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Q39024 (MPK4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 4

Short name=AtMPK4
Short name=MAP kinase 4
EC=2.7.11.24
Gene names
Name:MPK4
Ordered Locus Names:At4g01370
ORF Names:F2N1.1, F2N1_2-t
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.10 Ref.16 Ref.17 Ref.18 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.20 Ref.21 Ref.25 Ref.26 Ref.27

Subunit structure

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. Ref.8 Ref.17 Ref.18 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27

Subcellular location

Cytoplasm. Nucleus. Cytoplasmcytoskeleton. Note: Translocated into the nucleus in response to phosphorylation Probable. localized to the cell plate. Ref.18 Ref.25

Tissue specificity

Ubiquitous. Expressed in the veins and stomatal guard cells of leaf plates, petioles, stem, roots and flowers. Ref.10 Ref.24 Ref.27

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. Ref.24

Domain

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

Post-translational modification

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. Ref.9 Ref.11 Ref.12 Ref.26

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. Ref.22 Ref.24 Ref.25 Ref.27

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processImmunity
Innate immunity
Plant defense
Stress response
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcortical microtubule organization

Inferred from mutant phenotype Ref.24. Source: UniProtKB

cytokinesis by cell plate formation

Inferred from mutant phenotype Ref.25. Source: UniProtKB

hyperosmotic response

Inferred from mutant phenotype Ref.16. Source: TAIR

hypotonic salinity response

Inferred from direct assay Ref.16. Source: TAIR

jasmonic acid and ethylene-dependent systemic resistance

Inferred from mutant phenotype PubMed 16813576. Source: TAIR

jasmonic acid and ethylene-dependent systemic resistance, jasmonic acid mediated signaling pathway

Traceable author statement PubMed 11544109. Source: TAIR

male meiosis cytokinesis

Inferred from mutant phenotype Ref.27. Source: TAIR

phosphorylation

Inferred from direct assay Ref.18. Source: TAIR

pollen development

Inferred from mutant phenotype Ref.27. Source: TAIR

protein phosphorylation

Inferred from direct assay PubMed 19616764PubMed 22643122. Source: UniProtKB

response to abscisic acid

Inferred from expression pattern PubMed 18248592. Source: TAIR

response to cold

Inferred from direct assay Ref.17. Source: TAIR

response to fungus

Inferred from mutant phenotype PubMed 16813576. Source: TAIR

response to salt stress

Inferred from direct assay Ref.17. Source: TAIR

systemic acquired resistance, salicylic acid mediated signaling pathway

Inferred from mutant phenotype PubMed 16813576. Source: TAIR

   Cellular_componentcell plate

Inferred from direct assay Ref.25. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.25. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase activity

Inferred from direct assay Ref.18. Source: TAIR

kinase activity

Inferred from direct assay PubMed 19616764. Source: UniProtKB

protein kinase activity

Inferred from direct assay PubMed 22643122. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Mitogen-activated protein kinase 4
PRO_0000186313

Regions

Domain43 – 329287Protein kinase
Nucleotide binding49 – 579ATP By similarity
Motif201 – 2033TXY

Sites

Active site1691Proton acceptor By similarity
Binding site721ATP By similarity

Amino acid modifications

Modified residue2011Phosphothreonine
Modified residue2031Phosphotyrosine
Modified residue2061Phosphothreonine By similarity

Natural variations

Natural variant1151E → Q in strain: cv. C24, cv. Lz-0, cv. Wei-0, cv. Yo-0. Ref.2
Natural variant2931A → V in strain: cv. Ak-1, cv. Bay-0, cv. Di-0, cv. Landsberg erecta, cv. Tsu-0, cv. Wei-0. Ref.2

Experimental info

Mutagenesis1871D → A: Loss of kinase activity. Ref.12
Mutagenesis2011T → A: Loss of kinase activity; when associated with Y-203. Ref.10
Mutagenesis2031Y → F: Loss of kinase activity; when associated with T-201. Ref.10
Sequence conflict3131D → E in BAA04867. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q39024 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 448F65C25C95AAEB

FASTA37642,852
        10         20         30         40         50         60 
MSAESCFGSS GDQSSSKGVA THGGSYVQYN VYGNLFEVSR KYVPPLRPIG RGAYGIVCAA 

        70         80         90        100        110        120 
TNSETGEEVA IKKIGNAFDN IIDAKRTLRE IKLLKHMDHE NVIAVKDIIK PPQRENFNDV 

       130        140        150        160        170        180 
YIVYELMDTD LHQIIRSNQP LTDDHCRFFL YQLLRGLKYV HSANVLHRDL KPSNLLLNAN 

       190        200        210        220        230        240 
CDLKLGDFGL ARTKSETDFM TEYVVTRWYR APELLLNCSE YTAAIDIWSV GCILGETMTR 

       250        260        270        280        290        300 
EPLFPGKDYV HQLRLITELI GSPDDSSLGF LRSDNARRYV RQLPQYPRQN FAARFPNMSA 

       310        320        330        340        350        360 
GAVDLLEKML VFDPSRRITV DEALCHPYLA PLHDINEEPV CVRPFNFDFE QPTLTEENIK 

       370 
ELIYRETVKF NPQDSV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Arabidopsis MAP kinase 4 negatively regulates systemic acquired resistance."
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.
Cell 103:1111-1120(2000) [PubMed] [Europe PMC] [Abstract]
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.
[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]"The MAP kinase substrate MKS1 is a regulator of plant defense responses."
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.
EMBO J. 24:2579-2589(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH MKS1.
[19]"Ancient signals: comparative genomics of plant MAPK and MAPKK gene families."
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.
Trends Plant Sci. 11:192-198(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS40470.
RefSeqNP_192046.1. NM_116367.2.
UniGeneAt.19915.

3D structure databases

ProteinModelPortalQ39024.
SMRQ39024. Positions 36-373.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid13440. 11 interactions.
IntActQ39024. 7 interactions.
MINTMINT-7232331.
STRING3702.AT4G01370.1-P.

Proteomic databases

PaxDbQ39024.
PRIDEQ39024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G01370.1; AT4G01370.1; AT4G01370.
GeneID828151.
KEGGath:AT4G01370.

Organism-specific databases

GeneFarm827. 89.
TAIRAT4G01370.

Phylogenomic databases

eggNOGCOG0515.
InParanoidQ39024.
KOK04371.
OMACAATNSE.
PhylomeDBQ39024.
ProtClustDBCLSN2915881.

Enzyme and pathway databases

BioCycARA:AT4G01370-MONOMER.
BRENDA2.7.11.24. 399.

Gene expression databases

GenevestigatorQ39024.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ39024.

Entry information

Entry nameMPK4_ARATH
AccessionPrimary (citable) accession number: Q39024
Secondary accession number(s): B2BDE5 expand/collapse secondary AC list , B2BDE6, B2BDE8, B2BDG2, O04597, Q45V20, Q9M136
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: April 16, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names