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P48968

- MPIP3_MESAU

UniProt

P48968 - MPIP3_MESAU

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Protein
M-phase inducer phosphatase 3
Gene
CDC25C
Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. Directly dephosphorylates CDK1 and activates its kinase activity. When phosphorylated, highly effective in activating G2 cells into prophase By similarity.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei322 – 3221 By similarity

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase 3 (EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase Cdc25C
Gene namesi
Name:CDC25C
OrganismiMesocricetus auratus (Golden hamster)
Taxonomic identifieri10036 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 420419M-phase inducer phosphatase 3
PRO_0000198649Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei38 – 381Phosphoserine By similarity
Modified residuei54 – 541Phosphoserine By similarity
Modified residuei58 – 581Phosphoserine By similarity
Modified residuei61 – 611Phosphoserine By similarity
Modified residuei64 – 641Phosphothreonine; by CDK1 By similarity
Modified residuei126 – 1261Phosphoserine By similarity
Modified residuei127 – 1271Phosphothreonine; by CDK1 By similarity
Modified residuei198 – 1981Phosphoserine; by CDK1 By similarity
Modified residuei219 – 2191Phosphoserine; by PLK3 By similarity
Modified residuei226 – 2261Phosphoserine; by PLK3 By similarity
Modified residuei418 – 4181Phosphoserine By similarity

Post-translational modificationi

Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-219 promotes nuclear translocation. Ser-226 is a minor phosphorylation site By similarity. Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity By similarity.

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Interacts with MAPK14 and 14-3-3 proteins By similarity. When phosphorylated at Ser-126 and/or Thr-127, interacts with PLK1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliP48968.
SMRiP48968. Positions 232-386.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini266 – 373108Rhodanese
Add
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.
Contains 1 rhodanese domain.

Phylogenomic databases

HOVERGENiHBG052501.

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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P48968-1 [UniParc]FASTAAdd to Basket

« Hide

MSTGPFPSSR REESSVSAPS FRFSQRKMLN LLLERNTSFT QDFPRSPGDK    50
LLDSTNLSIL SGGTPKRCLD LSNLSNGEMS ASPLITSADF DDTGSLDSSG 100
PQDVQLTEKN HHQDPMKGIP VQLLCSTPNA LDHSHRKKDA VRGLSANKEN 150
INTNLKTLQW ESPRIPRFQN TPGDPLASPL PLLGNGVSMD TEVRSLGSPI 200
TAVPKLSKNL NLEDQEEISE EPMEFSLEDH DTKECVLPTV SGKHQDLKYI 250
TPDTVAALLS GKFQGLIEKF YIIDCRYPYE YLGGHILGAI NLCSQKELHE 300
FFLKKPIVPL DIQKRVIIVF LCEFSSERGP RMCRSLRRKD RALNQYPALY 350
YPELYILKGG YRDFFPEYTE LCEPQGYCPM HHQDHQAELL MWRNQSKAQE 400
GERQLSEQIA LLMKKGVSLP 420
Length:420
Mass (Da):47,327
Last modified:February 1, 1996 - v1
Checksum:iD7564B0AF2124783
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10878 mRNA. Translation: BAA01646.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D10878 mRNA. Translation: BAA01646.1 .

3D structure databases

ProteinModelPortali P48968.
SMRi P48968. Positions 232-386.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG052501.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view ]
Pfami PF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR00716. MPIPHPHTASE.
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Chromosome condensation caused by loss of RCC1 function requires the cdc25C protein that is located in the cytoplasm."
    Seki T., Yamashita K., Nishitani H., Takagi T., Russell P., Nishimoto T.
    Mol. Biol. Cell 3:1373-1388(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiMPIP3_MESAU
AccessioniPrimary (citable) accession number: P48968
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: September 3, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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