFSGQGKLRKGLCLubiquitination[1]
260RKGLCLKKTVSLCDIubiquitination[1]
298ALPTVSGKHQDLKYVubiquitination[1]
317VAALLSGKFQGLIEKubiquitination[1]
360LFNFFLKKPIVPLDTubiquitination[1]
413YPELYILKGGYRDFFubiquitination[1, 2]
469EQIALLVKDMSP***ubiquitination[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] 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
Functional Description
 Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity. 
Sequence Annotation
 DOMAIN 321 428 Rhodanese.
 REGION 334 379 HIV-1 Vpr binding site.
 ACT_SITE 377 377 By similarity.
 MOD_RES 38 38 Phosphoserine.
 MOD_RES 48 48 Phosphothreonine.
 MOD_RES 57 57 Phosphoserine.
 MOD_RES 61 61 Phosphoserine.
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 67 67 Phosphothreonine.
 MOD_RES 122 122 Phosphoserine; by CDK1 (Probable).
 MOD_RES 129 129 Phosphoserine.
 MOD_RES 130 130 Phosphothreonine; by CDK1 (Probable).
 MOD_RES 168 168 Phosphoserine.
 MOD_RES 191 191 Phosphoserine; by PLK3.
 MOD_RES 198 198 Phosphoserine; by PLK3.
 MOD_RES 214 214 Phosphoserine; by CDK1 (Probable).
 MOD_RES 216 216 Phosphoserine; by CHEK1, CHEK2, BRSK1 and
 MOD_RES 472 472 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Host-virus interaction; Hydrolase; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 473 AA 
Protein Sequence
MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 60
SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK 120
CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP 180
NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK 240
VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 300
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK 360
PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF 420
PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP 473 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004725; F:protein tyrosine phosphatase activity; NAS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:UniProtKB.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; IGI:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB.
 GO:0007088; P:regulation of mitosis; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR000751; MPI_Phosphatase.
 IPR001763; Rhodanese-like_dom. 
Pfam
 PF06617; M-inducer_phosp
 PF00581; Rhodanese 
SMART
 SM00450; RHOD 
PROSITE
 PS50206; RHODANESE_3 
PRINTS
 PR00716; MPIPHPHTASE.