Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Mitogen-activated protein kinase 4 (AtMPK4) (MAP kinase 4) (EC 2.7.11.24)

 MPK4_ARATH              Reviewed;         376 AA.
Q39024; B2BDE5; B2BDE6; B2BDE8; B2BDG2; O04597; Q45V20; Q9M136;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
06-JUN-2002, sequence version 2.
27-SEP-2017, entry version 165.
RecName: Full=Mitogen-activated protein kinase 4;
Short=AtMPK4;
Short=MAP kinase 4;
EC=2.7.11.24;
Name=MPK4; OrderedLocusNames=At4g01370; ORFNames=F2N1.1, F2N1_2-t;
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=8282107; DOI=10.1016/0014-5793(93)80852-L;
Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
Shinozaki K.;
"ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana.";
FEBS Lett. 336:440-444(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-115 AND VAL-293.
STRAIN=cv. Aa-0, cv. Ak-1, cv. Bay-0, cv. C24, cv. Columbia,
cv. Cvi-0, cv. Di-0, cv. Ei-2, cv. Gu-0, cv. HOG,
cv. Landsberg erecta, cv. Lz-0, cv. N13 Konchezero, cv. Nd-1, cv. Sha,
cv. Sorbo, cv. Tsu-0, cv. Wassilewskija, cv. Wei-0, and cv. Yo-0;
PubMed=19064707; DOI=10.1534/genetics.108.097279;
Caldwell K.S., Michelmore R.W.;
"Arabidopsis thaliana genes encoding defense signaling and recognition
proteins exhibit contrasting evolutionary dynamics.";
Genetics 181:671-684(2009).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Sharma P.K., Kumar R., Garg G.K., Khan G.;
"MAP kinase 4 genomic sequence from Arabidopsis thaliana.";
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
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.
[8]
SUBUNIT, AND INTERACTION WITH MEKK1; MKK1 AND MKK2.
PubMed=9878570; DOI=10.1006/bbrc.1998.9796;
Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J.,
Matsumoto K., Shinozaki K.;
"Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting
proteins and analysis of a MAP kinase cascade in Arabidopsis.";
Biochem. Biophys. Res. Commun. 253:532-543(1998).
[9]
ENZYME REGULATION, AND DEPHOSPHORYLATION.
STRAIN=cv. Columbia;
PubMed=10036776; DOI=10.1046/j.1365-313x.1998.00327.x;
Gupta R., Huang Y., Kieber J., Luan S.;
"Identification of a dual-specificity protein phosphatase that
inactivates a MAP kinase from Arabidopsis.";
Plant J. 16:581-589(1998).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-201 AND TYR-203.
PubMed=11163186; DOI=10.1016/S0092-8674(00)00213-0;
Petersen M., Brodersen P., Naested H., Andreasson E., Lindhart U.,
Johansen B., Nielsen H.B., Lacy M., Austin M.J., Parker J.E.,
Sharma S.B., Klessig D.F., Martienssen R., Mattsson O., Jensen A.B.,
Mundy J.;
"Arabidopsis MAP kinase 4 negatively regulates systemic acquired
resistance.";
Cell 103:1111-1120(2000).
[11]
ENZYME REGULATION, AND PHOSPHORYLATION AT THR-201 AND TYR-203.
PubMed=11123804; DOI=10.1046/j.1365-313x.2000.00913.x;
Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K.;
"Various abiotic stresses rapidly activate Arabidopsis MAP kinases
ATMPK4 and ATMPK6.";
Plant J. 24:655-665(2000).
[12]
ENZYME REGULATION, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-187.
PubMed=10759527; DOI=10.1104/pp.122.4.1301;
Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.;
"ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase,
is activated in vitro by AtMEK1 through threonine phosphorylation.";
Plant Physiol. 122:1301-1310(2000).
[13]
ENZYME REGULATION.
PubMed=11500556; DOI=10.1104/pp.126.4.1579;
Desikan R., Hancock J.T., Ichimura K., Shinozaki K., Neill S.J.;
"Harpin induces activation of the Arabidopsis mitogen-activated
protein kinases AtMPK4 and AtMPK6.";
Plant Physiol. 126:1579-1587(2001).
[14]
ENZYME REGULATION.
PubMed=11874576; DOI=10.1046/j.0960-7412.2001.01246.x;
Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T.;
"Activation of AtMEK1, an Arabidopsis mitogen-activated protein kinase
kinase, in vitro and in vivo: analysis of active mutants expressed in
E. coli and generation of the active form in stress response in
seedlings.";
Plant J. 29:637-647(2002).
[15]
GENE FAMILY, AND NOMENCLATURE.
PubMed=12119167; DOI=10.1016/S1360-1385(02)02302-6;
MAPK group;
"Mitogen-activated protein kinase cascades in plants: a new
nomenclature.";
Trends Plant Sci. 7:301-308(2002).
[16]
FUNCTION, AND ENZYME REGULATION.
PubMed=15358537; DOI=10.1016/j.febslet.2004.08.001;
Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.;
"Involvement of MPK4 in osmotic stress response pathways in cell
suspensions and plantlets of Arabidopsis thaliana: activation by
hypoosmolarity and negative role in hyperosmolarity tolerance.";
FEBS Lett. 574:42-48(2004).
[17]
FUNCTION, ENZYME REGULATION, AND INTERACTION WITH MKK2.
PubMed=15225555; DOI=10.1016/j.molcel.2004.06.023;
Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K.,
Dangl J.L., Hirt H.;
"The MKK2 pathway mediates cold and salt stress signaling in
Arabidopsis.";
Mol. Cell 15:141-152(2004).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MKS1.
PubMed=15990873; DOI=10.1038/sj.emboj.7600737;
Andreasson E., Jenkins T., Brodersen P., Thorgrimsen S.,
Petersen N.H.T., Zhu S., Qiu J.-L., Micheelsen P., Rocher A.,
Petersen M., Newman M.-A., Bjoern Nielsen H., Hirt H., Somssich I.E.,
Mattsson O., Mundy J.;
"The MAP kinase substrate MKS1 is a regulator of plant defense
responses.";
EMBO J. 24:2579-2589(2005).
[19]
GENE FAMILY.
PubMed=16537113; DOI=10.1016/j.tplants.2006.02.007;
Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M.,
Ehlting J., Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G.,
Mundy J., Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S.,
Seguin A., Ellis B.E.;
"Ancient signals: comparative genomics of plant MAPK and MAPKK gene
families.";
Trends Plant Sci. 11:192-198(2006).
[20]
ENZYME REGULATION.
PubMed=17506336; DOI=10.1094/MPMI-20-5-0589;
Brader G., Djamei A., Teige M., Palva E.T., Hirt H.;
"The MAP kinase kinase MKK2 affects disease resistance in
Arabidopsis.";
Mol. Plant Microbe Interact. 20:589-596(2007).
[21]
ENZYME REGULATION, AND INTERACTION WITH AP2C1.
PubMed=17630279; DOI=10.1105/tpc.106.049585;
Schweighofer A., Kazanaviciute V., Scheikl E., Teige M., Doczi R.,
Hirt H., Schwanninger M., Kant M., Schuurink R., Mauch F., Buchala A.,
Cardinale F., Meskiene I.;
"The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and
MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in
Arabidopsis.";
Plant Cell 19:2213-2224(2007).
[22]
FUNCTION, INTERACTION WITH MEKK1; MKK1 AND MKK2, AND DISRUPTION
PHENOTYPE.
PubMed=18982020; DOI=10.1038/cr.2008.300;
Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.;
"MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated
protein kinase cascade to regulate innate immunity in plants.";
Cell Res. 18:1190-1198(2008).
[23]
INTERACTION WITH MKK1; MKK2 AND MKK6.
PubMed=19513235; DOI=10.4161/psb.3.12.6848;
Lee J.S., Huh K.W., Bhargava A., Ellis B.E.;
"Comprehensive analysis of protein-protein interactions between
Arabidopsis MAPKs and MAPK kinases helps define potential MAPK
signalling modules.";
Plant Signal. Behav. 3:1037-1041(2008).
[24]
FUNCTION, INTERACTION WITH MAP65-1, DISRUPTION PHENOTYPE, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=20215588; DOI=10.1105/tpc.109.071746;
Beck M., Komis G., Mueller J., Menzel D., Samaj J.;
"Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2
and 3 and mitogen-activated protein kinase 4 are essential for
microtubule organization.";
Plant Cell 22:755-771(2010).
[25]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
PubMed=21098735; DOI=10.1105/tpc.110.077164;
Kosetsu K., Matsunaga S., Nakagami H., Colcombet J., Sasabe M.,
Soyano T., Takahashi Y., Hirt H., Machida Y.;
"The MAP kinase MPK4 is required for cytokinesis in Arabidopsis
thaliana.";
Plant Cell 22:3778-3790(2010).
[26]
FUNCTION, ENZYME REGULATION, PHOSPHORYLATION BY MKK6, AND INTERACTION
WITH MKK6.
PubMed=20802223; DOI=10.1093/pcp/pcq135;
Takahashi Y., Soyano T., Kosetsu K., Sasabe M., Machida Y.;
"HINKEL kinesin, ANP MAPKKKs and MKK6/ANQ MAPKK, which phosphorylates
and activates MPK4 MAPK, constitute a pathway that is required for
cytokinesis in Arabidopsis thaliana.";
Plant Cell Physiol. 51:1766-1776(2010).
[27]
FUNCTION, DISRUPTION PHENOTYPE, ENZYME REGULATION, INTERACTION WITH
MKK1 AND MKK6, AND TISSUE SPECIFICITY.
PubMed=21575092; DOI=10.1111/j.1365-313X.2011.04642.x;
Zeng Q., Chen J.G., Ellis B.E.;
"AtMPK4 is required for male-specific meiotic cytokinesis in
Arabidopsis.";
Plant J. 67:895-906(2011).
[28]
FUNCTION, AND INTERACTION WITH MEKK2.
PubMed=22643122; DOI=10.1105/tpc.112.097253;
Kong Q., Qu N., Gao M., Zhang Z., Ding X., Yang F., Li Y., Dong O.X.,
Chen S., Li X., Zhang Y.;
"The MEKK1-MKK1/MKK2-MPK4 kinase cascade negatively regulates immunity
mediated by a mitogen-activated protein kinase kinase kinase in
Arabidopsis.";
Plant Cell 24:2225-2236(2012).
[29]
LACK OF INTERACTION WITH RACK1A; RACK1B OR RACK1C.
PubMed=25731164; DOI=10.1038/nature14243;
Cheng Z., Li J.F., Niu Y., Zhang X.C., Woody O.Z., Xiong Y.,
Djonovic S., Millet Y., Bush J., McConkey B.J., Sheen J.,
Ausubel F.M.;
"Pathogen-secreted proteases activate a novel plant immune pathway.";
Nature 521:213-216(2015).
[30]
FUNCTION, AND INTERACTION WITH ASR3.
STRAIN=cv. Columbia;
PubMed=25770109; DOI=10.1105/tpc.114.134809;
Li B., Jiang S., Yu X., Cheng C., Chen S., Cheng Y., Yuan J.S.,
Jiang D., He P., Shan L.;
"Phosphorylation of trihelix transcriptional repressor ASR3 by MAP
KINASE4 negatively regulates Arabidopsis immunity.";
Plant Cell 27:839-856(2015).
-!- FUNCTION: The ANPs-MKK6-MPK4 module is involved in the regulation
of plant cytokinesis during meiosis and mitosis. Essential to
promote the progression of cytokinesis and for cellularization
(formation of the cell plate) during male-specific meiotic.
Involved in cortical microtubules organization and stabilization
by regulating the phosphorylation state of microtubule-associated
proteins such as MAP65-1. Involved in root hair development
process. Negative regulator of systemic acquired resistance (SAR)
and salicylic acid- (SA) mediated defense response. Required for
jasmonic acid- (JA) mediated defense gene expression. May regulate
activity of transcription factor controlling pathogenesis-related
(PR) gene expression. Seems to act independently of the SAR
regulatory protein NPR1 (Nonexpresser of PR1). Phosphorylates MKS1
and transcription factors WRKY25 and WRKY33. The MEKK1, MKK1/MKK2
and MPK4 function in a signaling pathway that modulates the
expression of genes responding to biotic and abiotic stresses and
also plays an important role in pathogen defense by negatively
regulating innate immunity (PubMed:11163186, PubMed:15225555,
PubMed:15358537, PubMed:15990873, PubMed:18982020,
PubMed:20215588, PubMed:20802223, PubMed:21098735,
PubMed:21575092, PubMed:25770109). Phosphorylates MEKK2 upon
treatment with flg22 (PubMed:22643122).
{ECO:0000269|PubMed:11163186, ECO:0000269|PubMed:15225555,
ECO:0000269|PubMed:15358537, ECO:0000269|PubMed:15990873,
ECO:0000269|PubMed:18982020, ECO:0000269|PubMed:20215588,
ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21098735,
ECO:0000269|PubMed:21575092, ECO:0000269|PubMed:22643122,
ECO:0000269|PubMed:25770109}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by threonine and tyrosine
phosphorylation. Activated by the MAP kinase kinases MKK1 and
MKK2. Activated in response to touch, wounding, low temperature,
low humidity, salt stress and the bacterial elicitors flagellin
and harpin. Activated upon Pseudomonas syringae pv. tomato DC3000
infection. Repressed by the protein phosphatase 2C AP2C1.
Repressed by DSPTP1-mediated dephosphorylation. Activated by the
MAP kinase kinase MKK6 in vitro. {ECO:0000269|PubMed:10036776,
ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:11123804,
ECO:0000269|PubMed:11500556, ECO:0000269|PubMed:11874576,
ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15358537,
ECO:0000269|PubMed:17506336, ECO:0000269|PubMed:17630279,
ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21098735,
ECO:0000269|PubMed:21575092}.
-!- SUBUNIT: Interacts with MEKK1, MKK1, MKK2 and MKK6. May form a
ternary complex composed of MEKK1 and MKK1/MKK2 and MPK4.
Interacts with MKS1 and AP2C1. May form a ternary or larger
complex with MKS1 and WRKY25 and/or WRKY33. Interacts with MAP65-1
(PubMed:15225555, PubMed:15990873, PubMed:17630279,
PubMed:18982020, PubMed:19513235, PubMed:20215588,
PubMed:20802223, PubMed:21575092, PubMed:9878570). No interactions
with RACK1A, RACK1B or RACK1C (PubMed:25731164). Interacts
directly with ASR3 and mediates its phosphorylation
(PubMed:25770109). Binds to MEKK2 (PubMed:22643122).
{ECO:0000269|PubMed:15225555, ECO:0000269|PubMed:15990873,
ECO:0000269|PubMed:17630279, ECO:0000269|PubMed:18982020,
ECO:0000269|PubMed:19513235, ECO:0000269|PubMed:20215588,
ECO:0000269|PubMed:20802223, ECO:0000269|PubMed:21575092,
ECO:0000269|PubMed:22643122, ECO:0000269|PubMed:25731164,
ECO:0000269|PubMed:25770109, ECO:0000269|PubMed:9878570}.
-!- INTERACTION:
O81472:MEKK2; NbExp=3; IntAct=EBI-994375, EBI-6271434;
Q94A06:MKK1; NbExp=6; IntAct=EBI-994375, EBI-994464;
Q9S7U9:MKK2; NbExp=5; IntAct=EBI-994375, EBI-994350;
Q8LGD5:MKS1; NbExp=9; IntAct=EBI-994375, EBI-1392198;
O22921:WRKY25; NbExp=2; IntAct=EBI-994375, EBI-1392386;
Q8S8P5:WRKY33; NbExp=2; IntAct=EBI-994375, EBI-1392374;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton.
Note=Translocated into the nucleus in response to phosphorylation
(Probable). localized to the cell plate. {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the veins and
stomatal guard cells of leaf plates, petioles, stem, roots and
flowers. {ECO:0000269|PubMed:11163186,
ECO:0000269|PubMed:20215588, ECO:0000269|PubMed:21575092}.
-!- DEVELOPMENTAL STAGE: Observed in root epidermal cells and root
hairs, especially in the root hair formation zone. During root
hair development, both observed in root hair bulges and in young
outgrowing root hairs. {ECO:0000269|PubMed:20215588}.
-!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
whose phosphorylation activates the MAP kinases.
-!- PTM: Dually phosphorylated on Thr-201 and Tyr-203, which activates
the enzyme. Autophosphorylated on serine and tyrosine residues.
Dephosphorylated by DSPTP1. Phosphorylated by MKK6 in vitro.
{ECO:0000269|PubMed:10759527, ECO:0000269|PubMed:11123804,
ECO:0000269|PubMed:20802223}.
-!- DISRUPTION PHENOTYPE: Dwarf plants with cytokinetic defects in
leaf epidermal cells. Abnormally developed and branched root
hairs. Retarded root growth with the protrusion of many epidermal
cells from roots. Heavily bundled and disoriented cortical
microtubules resistant to oryzalin. Exhibits a seedling-lethality
phenotype. Defects in the formation of the cell plate. Abnormal
mature pollen grains. {ECO:0000269|PubMed:18982020,
ECO:0000269|PubMed:20215588, ECO:0000269|PubMed:21098735,
ECO:0000269|PubMed:21575092}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. MAP kinase subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB61033.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D21840; BAA04867.1; -; mRNA.
EMBL; EF470667; ABR46145.1; -; Genomic_DNA.
EMBL; EF470668; ABR46146.1; -; Genomic_DNA.
EMBL; EF470669; ABR46147.1; -; Genomic_DNA.
EMBL; EF470670; ABR46148.1; -; Genomic_DNA.
EMBL; EF470671; ABR46149.1; -; Genomic_DNA.
EMBL; EF470672; ABR46150.1; -; Genomic_DNA.
EMBL; EF470673; ABR46151.1; -; Genomic_DNA.
EMBL; EF470674; ABR46152.1; -; Genomic_DNA.
EMBL; EF470675; ABR46153.1; -; Genomic_DNA.
EMBL; EF470676; ABR46154.1; -; Genomic_DNA.
EMBL; EF470677; ABR46155.1; -; Genomic_DNA.
EMBL; EF470678; ABR46156.1; -; Genomic_DNA.
EMBL; EF470679; ABR46157.1; -; Genomic_DNA.
EMBL; EF470680; ABR46158.1; -; Genomic_DNA.
EMBL; EF470681; ABR46159.1; -; Genomic_DNA.
EMBL; EF470682; ABR46160.1; -; Genomic_DNA.
EMBL; EF470683; ABR46161.1; -; Genomic_DNA.
EMBL; EF470684; ABR46162.1; -; Genomic_DNA.
EMBL; EF470685; ABR46163.1; -; Genomic_DNA.
EMBL; EF470686; ABR46164.1; -; Genomic_DNA.
EMBL; DQ112072; AAZ20637.1; -; Genomic_DNA.
EMBL; AF007269; AAB61033.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161491; CAB80946.1; -; Genomic_DNA.
EMBL; CP002687; AEE82016.1; -; Genomic_DNA.
EMBL; AF360231; AAK25941.1; -; mRNA.
EMBL; AY040031; AAK64089.1; -; mRNA.
EMBL; AY088537; AAM66070.1; -; mRNA.
PIR; S40470; S40470.
RefSeq; NP_192046.1; NM_116367.3.
UniGene; At.19915; -.
ProteinModelPortal; Q39024; -.
SMR; Q39024; -.
BioGrid; 13440; 14.
IntAct; Q39024; 7.
MINT; MINT-7232331; -.
STRING; 3702.AT4G01370.1; -.
iPTMnet; Q39024; -.
PaxDb; Q39024; -.
PRIDE; Q39024; -.
EnsemblPlants; AT4G01370.1; AT4G01370.1; AT4G01370.
GeneID; 828151; -.
Gramene; AT4G01370.1; AT4G01370.1; AT4G01370.
KEGG; ath:AT4G01370; -.
Araport; AT4G01370; -.
TAIR; locus:2124943; AT4G01370.
eggNOG; KOG0660; Eukaryota.
eggNOG; ENOG410XNY0; LUCA.
InParanoid; Q39024; -.
KO; K20600; -.
OMA; WEERNKN; -.
OrthoDB; EOG09360BXQ; -.
PhylomeDB; Q39024; -.
BRENDA; 2.7.11.24; 399.
Reactome; R-ATH-110056; MAPK3 (ERK1) activation.
Reactome; R-ATH-112409; RAF-independent MAPK1/3 activation.
Reactome; R-ATH-112411; MAPK1 (ERK2) activation.
Reactome; R-ATH-198753; ERK/MAPK targets.
Reactome; R-ATH-198765; Signalling to ERK5.
Reactome; R-ATH-202670; ERKs are inactivated.
Reactome; R-ATH-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-ATH-375165; NCAM signaling for neurite out-growth.
Reactome; R-ATH-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-ATH-444257; RSK activation.
Reactome; R-ATH-445144; Signal transduction by L1.
Reactome; R-ATH-5673001; RAF/MAP kinase cascade.
Reactome; R-ATH-5674135; MAP2K and MAPK activation.
Reactome; R-ATH-5674499; Negative feedback regulation of MAPK pathway.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
PRO; PR:Q39024; -.
Proteomes; UP000006548; Chromosome 4.
Genevisible; Q39024; AT.
GO; GO:0009504; C:cell plate; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IDA:UniProtKB.
GO; GO:0004707; F:MAP kinase activity; IDA:TAIR.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
GO; GO:0000911; P:cytokinesis by cell plate formation; IMP:UniProtKB.
GO; GO:0006972; P:hyperosmotic response; IMP:TAIR.
GO; GO:0042539; P:hypotonic salinity response; IDA:TAIR.
GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:TAIR.
GO; GO:0009868; P:jasmonic acid and ethylene-dependent systemic resistance, jasmonic acid mediated signaling pathway; TAS:TAIR.
GO; GO:0007112; P:male meiosis cytokinesis; IMP:TAIR.
GO; GO:0016310; P:phosphorylation; IDA:TAIR.
GO; GO:0009555; P:pollen development; IMP:TAIR.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
GO; GO:0009409; P:response to cold; IDA:TAIR.
GO; GO:0009620; P:response to fungus; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IDA:TAIR.
GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR003527; MAP_kinase_CS.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01351; MAPK; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Immunity;
Innate immunity; Kinase; Microtubule; Nucleotide-binding; Nucleus;
Phosphoprotein; Plant defense; Reference proteome;
Serine/threonine-protein kinase; Stress response; Transferase.
CHAIN 1 376 Mitogen-activated protein kinase 4.
/FTId=PRO_0000186313.
DOMAIN 43 329 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 49 57 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 201 203 TXY.
ACT_SITE 169 169 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 72 72 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 201 201 Phosphothreonine.
{ECO:0000269|PubMed:11123804}.
MOD_RES 203 203 Phosphotyrosine.
{ECO:0000269|PubMed:11123804}.
MOD_RES 206 206 Phosphothreonine.
{ECO:0000250|UniProtKB:Q39026}.
VARIANT 115 115 E -> Q (in strain: cv. C24, cv. Lz-0, cv.
Wei-0, cv. Yo-0).
{ECO:0000269|PubMed:19064707}.
VARIANT 293 293 A -> V (in strain: cv. Ak-1, cv. Bay-0,
cv. Di-0, cv. Landsberg erecta, cv. Tsu-
0, cv. Wei-0).
{ECO:0000269|PubMed:19064707}.
MUTAGEN 187 187 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:10759527}.
MUTAGEN 201 201 T->A: Loss of kinase activity; when
associated with Y-203.
{ECO:0000269|PubMed:11163186}.
MUTAGEN 203 203 Y->F: Loss of kinase activity; when
associated with T-201.
{ECO:0000269|PubMed:11163186}.
CONFLICT 313 313 D -> E (in Ref. 1; BAA04867).
{ECO:0000305}.
SEQUENCE 376 AA; 42852 MW; 448F65C25C95AAEB CRC64;
MSAESCFGSS GDQSSSKGVA THGGSYVQYN VYGNLFEVSR KYVPPLRPIG RGAYGIVCAA
TNSETGEEVA IKKIGNAFDN IIDAKRTLRE IKLLKHMDHE NVIAVKDIIK PPQRENFNDV
YIVYELMDTD LHQIIRSNQP LTDDHCRFFL YQLLRGLKYV HSANVLHRDL KPSNLLLNAN
CDLKLGDFGL ARTKSETDFM TEYVVTRWYR APELLLNCSE YTAAIDIWSV GCILGETMTR
EPLFPGKDYV HQLRLITELI GSPDDSSLGF LRSDNARRYV RQLPQYPRQN FAARFPNMSA
GAVDLLEKML VFDPSRRITV DEALCHPYLA PLHDINEEPV CVRPFNFDFE QPTLTEENIK
ELIYRETVKF NPQDSV


Related products :

Catalog number Product name Quantity
EIAAB24970 Leucine zipper- and sterile alpha motif kinase ZAK,Mitogen-activated protein kinase kinase kinase MLT,Mixed lineage kinase-related kinase,MLK-like mitogen-activated protein triple kinase,MLK-related k
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.005 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.05 mg
10-782-55060 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.02 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.01 mg
10-782-55059 Mitogen-activated protein kinase 12 - EC 2.7.11.24; Extracellular signal-regulated kinase 6; ERK-6; ERK5; Stress-activated protein kinase 3; Mitogen-activated protein kinase p38 gamma; MAP kinase p38 0.001 mg
EIAAB24870 Homo sapiens,Human,MAP kinase 13,MAP kinase p38 delta,MAPK 13,MAPK13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,PRKM13,SAPK4,Stress-activated protein kinase 4
EIAAB24864 Homo sapiens,Human,MAP kinase 11,MAP kinase p38 beta,MAPK 11,MAPK11,Mitogen-activated protein kinase 11,Mitogen-activated protein kinase p38 beta,p38-2,p38b,PRKM11,SAPK2,Stress-activated protein kinas
U1206b CLIA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM1 96T
E1206b ELISA Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2,PRKM 96T
EIAAB24867 ERK6,ERK-6,Extracellular signal-regulated kinase 6,Homo sapiens,Human,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,MAPK12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,S
E1206b ELISA kit Bos taurus,Bovine,ERK2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAPK 1,MAPK 2,MAPK1,Mitogen-activated protein kinase 1,Mitogen-activated protein kinase 2 96T
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB24866 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Mouse,Mus musculus,Sapk3,
EIAAB24872 MAP kinase 13,MAP kinase p38 delta,MAPK 13,Mapk13,Mitogen-activated protein kinase 13,Mitogen-activated protein kinase p38 delta,Mouse,Mus musculus,Serk4,Stress-activated protein kinase 4
EIAAB24868 ERK-6,Extracellular signal-regulated kinase 6,MAP kinase 12,MAP kinase p38 gamma,MAPK 12,Mapk12,Mitogen-activated protein kinase 12,Mitogen-activated protein kinase p38 gamma,Rat,Rattus norvegicus,Sap
EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB24783 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
E1206m ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
E1206r ELISA kit Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protei 96T
U1206m CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T
U1206r CLIA Erk2,ERK-2,ERT1,Extracellular signal-regulated kinase 2,MAP kinase 1,MAP kinase 2,MAP kinase isoform p42,Mapk,MAPK 1,MAPK 2,Mapk1,Mitogen-activated protein kinase 1,Mitogen-activated protein kina 96T


 

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