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Q39022

- MPK2_ARATH

UniProt

Q39022 - MPK2_ARATH

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Protein

Mitogen-activated protein kinase 2

Gene
MPK2, At1g59580, T30E16.13
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation Inferred.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611ATP By similarity
Active sitei158 – 1581Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 469ATP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein phosphorylation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G59580-MONOMER.
ARA:GQT-1108-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 2 (EC:2.7.11.24)
Short name:
AtMPK2
Short name:
MAP kinase 2
Gene namesi
Name:MPK2
Ordered Locus Names:At1g59580
ORF Names:T30E16.13
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G59580.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Mitogen-activated protein kinase 2PRO_0000186311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911Phosphothreonine By similarity
Modified residuei193 – 1931Phosphotyrosine By similarity
Modified residuei196 – 1961Phosphothreonine By similarity

Post-translational modificationi

Dually phosphorylated on Thr-191 and Tyr-193, which activates the enzyme By similarity. Phosphorylated on Ser residue.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ39022.

Expressioni

Tissue specificityi

Highest levels in the stem. Present in the leaf, root and flower, but not in seeds.1 Publication

Gene expression databases

GenevestigatoriQ39022.

Interactioni

Subunit structurei

Interacts with MKK3.1 Publication

Protein-protein interaction databases

BioGridi27473. 1 interaction.
IntActiQ39022. 2 interactions.
STRINGi3702.AT1G59580.2-P.

Structurei

3D structure databases

ProteinModelPortaliQ39022.
SMRiQ39022. Positions 25-363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 319288Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi191 – 1933TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000233024.
InParanoidiQ39022.
KOiK04371.
OMAiNRESNER.
PhylomeDBiQ39022.

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_dom.
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.

Q39022-1 [UniParc]FASTAAdd to Basket

« Hide

MATPVDPPNG IRNQGKHYFS MWQTLFEIDT KYVPIKPIGR GAYGVVCSSV    50
NRESNERVAI KKIHNVFENR IDALRTLREL KLLRHLRHEN VVALKDVMMA 100
NHKRSFKDVY LVYELMDTDL HQIIKSSQVL SNDHCQYFLF QLLRGLKYIH 150
SANILHRDLK PGNLLVNANC DLKICDFGLA RTSNTKGQFM TEYVVTRWYR 200
APELLLCCDN YGTSIDVWSV GCIFAELLGR KPVFPGTECL NQIKLIINIL 250
GSQREEDLEF IDNPKAKRYI ESLPYSPGIS FSRLYPGANV LAIDLLQKML 300
VLDPSKRISV TEALQHPYMA PLYDPSANPP AQVPIDLDVD EDEDLGAEMI 350
RELMWKEMIH YHPEAATINN NEVSEF 376
Length:376
Mass (Da):43,125
Last modified:June 6, 2002 - v2
Checksum:iEDA07145A32CE25D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331V → M in BAA03536. 1 Publication
Sequence conflicti299 – 2991M → I in BAA03536. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14714 mRNA. Translation: BAA03536.1.
AC009317 Genomic DNA. Translation: AAF79750.1.
CP002684 Genomic DNA. Translation: AEE33590.1.
CP002684 Genomic DNA. Translation: AEE33591.1.
AY035134 mRNA. Translation: AAK59639.1.
AY113911 mRNA. Translation: AAM44959.1.
PIRiF96619.
RefSeqiNP_564746.1. NM_104651.4.
NP_974049.1. NM_202320.1.
UniGeneiAt.262.

Genome annotation databases

EnsemblPlantsiAT1G59580.1; AT1G59580.1; AT1G59580.
AT1G59580.2; AT1G59580.2; AT1G59580.
GeneIDi842248.
KEGGiath:AT1G59580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D14714 mRNA. Translation: BAA03536.1 .
AC009317 Genomic DNA. Translation: AAF79750.1 .
CP002684 Genomic DNA. Translation: AEE33590.1 .
CP002684 Genomic DNA. Translation: AEE33591.1 .
AY035134 mRNA. Translation: AAK59639.1 .
AY113911 mRNA. Translation: AAM44959.1 .
PIRi F96619.
RefSeqi NP_564746.1. NM_104651.4.
NP_974049.1. NM_202320.1.
UniGenei At.262.

3D structure databases

ProteinModelPortali Q39022.
SMRi Q39022. Positions 25-363.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 27473. 1 interaction.
IntActi Q39022. 2 interactions.
STRINGi 3702.AT1G59580.2-P.

Proteomic databases

PRIDEi Q39022.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G59580.1 ; AT1G59580.1 ; AT1G59580 .
AT1G59580.2 ; AT1G59580.2 ; AT1G59580 .
GeneIDi 842248.
KEGGi ath:AT1G59580.

Organism-specific databases

GeneFarmi 854. 89.
TAIRi AT1G59580.

Phylogenomic databases

HOGENOMi HOG000233024.
InParanoidi Q39022.
KOi K04371.
OMAi NRESNER.
PhylomeDBi Q39022.

Enzyme and pathway databases

BioCyci ARA:AT1G59580-MONOMER.
ARA:GQT-1108-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.

Gene expression databases

Genevestigatori Q39022.

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_dom.
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. "Characterization of two cDNAs that encode MAP kinase homologues in Arabidopsis thaliana and analysis of the possible role of auxin in activating such kinase activities in cultured cells."
    Mizoguchi T., Gotoh Y., Nishida E., Yamaguchi-Shinozaki K., Hayashida N., Iwasaki T., Kamada H., Shinozaki K.
    Plant J. 5:111-122(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME REGULATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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.
  6. Cited for: GENE FAMILY.
  7. "The Arabidopsis mitogen-activated protein kinase kinase MKK3 is upstream of group C mitogen-activated protein kinases and participates in pathogen signaling."
    Doczi R., Brader G., Pettko-Szandtner A., Rajh I., Djamei A., Pitzschke A., Teige M., Hirt H.
    Plant Cell 19:3266-3279(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKK3.

Entry informationi

Entry nameiMPK2_ARATH
AccessioniPrimary (citable) accession number: Q39022
Secondary accession number(s): Q9LQ58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: September 3, 2014
This is version 120 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

Similar proteinsi