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P30307

- MPIP3_HUMAN

UniProt

P30307 - MPIP3_HUMAN

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Protein

M-phase inducer phosphatase 3

Gene
CDC25C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as a dosage-dependent inducer in mitotic control. Tyrosine protein phosphatase required for progression of the cell cycle. When phosphorylated, highly effective in activating G2 cells into prophase. Directly dephosphorylates CDK1 and activates its kinase activity.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei377 – 3771 By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. protein kinase binding Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: UniProtKB
  4. WW domain binding Source: BHF-UCL

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. DNA replication Source: Reactome
  3. G2/M transition of mitotic cell cycle Source: UniProtKB
  4. mitotic cell cycle Source: Reactome
  5. mitotic nuclear division Source: UniProtKB-KW
  6. peptidyl-tyrosine dephosphorylation Source: GOC
  7. regulation of cell cycle Source: Reactome
  8. regulation of cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB
  9. regulation of mitosis Source: ProtInc
  10. spermatogenesis Source: Ensembl
  11. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Host-virus interaction, Mitosis

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_1006. Polo-like kinase mediated events.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_6769. Activation of ATR in response to replication stress.

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase inducer phosphatase 3 (EC:3.1.3.48)
Alternative name(s):
Dual specificity phosphatase Cdc25C
Gene namesi
Name:CDC25C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:1727. CDC25C.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291S → V: Loss of phosphorylation. Severely impairs PLK1-binding. 1 Publication
Mutagenesisi130 – 1301T → A: Loss of phosphorylation. Severely impairs PLK1-binding. 1 Publication
Mutagenesisi191 – 1911S → A: Facilitates nuclear exclusion. 1 Publication
Mutagenesisi191 – 1911S → D: Mimicks phosphorylation state, leading to enhanced accumulation in the nucleus. 1 Publication
Mutagenesisi352 – 3521E → K: Partial loss of HIV-1 Vpr binding. 1 Publication
Mutagenesisi359 – 3591K → E: No effect on HIV-1 Vpr binding. 1 Publication

Organism-specific databases

PharmGKBiPA100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 473472M-phase inducer phosphatase 3PRO_0000198647Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei38 – 381Phosphoserine1 Publication
Modified residuei48 – 481Phosphothreonine2 Publications
Modified residuei57 – 571Phosphoserine1 Publication
Modified residuei61 – 611Phosphoserine3 Publications
Modified residuei64 – 641Phosphoserine3 Publications
Modified residuei67 – 671Phosphothreonine3 Publications
Modified residuei122 – 1221Phosphoserine; by CDK1 Inferred
Modified residuei129 – 1291Phosphoserine
Modified residuei130 – 1301Phosphothreonine; by CDK1 Inferred
Modified residuei168 – 1681Phosphoserine2 Publications
Modified residuei191 – 1911Phosphoserine; by PLK31 Publication
Modified residuei198 – 1981Phosphoserine; by PLK31 Publication
Modified residuei214 – 2141Phosphoserine; by CDK1 Inferred
Modified residuei216 – 2161Phosphoserine; by CHEK1, CHEK2, BRSK1 and MAPK143 Publications
Modified residuei472 – 4721Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by CHEK1 and MAPK14 at Ser-216. This phosphorylation creates a binding site for 14-3-3 protein and inhibits the phosphatase. Phosphorylated by PLK4. Phosphorylated by PLK1, leading to activate the phosphatase activity. Phosphorylation by PLK3 at Ser-191 promotes nuclear translocation. Ser-198 is a minor phosphorylation site. Was initially reported to be phosphorylated by PLK3 at Ser-216 (1 Publication). However, such phosphorylation by PLK3 was not confirmed by other groups. Phosphorylation at Thr-48, Thr-67, Ser-122, Thr-130, Ser-168 and Ser-214 occurs at G2 and G2-M transition and is probably catalyzed by CDK1. Ser-168 phosphorylation levels are lower than those at the other 5 CDK1 sites. Phosphorylation by CDK1 leads to increased activity.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP30307.
PaxDbiP30307.
PRIDEiP30307.

PTM databases

PhosphoSiteiP30307.

Expressioni

Developmental stagei

Expressed predominantly in G2 phase.

Gene expression databases

ArrayExpressiP30307.
BgeeiP30307.
CleanExiHS_CDC25C.
GenevestigatoriP30307.

Organism-specific databases

HPAiCAB003800.

Interactioni

Subunit structurei

Interacts with HIV-1 Vpr, thereby inactivating CDC25C phosphatase activity. Interacts with MAPK14 and 14-3-3 proteins. When phosphorylated on Ser-129 and/or Thr-130, interacts with PLK1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK1P064932EBI-974439,EBI-444308
CHEK1O147572EBI-974439,EBI-974488
LZTS1Q9Y2502EBI-974439,EBI-1216080

Protein-protein interaction databases

BioGridi107430. 32 interactions.
DIPiDIP-24183N.
IntActiP30307. 7 interactions.
MINTiMINT-86355.
STRINGi9606.ENSP00000321656.

Structurei

Secondary structure

1
473
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1293
Beta strandi286 – 2894
Beta strandi300 – 3056
Helixi307 – 3148
Turni315 – 3217
Beta strandi322 – 3298
Helixi333 – 3375
Beta strandi339 – 3413
Helixi350 – 3578
Beta strandi369 – 3768
Helixi384 – 39714
Beta strandi409 – 4124
Helixi415 – 4195
Turni420 – 4223
Helixi424 – 4263
Beta strandi427 – 4304
Beta strandi438 – 4403

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OJXX-ray2.85E126-134[»]
3BZIX-ray2.10E126-134[»]
3OP3X-ray2.63A270-462[»]
ProteinModelPortaliP30307.
SMRiP30307. Positions 280-448.

Miscellaneous databases

EvolutionaryTraceiP30307.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini321 – 428108RhodaneseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 37946HIV-1 Vpr binding siteAdd
BLAST

Sequence similaritiesi

Belongs to the MPI phosphatase family.
Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG5105.
HOVERGENiHBG052501.
InParanoidiP30307.
KOiK05867.
OMAiTVSLCDI.
OrthoDBiEOG7288R1.
PhylomeDBiP30307.
TreeFamiTF101056.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR000751. MPI_Phosphatase.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF06617. M-inducer_phosp. 2 hits.
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 (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P30307-1) [UniParc]FASTAAdd to Basket

Also known as: CDC25C1

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

MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV    50
GKFLGDSANL SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD 100
SSGLQEVHLA GMNHDQHLMK CSPAQLLCST PNGLDRGHRK RDAMCSSSAN 150
KENDNGNLVD SEMKYLGSPI TTVPKLDKNP NLGEDQAEEI SDELMEFSLK 200
DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK VKKKYFSGQG 250
KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 300
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ 350
EELFNFFLKK PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ 400
YPALYYPELY ILKGGYRDFF PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ 450
SKVQEGERQL REQIALLVKD MSP 473
Length:473
Mass (Da):53,365
Last modified:October 17, 2006 - v2
Checksum:i0658A1F1B9B8996A
GO
Isoform 2 (identifier: P30307-2) [UniParc]FASTAAdd to Basket

Also known as: CDC25C2

The sequence of this isoform differs from the canonical sequence as follows:
     124-153: Missing.

Show »
Length:443
Mass (Da):50,122
Checksum:i11480DF49B3F04DD
GO
Isoform 3 (identifier: P30307-5)

Also known as: CDC25C3

Sequence is not available
Length:
Mass (Da):
Isoform 4 (identifier: P30307-3) [UniParc]FASTAAdd to Basket

Also known as: CDC25C4

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD

Note: Contains a phosphoserine at position 61.

Show »
Length:430
Mass (Da):48,851
Checksum:iF2DDF9DB1653BCEE
GO
Isoform 5 (identifier: P30307-4) [UniParc]FASTAAdd to Basket

Also known as: CDC25C5, Cdc25Cdm

The sequence of this isoform differs from the canonical sequence as follows:
     66-123: GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQEVHLAGMNHDQHLMKCSP → SPGFFRTSGSAFSWD
     124-153: Missing.

Note: Contains a phosphoserine at position 61.

Show »
Length:400
Mass (Da):45,608
Checksum:i212EA5FD75672289
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141S → N.
Corresponds to variant rs11567959 [ dbSNP | Ensembl ].
VAR_027922
Natural varianti70 – 701R → C.3 Publications
Corresponds to variant rs3734166 [ dbSNP | Ensembl ].
VAR_027923
Natural varianti78 – 781S → N.
Corresponds to variant rs11567962 [ dbSNP | Ensembl ].
VAR_027924
Natural varianti297 – 2971G → R.
Corresponds to variant rs11567997 [ dbSNP | Ensembl ].
VAR_020146

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei66 – 12358GTPKR…MKCSP → SPGFFRTSGSAFSWD in isoform 4 and isoform 5. VSP_000863Add
BLAST
Alternative sequencei124 – 15330Missing in isoform 2 and isoform 5. VSP_000864Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34065 mRNA. Translation: AAA35666.1.
AJ304504 mRNA. Translation: CAC19192.1.
AY497474 Genomic DNA. Translation: AAR32098.1.
CH471062 Genomic DNA. Translation: EAW62145.1.
CH471062 Genomic DNA. Translation: EAW62149.1.
BC019089 mRNA. Translation: AAH19089.1.
AF277723 mRNA. Translation: AAG41885.1.
AF277725 mRNA. Translation: AAG41887.1.
AF277726 mRNA. Translation: AAG41888.1.
AF312681 mRNA. Translation: AAL26835.1.
CCDSiCCDS4202.1. [P30307-1]
CCDS4203.1. [P30307-4]
PIRiI59168. A38874.
RefSeqiNP_001274511.1. NM_001287582.1. [P30307-1]
NP_001781.2. NM_001790.4. [P30307-1]
NP_073720.1. NM_022809.3. [P30307-4]
UniGeneiHs.656.

Genome annotation databases

EnsembliENST00000323760; ENSP00000321656; ENSG00000158402. [P30307-1]
ENST00000348983; ENSP00000345205; ENSG00000158402. [P30307-4]
ENST00000356505; ENSP00000348898; ENSG00000158402. [P30307-2]
ENST00000357274; ENSP00000349821; ENSG00000158402. [P30307-3]
ENST00000415130; ENSP00000392631; ENSG00000158402. [P30307-4]
ENST00000513970; ENSP00000424795; ENSG00000158402. [P30307-1]
ENST00000514555; ENSP00000425470; ENSG00000158402. [P30307-2]
GeneIDi995.
KEGGihsa:995.
UCSCiuc003lcp.1. human. [P30307-1]
uc003lcq.1. human. [P30307-4]

Polymorphism databases

DMDMi116242631.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M34065 mRNA. Translation: AAA35666.1 .
AJ304504 mRNA. Translation: CAC19192.1 .
AY497474 Genomic DNA. Translation: AAR32098.1 .
CH471062 Genomic DNA. Translation: EAW62145.1 .
CH471062 Genomic DNA. Translation: EAW62149.1 .
BC019089 mRNA. Translation: AAH19089.1 .
AF277723 mRNA. Translation: AAG41885.1 .
AF277725 mRNA. Translation: AAG41887.1 .
AF277726 mRNA. Translation: AAG41888.1 .
AF312681 mRNA. Translation: AAL26835.1 .
CCDSi CCDS4202.1. [P30307-1 ]
CCDS4203.1. [P30307-4 ]
PIRi I59168. A38874.
RefSeqi NP_001274511.1. NM_001287582.1. [P30307-1 ]
NP_001781.2. NM_001790.4. [P30307-1 ]
NP_073720.1. NM_022809.3. [P30307-4 ]
UniGenei Hs.656.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OJX X-ray 2.85 E 126-134 [» ]
3BZI X-ray 2.10 E 126-134 [» ]
3OP3 X-ray 2.63 A 270-462 [» ]
ProteinModelPortali P30307.
SMRi P30307. Positions 280-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107430. 32 interactions.
DIPi DIP-24183N.
IntActi P30307. 7 interactions.
MINTi MINT-86355.
STRINGi 9606.ENSP00000321656.

Chemistry

BindingDBi P30307.
ChEMBLi CHEMBL2378.

PTM databases

PhosphoSitei P30307.

Polymorphism databases

DMDMi 116242631.

Proteomic databases

MaxQBi P30307.
PaxDbi P30307.
PRIDEi P30307.

Protocols and materials databases

DNASUi 995.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323760 ; ENSP00000321656 ; ENSG00000158402 . [P30307-1 ]
ENST00000348983 ; ENSP00000345205 ; ENSG00000158402 . [P30307-4 ]
ENST00000356505 ; ENSP00000348898 ; ENSG00000158402 . [P30307-2 ]
ENST00000357274 ; ENSP00000349821 ; ENSG00000158402 . [P30307-3 ]
ENST00000415130 ; ENSP00000392631 ; ENSG00000158402 . [P30307-4 ]
ENST00000513970 ; ENSP00000424795 ; ENSG00000158402 . [P30307-1 ]
ENST00000514555 ; ENSP00000425470 ; ENSG00000158402 . [P30307-2 ]
GeneIDi 995.
KEGGi hsa:995.
UCSCi uc003lcp.1. human. [P30307-1 ]
uc003lcq.1. human. [P30307-4 ]

Organism-specific databases

CTDi 995.
GeneCardsi GC05M137620.
HGNCi HGNC:1727. CDC25C.
HPAi CAB003800.
MIMi 157680. gene.
neXtProti NX_P30307.
PharmGKBi PA100.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5105.
HOVERGENi HBG052501.
InParanoidi P30307.
KOi K05867.
OMAi TVSLCDI.
OrthoDBi EOG7288R1.
PhylomeDBi P30307.
TreeFami TF101056.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
Reactomei REACT_1006. Polo-like kinase mediated events.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_2101. Cyclin B2 mediated events.
REACT_407. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_6769. Activation of ATR in response to replication stress.

Miscellaneous databases

ChiTaRSi CDC25C. human.
EvolutionaryTracei P30307.
GeneWikii CDC25C.
GenomeRNAii 995.
NextBioi 4178.
PROi P30307.
SOURCEi Search...

Gene expression databases

ArrayExpressi P30307.
Bgeei P30307.
CleanExi HS_CDC25C.
Genevestigatori P30307.

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. 2 hits.
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. "Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2."
    Sadhu K., Reed B.I., Richardson H., Russell P.
    Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-70.
  2. "An additional transcript of the cdc25C gene from A431 cells encodes a functional protein."
    Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P.
    Int. J. Oncol. 17:1251-1258(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  3. NIEHS SNPs program
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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), VARIANT CYS-70.
    Tissue: Skin.
  6. "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 32-210 (ISOFORMS 2; 4 AND 5), VARIANT CYS-70.
  7. "Differential expression of cdc25 cell-cycle-activating phosphatases in human colorectal carcinoma."
    Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C., Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.
    Lab. Invest. 81:465-473(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    Tissue: Colon carcinoma.
  8. "Activation of p34cdc2 protein kinase by microinjection of human cdc25C into mammalian cells. Requirement for prior phosphorylation of cdc25C by p34cdc2 on sites phosphorylated at mitosis."
    Strausfeld U., Fernandez A., Capony J.P., Girard F., Lautredou N., Derancourt J., Labbe J.C., Lamb N.J.
    J. Biol. Chem. 269:5989-6000(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-48; THR-67; SER-122; THR-130; SER-168 AND SER-214.
  9. "The physical association and phosphorylation of Cdc25C protein phosphatase by Prk."
    Ouyang B., Li W., Pan H., Meadows J., Hoffmann I., Dai W.
    Oncogene 18:6029-6036(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PLK3.
  10. "The human polo-like kinase, PLK, regulates cdc2/cyclin B through phosphorylation and activation of the cdc25C phosphatase."
    Roshak A.K., Capper E.A., Imburgia C., Fornwald J., Scott G., Marshall L.A.
    Cell. Signal. 12:405-411(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PLK1.
  11. "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase."
    Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V., Potapova O., Appella E., Fornace A.J. Jr.
    Nature 411:102-107(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-216, INTERACTION WITH MAPK14 AND 14-3-3 PROTEINS.
  12. "Proteomic screen finds pSer/pThr-binding domain localizing Plk1 to mitotic substrates."
    Elia A.E., Cantley L.C., Yaffe M.B.
    Science 299:1228-1231(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLK1, MUTAGENESIS OF SER-129 AND THR-130.
  13. "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function."
    Lu R., Niida H., Nakanishi M.
    J. Biol. Chem. 279:31164-31170(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-216.
    Tissue: Testis.
  14. "Cdc25C phosphorylation on serine 191 by Plk3 promotes its nuclear translocation."
    Bahassi el M., Hennigan R.F., Myer D.L., Stambrook P.J.
    Oncogene 23:2658-2663(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-191 AND SER-198, MUTAGENESIS OF SER-191.
  15. "The human immunodeficiency virus Vpr protein binds Cdc25C: implications for G2 arrest."
    Goh W.C., Manel N., Emerman M.
    Virology 318:337-349(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 VPR, MUTAGENESIS OF GLU-352 AND LYS-359.
  16. "MAPKAP kinase-2 is a cell cycle checkpoint kinase that regulates the G2/M transition and S phase progression in response to UV irradiation."
    Manke I.A., Nguyen A., Lim D., Stewart M.Q., Elia A.E., Yaffe M.B.
    Mol. Cell 17:37-48(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-216 BY MAPKAPK2.
  17. "Human Plk4 phosphorylates Cdc25C."
    Bonni S., Ganuelas M.L., Petrinac S., Hudson J.W.
    Cell Cycle 7:545-547(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PLK4.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-168 AND SER-472, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 (ISOFORMS 4 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57; SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-64 AND THR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMPIP3_HUMAN
AccessioniPrimary (citable) accession number: P30307
Secondary accession number(s): D3DQB8
, Q96PL3, Q9H168, Q9H2E8, Q9H2E9, Q9H2F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 152 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 5
    Human chromosome 5: 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

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