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Protein phosphatase 2C 37 (AtPP2C37) (EC 3.1.3.16) (Protein ABA-HYPERSENSITIVE GERMINATION 3) (Protein phosphatase 2C A) (PP2CA)

 P2C37_ARATH             Reviewed;         399 AA.
P49598;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-APR-2018, entry version 142.
RecName: Full=Protein phosphatase 2C 37;
Short=AtPP2C37;
EC=3.1.3.16;
AltName: Full=Protein ABA-HYPERSENSITIVE GERMINATION 3;
AltName: Full=Protein phosphatase 2C A;
Short=PP2CA;
Name=PP2CA; Synonyms=AHG3; OrderedLocusNames=At3g11410;
ORFNames=F24K9.8;
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 [MRNA].
STRAIN=cv. Columbia;
PubMed=7816619; DOI=10.1093/nar/22.24.5296;
Kuromori T., Yamamoto M.;
"Cloning of cDNAs from Arabidopsis thaliana that encode putative
protein phosphatase 2C and a human Dr1-like protein by transformation
of a fission yeast mutant.";
Nucleic Acids Res. 22:5296-5301(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[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]
FUNCTION, AND MUTAGENESIS OF GLY-139 AND GLY-145.
PubMed=9448270; DOI=10.1073/pnas.95.3.975;
Sheen J.;
"Mutational analysis of protein phosphatase 2C involved in abscisic
acid signal transduction in higher plants.";
Proc. Natl. Acad. Sci. U.S.A. 95:975-980(1998).
[6]
INTERACTION WITH AKT2/AKT3.
PubMed=11181729; DOI=10.1093/jexbot/52.354.181;
Vranova E., Taehtiharju S., Sriprang R., Willekens H., Heino P.,
Palva E.T., Inze D., Van Camp W.;
"The AKT3 potassium channel protein interacts with the AtPP2CA protein
phosphatase 2C.";
J. Exp. Bot. 52:181-182(2001).
[7]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=11439132; DOI=10.1046/j.1365-313X.2001.01048.x;
Taehtiharju S., Palva T.;
"Antisense inhibition of protein phosphatase 2C accelerates cold
acclimation in Arabidopsis thaliana.";
Plant J. 26:461-470(2001).
[8]
FUNCTION, MUTAGENESIS OF GLY-139, TISSUE SPECIFICITY, INDUCTION BY
ABA, AND INTERACTION WITH AKT2/AKT3.
PubMed=12034902; DOI=10.1105/tpc.000943;
Cherel I., Michard E., Platet N., Mouline K., Alcon C., Sentenac H.,
Thibaud J.-B.;
"Physical and functional interaction of the Arabidopsis K(+) channel
AKT2 and phosphatase AtPP2CA.";
Plant Cell 14:1133-1146(2002).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=15130549; DOI=10.1016/j.tplants.2004.03.007;
Schweighofer A., Hirt H., Meskiene I.;
"Plant PP2C phosphatases: emerging functions in stress signaling.";
Trends Plant Sci. 9:236-243(2004).
[10]
INDUCTION BY COLD STRESS.
PubMed=16214899; DOI=10.1105/tpc.105.035568;
Lee B.-H., Henderson D.A., Zhu J.-K.;
"The Arabidopsis cold-responsive transcriptome and its regulation by
ICE1.";
Plant Cell 17:3155-3175(2005).
[11]
FUNCTION, INDUCTION BY ABA, MUTAGENESIS OF GLY-145 AND GLY-287, AND
TISSUE SPECIFICITY.
PubMed=16339800; DOI=10.1104/pp.105.070128;
Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T.,
Shinozaki K., Hirayama T.;
"ABA-hypersensitive germination3 encodes a protein phosphatase 2C
(AtPP2CA) that strongly regulates abscisic acid signaling during
germination among Arabidopsis protein phosphatase 2Cs.";
Plant Physiol. 140:115-126(2006).
[12]
FUNCTION, AND INDUCTION.
PubMed=16361522; DOI=10.1104/pp.105.070318;
Kuhn J.M., Boisson-Dernier A., Dizon M.B., Maktabi M.H.,
Schroeder J.I.;
"The protein phosphatase AtPP2CA negatively regulates abscisic acid
signal transduction in Arabidopsis, and effects of abh1 on AtPP2CA
mRNA.";
Plant Physiol. 140:127-139(2006).
[13]
FUNCTION, INDUCTION BY ABA, AND TISSUE SPECIFICITY.
PubMed=17461784; DOI=10.1111/j.1365-313X.2007.03107.x;
Nishimura N., Yoshida T., Kitahata N., Asami T., Shinozaki K.,
Hirayama T.;
"ABA-Hypersensitive Germination1 encodes a protein phosphatase 2C, an
essential component of abscisic acid signaling in Arabidopsis seed.";
Plant J. 50:935-949(2007).
[14]
GENE FAMILY, AND NOMENCLATURE.
PubMed=19021904; DOI=10.1186/1471-2164-9-550;
Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C.,
Zhong Y.;
"Genome-wide and expression analysis of protein phosphatase 2C in rice
and Arabidopsis.";
BMC Genomics 9:550-550(2008).
[15]
INDUCTION BY MYB44 AND SALT.
PubMed=18162593; DOI=10.1104/pp.107.110981;
Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H.,
Choi Y.D., Cheong J.-J.;
"Overexpression of AtMYB44 enhances stomatal closure to confer abiotic
stress tolerance in transgenic Arabidopsis.";
Plant Physiol. 146:623-635(2008).
[16]
FUNCTION, INTERACTION WITH SLAC1 AND SRK2E/OST1, AND MUTAGENESIS OF
GLY-139 AND GLY-145.
PubMed=19955427; DOI=10.1073/pnas.0910601106;
Lee S.C., Lan W., Buchanan B.B., Luan S.;
"A protein kinase-phosphatase pair interacts with an ion channel to
regulate ABA signaling in plant guard cells.";
Proc. Natl. Acad. Sci. U.S.A. 106:21419-21424(2009).
[17]
INTERACTION WITH PYR1; PYL1; PYL2; PYL3; PYL4; PYL9 AND PYL12, AND
ENZYME REGULATION.
PubMed=19407142; DOI=10.1126/science.1173041;
Park S.-Y., Fung P., Nishimura N., Jensen D.R., Fujii H., Zhao Y.,
Lumba S., Santiago J., Rodrigues A., Chow T.F., Alfred S.E.,
Bonetta D., Finkelstein R., Provart N.J., Desveaux D., Rodriguez P.L.,
McCourt P., Zhu J.-K., Schroeder J.I., Volkman B.F., Cutler S.R.;
"Abscisic acid inhibits type 2C protein phosphatases via the PYR/PYL
family of START proteins.";
Science 324:1068-1071(2009).
[18]
INTERACTION WITH CBL1; CBL2; CBL3; CBL4; CBL5; CBL6; CBL7 AND CBL9.
PubMed=21596690; DOI=10.1093/mp/ssr031;
Lan W.Z., Lee S.C., Che Y.F., Jiang Y.Q., Luan S.;
"Mechanistic analysis of AKT1 regulation by the CBL-CIPK-PP2CA
interactions.";
Mol. Plant 4:527-536(2011).
[19]
INTERACTION WITH RGLG1 AND RGLG5, AND UBIQUITINATION.
PubMed=27577789; DOI=10.1105/tpc.16.00364;
Wu Q., Zhang X., Peirats-Llobet M., Belda-Palazon B., Wang X., Cui S.,
Yu X., Rodriguez P.L., An C.;
"Ubiquitin ligases RGLG1 and RGLG5 regulate abscisic acid signaling by
controlling the turnover of phosphatase PP2CA.";
Plant Cell 0:0-0(2016).
[20]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 72-399 IN COMPLEX WITH
MAGNESIUM AND ZINC, AND INTERACTION WITH PYL13.
PubMed=24165892; DOI=10.1038/cr.2013.143;
Li W., Wang L., Sheng X., Yan C., Zhou R., Hang J., Yin P., Yan N.;
"Molecular basis for the selective and ABA-independent inhibition of
PP2CA by PYL13.";
Cell Res. 23:1369-1379(2013).
-!- FUNCTION: Major negative regulator of abscisic acid (ABA)
responses during seed germination and cold acclimation. Confers
insensitivity to ABA. Modulates negatively the AKT2/3 activity,
which mediates K(+) transport and membrane polarization during
stress situations, probably by dephosphorylation. Prevents stomata
closure by inactivating the S-type anion efflux channel SLAC1 and
its activator SRK2E. {ECO:0000269|PubMed:11439132,
ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:16339800,
ECO:0000269|PubMed:16361522, ECO:0000269|PubMed:17461784,
ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:9448270}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:24165892};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 magnesium or manganese ions per subunit.
{ECO:0000269|PubMed:24165892};
-!- ENZYME REGULATION: Repressed by PYR/PYL/RCAR ABA receptors in an
ABA-dependent manner. {ECO:0000269|PubMed:19407142}.
-!- SUBUNIT: Interacts with AKT2/AKT3. Interacts with ABA-bounded
PYR1, PYL1, PYL2, PYL3, PYL4, PYL9 and PYL12, and with free PYL2,
PYL3, PYL4 and PYL13. Binds to and inactivates SLAC1 and SRK2E.
The inactivation of SRK2E does not require phosphatase activity.
Interacts with CBL1, CBL2, CBL3, CBL5, and CBL7, but not CBL4,
CBL6, and CBL9 (PubMed:11181729, PubMed:12034902, PubMed:19407142,
PubMed:19955427, PubMed:21596690, PubMed:24165892). Interacts with
RGLG1 and RGLG5 (PubMed:27577789). {ECO:0000269|PubMed:11181729,
ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:19407142,
ECO:0000269|PubMed:19955427, ECO:0000269|PubMed:21596690,
ECO:0000269|PubMed:24165892, ECO:0000269|PubMed:27577789}.
-!- INTERACTION:
Q38898:AKT2; NbExp=5; IntAct=EBI-1764934, EBI-1552774;
O80920:PYL4; NbExp=2; IntAct=EBI-1764934, EBI-2349683;
Q940H6:SRK2E; NbExp=2; IntAct=EBI-1764934, EBI-782514;
-!- TISSUE SPECIFICITY: Mostly expressed in seeds and leaves, and, to
a lower extent, in roots, stems, and flowers, particularly in
siliques. Essentially found in the phloem.
{ECO:0000269|PubMed:11439132, ECO:0000269|PubMed:12034902,
ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:17461784}.
-!- INDUCTION: Repressed by MYB44. Induced by cold stress, drought,
high salt, and ABA. {ECO:0000269|PubMed:11439132,
ECO:0000269|PubMed:12034902, ECO:0000269|PubMed:16214899,
ECO:0000269|PubMed:16339800, ECO:0000269|PubMed:16361522,
ECO:0000269|PubMed:17461784, ECO:0000269|PubMed:18162593}.
-!- DOMAIN: The 'lock' site stabilizes the complex made of PP2C, ABA
and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch'
loops in closed positions. {ECO:0000250}.
-!- PTM: Ubiquitinated by RGLG1 and RGLG5 in response to abscisic acid
(ABA). Ubiquitination of PP2CA leads to its degradation by the
proteasome. {ECO:0000269|PubMed:27577789}.
-!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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EMBL; D38109; BAA07287.1; -; mRNA.
EMBL; AC008153; AAG51448.1; -; Genomic_DNA.
EMBL; CP002686; AEE75044.1; -; Genomic_DNA.
EMBL; AY074368; AAL67064.1; -; mRNA.
EMBL; AY091391; AAM14330.1; -; mRNA.
PIR; S55457; S55457.
RefSeq; NP_187748.1; NM_111974.4.
UniGene; At.20739; -.
PDB; 4N0G; X-ray; 2.38 A; A/B=72-399.
PDBsum; 4N0G; -.
ProteinModelPortal; P49598; -.
SMR; P49598; -.
BioGrid; 5648; 50.
DIP; DIP-40197N; -.
IntAct; P49598; 15.
MINT; P49598; -.
STRING; 3702.AT3G11410.1; -.
iPTMnet; P49598; -.
PaxDb; P49598; -.
PRIDE; P49598; -.
EnsemblPlants; AT3G11410.1; AT3G11410.1; AT3G11410.
GeneID; 820314; -.
Gramene; AT3G11410.1; AT3G11410.1; AT3G11410.
KEGG; ath:AT3G11410; -.
Araport; AT3G11410; -.
TAIR; locus:2080787; AT3G11410.
eggNOG; KOG0698; Eukaryota.
eggNOG; COG0631; LUCA.
HOGENOM; HOG000233896; -.
InParanoid; P49598; -.
KO; K14497; -.
OMA; HLIVANC; -.
OrthoDB; EOG09360IAR; -.
PhylomeDB; P49598; -.
PRO; PR:P49598; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P49598; baseline and differential.
Genevisible; P49598; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:TAIR.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IMP:TAIR.
GO; GO:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0009788; P:negative regulation of abscisic acid-activated signaling pathway; IMP:TAIR.
GO; GO:0010360; P:negative regulation of anion channel activity; IDA:UniProtKB.
GO; GO:0010119; P:regulation of stomatal movement; IMP:TAIR.
GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR000222; PP2C_BS.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00331; PP2C_SIG; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS01032; PPM_1; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Abscisic acid signaling pathway; Complete proteome;
Hydrolase; Magnesium; Manganese; Metal-binding; Protein phosphatase;
Reference proteome; Ubl conjugation; Zinc.
CHAIN 1 399 Protein phosphatase 2C 37.
/FTId=PRO_0000057769.
DOMAIN 104 389 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
METAL 142 142 Manganese 1. {ECO:0000250}.
METAL 142 142 Manganese 2. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 143 143 Manganese 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 146 146 Zinc. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 148 148 Zinc; via pros nitrogen.
{ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 208 208 Zinc. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 210 210 Zinc. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 327 327 Manganese 1. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 327 327 Manganese 2. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 331 331 Manganese 1. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
METAL 380 380 Manganese 2. {ECO:0000244|PDB:4N0G,
ECO:0000269|PubMed:24165892}.
SITE 280 280 Lock. {ECO:0000250}.
MUTAGEN 139 139 G->D: Loss of phosphatase activity. Loss
of kinase activity but intact binding and
repression of SRK2E; when associated with
D-145. {ECO:0000269|PubMed:12034902,
ECO:0000269|PubMed:19955427,
ECO:0000269|PubMed:9448270}.
MUTAGEN 145 145 G->D: Insensitive to ABA and loss of
phosphatase activity. Loss of kinase
activity but intact binding and
repression of SRK2E; when associated with
D-139. {ECO:0000269|PubMed:16339800,
ECO:0000269|PubMed:19955427,
ECO:0000269|PubMed:9448270}.
MUTAGEN 287 287 G->E: In ahg3-1; hypersensitivity to ABA
during seed germination, and loss of
phosphatase activity.
{ECO:0000269|PubMed:16339800}.
STRAND 105 110 {ECO:0000244|PDB:4N0G}.
STRAND 119 132 {ECO:0000244|PDB:4N0G}.
STRAND 134 147 {ECO:0000244|PDB:4N0G}.
HELIX 148 165 {ECO:0000244|PDB:4N0G}.
HELIX 173 189 {ECO:0000244|PDB:4N0G}.
TURN 209 212 {ECO:0000244|PDB:4N0G}.
HELIX 216 219 {ECO:0000244|PDB:4N0G}.
STRAND 224 229 {ECO:0000244|PDB:4N0G}.
STRAND 231 241 {ECO:0000244|PDB:4N0G}.
STRAND 243 248 {ECO:0000244|PDB:4N0G}.
STRAND 251 256 {ECO:0000244|PDB:4N0G}.
HELIX 264 272 {ECO:0000244|PDB:4N0G}.
STRAND 277 285 {ECO:0000244|PDB:4N0G}.
TURN 286 288 {ECO:0000244|PDB:4N0G}.
STRAND 289 293 {ECO:0000244|PDB:4N0G}.
HELIX 298 300 {ECO:0000244|PDB:4N0G}.
TURN 301 303 {ECO:0000244|PDB:4N0G}.
STRAND 309 314 {ECO:0000244|PDB:4N0G}.
STRAND 319 325 {ECO:0000244|PDB:4N0G}.
HELIX 327 330 {ECO:0000244|PDB:4N0G}.
HELIX 335 345 {ECO:0000244|PDB:4N0G}.
HELIX 361 375 {ECO:0000244|PDB:4N0G}.
STRAND 382 388 {ECO:0000244|PDB:4N0G}.
SEQUENCE 399 AA; 43350 MW; 83B82E32FEC71D4D CRC64;
MAGICCGVVG ETEPAAPVDS TSRASLRRRL DLLPSIKIVA DSAVAPPLEN CRKRQKRETV
VLSTLPGNLD LDSNVRSENK KARSAVTNSN SVTEAESFFS DVPKIGTTSV CGRRRDMEDA
VSIHPSFLQR NSENHHFYGV FDGHGCSHVA EKCRERLHDI VKKEVEVMAS DEWTETMVKS
FQKMDKEVSQ RECNLVVNGA TRSMKNSCRC ELQSPQCDAV GSTAVVSVVT PEKIIVSNCG
DSRAVLCRNG VAIPLSVDHK PDRPDELIRI QQAGGRVIYW DGARVLGVLA MSRAIGDNYL
KPYVIPDPEV TVTDRTDEDE CLILASDGLW DVVPNETACG VARMCLRGAG AGDDSDAAHN
ACSDAALLLT KLALARQSSD NVSVVVVDLR KRRNNQASS


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10-663-45544 Protein Phosphatase 2C alpha (PP2Ca) Human - EC 3.1.3.16; PP2C-alpha; IA; Protein phosphatase 1A N_A 1 mg
10-663-45544 Protein Phosphatase 2C alpha (PP2Ca) Human - EC 3.1.3.16; PP2C-alpha; IA; Protein phosphatase 1A N_A 0.01 mg
10-663-45544 Protein Phosphatase 2C alpha (PP2Ca) Human - EC 3.1.3.16; PP2C-alpha; IA; Protein phosphatase 1A N_A 0.05 mg
EIAAB32061 Homo sapiens,Human,p53-induced protein phosphatase 1,PP2C-delta,PPM1D,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,WIP1
EIAAB32069 Homo sapiens,Human,PP2C-gamma,PPM1C,PPM1G,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphatase magnesium-dependent 1 gamma
EIAAB32062 Mouse,Mus musculus,p53-induced protein phosphatase 1,PP2C-delta,Ppm1d,Protein phosphatase 1D,Protein phosphatase 2C isoform delta,Protein phosphatase magnesium-dependent 1 delta,Wip1
EIAAB12057 Dual specificity protein phosphatase 14,DUSP14,Homo sapiens,Human,MAP kinase phosphatase 6,Mitogen-activated protein kinase phosphatase 6,MKP-1-like protein tyrosine phosphatase,MKP6,MKP-6,MKP-L
EIAAB12042 3ch134,Dual specificity protein phosphatase 1,Dusp1,MAP kinase phosphatase 1,Mitogen-activated protein kinase phosphatase 1,Mkp1,MKP-1,Mouse,Mus musculus,Protein-tyrosine phosphatase 3CH134,Protein-ty
EIAAB12040 Cl100,Dual specificity protein phosphatase 1,Dusp1,MAP kinase phosphatase 1,Mitogen-activated protein kinase phosphatase 1,Mkp1,MKP-1,Protein-tyrosine phosphatase CL100,Protein-tyrosine phosphatase no
EIAAB33026 Mouse,Mus musculus,Protein tyrosine phosphatase DPZPTP,Protein tyrosine phosphatase PTP-BL,Protein-tyrosine phosphatase RIP,Ptp14,PTP36,Ptpn13,Tyrosine-protein phosphatase non-receptor type 13
EIAAB33052 HCP,Hematopoietic cell protein-tyrosine phosphatase,Homo sapiens,Human,Protein-tyrosine phosphatase 1C,Protein-tyrosine phosphatase SHP-1,PTP1C,PTP-1C,PTPN6,SH-PTP1,Tyrosine-protein phosphatase non-re
EIAAB33117 FMI,Homo sapiens,hPTP-J,Human,Pancreatic carcinoma phosphatase 2,PCP2,PCP-2,Protein-tyrosine phosphatase J,Protein-tyrosine phosphatase pi,Protein-tyrosine phosphatase receptor omicron,PTP pi,PTP-J,PT
15-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L Poly 0.05 mg
15-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L Poly 0.1 mg
EIAAB32070 Fibroblast growth factor-inducible protein 13,FIN13,Fin13,Mouse,Mus musculus,PP2C-gamma,Ppm1c,Ppm1g,Protein phosphatase 1C,Protein phosphatase 1G,Protein phosphatase 2C isoform gamma,Protein phosphata
29-710 ACP1 belongs to the phosphotyrosine protein phosphatase family of proteins. It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein 0.1 mg
10-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L 0.05 mg
10-288-22164F Dual specificity protein phosphatase 14 - EC 3.1.3.48; EC 3.1.3.16; Mitogen-activated protein kinase phosphatase 6; MAP kinase phosphatase 6; MKP-6; MKP-1-like protein tyrosine phosphatase; MKP-L 0.1 mg
EIAAB32068 Ca(2+)_calmodulin-dependent protein kinase phosphatase,CaM-kinase phosphatase,CaMKPase,hFem-2,Homo sapiens,Human,KIAA0015,Partner of PIX 2,POPX2,PPM1F,Protein fem-2 homolog,Protein phosphatase 1F
EIAAB12066 Dual specificity protein phosphatase 19,Dusp19,Mouse,Mus musculus,Protein phosphatase SKRP1,Skrp1,Stress-activated protein kinase pathway-regulating phosphatase 1
EIAAB12041 CL100,Dual specificity protein phosphatase 1,Dual specificity protein phosphatase hVH1,DUSP1,Homo sapiens,Human,MAP kinase phosphatase 1,Mitogen-activated protein kinase phosphatase 1,MKP1,MKP-1,Prote
EIAAB33119 Embryonic stem cell protein-tyrosine phosphatase,ES cell phosphatase,Esp,Osteotesticular protein-tyrosine phosphatase,OST-PTP,Ptprv,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase V,R
18-461-10260 Dual specificity protein phosphatase 22 - EC 3.1.3.48; EC 3.1.3.16; JNK-stimulatory phosphatase-1; JSP-1; Mitogen-activated protein kinase phosphatase x; LMW-DSP2 Polyclonal 0.05 ml


 

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