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Reviewed, UniProtKB/Swiss-Prot Q8GY31 (CDC25_ARATH)

Last modified February 9, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dual specificity phosphatase Cdc25
    EC=3.1.3.48
Alternative name(s):
    Arath;CDC25
Gene names
Name: CDC25
Ordered Locus Names: At5g03455
ORF Names: F12E4_220
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length146 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity. Ref.6

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.6

Enzyme regulation

Inhibited by NSC95397. Ref.6

Subcellular location

Nucleus Probable.

Miscellaneous

Binds 1 zinc ion which is not required for enzyme activity.

Sequence similarities

Belongs to the MPI phosphatase family.

Contains 1 rhodanese domain.

Biophysicochemical properties

Kinetic parameters:

KM=50 mM for para-nitrophenyl phosphate

Sequence caution

The sequence CAB83305.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 146146Dual specificity phosphatase Cdc25
PRO_0000198663

Regions

Domain34 – 135102Rhodanese
Region45 – 484Substrate-binding
Region68 – 714Substrate-binding
Region90 – 923Substrate-binding
Compositional bias11 – 144Poly-Lys

Sites

Active site861Phosphocysteine intermediate Probable
Metal binding531Zinc
Metal binding1341Zinc
Metal binding1361Zinc
Metal binding1411Zinc

Experimental info

Mutagenesis861C → S: Loss of phosphatase activity. Ref.6
Mutagenesis1451C → S: No major structural changes. Ref.5

Secondary structure

......................... 146
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8GY31-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EA2DD0E79784D538

FASTA14616,450
        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:823-826(2000) [PubMed: 11130714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Functional annotation of a full-length Arabidopsis cDNA collection."
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.
Science 296:141-145(2002) [PubMed: 11910074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed: 14593172] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Characterization of the Arabidopsis thaliana Arath;CDC25 dual-specificity tyrosine phosphatase."
Landrieu I., Hassan S., Sauty M., Dewitte F., Wieruszeski J.-M., Inze D., de Veylder L., Lippens G.
Biochem. Biophys. Res. Commun. 322:734-739(2004) [PubMed: 15336525] [Abstract]
Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-145.
[6]"A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana."
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. 101:13380-13385(2004) [PubMed: 15329414] [Abstract]
Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-86 MUTANT IN COMPLEX WITH ZINC, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-86.
[7]Erratum
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)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL162751 Genomic DNA. Translation: CAB83305.1. Sequence problems.
AK117898 mRNA. Translation: BAC42537.1.
BT003658 mRNA. Translation: AAO39886.1.
AY086729 mRNA. Translation: AAM63780.1. Different initiation.
IPIIPI00542538.
PIRT48370.
RefSeqNP_568119.1.
UniGeneAt.43043
Rra.26784
Rsa.15200

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3KNMR-A15-146[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8GY31.

Proteomic databases

PRIDEQ8GY31.

Genome annotation databases

GeneID831832.
GenomeReviewsGene locus AT5G03455 in contig BA000015_GR.
KEGGath:AT5G03455.
NMPDRfig|3702.1.peg.22431.

Organism-specific databases

TAIRAt5g03455.

Phylogenomic databases

eggNOGKOG3772.
HOGENOMHBG587364.
InParanoidQ8GY31.
OMARGPTCAR.
PhylomeDBQ8GY31.

Enzyme and pathway databases

BRENDA3.1.3.48. 302.

Gene expression databases

ArrayExpressQ8GY31.
GenevestigatorQ8GY31.
GermOnlineAT5G03455. Arabidopsis thaliana.

Family and domain databases

InterProIPR001763. Rhodanese-like.
[Graphical view]
Gene3DG3DSA:3.40.250.10. Rhodanese-like. 1 hit.
PfamPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTSM00450. RHOD. 1 hit.
[Graphical view]
PROSITEPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDC25_ARATH
AccessionPrimary (citable) accession number: Q8GY31
Secondary accession number(s): Q8LC90, Q9LZE1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 1, 2003
Last modified: February 9, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents