Q39024 (MPK4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	376 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. May be involved in the cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1, MEK1/MKK2 and MPK4/MPK6). May act as negative regulator of salt tolerance. Ref.10 Ref.16 Ref.17 Ref.18 Ref.20
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated by threonine and tyrosine phosphorylation. Activated by the MAP kinase kinases MEK1 and MKK2. Activated in response to touch, wounding, low temperature, low humidity, salt stress and the bacterial elicitors flagellin and harpin. Repressed by the protein phosphatase 2C AP2C1. Repressed by DSPTP1-mediated dephosphorylation. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.17 Ref.19
Subunit structure	Interacts with MEKK1, MEK1 and MKK2. May form a ternary complex with MEKK1 and MEK1 or MKK2. 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.19 Ref.20
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › cytoskeleton. Note: Translocated into the nucleus in response to phosphorylation Probable. Ref.18
Tissue specificity	Expressed in the veins and stomatal guard cells of leaf plates, petioles, stem, roots and flowers. Ref.10 Ref.20
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.20
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. Ref.9 Ref.11 Ref.12
Disruption phenotype	Dwarf plants with cytokinetic defects in leaf epidermal cells. Abnormally developed and branched root hairs. Heavily bundled and disoriented cortical microtubules resistant to oryzalin. Ref.20
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 process	Plant defense
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cortical microtubule organization Inferred from mutant phenotype Ref.20. 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, jasmonic acid mediated signaling pathway Traceable author statement PubMed 11544109. Source: TAIR male meiosis cytokinesis Inferred from mutant phenotype PubMed 21575092. Source: TAIR pollen development Inferred from mutant phenotype PubMed 21575092. Source: TAIR response to abscisic acid stimulus 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 systemic acquired resistance, salicylic acid mediated signaling pathway Inferred from mutant phenotype PubMed 16813576. Source: TAIR
Cellular_component	cytosol Inferred from direct assay PubMed 21166475. Source: TAIR microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from direct assay PubMed 15610358Ref.18. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase activity Inferred from direct assay Ref.18. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MKK1	Q94A06	5	EBI-994375,EBI-994464
MKK2	Q9S7U9	4	EBI-994375,EBI-994350
MKS1	Q8LGD5	9	EBI-994375,EBI-1392198
T15F16.3	O81472	3	EBI-994375,EBI-6271434
WRKY25	O22921	2	EBI-994375,EBI-1392386

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	Mitogen-activated protein kinase 4		PRO_0000186313
Regions
	Domain	43 – 329	287	Protein kinase
	Nucleotide binding	49 – 57	9	ATP By similarity
	Motif	201 – 203	3	TXY
Sites
	Active site	169	1	Proton acceptor By similarity
	Binding site	72	1	ATP By similarity
Amino acid modifications
	Modified residue	201	1	Phosphothreonine
	Modified residue	203	1	Phosphotyrosine
Natural variations
	Natural variant	115	1	E → Q in strain: cv. C24, cv. Lz-0, cv. Wei-0, cv. Yo-0. Ref.2
	Natural variant	293	1	A → 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
	Mutagenesis	187	1	D → A: Loss of kinase activity. Ref.12
	Mutagenesis	201	1	T → A: Loss of kinase activity; when associated with Y-203. Ref.10
	Mutagenesis	203	1	Y → F: Loss of kinase activity; when associated with T-201. Ref.10
	Sequence conflict	313	1	D → E in BAA04867. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q39024 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 448F65C25C95AAEB	FASTA	376	42,852
	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

References

	« Hide 'large scale' referencesShow '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. , 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; MEK1 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: 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]	"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.
[20]	"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.
+	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.
IPI	IPI00521890.
PIR	S40470.
RefSeq	NP_192046.1. NM_116367.2.
UniGene	At.19915.
3D structure databases
ProteinModelPortal	Q39024.
SMR	Q39024. Positions 36-373.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q39024. 6 interactions.
STRING	3702.AT4G01370.1-P.
Proteomic databases
PaxDb	Q39024.
PRIDE	Q39024.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G01370.1; AT4G01370.1; AT4G01370.
GeneID	828151.
KEGG	ath:AT4G01370.
Organism-specific databases
GeneFarm	827. 89.
TAIR	At4g01370.
Phylogenomic databases
eggNOG	COG0515.
InParanoid	Q39024.
KO	K04371.
OMA	PRRENFN.
PhylomeDB	Q39024.
ProtClustDB	CLSN2915881.
Enzyme and pathway databases
BRENDA	2.7.11.24. 399.
Gene expression databases
Genevestigator	Q39024.
GermOnline	AT4G01370. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR003527. MAP_kinase_CS. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MPK4_ARATH

Accession

Primary (citable) accession number: Q39024
Secondary accession number(s): B2BDE5 , B2BDE6, B2BDE8, B2BDG2, O04597, Q45V20, Q9M136

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	June 6, 2002
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program