GENTAUR Molecular Products.
Monoclonal Antibody, ELISA Kit, Polyclonal Antibody, Recombinant/Purified Protein.Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery
Dual specificity phosphatase Cdc25 (EC 3.1.3.48) (Arath;CDC25) (Arsenate reductase) (AtASR) (Arsenate reductase 2) (EC 1.20.4.1) (Sulfurtransferase 5) (AtStr5)
CDC25_ARATH Reviewed; 146 AA.
Q8GY31; Q8LC90; Q9LZE1;
29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 111.
RecName: Full=Dual specificity phosphatase Cdc25 {ECO:0000303|PubMed:15329414};
EC=3.1.3.48 {ECO:0000269|PubMed:15329414};
AltName: Full=Arath;CDC25 {ECO:0000303|PubMed:15329414};
AltName: Full=Arsenate reductase {ECO:0000303|PubMed:16507083};
Short=AtASR {ECO:0000303|PubMed:16507083};
AltName: Full=Arsenate reductase 2 {ECO:0000303|PubMed:16567632};
EC=1.20.4.1 {ECO:0000269|PubMed:16766666};
AltName: Full=Sulfurtransferase 5 {ECO:0000303|PubMed:17408957};
Short=AtStr5 {ECO:0000303|PubMed:17408957};
Name=CDC25 {ECO:0000303|PubMed:15329414};
Synonyms=ACR2 {ECO:0000303|PubMed:16567632},
ASR {ECO:0000303|PubMed:16507083}, STR5 {ECO:0000303|PubMed:17408957};
OrderedLocusNames=At5g03455 {ECO:0000312|Araport:AT5G03455};
ORFNames=F12E4_220 {ECO:0000312|EMBL:CAB83305.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
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]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=11910074; DOI=10.1126/science.1071006;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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).
[5]
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.
[6]
TISSUE SPECIFICITY.
PubMed=15720653; DOI=10.1111/j.1469-8137.2004.01288.x;
Sorrell D.A., Chrimes D., Dickinson J.R., Rogers H.J., Francis D.;
"The Arabidopsis CDC25 induces a short cell length when overexpressed
in fission yeast: evidence for cell cycle function.";
New Phytol. 165:425-428(2005).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16507083; DOI=10.1111/j.1365-313X.2005.02651.x;
Bleeker P.M., Hakvoort H.W., Bliek M., Souer E., Schat H.;
"Enhanced arsenate reduction by a CDC25-like tyrosine phosphatase
explains increased phytochelatin accumulation in arsenate-tolerant
Holcus lanatus.";
Plant J. 45:917-929(2006).
[8]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=16766666; DOI=10.1104/pp.106.084079;
Ellis D.R., Gumaelius L., Indriolo E., Pickering I.J., Banks J.A.,
Salt D.E.;
"A novel arsenate reductase from the arsenic hyperaccumulating fern
Pteris vittata.";
Plant Physiol. 141:1544-1554(2006).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16567632; DOI=10.1073/pnas.0509770102;
Dhankher O.P., Rosen B.P., McKinney E.C., Meagher R.B.;
"Hyperaccumulation of arsenic in the shoots of Arabidopsis silenced
for arsenate reductase (ACR2).";
Proc. Natl. Acad. Sci. U.S.A. 103:5413-5418(2006).
[10]
GENE FAMILY.
PubMed=17408957; DOI=10.1016/j.plaphy.2007.02.005;
Bartels A., Mock H.P., Papenbrock J.;
"Differential expression of Arabidopsis sulfurtransferases under
various growth conditions.";
Plant Physiol. Biochem. 45:178-187(2007).
[11]
DISRUPTION PHENOTYPE.
PubMed=20647223; DOI=10.1093/aob/mcq142;
Spadafora N.D., Doonan J.H., Herbert R.J., Bitonti M.B., Wallace E.,
Rogers H.J., Francis D.;
"Arabidopsis T-DNA insertional lines for CDC25 are hypersensitive to
hydroxyurea but not to zeocin or salt stress.";
Ann. Bot. 107:1183-1192(2011).
[12]
3D-STRUCTURE MODELING, AND FUNCTION.
PubMed=22562211; DOI=10.1007/s00894-012-1419-y;
Nahar N., Rahman A., Mos M., Warzecha T., Algerin M., Ghosh S.,
Johnson-Brousseau S., Mandal A.;
"In silico and in vivo studies of an Arabidopsis thaliana gene, ACR2,
putatively involved in arsenic accumulation in plants.";
J. Mol. Model. 18:4249-4262(2012).
[13]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=22879969; DOI=10.1371/journal.pone.0042408;
Liu W., Schat H., Bliek M., Chen Y., McGrath S.P., George G.,
Salt D.E., Zhao F.J.;
"Knocking out ACR2 does not affect arsenic redox status in Arabidopsis
thaliana: implications for as detoxification and accumulation in
plants.";
PLoS ONE 7:E42408-E42408(2012).
[14]
DISRUPTION PHENOTYPE.
PubMed=25099865; DOI=10.1038/ncomms5617;
Sanchez-Bermejo E., Castrillo G., del Llano B., Navarro C.,
Zarco-Fernandez S., Martinez-Herrera D.J., Leo-del Puerto Y.,
Munoz R., Camara C., Paz-Ares J., Alonso-Blanco C., Leyva A.;
"Natural variation in arsenate tolerance identifies an arsenate
reductase in Arabidopsis thaliana.";
Nat. Commun. 5:4617-4617(2014).
[15]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25464340; DOI=10.1371/journal.pbio.1002009;
Chao D.Y., Chen Y., Chen J., Shi S., Chen Z., Wang C., Danku J.M.,
Zhao F.J., Salt D.E.;
"Genome-wide association mapping identifies a new arsenate reductase
enzyme critical for limiting arsenic accumulation in plants.";
PLoS Biol. 12:E1002009-E1002009(2014).
[16]
STRUCTURE BY NMR OF 15-146 OF CYS-145 IN COMPLEX WITH ZINC,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-145.
PubMed=15336525; DOI=10.1016/j.bbrc.2004.07.182;
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).
[17]
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.
PubMed=15329414; DOI=10.1073/pnas.0405248101;
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).
[18]
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).
-!- FUNCTION: Tyrosine protein phosphatase that dephosphorylates CDK
complex and activate its kinase activity in vitro.
{ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:16766666}.
-!- FUNCTION: Arsenate reductase that plays a major role in the
reduction of arsenate to arsenite and arsenic retention in roots
(PubMed:16567632). Has an in vitro and in vivo arsenate reductase
activity (PubMed:16507083, PubMed:16766666, PubMed:22562211).
Plays no role in arsenic metabolism (PubMed:22879969,
PubMed:25464340). {ECO:0000269|PubMed:16507083,
ECO:0000269|PubMed:16567632, ECO:0000269|PubMed:16766666,
ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25464340}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000269|PubMed:15329414}.
-!- CATALYTIC ACTIVITY: Arsenate + glutaredoxin = arsenite +
glutaredoxin disulfide + H(2)O. {ECO:0000269|PubMed:16766666}.
-!- ENZYME REGULATION: Inhibited by NSC95397.
{ECO:0000269|PubMed:15329414}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=50 mM for para-nitrophenyl phosphate
{ECO:0000269|PubMed:15329414, ECO:0000269|PubMed:15336525};
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in roots and at lower levels in
shoots (at protein level). Expressed in leaves, stems and flowers.
{ECO:0000269|PubMed:15720653, ECO:0000269|PubMed:16567632,
ECO:0000269|PubMed:22879969}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but plants show reduced root size when grown in
presence of hydroxyurea (PubMed:20647223). No visible phenotype,
but decreased accumulation of total arsenic in shoots
(PubMed:16507083). No effect on arsenate sensitivity
(PubMed:25099865). No effect on the accumulation of arsenate in
roots, efflux of arsenite or uptake of arsenate, or the total
arsenic accumulation in shoots (PubMed:22879969, PubMed:25464340).
{ECO:0000269|PubMed:16507083, ECO:0000269|PubMed:20647223,
ECO:0000269|PubMed:22879969, ECO:0000269|PubMed:25099865,
ECO:0000269|PubMed:25464340}.
-!- MISCELLANEOUS: Binds 1 zinc ion which is not required for enzyme
activity (PubMed:15329414). Plants silencing ACR2 show increased
sensitivity to arsenate but not arsenite (PubMed:16567632).
{ECO:0000305|PubMed:15329414, ECO:0000305|PubMed:16567632}.
-!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM63780.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB83305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AL162751; CAB83305.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED90607.1; -; Genomic_DNA.
EMBL; AK117898; BAC42537.1; -; mRNA.
EMBL; BT003658; AAO39886.1; -; mRNA.
EMBL; AY086729; AAM63780.1; ALT_INIT; mRNA.
PIR; T48370; T48370.
RefSeq; NP_568119.1; NM_120425.3.
UniGene; At.43043; -.
PDB; 1T3K; NMR; -; A=15-146.
PDBsum; 1T3K; -.
DisProt; DP00916; -.
ProteinModelPortal; Q8GY31; -.
SMR; Q8GY31; -.
BioGrid; 17108; 3.
IntAct; Q8GY31; 3.
STRING; 3702.AT5G03455.1; -.
PaxDb; Q8GY31; -.
EnsemblPlants; AT5G03455.1; AT5G03455.1; AT5G03455.
GeneID; 831832; -.
Gramene; AT5G03455.1; AT5G03455.1; AT5G03455.
KEGG; ath:AT5G03455; -.
Araport; AT5G03455; -.
TAIR; locus:505006579; AT5G03455.
eggNOG; ENOG410IQGW; Eukaryota.
eggNOG; ENOG4111VH0; LUCA.
HOGENOM; HOG000162894; -.
InParanoid; Q8GY31; -.
KO; K18065; -.
OMA; DYIGGHI; -.
OrthoDB; EOG09360QPX; -.
PhylomeDB; Q8GY31; -.
BioCyc; ARA:AT5G03455-MONOMER; -.
SABIO-RK; Q8GY31; -.
EvolutionaryTrace; Q8GY31; -.
PRO; PR:Q8GY31; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8GY31; baseline and differential.
Genevisible; Q8GY31; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0008794; F:arsenate reductase (glutaredoxin) activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:TAIR.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
GO; GO:0046685; P:response to arsenic-containing substance; IMP:TAIR.
Gene3D; 3.40.250.10; -; 1.
InterPro; IPR001763; Rhodanese-like_dom.
InterPro; IPR036873; Rhodanese-like_dom_sf.
Pfam; PF00581; Rhodanese; 1.
SMART; SM00450; RHOD; 1.
SUPFAM; SSF52821; SSF52821; 1.
PROSITE; PS50206; RHODANESE_3; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Hydrolase;
Metal-binding; Mitosis; Nucleus; Oxidoreductase; Protein phosphatase;
Reference proteome; Zinc.
CHAIN 1 146 Dual specificity phosphatase Cdc25.
/FTId=PRO_0000198663.
DOMAIN 34 135 Rhodanese. {ECO:0000255|PROSITE-
ProRule:PRU00173}.
REGION 45 48 Substrate-binding.
REGION 68 71 Substrate-binding.
REGION 90 92 Substrate-binding.
COMPBIAS 11 14 Poly-Lys.
ACT_SITE 86 86 Cysteine persulfide intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00173}.
METAL 53 53 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 134 134 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 136 136 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
METAL 141 141 Zinc. {ECO:0000269|PubMed:15329414,
ECO:0000269|PubMed:15336525}.
MUTAGEN 86 86 C->S: Loss of phosphatase activity.
{ECO:0000269|PubMed:15329414}.
MUTAGEN 145 145 C->S: No major structural changes.
{ECO:0000269|PubMed:15336525}.
STRAND 19 24 {ECO:0000244|PDB:1T3K}.
TURN 26 31 {ECO:0000244|PDB:1T3K}.
STRAND 38 44 {ECO:0000244|PDB:1T3K}.
HELIX 47 50 {ECO:0000244|PDB:1T3K}.
STRAND 56 60 {ECO:0000244|PDB:1T3K}.
STRAND 63 66 {ECO:0000244|PDB:1T3K}.
HELIX 69 74 {ECO:0000244|PDB:1T3K}.
STRAND 81 87 {ECO:0000244|PDB:1T3K}.
STRAND 90 92 {ECO:0000244|PDB:1T3K}.
HELIX 93 106 {ECO:0000244|PDB:1T3K}.
STRAND 107 109 {ECO:0000244|PDB:1T3K}.
STRAND 113 121 {ECO:0000244|PDB:1T3K}.
HELIX 124 129 {ECO:0000244|PDB:1T3K}.
SEQUENCE 146 AA; 16450 MW; EA2DD0E79784D538 CRC64;
MGRSIFSFFT KKKKMAMARS ISYITSTQLL PLHRRPNIAI IDVRDEERNY DGHIAGSLHY
ASGSFDDKIS HLVQNVKDKD TLVFHCALSQ VRGPTCARRL VNYLDEKKED TGIKNIMILE
RGFNGWEASG KPVCRCAEVP CKGDCA
Related products :
GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45
Fax 0032 16 50 90 45
info@gentaur.com | Gentaur
GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur
GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50
Fax 01 43 25 01 60
RCS Paris B 484 237 888
SIRET 48423788800017
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
france@gentaur.com | Gentaur
GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88
Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur
GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com
Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123
GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel: 0208-080893 Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62 SWIFT RABONL2U
GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur
ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF
GENTAUR Poland Sp. z o.o.
ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX 058 710 33 48
poland@gentaur.com | Gentaur
Other countries
Österreich +43720880899
Canada Montreal +15149077481
Ceská republika Praha +420246019719
Danmark +4569918806
Finland Helsset +358942419041
Magyarország Budapest +3619980547
Ireland Dublin+35316526556
Luxembourg+35220880274
Norge Oslo+4721031366
Sverige Stockholm+46852503438
Schweiz Züri+41435006251
US New York+17185132983
GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo
Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur
Pathways :
WP1006: metapathway biotransformation
WP1124: metapathway biotransformation
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1337: MAPK signaling pathway
WP1348: Androgen Receptor Signaling Pathway
WP1378: Senescence and Autophagy
WP1393: Cell cycle
WP1403: AMPK signaling
WP1461: Photosynthetic Carbon Reduction
WP1566: Citrate cycle (TCA cycle)
WP1626: Benzoate degradation via CoA ligation
WP1634: Butanoate metabolism
WP1680: Oxidative phosphorylation
WP1681: Pantothenate and CoA biosynthesis
WP2230: Chlorophyll b degradation
WP2248: anthocyanin biosynthesis
WP2368: HMG-CoA reductase pathway
WP237: Glucocorticoid & Mineralcorticoid Metabolism
WP2409: New Pathway
WP305: Glucocorticoid Metabolism
WP495: Glucocorticoid & Mineralcorticoid Metabolism
WP668: Octadecanoid Pathway
WP702: metapathway biotransformation
Related Genes :
[DUSP26 DUSP24 LDP4 MKP8 NATA1 SKRP3] Dual specificity protein phosphatase 26 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP3) (Low-molecular-mass dual-specificity phosphatase 4) (DSP-4) (LDP-4) (Mitogen-activated protein kinase phosphatase 8) (MAP kinase phosphatase 8) (MKP-8) (Novel amplified gene in thyroid anaplastic cancer)
[DUSP19 DUSP17 LMWDSP3 SKRP1] Dual specificity protein phosphatase 19 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase TS-DSP1) (Low molecular weight dual specificity phosphatase 3) (LMW-DSP3) (Protein phosphatase SKRP1) (Stress-activated protein kinase pathway-regulating phosphatase 1) (SAPK pathway-regulating phosphatase 1)
[DUSP13 DUSP13B TMDP] Dual specificity protein phosphatase 13 isoform B (DUSP13B) (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP4) (Testis- and skeletal-muscle-specific DSP)
[DUSP5 VH3] Dual specificity protein phosphatase 5 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase hVH3)
[DUSP22 JSP1 LMWDSP2 MKPX] Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (JNK-stimulatory phosphatase-1) (JSP-1) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2) (Mitogen-activated protein kinase phosphatase x) (MAP kinase phosphatase x) (MKP-x)
[DUSP18 LMWDSP20] Dual specificity protein phosphatase 18 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 20) (LMW-DSP20)
[DUSP7 PYST2] Dual specificity protein phosphatase 7 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST2)
[DUSP3 VHR] Dual specificity protein phosphatase 3 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase VHR) (Vaccinia H1-related phosphatase) (VHR)
[DUSP12] Dual specificity protein phosphatase 12 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity tyrosine phosphatase YVH1)
[DUSP23 LDP3 VHZ] Dual specificity protein phosphatase 23 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular mass dual specificity phosphatase 3) (LDP-3) (VH1-like phosphatase Z)
[DUSP15 C20orf57 VHY] Dual specificity protein phosphatase 15 (EC 3.1.3.16) (EC 3.1.3.48) (VH1-related member Y) (Vaccinia virus VH1-related dual-specific protein phosphatase Y)
[DUSP6 MKP3 PYST1] Dual specificity protein phosphatase 6 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PYST1) (Mitogen-activated protein kinase phosphatase 3) (MAP kinase phosphatase 3) (MKP-3)
[DUSP1 CL100 MKP1 PTPN10 VH1] Dual specificity protein phosphatase 1 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase hVH1) (Mitogen-activated protein kinase phosphatase 1) (MAP kinase phosphatase 1) (MKP-1) (Protein-tyrosine phosphatase CL100)
[Dusp15] Dual specificity protein phosphatase 15 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase T-DSP10)
[DUSP21 LMWDSP21] Dual specificity protein phosphatase 21 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 21) (LMW-DSP21)
[DUSP4 MKP2 VH2] Dual specificity protein phosphatase 4 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase hVH2) (Mitogen-activated protein kinase phosphatase 2) (MAP kinase phosphatase 2) (MKP-2)
[DYRK1A DYRK MNB MNBH] Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (HP86) (Protein kinase minibrain homolog) (MNBH) (hMNB)
[Dusp22] Dual specificity protein phosphatase 22 (EC 3.1.3.16) (EC 3.1.3.48) (Low molecular weight dual specificity phosphatase 2) (LMW-DSP2)
[Dusp12 Gkap] Dual specificity protein phosphatase 12 (EC 3.1.3.16) (EC 3.1.3.48) (Glucokinase-associated dual specificity phosphatase) (GKAP)
[Dyrk1a Dyrk] Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.2) (Dual specificity YAK1-related kinase) (Protein kinase minibrain homolog) (MNBH) (RP86)
[Dyrk1a Dyrk] Dual specificity tyrosine-phosphorylation-regulated kinase 1A (EC 2.7.12.1) (Dual specificity YAK1-related kinase) (MP86) (Protein kinase minibrain homolog) (MNBH)
[YAK1 At5g35980 MEE13.9] Dual specificity protein kinase YAK1 homolog (AtYAK1) (EC 2.7.12.1) (Dual specificity tyrosine-phosphorylation-regulated kinase YAK1)
[DUOXA2] Dual oxidase maturation factor 2 (Dual oxidase activator 2)
[DUPD1 DUSP27] Dual specificity phosphatase DUPD1 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase 27)
[Dusp2 Pac-1 Pac1] Dual specificity protein phosphatase 2 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PAC-1)
[mbk-2 F49E11.1] Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2 (EC 2.7.12.1) (Dual specificity Yak1-related kinase mbk-2) (Minibrain Kinase 2)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41); Surface protein gp120 (SU) (Glycoprotein 120) (gp120)]
[DUSP2 PAC1] Dual specificity protein phosphatase 2 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity protein phosphatase PAC-1)
[Dusp26 Skrp3] Dual specificity protein phosphatase 26 (EC 3.1.3.16) (EC 3.1.3.48) (Dual specificity phosphatase SKRP3)
[mbk-2 CBG23998] Dual specificity tyrosine-phosphorylation-regulated kinase mbk-2 (EC 2.7.12.1) (Dual specificity Yak1-related kinase mbk-2) (Minibrain Kinase 2)
Bibliography :
No related Items
Enter catalog number :
Favorites Pages:
No Favorits