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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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CDC25B

Gene Name CDC25B (QuickGO)
Structure of phosphatase catalytic domain

PDB ID: 1QB0
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SynonymsCDC25B CDC25HU2
Protein NameM-phase inducer phosphatase 2
Alternative Name(s)
M-phase inducer phosphatase 2 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25B)
Ensembl Gene IDENSG00000101224
EntrezGene ID994
UniProt AC (Human)P30305 (protein sequence)
Enzyme ClassEC 3.1.3.48 (BRENDA )
Molecular Weight64987
Protein Length580
Phosphatase activityactive
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Structure-based FamilyFamily 3 (CATH: 3.40.250.10)Historical ClassPTPs >> Class III Cys-based PTPs (CDC25s)
Localization cytoplasm; cytoskeleton; cytosol; nucleus (PubMed: 10822367, 15456846, 1828290, 15311285 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesChEMBL
Gene ExpressionGene Expression Atlas

The Human Protein Atlas

Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. The three isoforms seem to have a different level of activity.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
Protein Sequence
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS PVTTLTQTMH DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS SESSESSDAG LCMDSPSPMD PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ SMPVRLLGHS PVLRNITNSQ APDGRRKSEA GSGAASSSGE DKENDGFVFK MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD RKMEVEELSP LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR RRSVTPPEEQ QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF LLQTVDGKHQ DLKYISPETM VALLTGKFSN IVDKFVIVDC RYPYEYEGGH IKTAVNLPLE RDAESFLLKS PIAPCSLDKR VILIFHCEFS SERGPRMCRF IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ DYRPMNHEAF KDELKTFRLK TRSWAGERSR RELCSRLQDQ
ELM motif
LIG_14-3-3_3Consensus derived from reported natural interactors which do not match the Mode 1 and Mode 2 ligands.
MOD_PLKSite phosphorylated by the Polo-like kinase.
Gene Ontology
GO:0000086G2/M transition of mitotic cell cycle
GO:0051301cell division
GO:0005829cytosol
GO:0005815microtubule organizing center
GO:0007067mitosis
GO:0005654nucleoplasm
GO:0008284positive regulation of cell proliferation
GO:0005515protein binding
GO:0004725protein tyrosine phosphatase activity

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