M-phase inducer phosphatase 1 - Rattus norvegicus (Rat)

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P48965 (MPIP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. History...

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

Documents (1) |

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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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.
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 CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages By similarity. Interacts with PIM1. Ref.2
Domain	The phosphodegron motif mediates interaction with specific F-box proteins when phosphorylated. Putative phosphorylation sites at Ser-79 and Ser-82 appear to be essential for this interaction By similarity.
Post-translational modification	Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-283, Ser-296 and Thr-508 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-283, and Ser-296 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-508 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-283 and Ser-296 may also promote ubiquitin-dependent proteolysis of CDC25A by the SCF complex. Phosphorylation of CDC25A at Ser-76 by CHEK1 primes it for subsequent phosphorylation at Ser-79, Ser-82 and Ser-88 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. Ref.2 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	G1/S transition of mitotic cell cycle Inferred from mutant phenotype Ref.1. Source: RGD 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 15139290. Source: RGD nucleus Inferred from direct assay PubMed 15139290. Source: RGD
Molecular_function	phosphoprotein phosphatase activity Inferred from direct assay Ref.2. Source: RGD 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 – 525

525

M-phase inducer phosphatase 1

PRO_0000198643

Regions

Domain

377 – 483

107

Rhodanese

Motif

74 – 84

Phosphodegron

Motif

141 – 143

KEN box

Sites

Active site

432

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

124

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

178

Phosphoserine; by CHEK1 By similarity

Modified residue

283

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

296

Phosphoserine; by CHEK1 and CHEK2 By similarity

Modified residue

508

Phosphothreonine; by CHEK1 By similarity

Modified residue

514

Phosphoserine; by PLK3 By similarity

Modified residue

520

Phosphoserine; by PLK3 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P48965 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A60EC0AF46D63A9C
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FASTA

525

59,218

        10         20         30         40         50         60 
MELGPEPPHR RRLLFTCSPT PAPQPTGKVQ FGASRAGGLS PVTNLTVTMD QLEGLGSDYE 

        70         80         90        100        110        120 
KPMDVRNSSS LQRMGSSEST DSGFCLDSPG PLDSKENLEI SLRRINCLPQ KLLGCSPALK 

       130        140        150        160        170        180 
RSHSDSLDHD IFQLIDQDEN KENEAFEFKK PIRPASRGCL NAHVHEESKD PFTHRQNSAP 

       190        200        210        220        230        240 
ARMLSSNESD ISESGNFSPL FTPQSPVKAS LSDEDDGFID LLDGENLKND EETPSCMSSL 

       250        260        270        280        290        300 
WTAPLVMRRP TNLADRCGLF DSPSPCSSTS SCSTRAVKRA DRSHEESPRG TKRRKSSEAS 

       310        320        330        340        350        360 
PVKADVPEPT QLPHQSLSLT SFPKGTIENI FHSDPRDLIG DFSKGYLFHT VSGKHQDLKY 

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

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

       490        500        510        520 
HCEPPSYRPM HHEDFKEDLK KFRTKSRTWA GEKSKREMYS RLKKL

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References

[1]	"Cdc25A is a novel phosphatase functioning early in the cell cycle." Jinno S., Suto K., Nagata A., Igarashi M., Kanaoka Y., Nojima H., Okayama H. EMBO J. 13:1549-1556(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NRK49F.
[2]	"Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway." Mochizuki T., Kitanaka C., Noguchi K., Muramatsu T., Asai A., Kuchino Y. J. Biol. Chem. 274:18659-18666(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PIM1, PHOSPHORYLATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D16236 mRNA. Translation: BAA03761.1.
IPI	IPI00324776.
RefSeq	NP_598255.1. NM_133571.1.
UniGene	Rn.11390.
3D structure databases
ProteinModelPortal	P48965.
SMR	P48965. Positions 338-497.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000028141.
PTM databases
PhosphoSite	P48965.
Proteomic databases
PRIDE	P48965.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	171102.
KEGG	rno:171102.
UCSC	RGD:621498. rat.
Organism-specific databases
CTD	993.
RGD	621498. Cdc25a.
Phylogenomic databases
eggNOG	COG5105.
HOGENOM	HOG000082672.
HOVERGEN	HBG052501.
InParanoid	P48965.
KO	K06645.
OrthoDB	EOG49P9Z6.
Gene expression databases
ArrayExpress	P48965.
Genevestigator	P48965.
GermOnline	ENSRNOG00000020737. Rattus norvegicus.
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
NextBio	621782.

Entry information

Entry name

MPIP1_RAT

Accession

Primary (citable) accession number: P48965

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 85 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

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

Protein-protein interaction 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