Reviewed, UniProtKB/Swiss-Prot Q94A06 (M2K1_ARATH)

Names and origin

Protein names

Recommended name:
    Mitogen-activated protein kinase kinase 1
      Short name=MAP kinase kinase 1
    EC=2.7.12.2
Alternative name(s):
    NMAPKK
    AtMEK1

Gene names

Name:	MKK1
Synonyms:	MEK1
Ordered Locus Names:	At4g26070
ORF Names:	F20B18.180

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May be involved in the cold and salinity stress-mediated MAP kinase signaling cascade (MEKK1, MEK1/MKK2 and MPK4/MPK6). Phosphorylates MPK4 in vitro. Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated through serine and threonine phosphorylation in response to wounding, cold, drought, salt stresses, hydrogen peroxide, bacterial flagellin and laminarin beta-glucan. Ref.9 Ref.11
Subunit structure	Interacts with MEKK1 (MAPKKK) and MPK4. May form a ternary complex with. Ref.6
Tissue specificity	Expressed in roots, stem, flowers and siliques. Ref.1
Induction	By wounding. Ref.9 Ref.11 Ref.1
Post-translational modification	Phosphorylated on Thr-218 and Ser-224, which activates the enzyme. Ref.9 Ref.8
Sequence similarities	Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response to bacterium Ref.11 Inferred from direct assay. Source: TAIR defense response, incompatible interaction Inferred from genetic interaction. Source: TAIR protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro response to hydrogen peroxide Ref.11 Inferred from direct assay. Source: TAIR response to molecule of bacterial origin Inferred from direct assay. Source: TAIR response to water deprivation Inferred from mutant phenotype. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Ref.7 Inferred from direct assay. Source: TAIR protein binding Ref.11 Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MPK11	Q9LMM5	1	EBI-994464,EBI-2358699
MPK12	Q8GYQ5	2	EBI-994464,EBI-2128461
MPK4	Q39024	5	EBI-994464,EBI-994375

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q94A06-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q94A06-2)

The sequence of this isoform differs from the canonical sequence as follows:
     308-308: C → W
     309-354: Missing.

Note: May be due to an intron retention. No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 354	354	Mitogen-activated protein kinase kinase 1		PRO_0000245821
Regions
	Domain	68 – 328	261	Protein kinase
	Nucleotide binding	74 – 82	9	ATP By similarity
Sites
	Active site	190	1	Proton acceptor By similarity
	Binding site	97	1	ATP By similarity
Amino acid modifications
	Modified residue	218	1	Phosphothreonine Ref.8
	Modified residue	220	1	Phosphoserine
	Modified residue	224	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	308	1	C → W in isoform 2.		VSP_019782
	Alternative sequence	309 – 354	46	Missing in isoform 2.		VSP_019783
Experimental info
	Mutagenesis	218	1	T → A: Loss of kinase activity in vitro; when associated with E-224. Ref.9 Ref.8
	Mutagenesis	218	1	T → E: Constitutively active; when associated with D-224. Increases kinase activity in vitro; when associated with E-224. Ref.9 Ref.8
	Mutagenesis	220	1	S → E: Increases kinase activity in vitro; when associated with E-224. Ref.9
	Mutagenesis	224	1	S → D: Constitutively active; when associated with E-218. Ref.9 Ref.8
	Mutagenesis	224	1	S → E: Increases kinase activity in vitro; when associated with E-218 or E-220. Ref.9 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: D889CFBB97653B8E	FASTA	354	39,210
	10 20 30 40 50 60 MNRGSLCPNP ICLPPLEQSI SKFLTQSGTF KDGDLRVNKD GIQTVSLSEP GAPPPIEPLD 70 80 90 100 110 120 NQLSLADLEV IKVIGKGSSG NVQLVKHKLT QQFFALKVIQ LNTEESTCRA ISQELRINLS 130 140 150 160 170 180 SQCPYLVSCY QSFYHNGLVS IILEFMDGGS LADLLKKVGK VPENMLSAIC KRVLRGLCYI 190 200 210 220 230 240 HHERRIIHRD LKPSNLLINH RGEVKITDFG VSKILTSTSS LANSFVGTYP YMSPERISGS 250 260 270 280 290 300 LYSNKSDIWS LGLVLLECAT GKFPYTPPEH KKGWSSVYEL VDAIVENPPP CAPSNLFSPE 310 320 330 340 350 FCSFISQCVQ KDPRDRKSAK ELLEHKFVKM FEDSDTNLSA YFTDAGSLIP PLAN
	Isoform 2. Checksum: 76E772A778D66F5E	FASTA	308	34,087
	10 20 30 40 50 60 MNRGSLCPNP ICLPPLEQSI SKFLTQSGTF KDGDLRVNKD GIQTVSLSEP GAPPPIEPLD 70 80 90 100 110 120 NQLSLADLEV IKVIGKGSSG NVQLVKHKLT QQFFALKVIQ LNTEESTCRA ISQELRINLS 130 140 150 160 170 180 SQCPYLVSCY QSFYHNGLVS IILEFMDGGS LADLLKKVGK VPENMLSAIC KRVLRGLCYI 190 200 210 220 230 240 HHERRIIHRD LKPSNLLINH RGEVKITDFG VSKILTSTSS LANSFVGTYP YMSPERISGS 250 260 270 280 290 300 LYSNKSDIWS LGLVLLECAT GKFPYTPPEH KKGWSSVYEL VDAIVENPPP CAPSNLFSPE FCSFISQW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterisation of MEK1, an Arabidopsis gene encoding a homologue of MAP kinase kinase." Morris P.C., Guerrier D., Leung J., Giraudat J. Plant Mol. Biol. 35:1057-1064(1997) [PubMed: 9426629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[2]	"Nucleotide sequence of plant mapkk subfamily." Nanmori T., Matsuoka D., Deguchi M., Ariga H. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: cv. Columbia.
[5]	"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] (ISOFORM 1).
[6]	"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: 9878570] [Abstract] Cited for: SUBUNIT, INTERACTION WITH MEKK1 AND MPK4.
[7]	"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: 10759527] [Abstract] Cited for: FUNCTION.
[8]	"MAP kinase signalling cascade in Arabidopsis innate immunity." Asai T., Tena G., Plotnikova J., Willmann M.R., Chiu W.-L., Gomez-Gomez L., Boller T., Ausubel F.M., Sheen J. Nature 415:977-983(2002) [PubMed: 11875555] [Abstract] Cited for: PHOSPHORYLATION AT THR-218 AND SER-224, MUTAGENESIS OF THR-218 AND SER-224.
[9]	"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: 11874576] [Abstract] Cited for: ENZYME REGULATION, PHOSPHORYLATION, MUTAGENESIS OF THR-218; SER-220 AND SER-224.
[10]	"Mitogen-activated protein kinase cascades in plants: a new nomenclature." MAPK group Trends Plant Sci. 7:301-308(2002) [PubMed: 12119167] [Abstract] Cited for: NOMENCLATURE.
[11]	"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: 15225555] [Abstract] Cited for: ENZYME REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF000977 mRNA. Translation: AAB97145.1. AB004796 mRNA. Translation: BAA24079.1. AL049483 Genomic DNA. Translation: CAB39672.1. AL161564 Genomic DNA. Translation: CAB79462.1. AY050774 mRNA. Translation: AAK92709.1. BT001935 mRNA. Translation: AAN71934.1. AY087065 mRNA. Translation: AAM64626.1.
IPI	IPI00532526. IPI00532754.
PIR	T04262.
RefSeq	NP_194337.1. NP_849446.1. NP_974619.1.
UniGene	At.21332 At.223
3D structure databases
SMR	Q94A06. Positions 61-345.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94A06. 4 interactions.
STRING	Q94A06.
Genome annotation databases
GeneID	828713.
GenomeReviews	Gene locus AT4G26070 in contig CT486007_GR.
KEGG	ath:AT4G26070.
NMPDR	fig|3702.1.peg.20524.
Organism-specific databases
GeneFarm	883. 89.
TAIR	At4g26070.
Phylogenomic databases
eggNOG	KOG0581.
HOGENOM	HBG755340.
InParanoid	Q94A06.
OMA	IRKKRNF.
PhylomeDB	Q94A06.
Enzyme and pathway databases
BRENDA	2.7.12.2. 302.
Gene expression databases
Genevestigator	Q94A06.
GermOnline	AT4G26070. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	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

M2K1_ARATH

Accession

Primary (citable) accession number: Q94A06
Secondary accession number(s): O04440, O04661

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 11, 2006
Last modified:	February 9, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)