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UniProtKB/Swiss-Prot entry P30307


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MPIP3_HUMAN
Primary accession number P30307
Secondary accession numbers Q96PL3 Q9H168 Q9H2E8 Q9H2E9 Q9H2F1
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on October 17, 2006 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 97)
Name and origin of the protein
Protein name M-phase inducer phosphatase 3
Synonyms EC 3.1.3.48
Dual specificity phosphatase Cdc25C
Gene name
Name: CDC25C
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-70.
DOI=10.1073/pnas.87.13.5139; PubMed=2195549 [NCBI, ExPASy, EBI, Israel, Japan]
Sadhu K., Reed B.I., Richardson H., Russell P.;
"Human homolog of fission yeast cdc25 mitotic inducer is predominantly expressed in G2.";
Proc. Natl. Acad. Sci. U.S.A. 87:5139-5143(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
PubMed=11078813 [NCBI, ExPASy, EBI, Israel, Japan]
Bureik M., Rief N., Drescher R., Jungbluth A., Montenarh M., Wagner P.;
"An additional transcript of the cdc25C gene from A431 cells encodes a functional protein.";
Int. J. Oncol. 17:1251-1258(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-70.
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-210 (ISOFORMS 2; 4 AND 5), AND VARIANT CYS-70.
DOI=10.1078/0171-9335-00115; PubMed=11139144 [NCBI, ExPASy, EBI, Israel, Japan]
Wegener S., Hampe W., Herrmann D., Schaller H.C.;
"Alternative splicing in the regulatory region of the human phosphatases CDC25A and CDC25C.";
Eur. J. Cell Biol. 79:810-815(2000).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
TISSUE=Colon carcinoma;
PubMed=11304565 [NCBI, ExPASy, EBI, Israel, Japan]
Hernandez S., Bessa X., Bea S., Hernandez L., Nadal A., Mallofre C., Muntane J., Castells A., Fernandez P.L., Cardesa A., Campo E.;
"Differential expression of cdc25 cell-cycle-activating phosphatases in human colorectal carcinoma.";
Lab. Invest. 81:465-473(2001).
[7]
PHOSPHORYLATION AT SER-216.
TISSUE=Testis;
DOI=10.1074/jbc.M404728200; PubMed=15150265 [NCBI, ExPASy, EBI, Israel, Japan]
Lu R., Niida H., Nakanishi M.;
"Human SAD1 kinase is involved in UV-induced DNA damage checkpoint function.";
J. Biol. Chem. 279:31164-31170(2004).
[8]
INTERACTION WITH HIV-1 VPR, AND MUTAGENESIS OF GLU-352 AND LYS-359.
DOI=10.1016/j.virol.2003.10.007; PubMed=14972559 [NCBI, ExPASy, EBI, Israel, Japan]
Goh W.C., Manel N., Emerman M.;
"The human immunodeficiency virus Vpr protein binds Cdc25C: implications for G2 arrest.";
Virology 318:337-349(2004).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-64; SER-168 AND SER-472, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-48; SER-57; SER-61; SER-64 AND THR-67, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M34065; AAA35666.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ304504; CAC19192.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY497474; AAR32098.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019089; AAH19089.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277723; AAG41885.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277725; AAG41887.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277726; AAG41888.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF312681; AAL26835.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216683; -.
IPI00216684; -.
IPI00216685; -.
IPI00640320; -.
PIR I59168; A38874.
RefSeq NP_001781.2; -.
NP_073720.1; -.
UniGene Hs.656
3D structure databases
PDB
3BZI; X-ray; 2.10 A; E=126-134.[ExPASy / RCSB / EBI]
PDBsum 3BZI; -.
ModBase P30307.
Protein-protein interaction databases
DIP DIP:24183N; -.
IntAct P30307; 4.
PTM databases
PhosphoSite P30307; -.
Enzyme and pathway databases
BRENDA 3.1.3.48; 247.
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
Organism-specific databases
GeneCards GC05M137648; -.
H-InvDB HIX0005209; -.
HGNC HGNC:1727; CDC25C.
GenAtlas CDC25C.
HPA CAB003800; -.
MIM 157680; gene. [NCBI / EBI]
PharmGKB PA100; -.
Gene expression databases
ArrayExpress P30307; -.
Bgee P30307; -.
CleanEx HS_CDC25C; -.
GermOnline ENSG00000158402; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (non-traceable author statement from UniProtKB).
GO:0050699; Molecular function: WW domain binding (inferred from physical interaction from UniProtKB).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0008283; Biological process: cell proliferation (traceable author statement from UniProtKB).
GO:0006260; Biological process: DNA replication (inferred from experiment from Reactome).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006470; Biological process: protein amino acid dephosphorylation (inferred from electronic annotation from InterPro).
GO:0000079; Biological process: regulation of cyclin-dependent protein kinase activity (traceable author statement from UniProtKB).
GO:0007088; Biological process: regulation of mitosis (traceable author statement from ProtInc).
GO:0007089; Biological process: traversing start control point of mitotic cell cycle (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000751; MPI_Phosphatase.
IPR001763; Rhodanese-like.
Graphical view of domain structure.
Gene3D G3DSA:3.40.250.10; Rhodanese-like; 1.
PANTHER PTHR10828; MPI_Phosphatase; 1.
Pfam PF06617; M-inducer_phosp; 1.
PF00581; Rhodanese; 1.
Pfam graphical view of domain structure.
PRINTS PR00716; MPIPHPHTASE.
SMART SM00450; RHOD; 1.
SMART graphical view of domain structure.
PROSITE PS50206; RHODANESE_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P30307; -.
Genome annotation databases
Ensembl ENSG00000158402; Homo sapiens. [Contig view]
GeneID 995; -.
KEGG hsa:995; -.
Phylogenomic databases
HOGENOM P30307; -.
HOVERGEN P30307; -.
OMA P30307; NKENDNG.
Other
NextBio 4178; -.
SOURCE CDC25C; Homo sapiens.
ProtoNet P30307.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell cycle; Cell division; Host-virus interaction; Hydrolase; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   473  473     M-phase inducer phosphatase 3. PRO_0000198647
DOMAIN   321   428  108     Rhodanese. 
REGION   334   379  46     HIV-1 Vpr binding site. 
ACT_SITE   377   377        By similarity. 
MOD_RES   15    15        Phosphoserine. 
MOD_RES   38    38        Phosphoserine. 
MOD_RES   48    48        Phosphothreonine. 
MOD_RES   57    57        Phosphoserine. 
MOD_RES   61    61        Phosphoserine. 
MOD_RES   64    64        Phosphoserine. 
MOD_RES   67    67        Phosphothreonine. 
MOD_RES   168   168        Phosphoserine. 
MOD_RES   216   216        Phosphoserine; by CHK1, CHK2 and BRSK1. 
MOD_RES   472   472        Phosphoserine. 
VAR_SEQ   66   123        GTPKRCLDLSNLSSGEITATQLTTSADLDETGHLDSSGLQ EVHLAGMNHDQHLMKCSP -> SPGFFRTSGSAFSWD (in isoform 4 and isoform 5). VSP_000863
VAR_SEQ   124   153        Missing (in isoform 2 and isoform 5). VSP_000864
VARIANT   14    14  1     S -> N (in dbSNP:rs11567959 [NCBI]). VAR_027922 
VARIANT   70    70  1     R -> C (in dbSNP:rs3734166 [NCBI]). VAR_027923 
VARIANT   78    78  1     S -> N (in dbSNP:rs11567962 [NCBI]). VAR_027924 
VARIANT   297   297  1     G -> R (in dbSNP:rs11567997 [NCBI]). VAR_020146 
MUTAGEN   352   352        E->K: Partial loss of HIV-1 Vpr binding. 
MUTAGEN   359   359        K->E: No effect on HIV-1 Vpr binding. 
STRAND   127   129  3      
Sequence information
Length: 473 AA [This is the length of the unprocessed precursor] Molecular weight: 53365 Da [This is the MW of the unprocessed precursor] CRC64: 0658A1F1B9B8996A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTELFSSTR EEGSSGSGPS FRSNQRKMLN LLLERDTSFT VCPDVPRTPV GKFLGDSANL 

        70         80         90        100        110        120 
SILSGGTPKR CLDLSNLSSG EITATQLTTS ADLDETGHLD SSGLQEVHLA GMNHDQHLMK 

       130        140        150        160        170        180 
CSPAQLLCST PNGLDRGHRK RDAMCSSSAN KENDNGNLVD SEMKYLGSPI TTVPKLDKNP 

       190        200        210        220        230        240 
NLGEDQAEEI SDELMEFSLK DQEAKVSRSG LYRSPSMPEN LNRPRLKQVE KFKDNTIPDK 

       250        260        270        280        290        300 
VKKKYFSGQG KLRKGLCLKK TVSLCDITIT QMLEEDSNQG HLIGDFSKVC ALPTVSGKHQ 

       310        320        330        340        350        360 
DLKYVNPETV AALLSGKFQG LIEKFYVIDC RYPYEYLGGH IQGALNLYSQ EELFNFFLKK 

       370        380        390        400        410        420 
PIVPLDTQKR IIIVFHCEFS SERGPRMCRC LREEDRSLNQ YPALYYPELY ILKGGYRDFF 

       430        440        450        460        470 
PEYMELCEPQ SYCPMHHQDH KTELLRCRSQ SKVQEGERQL REQIALLVKD MSP 

P30307 in FASTA format

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