SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8GY31

- CDC25_ARATH

UniProt

Q8GY31 - CDC25_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Dual specificity phosphatase Cdc25
Gene
CDC25, ACR2, STR5, At5g03455, F12E4_220
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.2 Publications
Arsenate reductase that plays a major role in the reduction of arsenate to arsenite and arsenic retention in roots.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.1 Publication

Enzyme regulationi

Inhibited by NSC95397.1 Publication

Kineticsi

  1. KM=50 mM for para-nitrophenyl phosphate2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Zinc
Active sitei86 – 861Phosphocysteine intermediate Inferred
Metal bindingi134 – 1341Zinc
Metal bindingi136 – 1361Zinc
Metal bindingi141 – 1411Zinc

GO - Molecular functioni

  1. arsenate reductase activity Source: TAIR
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: TAIR
  4. protein tyrosine phosphatase activity Source: TAIR
Complete GO annotation...

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. peptidyl-tyrosine dephosphorylation Source: GOC
  3. protein phosphorylation Source: TAIR
  4. response to arsenic-containing substance Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Oxidoreductase, Protein phosphatase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G03455-MONOMER.
SABIO-RKQ8GY31.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity phosphatase Cdc25 (EC:3.1.3.48)
Alternative name(s):
Arath;CDC25
Arsenate reductase 2 (EC:1.20.4.-)
Sulfurtransferase 5
Short name:
AtStr5
Gene namesi
Name:CDC25
Synonyms:ACR2, STR5
Ordered Locus Names:At5g03455
ORF Names:F12E4_220
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G03455.

Subcellular locationi

Nucleus Inferred

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. mitochondrion Source: TAIR
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but plants show reduced root size when grown in presence of hydroxyurea.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861C → S: Loss of phosphatase activity. 1 Publication
Mutagenesisi145 – 1451C → S: No major structural changes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 146146Dual specificity phosphatase Cdc25
PRO_0000198663Add
BLAST

Proteomic databases

PaxDbiQ8GY31.
PRIDEiQ8GY31.

Expressioni

Tissue specificityi

Expressed in roots and at lower levels in shoots (at protein level). Expressed in leaves, stems and flowers.2 Publications

Gene expression databases

GenevestigatoriQ8GY31.

Interactioni

Protein-protein interaction databases

BioGridi17108. 3 interactions.
IntActiQ8GY31. 3 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 246
Turni26 – 316
Beta strandi38 – 447
Helixi47 – 504
Beta strandi56 – 605
Beta strandi63 – 664
Helixi69 – 746
Beta strandi81 – 877
Beta strandi90 – 923
Helixi93 – 10614
Beta strandi107 – 1093
Beta strandi113 – 1219
Helixi124 – 1296

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T3KNMR-A15-146[»]
ProteinModelPortaliQ8GY31.
SMRiQ8GY31. Positions 15-146.

Miscellaneous databases

EvolutionaryTraceiQ8GY31.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 135102Rhodanese
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 484Substrate-binding
Regioni68 – 714Substrate-binding
Regioni90 – 923Substrate-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 144Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG294009.
HOGENOMiHOG000162894.
InParanoidiQ8GY31.
KOiK18065.
OMAiRSISYIT.
PhylomeDBiQ8GY31.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8GY31-1 [UniParc]FASTAAdd to Basket

« Hide

MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY    50
DGHIAGSLHY ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL 100
VNYLDEKKED TGIKNIMILE RGFNGWEASG KPVCRCAEVP CKGDCA 146
Length:146
Mass (Da):16,450
Last modified:March 1, 2003 - v1
Checksum:iEA2DD0E79784D538
GO

Sequence cautioni

The sequence AAM63780.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAB83305.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL162751 Genomic DNA. Translation: CAB83305.1. Sequence problems.
CP002688 Genomic DNA. Translation: AED90607.1.
AK117898 mRNA. Translation: BAC42537.1.
BT003658 mRNA. Translation: AAO39886.1.
AY086729 mRNA. Translation: AAM63780.1. Different initiation.
PIRiT48370.
RefSeqiNP_568119.1. NM_120425.2.
UniGeneiAt.43043.

Genome annotation databases

EnsemblPlantsiAT5G03455.1; AT5G03455.1; AT5G03455.
GeneIDi831832.
KEGGiath:AT5G03455.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL162751 Genomic DNA. Translation: CAB83305.1 . Sequence problems.
CP002688 Genomic DNA. Translation: AED90607.1 .
AK117898 mRNA. Translation: BAC42537.1 .
BT003658 mRNA. Translation: AAO39886.1 .
AY086729 mRNA. Translation: AAM63780.1 . Different initiation.
PIRi T48370.
RefSeqi NP_568119.1. NM_120425.2.
UniGenei At.43043.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T3K NMR - A 15-146 [» ]
ProteinModelPortali Q8GY31.
SMRi Q8GY31. Positions 15-146.
ModBasei Search...

Protein-protein interaction databases

BioGridi 17108. 3 interactions.
IntActi Q8GY31. 3 interactions.

Proteomic databases

PaxDbi Q8GY31.
PRIDEi Q8GY31.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G03455.1 ; AT5G03455.1 ; AT5G03455 .
GeneIDi 831832.
KEGGi ath:AT5G03455.

Organism-specific databases

TAIRi AT5G03455.

Phylogenomic databases

eggNOGi NOG294009.
HOGENOMi HOG000162894.
InParanoidi Q8GY31.
KOi K18065.
OMAi RSISYIT.
PhylomeDBi Q8GY31.

Enzyme and pathway databases

BioCyci ARA:AT5G03455-MONOMER.
SABIO-RK Q8GY31.

Miscellaneous databases

EvolutionaryTracei Q8GY31.

Gene expression databases

Genevestigatori Q8GY31.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR001763. Rhodanese-like_dom.
[Graphical view ]
Pfami PF00581. Rhodanese. 1 hit.
[Graphical view ]
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. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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].
  6. "The Arabidopsis CDC25 induces a short cell length when overexpressed in fission yeast: evidence for cell cycle function."
    Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.
    New Phytol. 165:425-428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. "Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced for arsenate reductase (ACR2)."
    Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.
    Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  8. "Differential expression of Arabidopsis sulfurtransferases under various growth conditions."
    Bartels A., Mock H.P., Papenbrock J.
    Plant Physiol. Biochem. 45:178-187(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY.
  9. "Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to hydroxyurea but not to zeocin or salt stress."
    Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E., Rogers H.J., Francis D.
    Ann. Bot. 107:1183-1192(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "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] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-145.
  11. 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.

Entry informationi

Entry nameiCDC25_ARATH
AccessioniPrimary (citable) accession number: Q8GY31
Secondary accession number(s): Q8LC90, Q9LZE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds 1 zinc ion which is not required for enzyme activity (1 Publication). Plants silencing ACR2 show increased sensitivity to arsenate but not arsenite (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi