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Protein

M-phase inducer phosphatase 2

Gene

CDC25B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Stimulated by B-type cyclins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei4871

GO - Molecular functioni

  • phosphoprotein phosphatase activity Source: Reactome
  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • female meiosis I Source: Ensembl
  • G2/M transition of mitotic cell cycle Source: UniProtKB
  • mitotic cell cycle Source: UniProtKB
  • mitotic nuclear division Source: ProtInc
  • oocyte maturation Source: Ensembl
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of cytokinesis Source: UniProtKB
  • positive regulation of mitotic cell cycle Source: UniProtKB
  • positive regulation of protein kinase activity Source: Ensembl
  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BioCyciZFISH:HS02223-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-157881. Cyclin B2 mediated events.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
SIGNORiP30305.

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase 2 (EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase Cdc25B
Gene namesi
Name:CDC25B
Synonyms:CDC25HU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:1726. CDC25B.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nucleoplasm Source: HPA
  • spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

DisGeNETi994.
OpenTargetsiENSG00000101224.
PharmGKBiPA26260.

Chemistry databases

ChEMBLiCHEMBL4804.

Polymorphism and mutation databases

DMDMi21264471.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001986441 – 580M-phase inducer phosphatase 2Add BLAST580

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42PhosphoserineBy similarity1
Modified residuei169Phosphoserine; by MELK1 Publication1
Modified residuei249PhosphoserineCombined sources1
Modified residuei323Phosphoserine; by MELK and MAPK14Combined sources3 Publications1
Modified residuei353Phosphoserine; by AURKACombined sources1 Publication1
Modified residuei375Phosphoserine; by BRSK1 and MAPK14Combined sources2 Publications1
Modified residuei470PhosphoserineCombined sources1
Modified residuei563PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-353 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-169 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-323 and Ser-375 by MAPK14 is required for binding to 14-3-3 proteins.8 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP30305.
MaxQBiP30305.
PaxDbiP30305.
PeptideAtlasiP30305.
PRIDEiP30305.

PTM databases

DEPODiP30305.
iPTMnetiP30305.
PhosphoSitePlusiP30305.

Expressioni

Gene expression databases

BgeeiENSG00000101224.
CleanExiHS_CDC25B.
ExpressionAtlasiP30305. baseline and differential.
GenevisibleiP30305. HS.

Organism-specific databases

HPAiCAB002663.
HPA038892.
HPA038893.

Interactioni

Subunit structurei

Interacts with MAPK14 and 14-3-3 proteins.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
YWHABP319465EBI-1051746,EBI-359815
YWHAHQ049174EBI-1051746,EBI-306940
YWHAZP631045EBI-1051746,EBI-347088

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107429. 34 interactors.
DIPiDIP-323N.
IntActiP30305. 16 interactors.
MINTiMINT-124404.
STRINGi9606.ENSP00000245960.

Chemistry databases

BindingDBiP30305.

Structurei

Secondary structure

1580
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi396 – 399Combined sources4
Helixi417 – 424Combined sources8
Turni425 – 431Combined sources7
Beta strandi432 – 439Combined sources8
Helixi443 – 447Combined sources5
Helixi460 – 468Combined sources9
Turni469 – 471Combined sources3
Beta strandi479 – 486Combined sources8
Beta strandi488 – 492Combined sources5
Helixi493 – 508Combined sources16
Beta strandi519 – 522Combined sources4
Helixi525 – 532Combined sources8
Helixi534 – 536Combined sources3
Beta strandi537 – 540Combined sources4
Helixi548 – 550Combined sources3
Helixi551 – 558Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CWRX-ray2.10A370-580[»]
1CWSX-ray2.00A370-580[»]
1CWTX-ray2.30A388-565[»]
1QB0X-ray1.91A370-580[»]
1YM9X-ray2.00A391-564[»]
1YMDX-ray1.70A391-564[»]
1YMKX-ray1.70A391-564[»]
1YMLX-ray1.70A391-564[»]
1YS0X-ray2.00A391-564[»]
2A2KX-ray1.52A391-564[»]
2IFDX-ray2.00A391-564[»]
2IFVX-ray1.60A391-564[»]
2UZQX-ray2.38A/B/C/D/E/F391-580[»]
3FQTX-ray1.80C38-46[»]
3FQUX-ray1.80C38-46[»]
4WH7X-ray1.62A386-565[»]
4WH9X-ray1.50A386-565[»]
ProteinModelPortaliP30305.
SMRiP30305.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30305.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini431 – 538RhodanesePROSITE-ProRule annotationAdd BLAST108

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3772. Eukaryota.
COG5105. LUCA.
GeneTreeiENSGT00390000018747.
HOVERGENiHBG052501.
InParanoidiP30305.
KOiK05866.
OMAiITPCSLD.
OrthoDBiEOG091G0H0D.
PhylomeDBiP30305.
TreeFamiTF101056.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: P30305-1) [UniParc]FASTAAdd to basket
Also known as: CDC25B3

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEVPQPEPAP GSALSPAGVC GGAQRPGHLP GLLLGSHGLL GSPVRAAASS
60 70 80 90 100
PVTTLTQTMH DLAGLGSETP KSQVGTLLFR SRSRLTHLSL SRRASESSLS
110 120 130 140 150
SESSESSDAG LCMDSPSPMD PHMAEQTFEQ AIQAASRIIR NEQFAIRRFQ
160 170 180 190 200
SMPVRLLGHS PVLRNITNSQ APDGRRKSEA GSGAASSSGE DKENDGFVFK
210 220 230 240 250
MPWKPTHPSS THALAEWASR REAFAQRPSS APDLMCLSPD RKMEVEELSP
260 270 280 290 300
LALGRFSLTP AEGDTEEDDG FVDILESDLK DDDAVPPGME SLISAPLVKT
310 320 330 340 350
LEKEEEKDLV MYSKCQRLFR SPSMPCSVIR PILKRLERPQ DRDTPVQNKR
360 370 380 390 400
RRSVTPPEEQ QEAEEPKARV LRSKSLCHDE IENLLDSDHR ELIGDYSKAF
410 420 430 440 450
LLQTVDGKHQ DLKYISPETM VALLTGKFSN IVDKFVIVDC RYPYEYEGGH
460 470 480 490 500
IKTAVNLPLE RDAESFLLKS PIAPCSLDKR VILIFHCEFS SERGPRMCRF
510 520 530 540 550
IRERDRAVND YPSLYYPEMY ILKGGYKEFF PQHPNFCEPQ DYRPMNHEAF
560 570 580
KDELKTFRLK TRSWAGERSR RELCSRLQDQ
Length:580
Mass (Da):64,987
Last modified:May 27, 2002 - v2
Checksum:iEDE24B0E84AC1BE3
GO
Isoform 1 (identifier: P30305-2) [UniParc]FASTAAdd to basket
Also known as: CDC25B1

The sequence of this isoform differs from the canonical sequence as follows:
     68-81: Missing.

Show »
Length:566
Mass (Da):63,443
Checksum:i7C54E3E799ECDA50
GO
Isoform 2 (identifier: P30305-3) [UniParc]FASTAAdd to basket
Also known as: CDC25B2

The sequence of this isoform differs from the canonical sequence as follows:
     154-194: Missing.

Show »
Length:539
Mass (Da):60,756
Checksum:iCDA92929F8183BE9
GO
Isoform 4 (identifier: P30305-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-81: Missing.
     194-194: N → NVRFWKAGVGALREEEGACWGGSLACEDPPLPSWLQ

Note: No experimental confirmation available.
Show »
Length:601
Mass (Da):67,241
Checksum:i8E32AEC15A3845D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti575S → D in AAB21139 (PubMed:1662986).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_020933548E → K.1 PublicationCorresponds to variant rs11570019dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00086168 – 81Missing in isoform 1 and isoform 4. 2 PublicationsAdd BLAST14
Alternative sequenceiVSP_000862154 – 194Missing in isoform 2. 1 PublicationAdd BLAST41
Alternative sequenceiVSP_012587194N → NVRFWKAGVGALREEEGACW GGSLACEDPPLPSWLQ in isoform 4. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81934 mRNA. Translation: AAA58416.1.
S78187 mRNA. Translation: AAB21139.1.
X96436 Genomic DNA. Translation: CAA65303.1.
Z68092 mRNA. Translation: CAA92108.1.
AY494082 Genomic DNA. Translation: AAR26469.1.
AL109804 Genomic DNA. Translation: CAC17548.1.
AL109804 Genomic DNA. Translation: CAC17549.1.
AL109804 Genomic DNA. Translation: CAI18847.1.
CH471133 Genomic DNA. Translation: EAX10491.1.
CH471133 Genomic DNA. Translation: EAX10492.1.
CH471133 Genomic DNA. Translation: EAX10493.1.
CH471133 Genomic DNA. Translation: EAX10494.1.
CH471133 Genomic DNA. Translation: EAX10496.1.
CH471133 Genomic DNA. Translation: EAX10497.1.
CH471133 Genomic DNA. Translation: EAX10498.1.
CH471133 Genomic DNA. Translation: EAX10499.1.
BC006395 mRNA. Translation: AAH06395.1.
BC009953 mRNA. Translation: AAH09953.1.
BC051711 mRNA. Translation: AAH51711.1.
AF036233 Genomic DNA. Translation: AAB94622.1.
AF036233 Genomic DNA. Translation: AAB94624.1.
CCDSiCCDS13065.1. [P30305-2]
CCDS13066.1. [P30305-3]
CCDS13067.1. [P30305-1]
PIRiB41648.
RefSeqiNP_001274448.1. NM_001287519.1.
NP_001274453.1. NM_001287524.1.
NP_004349.1. NM_004358.4. [P30305-2]
NP_068658.1. NM_021872.3. [P30305-3]
NP_068659.1. NM_021873.3. [P30305-1]
UniGeneiHs.153752.

Genome annotation databases

EnsembliENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
GeneIDi994.
KEGGihsa:994.
UCSCiuc002wjn.5. human. [P30305-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81934 mRNA. Translation: AAA58416.1.
S78187 mRNA. Translation: AAB21139.1.
X96436 Genomic DNA. Translation: CAA65303.1.
Z68092 mRNA. Translation: CAA92108.1.
AY494082 Genomic DNA. Translation: AAR26469.1.
AL109804 Genomic DNA. Translation: CAC17548.1.
AL109804 Genomic DNA. Translation: CAC17549.1.
AL109804 Genomic DNA. Translation: CAI18847.1.
CH471133 Genomic DNA. Translation: EAX10491.1.
CH471133 Genomic DNA. Translation: EAX10492.1.
CH471133 Genomic DNA. Translation: EAX10493.1.
CH471133 Genomic DNA. Translation: EAX10494.1.
CH471133 Genomic DNA. Translation: EAX10496.1.
CH471133 Genomic DNA. Translation: EAX10497.1.
CH471133 Genomic DNA. Translation: EAX10498.1.
CH471133 Genomic DNA. Translation: EAX10499.1.
BC006395 mRNA. Translation: AAH06395.1.
BC009953 mRNA. Translation: AAH09953.1.
BC051711 mRNA. Translation: AAH51711.1.
AF036233 Genomic DNA. Translation: AAB94622.1.
AF036233 Genomic DNA. Translation: AAB94624.1.
CCDSiCCDS13065.1. [P30305-2]
CCDS13066.1. [P30305-3]
CCDS13067.1. [P30305-1]
PIRiB41648.
RefSeqiNP_001274448.1. NM_001287519.1.
NP_001274453.1. NM_001287524.1.
NP_004349.1. NM_004358.4. [P30305-2]
NP_068658.1. NM_021872.3. [P30305-3]
NP_068659.1. NM_021873.3. [P30305-1]
UniGeneiHs.153752.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CWRX-ray2.10A370-580[»]
1CWSX-ray2.00A370-580[»]
1CWTX-ray2.30A388-565[»]
1QB0X-ray1.91A370-580[»]
1YM9X-ray2.00A391-564[»]
1YMDX-ray1.70A391-564[»]
1YMKX-ray1.70A391-564[»]
1YMLX-ray1.70A391-564[»]
1YS0X-ray2.00A391-564[»]
2A2KX-ray1.52A391-564[»]
2IFDX-ray2.00A391-564[»]
2IFVX-ray1.60A391-564[»]
2UZQX-ray2.38A/B/C/D/E/F391-580[»]
3FQTX-ray1.80C38-46[»]
3FQUX-ray1.80C38-46[»]
4WH7X-ray1.62A386-565[»]
4WH9X-ray1.50A386-565[»]
ProteinModelPortaliP30305.
SMRiP30305.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107429. 34 interactors.
DIPiDIP-323N.
IntActiP30305. 16 interactors.
MINTiMINT-124404.
STRINGi9606.ENSP00000245960.

Chemistry databases

BindingDBiP30305.
ChEMBLiCHEMBL4804.

PTM databases

DEPODiP30305.
iPTMnetiP30305.
PhosphoSitePlusiP30305.

Polymorphism and mutation databases

DMDMi21264471.

Proteomic databases

EPDiP30305.
MaxQBiP30305.
PaxDbiP30305.
PeptideAtlasiP30305.
PRIDEiP30305.

Protocols and materials databases

DNASUi994.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245960; ENSP00000245960; ENSG00000101224. [P30305-1]
ENST00000340833; ENSP00000339170; ENSG00000101224. [P30305-3]
ENST00000439880; ENSP00000405972; ENSG00000101224. [P30305-2]
GeneIDi994.
KEGGihsa:994.
UCSCiuc002wjn.5. human. [P30305-1]

Organism-specific databases

CTDi994.
DisGeNETi994.
GeneCardsiCDC25B.
HGNCiHGNC:1726. CDC25B.
HPAiCAB002663.
HPA038892.
HPA038893.
MIMi116949. gene.
neXtProtiNX_P30305.
OpenTargetsiENSG00000101224.
PharmGKBiPA26260.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3772. Eukaryota.
COG5105. LUCA.
GeneTreeiENSGT00390000018747.
HOVERGENiHBG052501.
InParanoidiP30305.
KOiK05866.
OMAiITPCSLD.
OrthoDBiEOG091G0H0D.
PhylomeDBiP30305.
TreeFamiTF101056.

Enzyme and pathway databases

BioCyciZFISH:HS02223-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-157881. Cyclin B2 mediated events.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
SIGNORiP30305.

Miscellaneous databases

ChiTaRSiCDC25B. human.
EvolutionaryTraceiP30305.
GeneWikiiCDC25B.
GenomeRNAii994.
PROiP30305.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101224.
CleanExiHS_CDC25B.
ExpressionAtlasiP30305. baseline and differential.
GenevisibleiP30305. HS.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR00716. MPIPHPHTASE.
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMPIP2_HUMAN
AccessioniPrimary (citable) accession number: P30305
Secondary accession number(s): D3DVY1
, D3DVY2, D3DVY3, D3DVY4, O43551, Q13971, Q5JX77, Q6RSS1, Q9BRA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 27, 2002
Last modified: November 30, 2016
This is version 180 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.