CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005858
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 M-phase inducer phosphatase 1 
Protein Synonyms/Alias
 Dual specificity phosphatase Cdc25A 
Gene Name
 CDC25A 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
66YEQPLEVKNNSNLQRubiquitination[1]
120LGCSPALKRSHSDSLubiquitination[2]
169SHGLQEGKDLFTQRQubiquitination[2]
257TNLDNRCKLFDSPSLubiquitination[2]
300SMSGASPKESTNPEKubiquitination[2]
343DLIGDFSKGYLFHTVubiquitination[1, 2, 3, 4]
353LFHTVAGKHQDLKYIubiquitination[2]
358AGKHQDLKYISPEIMubiquitination[2]
372MASVLNGKFANLIKEubiquitination[2]
378GKFANLIKEFVIIDCubiquitination[2]
415VEDFLLKKPIVPTDGubiquitination[2]
423PIVPTDGKRVIVVFHubiquitination[1]
471YVLKGGYKEFFMKCQubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro. 
Sequence Annotation
 DOMAIN 376 482 Rhodanese.
 MOTIF 74 84 Phosphodegron.
 MOTIF 141 143 KEN box.
 ACT_SITE 431 431
 MOD_RES 76 76 Phosphoserine; by CHEK1.
 MOD_RES 79 79 Phosphoserine; by NEK11.
 MOD_RES 82 82 Phosphoserine; by NEK11.
 MOD_RES 88 88 Phosphoserine; by NEK11.
 MOD_RES 124 124 Phosphoserine; by CHEK1 and CHEK2.
 MOD_RES 178 178 Phosphoserine; by CHEK1.
 MOD_RES 279 279 Phosphoserine; by CHEK1 and CHEK2.
 MOD_RES 293 293 Phosphoserine; by CHEK1 and CHEK2.
 MOD_RES 507 507 Phosphothreonine; by CHEK1.
 MOD_RES 513 513 Phosphoserine; by PLK3.
 MOD_RES 519 519 Phosphoserine; by PLK3.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Hydrolase; Mitosis; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 524 AA 
Protein Sequence
MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD QLQGLGSDYE 60
QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN PMRRIHSLPQ KLLGCSPALK 120
RSHSDSLDHD IFQLIDPDEN KENEAFEFKK PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP 180
ARMLSSNERD SSEPGNFIPL FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL 240
WTAPLVMRTT NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK 300
ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV AGKHQDLKYI 360
SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV NLHMEEEVED FLLKKPIVPT 420
DGKRVIVVFH CEFSSERGPR MCRYVRERDR LGNEYPKLHY PELYVLKGGY KEFFMKCQSY 480
CEPPSYRPMH HEDFKEDLKK FRTKSRTWAG EKSKREMYSR LKKL 524 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; TAS:UniProtKB.
 GO:0034644; P:cellular response to UV; IDA:UniProtKB.
 GO:0006260; P:DNA replication; TAS:Reactome.
 GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:UniProtKB. 
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.