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Q39025

- MPK5_ARATH

UniProt

Q39025 - MPK5_ARATH

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Protein

Mitogen-activated protein kinase 5

Gene
MPK5, At4g11330, F8L21.120
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation By similarity. Activated by the MAP kinase kinase MKK2. Activated by the MAP kinase kinase MKK6 in vitro.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATP By similarity
Active sitei169 – 1691Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi49 – 579ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity 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:AT4G11330-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 5 (EC:2.7.11.24)
Short name:
AtMPK5
Short name:
MAP kinase 5
Gene namesi
Name:MPK5
Ordered Locus Names:At4g11330
ORF Names:F8L21.120
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G11330.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 376376Mitogen-activated protein kinase 5PRO_0000186314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei201 – 2011Phosphothreonine By similarity
Modified residuei203 – 2031Phosphotyrosine By similarity
Modified residuei206 – 2061Phosphothreonine By similarity

Post-translational modificationi

Autophosphorylated on threonine and tyrosine residues By similarity.
Dually phosphorylated on Thr-201 and Tyr-203, which activates the enzyme By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ39025.
PRIDEiQ39025.

Expressioni

Gene expression databases

ArrayExpressiQ39025.
GenevestigatoriQ39025.

Interactioni

Protein-protein interaction databases

IntActiQ39025. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ39025.
SMRiQ39025. Positions 49-366.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 329287Protein kinaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 2033TXY

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiQ39025.
KOiK04371.
OMAiSETHEEI.
PhylomeDBiQ39025.

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.

Q39025-1 [UniParc]FASTAAdd to Basket

« Hide

MAKEIESATD LGDTNIKGVL VHGGRYFQYN VYGNLFEVSN KYVPPIRPIG    50
RGAYGFVCAA VDSETHEEIA IKKIGKAFDN KVDAKRTLRE IKLLRHLEHE 100
NVVVIKDIIR PPKKEDFVDV YIVFELMDTD LHQIIRSNQS LNDDHCQYFL 150
YQILRGLKYI HSANVLHRDL KPSNLLLNSN CDLKITDFGL ARTTSETEYM 200
TEYVVTRWYR APELLLNSSE YTSAIDVWSV GCIFAEIMTR EPLFPGKDYV 250
HQLKLITELI GSPDGASLEF LRSANARKYV KELPKFPRQN FSARFPSMNS 300
TAIDLLEKML VFDPVKRITV EEALCYPYLS ALHDLNDEPV CSNHFSFHFE 350
DPSSTEEEIK ELVWLESVKF NPLPSI 376
Length:376
Mass (Da):43,207
Last modified:June 6, 2002 - v2
Checksum:i2E8C0E5FC47685DF
GO

Sequence cautioni

The sequence CAB51417.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB81234.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591A → P in BAA04868. 1 Publication
Sequence conflicti276 – 2772AR → GG in BAA04868. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21841 mRNA. Translation: BAA04868.1.
AL096882 Genomic DNA. Translation: CAB51417.1. Sequence problems.
AL161531 Genomic DNA. Translation: CAB81234.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE82997.1.
AK176361 mRNA. Translation: BAD44124.1.
PIRiS40471.
T13024.
RefSeqiNP_567378.4. NM_117204.6.
UniGeneiAt.264.

Genome annotation databases

EnsemblPlantsiAT4G11330.1; AT4G11330.1; AT4G11330.
GeneIDi826735.
KEGGiath:AT4G11330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D21841 mRNA. Translation: BAA04868.1 .
AL096882 Genomic DNA. Translation: CAB51417.1 . Sequence problems.
AL161531 Genomic DNA. Translation: CAB81234.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE82997.1 .
AK176361 mRNA. Translation: BAD44124.1 .
PIRi S40471.
T13024.
RefSeqi NP_567378.4. NM_117204.6.
UniGenei At.264.

3D structure databases

ProteinModelPortali Q39025.
SMRi Q39025. Positions 49-366.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q39025. 1 interaction.

Proteomic databases

PaxDbi Q39025.
PRIDEi Q39025.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G11330.1 ; AT4G11330.1 ; AT4G11330 .
GeneIDi 826735.
KEGGi ath:AT4G11330.

Organism-specific databases

GeneFarmi 826. 89.
TAIRi AT4G11330.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
InParanoidi Q39025.
KOi K04371.
OMAi SETHEEI.
PhylomeDBi Q39025.

Enzyme and pathway databases

BioCyci ARA:AT4G11330-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

ArrayExpressi Q39025.
Genevestigatori Q39025.

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. "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. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    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: ENZYME REGULATION.
  7. Cited for: GENE FAMILY.
  8. "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: ENZYME REGULATION.

Entry informationi

Entry nameiMPK5_ARATH
AccessioniPrimary (citable) accession number: Q39025
Secondary accession number(s): Q67YV7, Q9SUS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: September 3, 2014
This is version 118 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