M-phase inducer phosphatase 1 - Mus musculus (Mouse)

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P48964 (MPIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
M-phase inducer phosphatase 1
EC=3.1.3.48

Alternative name(s):
Dual specificity phosphatase Cdc25A

Gene names

Name:	Cdc25a
Synonyms:	Cdc25m3

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Phosphorylation by PIM1 leads to an increase in phosphatase activity By similarity.
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
Enzyme regulation	Stimulated by B-type cyclins. 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. Interacts with PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages By similarity.
Tissue specificity	Ubiquitously expressed in most developing tissue. High levels in the testis and lower levels in the ovary, particularly in germ cells. Lower levels also in kidney, liver, heart and muscle. Ref.1
Developmental stage	First detected at the blastocyst stage. Ref.1
Domain	The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-77 and Ser-80 appear to be essential for this interaction By similarity.
Post-translational modification	Phosphorylated by CHEK1 on Ser-74, Ser-122, Ser-171, Ser-271, Ser-284 and Thr-497 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-122, Ser-271, and Ser-284 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-171 and Thr-497 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-74, Ser-122, Ser-171, Ser-271 and Ser-284 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-74 by CHEK1 primes it for subsequent phosphorylation at Ser-77, Ser-80 and Ser-86 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.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell 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 response to radiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 11981756. Source: MGI nucleus Inferred from direct assay PubMed 11981756. Source: MGI
Molecular_function	protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

M-phase inducer phosphatase 1

PRO_0000198642

Regions

Domain

366 – 472

107

Rhodanese

Motif

72 – 82

Phosphodegron

Motif

139 – 141

KEN box

Sites

Active site

421

By similarity

Amino acid modifications

Modified residue

Phosphoserine; by CHEK1 By similarity

Modified residue

Phosphoserine; by NEK11 By similarity

Modified residue

Phosphoserine; by NEK11 By similarity

Modified residue

Phosphoserine; by NEK11 By similarity

Modified residue

122

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

171

Phosphoserine; by CHEK1 By similarity

Modified residue

271

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

284

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

497

Phosphothreonine; by CHEK1 By similarity

Modified residue

509

Phosphoserine; by PLK3 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P48964 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 4FFB5BCCFEAE411D
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FASTA

514

57,758

        10         20         30         40         50         60 
MELGPSPPPR RLFFACSPTP ASQPTGKMLF GASAAGGLSP VTNLTVTMDQ LEGLGSDCEK 

        70         80         90        100        110        120 
MEVRNNSSLQ RMGSSESTDS GFCLDSPGPL DSKENLEISL TRINSLPQKL LGCSPALKRS 

       130        140        150        160        170        180 
HSDSLDQDTF HLIDQDKNKE NEAFEPKKQY DLHLSSHLQE SKDLYTQRQN SAQLGMLSSN 

       190        200        210        220        230        240 
ESESGNFSPL FTPQSPVKAT LSDEDDGFID LLDGENLKND EETPTSMVSL WTAPLVMRRP 

       250        260        270        280        290        300 
ANLADRLRGL FDSPSPCGSS TRAVLKRADR SHEEPPRGTK RRKSVPSPVK AKADVPEPAQ 

       310        320        330        340        350        360 
LPSQSLSLMS SPKGTIENIL DSDPRDLIGD FSKGYLFNTV SGKHQDLKYI SPEIMASVLN 

       370        380        390        400        410        420 
GKFASLIKEF VIIDCRYPYE YEGGHIKGAV NLHMEEEVED FLLKNPIVPT DGKRVIVVFH 

       430        440        450        460        470        480 
CEFSSERGPR MCRYVRERDR LGNEYPKLHY PELYVLKGGY KEFFLKCQSH CEPPSYRPMH 

       490        500        510 
HEDFKEDLKK FRTKSRTWAG EKRKREMYSR LKKL

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References

[1]	"Two CDC25 homologues are differentially expressed during mouse development." Wickramasinghe D., Becker S., Ernst M.K., Resnick J.L., Centanni J.M., Tessarollo L., Grabel L.B., Donovan P.J. Development 121:2047-2056(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U27323 mRNA. Translation: AAA85580.1.
IPI	IPI00115568.
UniGene	Mm.307103.
3D structure databases
ProteinModelPortal	P48964.
SMR	P48964. Positions 327-486.
ModBase	Search...
PTM databases
PhosphoSite	P48964.
Proteomic databases
PRIDE	P48964.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc009rsw.1. mouse.
Organism-specific databases
MGI	MGI:103198. Cdc25a.
Phylogenomic databases
eggNOG	COG5105.
HOVERGEN	HBG052501.
Gene expression databases
CleanEx	MM_CDC25A.
Genevestigator	P48964.
GermOnline	ENSMUSG00000032477. Mus musculus.
Family and domain databases
Gene3D	3.40.250.10. 1 hit.
InterPro	IPR000751. MPI_Phosphatase. IPR001763. Rhodanese-like_dom. [Graphical view]
PANTHER	PTHR10828. PTHR10828. 1 hit.
Pfam	PF06617. M-inducer_phosp. 1 hit. PF00581. Rhodanese. 1 hit. [Graphical view]
PRINTS	PR00716. MPIPHPHTASE.
SMART	SM00450. RHOD. 1 hit. [Graphical view]
SUPFAM	SSF52821. Rhodanese-like. 1 hit.
PROSITE	PS50206. RHODANESE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

MPIP1_MOUSE

Accession

Primary (citable) accession number: P48964

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents