Q9S7U9 (M2K2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mitogen-activated protein kinase kinase 2
Short name=AtMAP2Kbeta
Short name=AtMKK2
Short name=MAP kinase kinase 2
EC=2.7.12.2

Gene names

Name:	MKK2
Synonyms:	MAP2K, MK1
Ordered Locus Names:	At4g29810
ORF Names:	F27B13.50

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	363 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). Activates by phosphorylation the downstream MPK4 and MPK6. Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Activated in response to cold and salt stresses through serine and threonine phosphorylation by MEKK1. Ref.9
Subunit structure	Interacts with MEKK1, MPK4 and MPK6. Ref.1 Ref.9
Post-translational modification	Phosphorylated on Thr-220 and Thr-226, which activates the enzyme. Ref.1 Ref.7 Ref.9 Ref.10
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 Reference proteome
Gene Ontology (GO)
Biological process	MAPKKK cascade Inferred from genetic interaction Ref.1. Source: TAIR cold acclimation Inferred from mutant phenotype Ref.9. Source: TAIR defense response, incompatible interaction Inferred from genetic interaction. Source: TAIR response to salt stress Inferred from direct assay Ref.9. Source: TAIR
Cellular component	cytoplasm Inferred from direct assay. Source: TAIR plasma membrane Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW MAP kinase kinase activity Inferred from direct assay Ref.9. Source: TAIR protein binding Inferred from physical interaction Ref.9. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MPK10	Q9M1Z5	2	EBI-994350,EBI-2358527
MPK11	Q9LMM5	2	EBI-994350,EBI-2358699
MPK13	Q9LQQ9	2	EBI-994350,EBI-2358762
MPK4	Q39024	4	EBI-994350,EBI-994375
MPK6	Q39026	5	EBI-994350,EBI-349548

Alternative products

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

Isoform 1 (identifier: Q9S7U9-1)

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: Q9S7U9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     26-26: L → LRKGFGSLCR

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Mitogen-activated protein kinase kinase 2		PRO_0000245822
Regions
	Domain	70 – 330	261	Protein kinase
	Nucleotide binding	76 – 84	9	ATP By similarity
Sites
	Active site	192	1	Proton acceptor By similarity
	Binding site	99	1	ATP By similarity
Amino acid modifications
	Modified residue	56	1	Phosphoserine Ref.10
	Modified residue	220	1	Phosphothreonine Ref.1 Ref.7 Ref.9
	Modified residue	226	1	Phosphothreonine Ref.1 Ref.7 Ref.9
Natural variations
	Alternative sequence	26	1	L → LRKGFGSLCR in isoform 2.		VSP_019784
Experimental info
	Mutagenesis	99	1	K → R: Loss of interaction with MEKK1. Ref.1
	Mutagenesis	220	1	T → A: Loss of interaction with MEKK1. Ref.1 Ref.7 Ref.9
	Mutagenesis	220	1	T → E: Constitutively active; when associated with E-226. Ref.1 Ref.7 Ref.9
	Mutagenesis	226	1	T → A: Loss of interaction with MEKK1. Ref.1 Ref.7 Ref.9
	Mutagenesis	226	1	T → E: Constitutively active; when associated with E-220. Ref.1 Ref.7 Ref.9
	Sequence conflict	314	1	D → E in CAA07281. Ref.2
	Sequence conflict	314	1	D → E in AAC72754. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 11, 2006. Version 2. Checksum: 3E7EFC6D3A831D93	FASTA	363	39,848
	10 20 30 40 50 60 MKKGGFSNNL KLAIPVAGEQ SITKFLTQSG TFKDGDLRVN KDGVRIISQL EPEVLSPIKP 70 80 90 100 110 120 ADDQLSLSDL DMVKVIGKGS SGVVQLVQHK WTGQFFALKV IQLNIDEAIR KAIAQELKIN 130 140 150 160 170 180 QSSQCPNLVT SYQSFYDNGA ISLILEYMDG GSLADFLKSV KAIPDSYLSA IFRQVLQGLI 190 200 210 220 230 240 YLHHDRHIIH RDLKPSNLLI NHRGEVKITD FGVSTVMTNT AGLANTFVGT YNYMSPERIV 250 260 270 280 290 300 GNKYGNKSDI WSLGLVVLEC ATGKFPYAPP NQEETWTSVF ELMEAIVDQP PPALPSGNFS 310 320 330 340 350 360 PELSSFISTC LQKDPNSRSS AKELMEHPFL NKYDYSGINL ASYFTDAGSP LATLGNLSGT FSV
	Isoform 2 [UniParc]. Checksum: 7D682428D1CCFE22	FASTA	372	40,854
	10 20 30 40 50 60 MKKGGFSNNL KLAIPVAGEQ SITKFLRKGF GSLCRTQSGT FKDGDLRVNK DGVRIISQLE 70 80 90 100 110 120 PEVLSPIKPA DDQLSLSDLD MVKVIGKGSS GVVQLVQHKW TGQFFALKVI QLNIDEAIRK 130 140 150 160 170 180 AIAQELKINQ SSQCPNLVTS YQSFYDNGAI SLILEYMDGG SLADFLKSVK AIPDSYLSAI 190 200 210 220 230 240 FRQVLQGLIY LHHDRHIIHR DLKPSNLLIN HRGEVKITDF GVSTVMTNTA GLANTFVGTY 250 260 270 280 290 300 NYMSPERIVG NKYGNKSDIW SLGLVVLECA TGKFPYAPPN QEETWTSVFE LMEAIVDQPP 310 320 330 340 350 360 PALPSGNFSP ELSSFISTCL QKDPNSRSSA KELMEHPFLN KYDYSGINLA SYFTDAGSPL 370 ATLGNLSGTF SV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, TISSUE SPECIFICITY, INTERACTION WITH MEKK1 AND MPK4, MUTAGENESIS OF LYS-99; THR-220 AND THR-226, PHOSPHORYLATION AT THR-220 AND THR-226. Strain: cv. Columbia.
[2]	"Molecular characterization and expression of an Arabidopsis thaliana L. MAP kinase kinase cDNA AtMAP2Kalpha." Hamal A., Jouannic S., Leprince A.-S., Kreis M., Henry Y. Plant Sci. 140:41-52(1999) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: cv. Columbia. Tissue: Root.
[3]	"AMK1, a MAP kinase kinase from Arabidopsis thaliana is a functional homolog of PBS2, the MAPKK of the osmolarity pathway in yeast Saccharomyces cerevisiae." Sherman A., Fink G.R. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: cv. Columbia.
[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: 10617198] [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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: cv. Columbia.
[7]	"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-220 AND THR-226, MUTAGENESIS OF THR-220 AND THR-226.
[8]	"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.
[9]	"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: FUNCTION, ENZYME REGULATION, INTERACTION WITH MPK4 AND MAPK6, PHOSPHORYLATION AT THR-220 AND THR-226, MUTAGENESIS OF THR-220 AND THR-226.
[10]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB015313 mRNA. Translation: BAA28828.1. AJ006871 mRNA. Translation: CAA07281.1. AF067792 mRNA. Translation: AAC72754.1. AL050352 Genomic DNA. Translation: CAB43656.1. AL161575 Genomic DNA. Translation: CAB79739.1. CP002687 Genomic DNA. Translation: AEE85679.1. CP002687 Genomic DNA. Translation: AEE85680.1. AF385688 mRNA. Translation: AAK60281.1. AY078009 mRNA. Translation: AAL77710.1.
IPI	IPI00520140. IPI00656994.
PIR	T08542. T51735.
RefSeq	NP_001031751.1. NM_001036674.1. NP_194710.1. NM_119127.3.
UniGene	At.1001. At.24272.
3D structure databases
ProteinModelPortal	Q9S7U9.
SMR	Q9S7U9. Positions 65-347.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9S7U9. 7 interactions.
STRING	Q9S7U9.
Proteomic databases
PRIDE	Q9S7U9.
ProMEX	Q9S7U9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G29810.1; AT4G29810.1; AT4G29810.
GeneID	829103.
GenomeReviews	Gene locus AT4G29810 in contig CT486007_GR.
KEGG	ath:AT4G29810.
NMPDR	fig|3702.1.peg.20954.
Organism-specific databases
GeneFarm	887. 89.
TAIR	At4g29810.
Phylogenomic databases
GeneTree	EPGT00070000029225.
HOGENOM	HBG755340.
InParanoid	Q9S7U9.
OMA	KVIQLNI.
PhylomeDB	Q9S7U9.
ProtClustDB	CLSN2685391.
Gene expression databases
Genevestigator	Q9S7U9.
GermOnline	AT4G29810. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR017442. Se/Thr_kinase-like_dom. IPR008271. Ser/Thr_kinase_AS. IPR002290. Ser/Thr_kinase_dom. [Graphical view]
KO	K04368.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
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

M2K2_ARATH

Accession

Primary (citable) accession number: Q9S7U9
Secondary accession number(s): O80395

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	July 11, 2006
Last modified:	December 14, 2011
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program