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Protein

M-phase inducer phosphatase 3

Gene

CDC25C

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei406By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-SSC-156711. Polo-like kinase mediated events.
R-SSC-176187. Activation of ATR in response to replication stress.
R-SSC-5625740. RHO GTPases activate PKNs.
R-SSC-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-SSC-69273. Cyclin A/B1 associated events during G2/M transition.
R-SSC-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

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
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001986501 – 502M-phase inducer phosphatase 3Add BLAST502

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei12PhosphoserineBy similarity1
Modified residuei30PhosphoserineBy similarity1
Modified residuei40Phosphothreonine; by CDK1By similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei54PhosphoserineBy similarity1
Modified residuei57PhosphoserineBy similarity1
Modified residuei60Phosphothreonine; by CDK1By similarity1
Modified residuei115Phosphoserine; by CDK1By similarity1
Modified residuei122PhosphoserineBy similarity1
Modified residuei123PhosphothreonineBy similarity1
Modified residuei194Phosphoserine; by CDK1By similarity1
Modified residuei217Phosphoserine; by PLK3By similarity1
Modified residuei224Phosphoserine; by PLK3By similarity1
Modified residuei243Phosphoserine; by CDK1By similarity1
Modified residuei245Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14By similarity1
Modified residuei501PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by CHEK1 and MAPK14 at Ser-245. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase (By similarity). Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-217 promotes nuclear translocation. Ser-224 is a minor phosphorylation site (By similarity). Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ29029.
PRIDEiQ29029.

Expressioni

Gene expression databases

BgeeiENSSSCG00000014329.
GenevisibleiQ29029. SS.

Interactioni

Subunit structurei

Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated at Ser-122 and/or Thr-123, interacts with PLK1.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015242.

Structurei

3D structure databases

ProteinModelPortaliQ29029.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini350 – 457RhodanesePROSITE-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.
HOGENOMiHOG000082672.
HOVERGENiHBG052501.
InParanoidiQ29029.
KOiK05867.
OMAiTVSLCDI.
OrthoDBiEOG091G0H0D.
TreeFamiTF101056.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. 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.

Q29029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEGGRPGSG PSFRSNHRKI LNLLLERETS FSMSSDRPGT PLKKKLFGDS
60 70 80 90 100
ANLSILSGGT PKRCLDLSNL SSGEMSATQF TTSADLDETG HLDSTGSEEI
110 120 130 140 150
QLAGMSYHQH LLKCSPAQLL CSTPNALDHG RRKKDAICSS SENKENENNT
160 170 180 190 200
SKPLEWWAHR NLLFQKRPGG PYMSPLSLLD NGNLVEGEMK HLGSPITAVS
210 220 230 240 250
KLDKNPERGE DQAEEISDEL MEFSLEDQEE AKVSLNTSCL YRSFSLPDSL
260 270 280 290 300
NSPGLKQVVK FKDHTLPDKV KKKYCSSHEE LRKGLGVKKM VSLCNINMIQ
310 320 330 340 350
MLEEDSNQGP LIGDFSKVCA LPTVSGRHQD LKYVNPETVA ALLSGKFQGL
360 370 380 390 400
IEKFYIIDCR YPYEYLGGHI QGALNLYSQE ELCNFFLKKP IIPLDTQKRI
410 420 430 440 450
IVVFHCEFSS ERGPRMCRSL REEDRALNQY PALYYPELYI LKGGYRDFFP
460 470 480 490 500
EYMELCEPQS YCPMHHQDHK AELLRCRSQN KAWEGERQLQ EQIALLVKDV

SP
Length:502
Mass (Da):56,639
Last modified:November 1, 1997 - v1
Checksum:i02E28CE42C0EDA70
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78317 Genomic DNA. Translation: CAA55123.1.
PIRiS43123.
RefSeqiNP_001116567.1. NM_001123095.1.
XP_005661723.1. XM_005661666.2.
XP_005661725.1. XM_005661668.2.
XP_013850591.1. XM_013995137.1.
XP_013850592.1. XM_013995138.1.
XP_013850593.1. XM_013995139.1.
XP_013850594.1. XM_013995140.1.
UniGeneiSsc.26311.

Genome annotation databases

EnsembliENSSSCT00000015655; ENSSSCP00000015242; ENSSSCG00000014329.
GeneIDi100144474.
KEGGissc:100144474.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78317 Genomic DNA. Translation: CAA55123.1.
PIRiS43123.
RefSeqiNP_001116567.1. NM_001123095.1.
XP_005661723.1. XM_005661666.2.
XP_005661725.1. XM_005661668.2.
XP_013850591.1. XM_013995137.1.
XP_013850592.1. XM_013995138.1.
XP_013850593.1. XM_013995139.1.
XP_013850594.1. XM_013995140.1.
UniGeneiSsc.26311.

3D structure databases

ProteinModelPortaliQ29029.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000015242.

Proteomic databases

PaxDbiQ29029.
PRIDEiQ29029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000015655; ENSSSCP00000015242; ENSSSCG00000014329.
GeneIDi100144474.
KEGGissc:100144474.

Organism-specific databases

CTDi995.

Phylogenomic databases

eggNOGiKOG3772. Eukaryota.
COG5105. LUCA.
GeneTreeiENSGT00390000018747.
HOGENOMiHOG000082672.
HOVERGENiHBG052501.
InParanoidiQ29029.
KOiK05867.
OMAiTVSLCDI.
OrthoDBiEOG091G0H0D.
TreeFamiTF101056.

Enzyme and pathway databases

ReactomeiR-SSC-156711. Polo-like kinase mediated events.
R-SSC-176187. Activation of ATR in response to replication stress.
R-SSC-5625740. RHO GTPases activate PKNs.
R-SSC-6804115. TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
R-SSC-69273. Cyclin A/B1 associated events during G2/M transition.
R-SSC-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Gene expression databases

BgeeiENSSSCG00000014329.
GenevisibleiQ29029. SS.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. 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 nameiMPIP3_PIG
AccessioniPrimary (citable) accession number: Q29029
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: October 5, 2016
This is version 108 of the entry and version 1 of the sequence. [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

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.