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Protein

Mitogen-activated protein kinase 14

Gene

MPK14

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611ATPPROSITE-ProRule annotation
Active sitei158 – 1581Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi38 – 469ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • MAP kinase activity Source: TAIR

GO - Biological processi

  • MAPK cascade Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT4G36450-MONOMER.
ReactomeiREACT_273308. ERK/MAPK targets.
REACT_274021. ERK2 activation.
REACT_310320. CREB phosphorylation through the activation of Ras.
REACT_310958. ERKs are inactivated.
REACT_322522. Signalling to ERK5.
REACT_330337. Signal transduction by L1.
REACT_340308. ERK1 activation.
REACT_340626. Regulation of HSF1-mediated heat shock response.
REACT_357967. Signaling by FGFR2.
REACT_358851. Signaling by FGFR1.
REACT_359363. Signaling by FGFR4.
REACT_360532. Signaling by FGFR3.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14 (EC:2.7.11.24)
Short name:
AtMPK14
Short name:
MAP kinase 14
Gene namesi
Name:MPK14
Ordered Locus Names:At4g36450
ORF Names:AP22.98, C7A10.910
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G36450.

Subcellular locationi

GO - Cellular componenti

  • intracellular Source: GOC
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Mitogen-activated protein kinase 14PRO_0000245814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei188 – 1881PhosphothreonineBy similarity
Modified residuei190 – 1901PhosphotyrosineBy similarity
Modified residuei193 – 1931PhosphothreonineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-188 and Tyr-190, which activates the enzyme.By similarity

Keywords - PTMi

Phosphoprotein

Expressioni

Gene expression databases

ExpressionAtlasiO23236. baseline and differential.

Interactioni

Subunit structurei

Interacts with MKK3.1 Publication

Protein-protein interaction databases

IntActiO23236. 1 interaction.
STRINGi3702.AT4G36450.1.

Structurei

3D structure databases

ProteinModelPortaliO23236.
SMRiO23236. Positions 25-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 316285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi188 – 1903TXY

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiO23236.
KOiK04371.
OMAiREMMWEE.
PhylomeDBiO23236.

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.
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.

O23236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMLVDPPNG IRQEGKHYYT MWQTLFEIDT KYVPIKPIGR GAYGVVCSSI
60 70 80 90 100
NSETNERVAI KKIHNVFENR IDALRTLREL KLLRHVRHEN VISLKDVMLP
110 120 130 140 150
THRYSFRDVY LVYELMDSDL NQIIKSSQSL SDDHCKYFLF QLLRGLKYLH
160 170 180 190 200
SANILHRDLK PGNLLVNANC DLKICDFGLA RTYEQFMTEY VVTRWYRAPE
210 220 230 240 250
LLLCCDNYGT SIDVWSVGCI FAEILGRKPI FPGTECLNQL KLIINVVGSQ
260 270 280 290 300
QDWDLQFIDN QKARRFIKSL PFSKGTHFSH IYPHANPLAI DLLQRMLVFD
310 320 330 340 350
PTKRISVSDA LLHPYMEGLL EPECNPSENV PVSSLEIDEN MEGDMIREMM
360
WEEMLHYLPR A
Length:361
Mass (Da):41,976
Last modified:January 1, 1998 - v1
Checksum:iFECE45953F45F738
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z99708 Genomic DNA. Translation: CAB16812.1.
AL161589 Genomic DNA. Translation: CAB80311.1.
CP002687 Genomic DNA. Translation: AEE86657.1.
DQ056668 mRNA. Translation: AAY78814.1.
PIRiC85430.
RefSeqiNP_195363.1. NM_119808.1.
UniGeneiAt.54629.

Genome annotation databases

EnsemblPlantsiAT4G36450.1; AT4G36450.1; AT4G36450.
GeneIDi829797.
KEGGiath:AT4G36450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z99708 Genomic DNA. Translation: CAB16812.1.
AL161589 Genomic DNA. Translation: CAB80311.1.
CP002687 Genomic DNA. Translation: AEE86657.1.
DQ056668 mRNA. Translation: AAY78814.1.
PIRiC85430.
RefSeqiNP_195363.1. NM_119808.1.
UniGeneiAt.54629.

3D structure databases

ProteinModelPortaliO23236.
SMRiO23236. Positions 25-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO23236. 1 interaction.
STRINGi3702.AT4G36450.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G36450.1; AT4G36450.1; AT4G36450.
GeneIDi829797.
KEGGiath:AT4G36450.

Organism-specific databases

GeneFarmi879. 89.
TAIRiAT4G36450.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233024.
InParanoidiO23236.
KOiK04371.
OMAiREMMWEE.
PhylomeDBiO23236.

Enzyme and pathway databases

BioCyciARA:AT4G36450-MONOMER.
ReactomeiREACT_273308. ERK/MAPK targets.
REACT_274021. ERK2 activation.
REACT_310320. CREB phosphorylation through the activation of Ras.
REACT_310958. ERKs are inactivated.
REACT_322522. Signalling to ERK5.
REACT_330337. Signal transduction by L1.
REACT_340308. ERK1 activation.
REACT_340626. Regulation of HSF1-mediated heat shock response.
REACT_357967. Signaling by FGFR2.
REACT_358851. Signaling by FGFR1.
REACT_359363. Signaling by FGFR4.
REACT_360532. Signaling by FGFR3.

Miscellaneous databases

PROiO23236.

Gene expression databases

ExpressionAtlasiO23236. baseline and differential.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis thaliana."
    Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C., Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P., Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.
    , Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R., De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M., Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M., Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A., Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D., Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A., Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S., Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G., Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.
    Nature 391:485-488(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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. Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W., Redman J.C., Wu H.C., Utterback T., Town C.D.
    Submitted (MAY-2005) 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: GENE FAMILY.
  7. "Comprehensive analysis of protein-protein interactions between Arabidopsis MAPKs and MAPK kinases helps define potential MAPK signalling modules."
    Lee J.S., Huh K.W., Bhargava A., Ellis B.E.
    Plant Signal. Behav. 3:1037-1041(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MKK3.

Entry informationi

Entry nameiMPK14_ARATH
AccessioniPrimary (citable) accession number: O23236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 115 of the entry and version 1 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.