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Protein

M-phase inducer phosphatase 2

Gene

Cdc25b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

Stimulated by B-type cyclins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei481By similarity1

GO - Molecular functioni

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic cell cycle Source: RGD
  • positive regulation of cell cycle G2/M phase transition Source: InterPro

Keywordsi

Molecular functionHydrolase, Protein phosphatase
Biological processCell cycle, Cell division, Mitosis

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621500. Cdc25b.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001986461 – 574M-phase inducer phosphatase 2Add BLAST574

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei42PhosphoserineCombined sources1
Modified residuei166Phosphoserine; by MELKBy similarity1
Modified residuei246PhosphoserineBy similarity1
Modified residuei319Phosphoserine; by MAPKAPK2 and MELKBy similarity1
Modified residuei319Phosphoserine; by MELK and MAPK14By similarity1
Modified residuei349Phosphoserine; by AURKABy similarity1
Modified residuei370Phosphoserine; by BRSK1 and MAPK14By similarity1
Modified residuei557PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by BRSK1 in vitro. Phosphorylated by CHEK1, which inhibits the activity of this protein. Phosphorylation at Ser-349 by AURKA might locally participate in the control of the onset of mitosis. Phosphorylation by MELK at Ser-166 promotes localization to the centrosome and the spindle poles during mitosis. Phosphorylation at Ser-319 and Ser-370 by MAPK14 is required for binding to 14-3-3 proteins (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP48966.
PRIDEiP48966.

PTM databases

iPTMnetiP48966.
PhosphoSitePlusiP48966.

Interactioni

Subunit structurei

Interacts with MAPK14 and 14-3-3 proteins.By similarity

Protein-protein interaction databases

BioGridi251111. 2 interactors.
STRINGi10116.ENSRNOP00000051129.

Structurei

3D structure databases

ProteinModelPortaliP48966.
SMRiP48966.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini425 – 532RhodanesePROSITE-ProRule annotationAdd BLAST108

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated

Phylogenomic databases

eggNOGiKOG3772. Eukaryota.
COG5105. LUCA.
HOGENOMiHOG000082672.
HOVERGENiHBG052501.
InParanoidiP48966.
KOiK05866.
PhylomeDBiP48966.

Family and domain databases

CDDicd01530. Cdc25. 1 hit.
Gene3Di3.40.250.10. 1 hit.
InterProiView protein in InterPro
IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
PfamiView protein in Pfam
PF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
PRINTSiPR00716. MPIPHPHTASE.
SMARTiView protein in SMART
SM00450. RHOD. 1 hit.
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiView protein in PROSITE
PS50206. RHODANESE_3. 1 hit.

Sequencei

Sequence statusi: Complete.

P48966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVPPQKSAP GSALSTARVL GGIQRPRHLS GFGFGSDGLL GSPERAASSS
60 70 80 90 100
PVTTLTQTMY NLAGLGSETP KTQVGSLSFQ NRLTDLSLSR RTSECSLSSE
110 120 130 140 150
SSESSDAGLC MDSPSPMDPQ TAERTFEQAI QAASRVIQKM QFTIKASVFA
160 170 180 190 200
SEAAGHSPVL QNITNSQALD SWEKDEAGYR AASSPGEDKE NDGYIFKMPQ
210 220 230 240 250
KLPHSSSARA LAEWASRREA FTQRPSSAPD LMCLTTDGKM DVEEASPVAQ
260 270 280 290 300
SSSLTPVERA CEEDDGFVDI LESDLKDDDM VPAGMENLIS APLVKKLDKE
310 320 330 340 350
EEQDLIMFSK CQRLFRSPSM PCSVIRPILK RLERPHDRDV PVLSKRRKSG
360 370 380 390 400
TPLEEQQLEE PKARVFRSKS LCHEIESILD SDHRGLIGDY SKAFLLQTVD
410 420 430 440 450
GKHQDLKYIS PETMVALLTG KFSNIVEKFV IVDCRYPYEY EGGHIKNAVN
460 470 480 490 500
LPLEPDAETF LLKHPITPCN LDKRIILIFH CEFSSERGPR MCRFIRERDR
510 520 530 540 550
AANDYPSLYY PEMYILKGGY KEFFPQHPNF CEPQDYRPMN HAAFRDELRN
560 570
FRLKTRSWAG ERSTTQLCSR LQDQ
Length:574
Mass (Da):64,287
Last modified:February 1, 1996 - v1
Checksum:i9367CE203B15FAAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16237 mRNA. Translation: BAA03762.1.
RefSeqiNP_598256.1. NM_133572.1.
UniGeneiRn.11312.

Genome annotation databases

GeneIDi171103.
KEGGirno:171103.

Similar proteinsi

Entry informationi

Entry nameiMPIP2_RAT
AccessioniPrimary (citable) accession number: P48966
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 27, 2017
This is version 121 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families