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A7MBD1 (MPIP1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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

Names and origin

Protein namesRecommended name:
M-phase inducer phosphatase 1

EC=3.1.3.48
Alternative name(s):
Dual specificity phosphatase Cdc25A
Gene names
Name:CDC25A
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Stimulated by B-type cyclins By similarity. Stimulated by PIM1-mediated phosphorylation By similarity.

Subunit structure

Interacts with CCNB1/cyclin B1. Interacts with YWHAE/14-3-3 epsilon when phosphorylated. Interacts with CUL1 specifically when CUL1 is neddylated and active. Interacts with BTRC/BTRCP1 and FBXW11/BTRCP2. Interactions with CUL1, BTRC and FBXW11 are enhanced upon DNA damage By similarity. Interacts with PIM1 By similarity.

Domain

The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-78 and Ser-81 appear to be essential for this interaction By similarity.

Post-translational modification

Phosphorylated by CHEK1 on Ser-75, Ser-123, Ser-177, Ser-279, Ser-293 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-123, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-177 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-75, Ser-123, Ser-177, Ser-279 and Ser-293 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-75 by CHEK1 primes it for subsequent phosphorylation at Ser-78, Ser-81 and Ser-87 by NEK11. Phosphorylation by NEK11 is required for BTRC-mediated polyubiquitination and degradation. Phosphorylation by PIM1 leads to an increase in phosphatase activity. Phosphorylated by PLK3 following DNA damage, leading to promote its ubiquitination and degradation By similarity.

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C) ubiquitin ligase complex that contains FZR1/CDH1 during G1 phase leading to its degradation by the proteasome. Ubiquitinated by a SCF complex containing BTRC and FBXW11 during S phase leading to its degradation by the proteasome. Deubiquitination by USP17L2/DUB3 leads to its stabilization By similarity.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525M-phase inducer phosphatase 1
PRO_0000365161

Regions

Domain377 – 483107Rhodanese
Motif73 – 8311Phosphodegron
Motif140 – 1423KEN box

Sites

Active site4321 By similarity

Amino acid modifications

Modified residue751Phosphoserine; by CHEK1 By similarity
Modified residue781Phosphoserine; by NEK11 By similarity
Modified residue811Phosphoserine; by NEK11 By similarity
Modified residue871Phosphoserine; by NEK11 By similarity
Modified residue1231Phosphoserine; by CHEK1 and CHEK2 By similarity
Modified residue1771Phosphoserine; by CHEK1 By similarity
Modified residue2791Phosphoserine; by CHEK1 and CHEK2 By similarity
Modified residue2931Phosphoserine; by CHEK1 and CHEK2 By similarity
Modified residue5081Phosphothreonine; by CHEK1 By similarity
Modified residue5141Phosphoserine; by PLK3 By similarity
Modified residue5201Phosphoserine; by PLK3 By similarity

Sequences

Sequence LengthMass (Da)Tools
A7MBD1 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: 3608ED70EE8293BB

FASTA52559,142
        10         20         30         40         50         60 
MELGPEPPHR RRLLFACSPP PAPQPVVKAL FGTPAAGGLS PVTNLTVTMD QLQGLGSEYE 

        70         80         90        100        110        120 
QPIEVKNSSL QRMGSSESTD SGFCLDSPGP LDSKENLENP MRRINSLPQK LLGCSPALKR 

       130        140        150        160        170        180 
SHSDSLDHDV FQLIDQDENK ENQVFEFKKP IRPASRGCLH VHGLEEGKDV FTQRQNSAPA 

       190        200        210        220        230        240 
RMLSSNERDG NEPGNSIPFM PQSPVTPTLS DEDDGFMDLL DGENLKNDEE TPSCMASLWT 

       250        260        270        280        290        300 
APLVMRRTNN LGNRCKLFDS PSASCSSTIR SMLKRPDRSL EESPGGSRKR RKSVAGASPE 

       310        320        330        340        350        360 
EAASPEKPQE ILHHQSLSLA SSPKGTIENI LDNDPRDLIG DFSKGYLFHT VAGKHQDLKY 

       370        380        390        400        410        420 
ISPEIITSVL NGKFANLIKE FVIIDCRYPY EYEGGHIKGA VNLHMEEEVE EFLLKKPIVP 

       430        440        450        460        470        480 
TDGKRVIVVF HCEFSSERGP RMCRYVRERD RLGNEYPKLH YPELYVLKGG YKEFFLKCQS 

       490        500        510        520 
HCEPPSYRPM HHEDFKEDLK KFRTKSRTWA GEKSKREMYS RLKKL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC151493 mRNA. Translation: AAI51494.1.
RefSeqNP_001094570.1. NM_001101100.2.
UniGeneBt.62587.

3D structure databases

ProteinModelPortalA7MBD1.
SMRA7MBD1. Positions 338-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000012611.

Proteomic databases

PRIDEA7MBD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000012611; ENSBTAP00000012611; ENSBTAG00000009586.
GeneID520188.
KEGGbta:520188.

Organism-specific databases

CTD993.

Phylogenomic databases

eggNOGCOG5105.
GeneTreeENSGT00390000018747.
HOGENOMHOG000082672.
HOVERGENHBG052501.
InParanoidA7MBD1.
KOK06645.
OMANLTVTMD.
OrthoDBEOG7288R1.
TreeFamTF101056.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamPF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR00716. MPIPHPHTASE.
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20873047.

Entry information

Entry nameMPIP1_BOVIN
AccessionPrimary (citable) accession number: A7MBD1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 52 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