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UniProtKB/Swiss-Prot entry Q8GY31


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

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Entry information
Entry name CDC25_ARATH
Primary accession number Q8GY31
Secondary accession numbers Q8LC90 Q9LZE1
Integrated into Swiss-Prot on March 29, 2005
Sequence was last modified on March 1, 2003 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 45)
Name and origin of the protein
Protein name Dual specificity phosphatase Cdc25
Synonyms EC 3.1.3.48
Arath;CDC25
Gene name
Name: CDC25
OrderedLocusNames: At5g03455
ORFNames: F12E4_220
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-145.
DOI=10.1016/j.bbrc.2004.07.182; PubMed=15336525 [NCBI, ExPASy, EBI, Israel, Japan]
Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D., de Veylder L., Lippens G.;
"Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase.";
Biochem. Biophys. Res. Commun. 322:734-739(2004).
[6]
STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-86.
DOI=10.1073/pnas.0405248101; PubMed=15329414 [NCBI, ExPASy, EBI, Israel, Japan]
Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K., Hassan S., Wieruszeski J.-M., Corellou F., Faure J.-D., Van Montagu M., Inze D., Lippens G.;
"A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 101:13380-13385(2004).
[7]
ERRATUM.
DOI=10.1073/pnas.0407263101
Landrieu I., da Costa M., de Veylder L., Dewitte F., Vandepoele K., Hassan S., Wieruszeski J.M., Corellou F., Faure J.D., Van Montagu M., Inze D., Lippens G.;
Proc. Natl. Acad. Sci. U.S.A. 101:16391-16391(2004).
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
AL162751; CAB83305.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK117898; BAC42537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT003658; AAO39886.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086729; AAM63780.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T48370; T48370.
RefSeq NP_568119.1; -.
UniGene At.43043
3D structure databases
PDB
1T3K; NMR; -; A=15-146.[ExPASy / RCSB / EBI]
PDBsum 1T3K; -.
ModBase Q8GY31.
Organism-specific databases
TAIR At5g03455; -.
Gene expression databases
ArrayExpress Q8GY31; -.
GermOnline AT5G03455; Arabidopsis thaliana.
Ontologies
GO
GO:0009507; Cellular component: chloroplast (inferred from direct assay from TAIR).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0030611; Molecular function: arsenate reductase activity (inferred from genetic interaction from TAIR).
GO:0004725; Molecular function: protein tyrosine phosphatase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0051301; Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
GO:0007067; Biological process: mitosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (inferred from direct assay from TAIR).
GO:0046685; Biological process: response to arsenic (inferred from mutant phenotype from TAIR).
QuickGo view.
Family and domain databases
InterPro IPR001763; Rhodanese-like.
IPR001307; Thiosulphate_sulphurtransf_CS.
Graphical view of domain structure.
Gene3D G3DSA:3.40.250.10; Rhodanese-like; 1.
SMART SM00450; RHOD; 1.
SMART graphical view of domain structure.
PROSITE PS50206; RHODANESE_3; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q8GY31; -.
Genome annotation databases
GeneID 831832; -.
GenomeReviews BA000015_GR; AT5G03455.
KEGG ath:AT5G03455; -.
NMPDR fig|3702.1.peg.22431; -.
Other
ProtoNet Q8GY31.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell cycle; Cell division; Complete proteome; Hydrolase; Metal-binding; Mitosis; Nucleus; Protein phosphatase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   146  146     Dual specificity phosphatase Cdc25. PRO_0000198663
DOMAIN   34   135  102     Rhodanese. 
REGION   45    48  4     Substrate-binding. 
REGION   68    71  4     Substrate-binding. 
REGION   90    92  3     Substrate-binding. 
COMPBIAS   11    14  4     Poly-Lys. 
ACT_SITE   86    86        Phosphocysteine intermediate (Probable). 
METAL   53    53        Zinc. 
METAL   134   134        Zinc. 
METAL   136   136        Zinc. 
METAL   141   141        Zinc. 
MUTAGEN   86    86        C->S: Loss of phosphatase activity. 
MUTAGEN   145   145        C->S: No major structural changes. 
STRAND   19    24  6      
TURN   26    31  6      
STRAND   38    44  7      
HELIX   47    50  4      
STRAND   56    60  5      
STRAND   63    66  4      
HELIX   69    74  6      
STRAND   81    87  7      
STRAND   90    92  3      
HELIX   93   106  14      
STRAND   107   109  3      
STRAND   113   121  9      
HELIX   124   129  6      
Sequence information
Length: 146 AA [This is the length of the unprocessed precursor] Molecular weight: 16450 Da [This is the MW of the unprocessed precursor] CRC64: EA2DD0E79784D538 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY 

        70         80         90        100        110        120 
ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE 

       130        140 
RGFNGWEASG KPVCRCAEVP CKGDCA 

Q8GY31 in FASTA format

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