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P30304

- MPIP1_HUMAN

UniProt

P30304 - MPIP1_HUMAN

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Protein

M-phase inducer phosphatase 1

Gene

CDC25A

Organism
Homo sapiens (Human)
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.

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei431 – 4311

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. cellular response to UV Source: UniProtKB
  3. DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. mitotic cell cycle Source: Reactome
  7. mitotic nuclear division Source: UniProtKB-KW
  8. regulation of cell cycle Source: Reactome
  9. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  10. response to radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.
REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_2160. p53-Independent DNA Damage Response.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6769. Activation of ATR in response to replication stress.
REACT_683. G1/S-Specific Transcription.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:1725. CDC25A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761S → A: Abolishes ubiquitination and impairs CHEK1-dependent degradation following checkpoint activation. 2 Publications
Mutagenesisi79 – 791S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication
Mutagenesisi81 – 811D → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication
Mutagenesisi82 – 821S → A: Abrogates interactions with BTRC and FBXW11 and prevents ubiquitination. 1 Publication
Mutagenesisi124 – 1241S → A: Abrogates phosphorylation by CHEK2 and infrared-induced degradation. Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-178; A-279 and A-293. 4 Publications
Mutagenesisi141 – 1433KEN → AAA: Prevents ubiquitination and subsequent degradation by the APC/C ubiquitin ligase complex. 1 Publication
Mutagenesisi178 – 1781S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-279 and A-293. Abrogates 14-3-3 protein binding. 3 Publications
Mutagenesisi279 – 2791S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-293. 1 Publication
Mutagenesisi293 – 2931S → A: Increases basal stability and impairs CHEK1-dependent degradation following checkpoint activation; when associated with A-124; A-178 and A-279. 1 Publication
Mutagenesisi431 – 4311C → S: Abolishes phosphatase activity. 2 Publications
Mutagenesisi507 – 5071T → A: Abrogates 14-3-3 protein binding; increases binding to cyclin B1. 1 Publication
Mutagenesisi513 – 5131S → A: Increased stability following IR treatment. 1 Publication
Mutagenesisi513 – 5131S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 1 Publication
Mutagenesisi514 – 5141K → L: Abrogates binding to CCNB1; when associated with L-520. 1 Publication
Mutagenesisi519 – 5191S → A: Increased stability following IR treatment. 1 Publication
Mutagenesisi519 – 5191S → D: Mimicks phosphorylation state, leading to promote degradation following IR treatment. 1 Publication
Mutagenesisi520 – 5201R → L: Abrogates binding to CCNB1; when associated with L-514. 1 Publication

Organism-specific databases

PharmGKBiPA26259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 524524M-phase inducer phosphatase 1PRO_0000198641Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei76 – 761Phosphoserine; by CHEK12 Publications
Modified residuei79 – 791Phosphoserine; by NEK111 Publication
Modified residuei82 – 821Phosphoserine; by NEK112 Publications
Modified residuei88 – 881Phosphoserine; by NEK112 Publications
Modified residuei124 – 1241Phosphoserine; by CHEK1 and CHEK25 Publications
Modified residuei178 – 1781Phosphoserine; by CHEK13 Publications
Modified residuei279 – 2791Phosphoserine; by CHEK1 and CHEK21 Publication
Modified residuei293 – 2931Phosphoserine; by CHEK1 and CHEK21 Publication
Modified residuei507 – 5071Phosphothreonine; by CHEK11 Publication
Modified residuei513 – 5131Phosphoserine; by PLK31 Publication
Modified residuei519 – 5191Phosphoserine; by PLK31 Publication

Post-translational modificationi

Phosphorylated by CHEK1 on Ser-76, Ser-124, Ser-178, Ser-279, Ser-293 and Thr-507 during checkpoint mediated cell cycle arrest. Also phosphorylated by CHEK2 on Ser-124, Ser-279, and Ser-293 during checkpoint mediated cell cycle arrest. Phosphorylation on Ser-178 and Thr-507 creates binding sites for YWHAE/14-3-3 epsilon which inhibits CDC25A. Phosphorylation on Ser-76, Ser-124, Ser-178, Ser-279 and Ser-293 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.11 Publications
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.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP30304.
PaxDbiP30304.
PRIDEiP30304.

PTM databases

PhosphoSiteiP30304.

Expressioni

Gene expression databases

BgeeiP30304.
CleanExiHS_CDC25A.
ExpressionAtlasiP30304. baseline and differential.
GenevestigatoriP30304.

Organism-specific databases

HPAiHPA005855.

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 PIM1. Interacts with CHEK2; mediates CDC25A phosphorylation and degradation in response to infrared-induced DNA damages.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
RAF1P040494EBI-747671,EBI-365996
YWHABP319468EBI-747671,EBI-359815
YWHAZP631042EBI-747671,EBI-347088

Protein-protein interaction databases

BioGridi107428. 51 interactions.
DIPiDIP-166N.
IntActiP30304. 35 interactions.
MINTiMINT-124723.
STRINGi9606.ENSP00000303706.

Structurei

Secondary structure

1
524
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi341 – 3444Combined sources
Helixi362 – 3698Combined sources
Turni370 – 3767Combined sources
Beta strandi377 – 3848Combined sources
Helixi388 – 3925Combined sources
Helixi405 – 4117Combined sources
Turni412 – 4143Combined sources
Beta strandi423 – 4308Combined sources
Beta strandi432 – 4365Combined sources
Helixi437 – 45115Combined sources
Beta strandi463 – 4664Combined sources
Helixi469 – 4779Combined sources
Helixi478 – 4803Combined sources
Beta strandi481 – 4844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C25X-ray2.30A337-496[»]
ProteinModelPortaliP30304.
SMRiP30304. Positions 337-496.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30304.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini376 – 482107RhodanesePROSITE-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.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5105.
GeneTreeiENSGT00390000018747.
HOGENOMiHOG000082672.
HOVERGENiHBG052501.
InParanoidiP30304.
KOiK06645.
OMAiNLTVTMD.
OrthoDBiEOG7288R1.
PhylomeDBiP30304.
TreeFamiTF101056.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P30304-1) [UniParc]FASTAAdd to Basket

Also known as: CDC25A1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELGPEPPHR RRLLFACSPP PASQPVVKAL FGASAAGGLS PVTNLTVTMD
60 70 80 90 100
QLQGLGSDYE QPLEVKNNSN LQRMGSSEST DSGFCLDSPG PLDSKENLEN
110 120 130 140 150
PMRRIHSLPQ KLLGCSPALK RSHSDSLDHD IFQLIDPDEN KENEAFEFKK
160 170 180 190 200
PVRPVSRGCL HSHGLQEGKD LFTQRQNSAP ARMLSSNERD SSEPGNFIPL
210 220 230 240 250
FTPQSPVTAT LSDEDDGFVD LLDGENLKNE EETPSCMASL WTAPLVMRTT
260 270 280 290 300
NLDNRCKLFD SPSLCSSSTR SVLKRPERSQ EESPPGSTKR RKSMSGASPK
310 320 330 340 350
ESTNPEKAHE TLHQSLSLAS SPKGTIENIL DNDPRDLIGD FSKGYLFHTV
360 370 380 390 400
AGKHQDLKYI SPEIMASVLN GKFANLIKEF VIIDCRYPYE YEGGHIKGAV
410 420 430 440 450
NLHMEEEVED FLLKKPIVPT DGKRVIVVFH CEFSSERGPR MCRYVRERDR
460 470 480 490 500
LGNEYPKLHY PELYVLKGGY KEFFMKCQSY CEPPSYRPMH HEDFKEDLKK
510 520
FRTKSRTWAG EKSKREMYSR LKKL
Length:524
Mass (Da):59,087
Last modified:July 19, 2004 - v2
Checksum:iB2F6B792D4E6122B
GO
Isoform 2 (identifier: P30304-2) [UniParc]FASTAAdd to Basket

Also known as: CDC25A2

The sequence of this isoform differs from the canonical sequence as follows:
     144-183: Missing.

Show »
Length:484
Mass (Da):54,551
Checksum:iAE6326F34B704D4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 105EPPHR → SPAP in AAA58415. (PubMed:1836978)Curated
Sequence conflicti180 – 1812PA → QL in AAA58415. (PubMed:1836978)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881S → F.1 Publication
Corresponds to variant rs3731499 [ dbSNP | Ensembl ].
VAR_020932
Natural varianti182 – 1821R → G.1 Publication
Corresponds to variant rs6771386 [ dbSNP | Ensembl ].
VAR_023532
Natural varianti182 – 1821R → W.
Corresponds to variant rs6771386 [ dbSNP | Ensembl ].
VAR_023533

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei144 – 18340Missing in isoform 2. 2 PublicationsVSP_000860Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81933 mRNA. Translation: AAA58415.1.
AY137580 mRNA. Translation: AAN11305.1.
AF527417 Genomic DNA. Translation: AAM77917.1.
BC007401 mRNA. Translation: AAH07401.1.
BC018642 mRNA. Translation: AAH18642.1.
AF277722 mRNA. Translation: AAG41884.1.
CCDSiCCDS2760.1. [P30304-1]
CCDS2761.1. [P30304-2]
PIRiA41648.
RefSeqiNP_001780.2. NM_001789.2. [P30304-1]
NP_963861.1. NM_201567.1. [P30304-2]
UniGeneiHs.437705.

Genome annotation databases

EnsembliENST00000302506; ENSP00000303706; ENSG00000164045. [P30304-1]
ENST00000351231; ENSP00000343166; ENSG00000164045. [P30304-2]
GeneIDi993.
KEGGihsa:993.
UCSCiuc003csh.1. human. [P30304-1]
uc003csi.1. human. [P30304-2]

Polymorphism databases

DMDMi50403734.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81933 mRNA. Translation: AAA58415.1 .
AY137580 mRNA. Translation: AAN11305.1 .
AF527417 Genomic DNA. Translation: AAM77917.1 .
BC007401 mRNA. Translation: AAH07401.1 .
BC018642 mRNA. Translation: AAH18642.1 .
AF277722 mRNA. Translation: AAG41884.1 .
CCDSi CCDS2760.1. [P30304-1 ]
CCDS2761.1. [P30304-2 ]
PIRi A41648.
RefSeqi NP_001780.2. NM_001789.2. [P30304-1 ]
NP_963861.1. NM_201567.1. [P30304-2 ]
UniGenei Hs.437705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C25 X-ray 2.30 A 337-496 [» ]
ProteinModelPortali P30304.
SMRi P30304. Positions 337-496.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107428. 51 interactions.
DIPi DIP-166N.
IntActi P30304. 35 interactions.
MINTi MINT-124723.
STRINGi 9606.ENSP00000303706.

Chemistry

BindingDBi P30304.
ChEMBLi CHEMBL3775.

PTM databases

PhosphoSitei P30304.

Polymorphism databases

DMDMi 50403734.

Proteomic databases

MaxQBi P30304.
PaxDbi P30304.
PRIDEi P30304.

Protocols and materials databases

DNASUi 993.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302506 ; ENSP00000303706 ; ENSG00000164045 . [P30304-1 ]
ENST00000351231 ; ENSP00000343166 ; ENSG00000164045 . [P30304-2 ]
GeneIDi 993.
KEGGi hsa:993.
UCSCi uc003csh.1. human. [P30304-1 ]
uc003csi.1. human. [P30304-2 ]

Organism-specific databases

CTDi 993.
GeneCardsi GC03M048173.
HGNCi HGNC:1725. CDC25A.
HPAi HPA005855.
MIMi 116947. gene.
neXtProti NX_P30304.
PharmGKBi PA26259.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5105.
GeneTreei ENSGT00390000018747.
HOGENOMi HOG000082672.
HOVERGENi HBG052501.
InParanoidi P30304.
KOi K06645.
OMAi NLTVTMD.
OrthoDBi EOG7288R1.
PhylomeDBi P30304.
TreeFami TF101056.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_111214. G0 and Early G1.
REACT_1321. E2F-enabled inhibition of pre-replication complex formation.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_2160. p53-Independent DNA Damage Response.
REACT_471. E2F mediated regulation of DNA replication.
REACT_6769. Activation of ATR in response to replication stress.
REACT_683. G1/S-Specific Transcription.
REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.

Miscellaneous databases

ChiTaRSi CDC25A. human.
EvolutionaryTracei P30304.
GeneWikii CDC25A.
GenomeRNAii 993.
NextBioi 4164.
PROi P30304.
SOURCEi Search...

Gene expression databases

Bgeei P30304.
CleanExi HS_CDC25A.
ExpressionAtlasi P30304. baseline and differential.
Genevestigatori P30304.

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

« Hide 'large scale' publications
  1. "Specific activation of cdc25 tyrosine phosphatases by B-type cyclins: evidence for multiple roles of mitotic cyclins."
    Galaktionov K.I., Beach D.
    Cell 67:1181-1194(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-182.
  2. Varmeh-Ziaie S., Manfredi J.J.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. NIEHS SNPs program
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-88.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  5. "Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C."
    Wegener S., Hampe W., Herrmann D., Schaller H.C.
    Eur. J. Cell Biol. 79:810-815(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 37-234 (ISOFORM 2).
  6. "The ATM-Chk2-Cdc25A checkpoint pathway guards against radioresistant DNA synthesis."
    Falck J., Mailand N., Syljuaasen R.G., Bartek J., Lukas J.
    Nature 410:842-847(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHEK2, PHOSPHORYLATION AT SER-124 BY CHEK2, MUTAGENESIS OF SER-124.
  7. Cited for: UBIQUITINATION BY THE APC/C UBIQUITIN LIGASE COMPLEX, DOMAIN KEN BOX MOTIF, MUTAGENESIS OF 141-LYS--ASN-143.
  8. "Disruption of the checkpoint kinase 1/cell division cycle 25A pathway abrogates ionizing radiation-induced S and G2 checkpoints."
    Zhao H., Watkins J.L., Piwnica-Worms H.
    Proc. Natl. Acad. Sci. U.S.A. 99:14795-14800(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-124, MUTAGENESIS OF SER-124.
  9. "Chk1 regulates the S phase checkpoint by coupling the physiological turnover and ionizing radiation-induced accelerated proteolysis of Cdc25A."
    Soerensen C.S., Syljuaesen R.G., Falck J., Schroeder T., Roennstrand L., Khanna K.K., Zhou B.-B., Bartek J., Lukas J.
    Cancer Cell 3:247-258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-124; SER-178; SER-279 AND SER-293, MUTAGENESIS OF SER-124; SER-178; SER-279 AND SER-293.
  10. "SCFbeta-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase."
    Jin J., Shirogane T., Xu L., Nalepa G., Qin J., Elledge S.J., Harper J.W.
    Genes Dev. 17:3062-3074(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTRC; CUL1 AND FBXW11, PHOSPHODEGRON MOTIF, PHOSPHORYLATION AT SER-76 AND SER-124, UBIQUITINATION, MUTAGENESIS OF SER-76; SER-79; ASP-81 AND SER-82.
  11. "Chk1 mediates S and G2 arrests through Cdc25A degradation in response to DNA-damaging agents."
    Xiao Z., Chen Z., Gunasekera A.H., Sowin T.J., Rosenberg S.H., Fesik S., Zhang H.
    J. Biol. Chem. 278:21767-21773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF CYS-431.
  12. "Phosphorylation at serine 75 is required for UV-mediated degradation of human Cdc25A phosphatase at the S-phase checkpoint."
    Hassepass I., Voit R., Hoffmann I.
    J. Biol. Chem. 278:29824-29829(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-76; SER-124 AND SER-178, MUTAGENESIS OF SER-76; SER-124 AND SER-178.
  13. "Chk1 kinase negatively regulates mitotic function of Cdc25A phosphatase through 14-3-3 binding."
    Chen M.-S., Ryan C.E., Piwnica-Worms H.
    Mol. Cell. Biol. 23:7488-7497(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNB1 AND YWHAE, PHOSPHORYLATION AT SER-178 AND THR-507, MUTAGENESIS OF SER-178; CYS-431; THR-507; LYS-514 AND ARG-520.
  14. "The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C."
    Bachmann M., Kosan C., Xing P.X., Montenarh M., Hoffmann I., Moroy T.
    Int. J. Biochem. Cell Biol. 38:430-443(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIM1.
  15. "NEK11 regulates CDC25A degradation and the IR-induced G2/M checkpoint."
    Melixetian M., Klein D.K., Soerensen C.S., Helin K.
    Nat. Cell Biol. 11:1247-1253(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-79; SER-82 AND SER-88.
  16. "NEK11: linking CHK1 and CDC25A in DNA damage checkpoint signaling."
    Soerensen C.S., Melixetian M., Klein D.K., Helin K.
    Cell Cycle 9:450-455(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-82 AND SER-88.
  17. "Ubiquitin hydrolase Dub3 promotes oncogenic transformation by stabilizing Cdc25A."
    Pereg Y., Liu B.Y., O'Rourke K.M., Sagolla M., Dey A., Komuves L., French D.M., Dixit V.M.
    Nat. Cell Biol. 12:400-406(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEUBIQUITINATION BY USP17L2.
  18. "Absence of polo-like kinase 3 in mice stabilizes Cdc25A after DNA damage but is not sufficient to produce tumors."
    Myer D.L., Robbins S.B., Yin M., Boivin G.P., Liu Y., Greis K.D., Bahassi el M., Stambrook P.J.
    Mutat. Res. 714:1-10(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-513 AND SER-519 BY PLK3, UBIQUITINATION, MUTAGENESIS OF SER-513 AND SER-519.
  19. "Crystal structure of the catalytic domain of the human cell cycle control phosphatase, Cdc25A."
    Fauman E.B., Cogswell J.P., Lovejoy B., Rocque W.J., Holmes W., Montana V.G., Piwnica-Worms H., Rink M.J., Saper M.A.
    Cell 93:617-625(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 336-496.

Entry informationi

Entry nameiMPIP1_HUMAN
AccessioniPrimary (citable) accession number: P30304
Secondary accession number(s): Q8IZH5, Q96IL3, Q9H2F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: July 19, 2004
Last modified: November 26, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3