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Q9LM33

- MPK8_ARATH

UniProt

Q9LM33 - MPK8_ARATH

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Protein

Mitogen-activated protein kinase 8

Gene

MPK8

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

MKK3-MPK8 and CAMs-MPK8 modules negatively regulates ROS accumulation through controlling expression of the RBOHD gene during wounding.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by threonine and tyrosine phosphorylation (By similarity). Activated by two independent mechanisms, the binding of CAMs in a calcium-dependent manner and the phosphorylation by MAP kinase kinase MKK3. Activated in response to mechanical wounding, hydrogen peroxide and jasmonic acid (JA).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331ATPPROSITE-ProRule annotation
Active sitei230 – 2301Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi110 – 1189ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. MAPK cascade Source: GOC
  2. response to hydrogen peroxide Source: TAIR
  3. response to jasmonic acid Source: TAIR
  4. response to reactive oxygen species Source: TAIR
  5. response to wounding 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:AT1G18150-MONOMER.
ARA:GQT-1005-MONOMER.
ARA:GQT-1590-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 8 (EC:2.7.11.24)
Short name:
AtMPK8
Short name:
MAP kinase 8
Gene namesi
Name:MPK8
Ordered Locus Names:At1g18150
ORF Names:T10F20.15, T10O22.12
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G18150.

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

More succeptible to oxidative stress.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331K → M: Abolishes CAM4-dependent activity. 1 Publication
Mutagenesisi134 – 1341K → R: Abolishes CAM4-dependent activity. 1 Publication
Mutagenesisi266 – 2661T → A: Do not affect CAM4-dependent activity; when associated with F-268. 1 Publication
Mutagenesisi268 – 2681Y → F: Do not affect CAM4-dependent activity; when associated with A-266. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Mitogen-activated protein kinase 8PRO_0000245808Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661PhosphothreonineBy similarity
Modified residuei268 – 2681PhosphotyrosineBy similarity
Modified residuei271 – 2711PhosphothreonineBy similarity

Post-translational modificationi

Dually phosphorylated on Thr-266 and Tyr-268, which activates the enzyme (By similarity). Autophosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9LM33.
PRIDEiQ9LM33.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

GenevestigatoriQ9LM33.

Interactioni

Subunit structurei

Interacts with CAM3, CAM4 AND CAM7 in an calcium-dependent manner.1 Publication

Protein-protein interaction databases

BioGridi23633. 2 interactions.
IntActiQ9LM33. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9LM33.
SMRiQ9LM33. Positions 76-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 395292Protein kinasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi266 – 2683TXY

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.
InParanoidiQ9LM33.
OMAiNSEREPT.
PhylomeDBiQ9LM33.

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.
[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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9LM33-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGGGGNLVDG VRRWLFQRPS SSSSSSSSNN NNNNHEQPIF NSSSFSSSSN
60 70 80 90 100
PNHSANSGEL IIEEDLDFSG LTLINVPKRN HLPMDPHKKG ETEFFTEYGE
110 120 130 140 150
ANRYQIQEVV GKGSYGVVAS AVDSHTGERV AIKKINDVFE HVSDATRILR
160 170 180 190 200
EIKLLRLLRH PDVVEIKHIM LPPSRREFRD IYVVFELMES DLHQVIKAND
210 220 230 240 250
DLTPEHYQFF LYQLLRGLKY VHAANVFHRD LKPKNILANA DCKLKICDFG
260 270 280 290 300
LARVSFNDAP TAIFWTDYVA TRWYRAPELC GSFFSKYTPA IDIWSVGCIF
310 320 330 340 350
AEMLLGKPLF PGKNVVHQLD LMTDFLGTPP PESISRIRNE KARRYLSSMR
360 370 380 390 400
KKQPVPFSHK FPKADPLALR LLERLLAFDP KDRASAEDAL ADPYFSGLSN
410 420 430 440 450
SEREPTTQPI SKLEFDFERK KLVKDDVREL IYREILEYHP QMLEEYLRGG
460 470 480 490 500
DQLSFMYPSG VDRFKRQFAH LEENQGKPGA AGGGRSTALH RHHASLPRER
510 520 530 540 550
VPAPNGETAE ESSDVERRAA AAVASTLESE EADNGGGYSA RNLMKSASIS
560 570 580
GSKCIGVQSK TDKEDTIAEE EDNETVAELT DKVASLHNS
Length:589
Mass (Da):66,231
Last modified:July 11, 2006 - v2
Checksum:i96769BA5E164BD74
GO

Sequence cautioni

The sequence AAF78388.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAA92222.1 differs from that shown. Reason: Frameshift at position 532. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1802RD → PH in BAA92222. 1 PublicationCurated
Sequence conflicti365 – 3651D → E in BAA92222. 1 PublicationCurated
Sequence conflicti431 – 4311I → L in BAA92222. 1 PublicationCurated
Sequence conflicti479 – 4791G → V in BAA92222. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038693 mRNA. Translation: BAA92222.1. Frameshift.
AC034107 Genomic DNA. Translation: AAF97831.1.
AC069551 Genomic DNA. Translation: AAF78388.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE29679.1.
CP002684 Genomic DNA. Translation: AEE29680.1.
CP002684 Genomic DNA. Translation: AEE29681.1.
AY045931 mRNA. Translation: AAK76605.1.
AY142618 mRNA. Translation: AAN13187.1.
RefSeqiNP_001185027.1. NM_001198098.1.
NP_173253.1. NM_101675.3.
NP_849685.1. NM_179354.2.
UniGeneiAt.15885.

Genome annotation databases

EnsemblPlantsiAT1G18150.1; AT1G18150.1; AT1G18150.
AT1G18150.2; AT1G18150.2; AT1G18150.
AT1G18150.3; AT1G18150.3; AT1G18150.
GeneIDi838394.
KEGGiath:AT1G18150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB038693 mRNA. Translation: BAA92222.1 . Frameshift.
AC034107 Genomic DNA. Translation: AAF97831.1 .
AC069551 Genomic DNA. Translation: AAF78388.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE29679.1 .
CP002684 Genomic DNA. Translation: AEE29680.1 .
CP002684 Genomic DNA. Translation: AEE29681.1 .
AY045931 mRNA. Translation: AAK76605.1 .
AY142618 mRNA. Translation: AAN13187.1 .
RefSeqi NP_001185027.1. NM_001198098.1.
NP_173253.1. NM_101675.3.
NP_849685.1. NM_179354.2.
UniGenei At.15885.

3D structure databases

ProteinModelPortali Q9LM33.
SMRi Q9LM33. Positions 76-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 23633. 2 interactions.
IntActi Q9LM33. 1 interaction.

Proteomic databases

PaxDbi Q9LM33.
PRIDEi Q9LM33.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G18150.1 ; AT1G18150.1 ; AT1G18150 .
AT1G18150.2 ; AT1G18150.2 ; AT1G18150 .
AT1G18150.3 ; AT1G18150.3 ; AT1G18150 .
GeneIDi 838394.
KEGGi ath:AT1G18150.

Organism-specific databases

GeneFarmi 851. 89.
TAIRi AT1G18150.

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233024.
InParanoidi Q9LM33.
OMAi NSEREPT.
PhylomeDBi Q9LM33.

Enzyme and pathway databases

BioCyci ARA:AT1G18150-MONOMER.
ARA:GQT-1005-MONOMER.
ARA:GQT-1590-MONOMER.

Gene expression databases

Genevestigatori Q9LM33.

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.
[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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Arabidopsis thaliana mRNA for MAP kinase."
    Mizoguchi T., Ichimura K., Shinozaki K.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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. "Calmodulin-dependent activation of MAP kinase for ROS homeostasis in Arabidopsis."
    Takahashi F., Mizoguchi T., Yoshida R., Ichimura K., Shinozaki K.
    Mol. Cell 41:649-660(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH CAM3; CAM4 AND CAM7, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-133; LYS-134; THR-266 AND TYR-268.

Entry informationi

Entry nameiMPK8_ARATH
AccessioniPrimary (citable) accession number: Q9LM33
Secondary accession number(s): Q9LMS2, Q9MB23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: November 26, 2014
This is version 104 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