CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005859
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 M-phase inducer phosphatase 2 
Protein Synonyms/Alias
 Dual specificity phosphatase Cdc25B 
Gene Name
 CDC25B 
Gene Synonyms/Alias
 CDC25HU2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
71GLGSETPKSQVGTLLubiquitination[1]
177QAPDGRRKSEAGSGAubiquitination[1]
204FVFKMPWKPTHPSSTubiquitination[1]
242MCLSPDRKMEVEELSubiquitination[1, 2]
299LISAPLVKTLEKEEEubiquitination[3]
303PLVKTLEKEEEKDLVubiquitination[1, 2]
307TLEKEEEKDLVMYSKubiquitination[2]
334SVIRPILKRLERPQDubiquitination[1]
349RDTPVQNKRRRSVTPubiquitination[1]
374KARVLRSKSLCHDEIubiquitination[1]
398ELIGDYSKAFLLQTVubiquitination[2, 3, 4]
408LLQTVDGKHQDLKYIubiquitination[1, 2]
434KFSNIVDKFVIVDCRubiquitination[1, 2]
452EYEGGHIKTAVNLPLubiquitination[1, 2]
469DAESFLLKSPIAPCSubiquitination[1]
479IAPCSLDKRVILIFHubiquitination[1]
523YPEMYILKGGYKEFFubiquitination[2]
527YILKGGYKEFFPQHPubiquitination[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] 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]
 [4] 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
 Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity. 
Sequence Annotation
 DOMAIN 431 538 Rhodanese.
 ACT_SITE 487 487
 MOD_RES 169 169 Phosphoserine; by MELK.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 323 323 Phosphoserine; by MELK and MAPK14.
 MOD_RES 353 353 Phosphoserine; by AURKA.
 MOD_RES 375 375 Phosphoserine; by BRSK1 and MAPK14.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 580 AA 
Protein Sequence
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH 60
DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD 120
PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPVRLLGHS PVLRNITNSQ APDGRRKSEA 180
GSGAASSSGE DKENDGFVFK MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD 240
RKMEVEELSP LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT 300
LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR RRSVTPPEEQ 360
QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF LLQTVDGKHQ DLKYISPETM 420
VALLTGKFSN IVDKFVIVDC RYPYEYEGGH IKTAVNLPLE RDAESFLLKS PIAPCSLDKR 480
VILIFHCEFS SERGPRMCRF IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ 540
DYRPMNHEAF KDELKTFRLK TRSWAGERSR RELCSRLQDQ 580 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0000922; C:spindle pole; IDA:UniProtKB.
 GO:0004725; F:protein tyrosine phosphatase activity; TAS:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007144; P:female meiosis I; IEA:Compara.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:UniProtKB.
 GO:0007067; P:mitosis; TAS:ProtInc.
 GO:0001556; P:oocyte maturation; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
 GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
 GO:0045860; P:positive regulation of protein kinase activity; IEA:Compara.
 GO:0006468; P:protein phosphorylation; IDA: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.