Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5D7P0 (MPIP3_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
M-phase inducer phosphatase 3
EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25C
Gene names
Name:CDC25C
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with MAPK14 and 14-3-3 proteins By similarity. When phosphorylated on Ser-130 and/or Thr-131, interacts with PLK1 By similarity.

Subcellular location

Nucleus By similarity.

Developmental stage

Expressed predominantly in G2 phase.

Post-translational modification

Phosphorylated by CHEK1 and MAPK14 at Ser-220. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-192 promotes nuclear translocation. Ser-199 is a minor phosphorylation site By similarity. Phosphorylation by CDK1 occurs at G2 and G2-M transition and leads to increased activity By similarity.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentNucleus
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell division

Inferred from electronic annotation. Source: UniProtKB-KW

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

peptidyl-tyrosine dephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477M-phase inducer phosphatase 3
PRO_0000365162

Regions

Domain325 – 432108Rhodanese

Sites

Active site3811 By similarity

Amino acid modifications

Modified residue381Phosphoserine By similarity
Modified residue481Phosphothreonine; by CDK1 By similarity
Modified residue581Phosphoserine By similarity
Modified residue621Phosphoserine By similarity
Modified residue651Phosphoserine By similarity
Modified residue681Phosphothreonine; by CDK1 By similarity
Modified residue1231Phosphoserine; by CDK1 By similarity
Modified residue1301Phosphoserine By similarity
Modified residue1311Phosphothreonine; by CDK1 By similarity
Modified residue1691Phosphoserine; by CDK1 By similarity
Modified residue1921Phosphoserine; by PLK3 By similarity
Modified residue1991Phosphoserine; by PLK3 By similarity
Modified residue2181Phosphoserine; by CDK1 By similarity
Modified residue2201Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK14 By similarity
Modified residue4761Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5D7P0 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: BC73134038B99915

FASTA47753,794
        10         20         30         40         50         60 
MSAEFFSSKR EEGSLASGPS FRSNQRKILN LLLERDASFS ISSDLPTTPV EKKLFGDSAN 

        70         80         90        100        110        120 
LSILSGGTPK RCLDLSNLSS GEMSATQLTA SADLDETGHL ESTGPEQVRL AGMNYRQHLI 

       130        140        150        160        170        180 
KCSPAQLFCS TPNALEHGRR KKDAICGSSA NKENDNGNLV ENEMKHLGSP ITTVSKLHKN 

       190        200        210        220        230        240 
PELAEDQAEE ISDELMEFSL EDQEKAKPPL NWSSLYRSSS LPDSLNSPSL KQVVKFKDST 

       250        260        270        280        290        300 
IPDKLKKKYC SNQKELGKGL GLKKMVSLCD INMTQMLEED SNQGPLIGDF SKVCALPTVS 

       310        320        330        340        350        360 
GKHQDLKYVN PETVAALLSG EFQGLIEKFY IIDCRYPYEY LGGHIQGALN LHSQEELYNF 

       370        380        390        400        410        420 
FLKKPIVPWD NQKRIVIVFH CEFSSERGPR MCRSLREEDR TLNQYPALYY PELYILKGGY 

       430        440        450        460        470 
RDFFPEYMEL CEPQSYCPMH HQDHKAELLR CRNQSKAWEG ERQLQEQIAL LVKDVSP

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC140630 mRNA. Translation: AAI40631.1.
IPIIPI00692550.
RefSeqNP_001091465.1. NM_001097996.2.
UniGeneBt.43933.

3D structure databases

ProteinModelPortalA5D7P0.
SMRA5D7P0. Positions 286-445.
ModBaseSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000006968.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000006968; ENSBTAP00000006968; ENSBTAG00000005293.
GeneID507731.
KEGGbta:507731.

Organism-specific databases

CTD995.

Phylogenomic databases

eggNOGCOG5105.
GeneTreeENSGT00390000018747.
HOGENOMHOG000082672.
HOVERGENHBG052501.
InParanoidA5D7P0.
KOK05867.
OMAFRSNQRK.
OrthoDBEOG47D9G1.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PANTHERPTHR10828. PTHR10828. 1 hit.
PfamPF06617. M-inducer_phosp. 2 hits.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. Rhodanese-like. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20868200.

Entry information

Entry nameMPIP3_BOVIN
AccessionPrimary (citable) accession number: A5D7P0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: June 12, 2007
Last modified: April 3, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents