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P48965

- MPIP1_RAT

UniProt

P48965 - MPIP1_RAT

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Protein

M-phase inducer phosphatase 1

Gene

Cdc25a

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei432 – 4321By similarity

GO - Molecular functioni

  1. phosphoprotein phosphatase activity Source: RGD
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: RGD
  2. mitotic nuclear division Source: UniProtKB-KW
  3. response to radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase 1 (EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase Cdc25A
Gene namesi
Name:Cdc25a
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi621498. Cdc25a.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. nucleus Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 525525M-phase inducer phosphatase 1PRO_0000198643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Phosphoserine; by CHEK1By similarity
Modified residuei79 – 791Phosphoserine; by NEK11By similarity
Modified residuei82 – 821Phosphoserine; by NEK11By similarity
Modified residuei88 – 881Phosphoserine; by NEK11By similarity
Modified residuei124 – 1241Phosphoserine; by CHEK1 and CHEK2By similarity
Modified residuei178 – 1781Phosphoserine; by CHEK1By similarity
Modified residuei283 – 2831Phosphoserine; by CHEK1 and CHEK2By similarity
Modified residuei296 – 2961Phosphoserine; by CHEK1 and CHEK2By similarity
Modified residuei508 – 5081Phosphothreonine; by CHEK1By similarity
Modified residuei514 – 5141Phosphoserine; by PLK3By similarity
Modified residuei520 – 5201Phosphoserine; by PLK3By similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP48965.

PTM databases

PhosphoSiteiP48965.

Expressioni

Gene expression databases

GenevestigatoriP48965.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000028141.

Structurei

3D structure databases

ProteinModelPortaliP48965.
SMRiP48965. Positions 338-497.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini377 – 483107RhodanesePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi74 – 8411PhosphodegronAdd
BLAST
Motifi141 – 1433KEN box

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the MPI phosphatase family.Curated
Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5105.
HOGENOMiHOG000082672.
HOVERGENiHBG052501.
InParanoidiP48965.
KOiK06645.
PhylomeDBiP48965.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF06617. M-inducer_phosp. 1 hit.
PF00581. 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.

P48965-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELGPEPPHR RRLLFTCSPT PAPQPTGKVQ FGASRAGGLS PVTNLTVTMD
60 70 80 90 100
QLEGLGSDYE KPMDVRNSSS LQRMGSSEST DSGFCLDSPG PLDSKENLEI
110 120 130 140 150
SLRRINCLPQ KLLGCSPALK RSHSDSLDHD IFQLIDQDEN KENEAFEFKK
160 170 180 190 200
PIRPASRGCL NAHVHEESKD PFTHRQNSAP ARMLSSNESD ISESGNFSPL
210 220 230 240 250
FTPQSPVKAS LSDEDDGFID LLDGENLKND EETPSCMSSL WTAPLVMRRP
260 270 280 290 300
TNLADRCGLF DSPSPCSSTS SCSTRAVKRA DRSHEESPRG TKRRKSSEAS
310 320 330 340 350
PVKADVPEPT QLPHQSLSLT SFPKGTIENI FHSDPRDLIG DFSKGYLFHT
360 370 380 390 400
VSGKHQDLKY ISPEIMASVL NGKFANLIKE FVIIDCRYPY EYEGGHIKGA
410 420 430 440 450
VNLHMEEEVE EFLLKKPIVP ADGKRVIVVF HCEFSSERGP RMCRYVRERD
460 470 480 490 500
RLGNEYPKLH YPELYVLKGG YKEFFLKCQS HCEPPSYRPM HHEDFKEDLK
510 520
KFRTKSRTWA GEKSKREMYS RLKKL
Length:525
Mass (Da):59,218
Last modified:February 1, 1996 - v1
Checksum:iA60EC0AF46D63A9C
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16236 mRNA. Translation: BAA03761.1.
RefSeqiNP_598255.1. NM_133571.1.
UniGeneiRn.11390.

Genome annotation databases

GeneIDi171102.
KEGGirno:171102.
UCSCiRGD:621498. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D16236 mRNA. Translation: BAA03761.1 .
RefSeqi NP_598255.1. NM_133571.1.
UniGenei Rn.11390.

3D structure databases

ProteinModelPortali P48965.
SMRi P48965. Positions 338-497.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000028141.

PTM databases

PhosphoSitei P48965.

Proteomic databases

PRIDEi P48965.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 171102.
KEGGi rno:171102.
UCSCi RGD:621498. rat.

Organism-specific databases

CTDi 993.
RGDi 621498. Cdc25a.

Phylogenomic databases

eggNOGi COG5105.
HOGENOMi HOG000082672.
HOVERGENi HBG052501.
InParanoidi P48965.
KOi K06645.
PhylomeDBi P48965.

Miscellaneous databases

NextBioi 621782.
PROi P48965.

Gene expression databases

Genevestigatori P48965.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view ]
Pfami PF06617. M-inducer_phosp. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR00716. MPIPHPHTASE.
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiMPIP1_RAT
AccessioniPrimary (citable) accession number: P48965
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 1, 2014
This is version 95 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

External Data

Dasty 3