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Q39024

- MPK4_ARATH

UniProt

Q39024 - MPK4_ARATH

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Protein

Mitogen-activated protein kinase 4

Gene

MPK4

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATPPROSITE-ProRule annotation
Active sitei169 – 1691Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB
  3. MAP kinase activity Source: TAIR
  4. protein kinase activity Source: UniProtKB

GO - Biological processi

  1. cortical microtubule organization Source: UniProtKB
  2. cytokinesis by cell plate formation Source: UniProtKB
  3. hyperosmotic response Source: TAIR
  4. hypotonic salinity response Source: TAIR
  5. jasmonic acid and ethylene-dependent systemic resistance Source: TAIR
  6. jasmonic acid and ethylene-dependent systemic resistance, jasmonic acid mediated signaling pathway Source: TAIR
  7. male meiosis cytokinesis Source: TAIR
  8. phosphorylation Source: TAIR
  9. pollen development Source: TAIR
  10. protein phosphorylation Source: UniProtKB
  11. response to abscisic acid Source: TAIR
  12. response to cold Source: TAIR
  13. response to fungus Source: TAIR
  14. response to salt stress Source: TAIR
  15. systemic acquired resistance, salicylic acid mediated signaling pathway Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Immunity, Innate immunity, Plant defense, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G01370-MONOMER.
BRENDAi2.7.11.24. 399.
ReactomeiREACT_190855. CREB phosphorylation through the activation of Ras.
REACT_190946. KSRP destabilizes mRNA.
REACT_202229. ERK1 activation.
REACT_208246. ERKs are inactivated.
REACT_209747. ERK2 activation.
REACT_216613. Signalling to ERK5.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 4 (EC:2.7.11.24)
Short name:
AtMPK4
Short name:
MAP kinase 4
Gene namesi
Name:MPK4
Ordered Locus Names:At4g01370
ORF Names:F2N1.1, F2N1_2-t
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G01370.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmcytoskeleton
Note: Translocated into the nucleus in response to phosphorylation (Probable). localized to the cell plate.Curated

GO - Cellular componenti

  1. cell plate Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: TAIR
  4. microtubule Source: UniProtKB-KW
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871D → A: Loss of kinase activity. 1 Publication
Mutagenesisi201 – 2011T → A: Loss of kinase activity; when associated with Y-203. 1 Publication
Mutagenesisi203 – 2031Y → F: Loss of kinase activity; when associated with T-201. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Mitogen-activated protein kinase 4PRO_0000186313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011Phosphothreonine1 Publication
Modified residuei203 – 2031Phosphotyrosine1 Publication
Modified residuei206 – 2061PhosphothreonineBy similarity

Post-translational modificationi

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.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ39024.
PRIDEiQ39024.

Expressioni

Tissue specificityi

Ubiquitous. Expressed in the veins and stomatal guard cells of leaf plates, petioles, stem, roots and flowers.3 Publications

Developmental stagei

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.1 Publication

Gene expression databases

GenevestigatoriQ39024.

Interactioni

Subunit structurei

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 MAP65-1.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MKK1Q94A066EBI-994375,EBI-994464
MKK2Q9S7U95EBI-994375,EBI-994350
MKS1Q8LGD59EBI-994375,EBI-1392198
T15F16.3O814723EBI-994375,EBI-6271434
WRKY25O229212EBI-994375,EBI-1392386
WRKY33Q8S8P52EBI-994375,EBI-1392374

Protein-protein interaction databases

BioGridi13440. 11 interactions.
IntActiQ39024. 7 interactions.
MINTiMINT-7232331.
STRINGi3702.AT4G01370.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ39024.
SMRiQ39024. Positions 36-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 329287Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 2033TXY

Domaini

The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiQ39024.
KOiK04371.
OMAiWREALKF.
PhylomeDBiQ39024.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39024-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAESCFGSS GDQSSSKGVA THGGSYVQYN VYGNLFEVSR KYVPPLRPIG
60 70 80 90 100
RGAYGIVCAA TNSETGEEVA IKKIGNAFDN IIDAKRTLRE IKLLKHMDHE
110 120 130 140 150
NVIAVKDIIK PPQRENFNDV YIVYELMDTD LHQIIRSNQP LTDDHCRFFL
160 170 180 190 200
YQLLRGLKYV HSANVLHRDL KPSNLLLNAN CDLKLGDFGL ARTKSETDFM
210 220 230 240 250
TEYVVTRWYR APELLLNCSE YTAAIDIWSV GCILGETMTR EPLFPGKDYV
260 270 280 290 300
HQLRLITELI GSPDDSSLGF LRSDNARRYV RQLPQYPRQN FAARFPNMSA
310 320 330 340 350
GAVDLLEKML VFDPSRRITV DEALCHPYLA PLHDINEEPV CVRPFNFDFE
360 370
QPTLTEENIK ELIYRETVKF NPQDSV
Length:376
Mass (Da):42,852
Last modified:June 6, 2002 - v2
Checksum:i448F65C25C95AAEB
GO

Sequence cautioni

The sequence AAB61033.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131D → E in BAA04867. (PubMed:8282107)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151E → Q in strain: cv. C24, cv. Lz-0, cv. Wei-0, cv. Yo-0. 1 Publication
Natural varianti293 – 2931A → V in strain: cv. Ak-1, cv. Bay-0, cv. Di-0, cv. Landsberg erecta, cv. Tsu-0, cv. Wei-0. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21840 mRNA. Translation: BAA04867.1.
EF470667 Genomic DNA. Translation: ABR46145.1.
EF470668 Genomic DNA. Translation: ABR46146.1.
EF470669 Genomic DNA. Translation: ABR46147.1.
EF470670 Genomic DNA. Translation: ABR46148.1.
EF470671 Genomic DNA. Translation: ABR46149.1.
EF470672 Genomic DNA. Translation: ABR46150.1.
EF470673 Genomic DNA. Translation: ABR46151.1.
EF470674 Genomic DNA. Translation: ABR46152.1.
EF470675 Genomic DNA. Translation: ABR46153.1.
EF470676 Genomic DNA. Translation: ABR46154.1.
EF470677 Genomic DNA. Translation: ABR46155.1.
EF470678 Genomic DNA. Translation: ABR46156.1.
EF470679 Genomic DNA. Translation: ABR46157.1.
EF470680 Genomic DNA. Translation: ABR46158.1.
EF470681 Genomic DNA. Translation: ABR46159.1.
EF470682 Genomic DNA. Translation: ABR46160.1.
EF470683 Genomic DNA. Translation: ABR46161.1.
EF470684 Genomic DNA. Translation: ABR46162.1.
EF470685 Genomic DNA. Translation: ABR46163.1.
EF470686 Genomic DNA. Translation: ABR46164.1.
DQ112072 Genomic DNA. Translation: AAZ20637.1.
AF007269 Genomic DNA. Translation: AAB61033.1. Sequence problems.
AL161491 Genomic DNA. Translation: CAB80946.1.
CP002687 Genomic DNA. Translation: AEE82016.1.
AF360231 mRNA. Translation: AAK25941.1.
AY040031 mRNA. Translation: AAK64089.1.
AY088537 mRNA. Translation: AAM66070.1.
PIRiS40470.
RefSeqiNP_192046.1. NM_116367.2.
UniGeneiAt.19915.

Genome annotation databases

EnsemblPlantsiAT4G01370.1; AT4G01370.1; AT4G01370.
GeneIDi828151.
KEGGiath:AT4G01370.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21840 mRNA. Translation: BAA04867.1 .
EF470667 Genomic DNA. Translation: ABR46145.1 .
EF470668 Genomic DNA. Translation: ABR46146.1 .
EF470669 Genomic DNA. Translation: ABR46147.1 .
EF470670 Genomic DNA. Translation: ABR46148.1 .
EF470671 Genomic DNA. Translation: ABR46149.1 .
EF470672 Genomic DNA. Translation: ABR46150.1 .
EF470673 Genomic DNA. Translation: ABR46151.1 .
EF470674 Genomic DNA. Translation: ABR46152.1 .
EF470675 Genomic DNA. Translation: ABR46153.1 .
EF470676 Genomic DNA. Translation: ABR46154.1 .
EF470677 Genomic DNA. Translation: ABR46155.1 .
EF470678 Genomic DNA. Translation: ABR46156.1 .
EF470679 Genomic DNA. Translation: ABR46157.1 .
EF470680 Genomic DNA. Translation: ABR46158.1 .
EF470681 Genomic DNA. Translation: ABR46159.1 .
EF470682 Genomic DNA. Translation: ABR46160.1 .
EF470683 Genomic DNA. Translation: ABR46161.1 .
EF470684 Genomic DNA. Translation: ABR46162.1 .
EF470685 Genomic DNA. Translation: ABR46163.1 .
EF470686 Genomic DNA. Translation: ABR46164.1 .
DQ112072 Genomic DNA. Translation: AAZ20637.1 .
AF007269 Genomic DNA. Translation: AAB61033.1 . Sequence problems.
AL161491 Genomic DNA. Translation: CAB80946.1 .
CP002687 Genomic DNA. Translation: AEE82016.1 .
AF360231 mRNA. Translation: AAK25941.1 .
AY040031 mRNA. Translation: AAK64089.1 .
AY088537 mRNA. Translation: AAM66070.1 .
PIRi S40470.
RefSeqi NP_192046.1. NM_116367.2.
UniGenei At.19915.

3D structure databases

ProteinModelPortali Q39024.
SMRi Q39024. Positions 36-373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 13440. 11 interactions.
IntActi Q39024. 7 interactions.
MINTi MINT-7232331.
STRINGi 3702.AT4G01370.1-P.

Proteomic databases

PaxDbi Q39024.
PRIDEi Q39024.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G01370.1 ; AT4G01370.1 ; AT4G01370 .
GeneIDi 828151.
KEGGi ath:AT4G01370.

Organism-specific databases

GeneFarmi 827. 89.
TAIRi AT4G01370.

Phylogenomic databases

eggNOGi COG0515.
InParanoidi Q39024.
KOi K04371.
OMAi WREALKF.
PhylomeDBi Q39024.

Enzyme and pathway databases

BioCyci ARA:AT4G01370-MONOMER.
BRENDAi 2.7.11.24. 399.
Reactomei REACT_190855. CREB phosphorylation through the activation of Ras.
REACT_190946. KSRP destabilizes mRNA.
REACT_202229. ERK1 activation.
REACT_208246. ERKs are inactivated.
REACT_209747. ERK2 activation.
REACT_216613. Signalling to ERK5.

Miscellaneous databases

PROi Q39024.

Gene expression databases

Genevestigatori Q39024.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana."
    Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H., Shinozaki K.
    FEBS Lett. 336:440-444(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
  2. "Arabidopsis thaliana genes encoding defense signaling and recognition proteins exhibit contrasting evolutionary dynamics."
    Caldwell K.S., Michelmore R.W.
    Genetics 181:671-684(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], 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.
  3. "MAP kinase 4 genomic sequence from Arabidopsis thaliana."
    Sharma P.K., Kumar R., Garg G.K., Khan G.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    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.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "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.
  7. "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].
  8. "Isolation of ATMEKK1 (a MAP kinase kinase kinase)-interacting proteins and analysis of a MAP kinase cascade in Arabidopsis."
    Ichimura K., Mizoguchi T., Irie K., Morris P.C., Giraudat J., Matsumoto K., Shinozaki K.
    Biochem. Biophys. Res. Commun. 253:532-543(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH MEKK1; MKK1 AND MKK2.
  9. "Identification of a dual-specificity protein phosphatase that inactivates a MAP kinase from Arabidopsis."
    Gupta R., Huang Y., Kieber J., Luan S.
    Plant J. 16:581-589(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, DEPHOSPHORYLATION.
    Strain: cv. Columbia.
  10. Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF THR-201 AND TYR-203.
  11. "Various abiotic stresses rapidly activate Arabidopsis MAP kinases ATMPK4 and ATMPK6."
    Ichimura K., Mizoguchi T., Yoshida R., Yuasa T., Shinozaki K.
    Plant J. 24:655-665(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-201 AND TYR-203.
  12. "ATMPK4, an Arabidopsis homolog of mitogen-activated protein kinase, is activated in vitro by AtMEK1 through threonine phosphorylation."
    Huang Y., Li H., Gupta R., Morris P.C., Luan S., Kieber J.J.
    Plant Physiol. 122:1301-1310(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION, MUTAGENESIS OF ASP-187.
  13. "Harpin induces activation of the Arabidopsis mitogen-activated protein kinases AtMPK4 and AtMPK6."
    Desikan R., Hancock J.T., Ichimura K., Shinozaki K., Neill S.J.
    Plant Physiol. 126:1579-1587(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  14. "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."
    Matsuoka D., Nanmori T., Sato K., Fukami Y., Kikkawa U., Yasuda T.
    Plant J. 29:637-647(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  15. "Mitogen-activated protein kinase cascades in plants: a new nomenclature."
    MAPK group
    Trends Plant Sci. 7:301-308(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  16. "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."
    Droillard M.-J., Boudsocq M., Barbier-Brygoo H., Lauriere C.
    FEBS Lett. 574:42-48(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION.
  17. "The MKK2 pathway mediates cold and salt stress signaling in Arabidopsis."
    Teige M., Scheikl E., Eulgem T., Doczi R., Ichimura K., Shinozaki K., Dangl J.L., Hirt H.
    Mol. Cell 15:141-152(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MKK2.
  18. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MKS1.
  19. Cited for: GENE FAMILY.
  20. "The MAP kinase kinase MKK2 affects disease resistance in Arabidopsis."
    Brader G., Djamei A., Teige M., Palva E.T., Hirt H.
    Mol. Plant Microbe Interact. 20:589-596(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  21. "The PP2C-type phosphatase AP2C1, which negatively regulates MPK4 and MPK6, modulates innate immunity, jasmonic acid, and ethylene levels in Arabidopsis."
    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.
    Plant Cell 19:2213-2224(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH AP2C1.
  22. "MEKK1, MKK1/MKK2 and MPK4 function together in a mitogen-activated protein kinase cascade to regulate innate immunity in plants."
    Gao M., Liu J., Bi D., Zhang Z., Cheng F., Chen S., Zhang Y.
    Cell Res. 18:1190-1198(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEKK1; MKK1 AND MKK2, DISRUPTION PHENOTYPE.
  23. "Comprehensive analysis of protein-protein interactions between Arabidopsis MAPKs and MAPK kinases helps define potential MAPK signalling modules."
    Lee J.S., Huh K.W., Bhargava A., Ellis B.E.
    Plant Signal. Behav. 3:1037-1041(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKK1; MKK2 AND MKK6.
  24. "Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2 and 3 and mitogen-activated protein kinase 4 are essential for microtubule organization."
    Beck M., Komis G., Mueller J., Menzel D., Samaj J.
    Plant Cell 22:755-771(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP65-1, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  25. "The MAP kinase MPK4 is required for cytokinesis in Arabidopsis thaliana."
    Kosetsu K., Matsunaga S., Nakagami H., Colcombet J., Sasabe M., Soyano T., Takahashi Y., Hirt H., Machida Y.
    Plant Cell 22:3778-3790(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, ENZYME REGULATION.
  26. "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."
    Takahashi Y., Soyano T., Kosetsu K., Sasabe M., Machida Y.
    Plant Cell Physiol. 51:1766-1776(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, PHOSPHORYLATION BY MKK6, INTERACTION WITH MKK6.
  27. "AtMPK4 is required for male-specific meiotic cytokinesis in Arabidopsis."
    Zeng Q., Chen J.G., Ellis B.E.
    Plant J. 67:895-906(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, ENZYME REGULATION, INTERACTION WITH MKK1 AND MKK6, TISSUE SPECIFICITY.

Entry informationi

Entry nameiMPK4_ARATH
AccessioniPrimary (citable) accession number: Q39024
Secondary accession number(s): B2BDE5
, B2BDE6, B2BDE8, B2BDG2, O04597, Q45V20, Q9M136
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: October 29, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3