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Q9C5C0 (MPK18_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 18

Short name=AtMPK18
Short name=MAP kinase 18
EC=2.7.11.24
Gene names
Name:MPK18
Ordered Locus Names:At1g53510
ORF Names:F22G10.12, T3F20.17
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitogen-activated protein kinase (MAPK) that is specifically regulated by PHS1 and mediates signaling that regulates cortical microtubule functions, maybe through regulation of microtubule dynamic instability. Ref.6

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation Probable. Inactivated by phosphatase PHS1. Ref.6

Subunit structure

Interacts with PHS1. Ref.6

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Widely expressed. Ref.6

Domain

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

Post-translational modification

Dually phosphorylated on Thr-187 and Tyr-189, which activates the enzyme By similarity.

Disruption phenotype

No visible phenotype under normal growth condition, but mutant plants show reduced sensitivity to microtubule-disrupting drugs. Ref.6

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.

Contains 1 protein kinase domain.

Sequence caution

The sequence AAF78438.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAG51978.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PHS1Q75QN63EBI-1238534,EBI-2349366

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 615615Mitogen-activated protein kinase 18
PRO_0000245818

Regions

Domain25 – 316292Protein kinase
Nucleotide binding31 – 399ATP By similarity
Motif187 – 1893TXY

Sites

Active site1511Proton acceptor By similarity
Binding site541ATP By similarity

Amino acid modifications

Modified residue1871Phosphothreonine By similarity
Modified residue1891Phosphotyrosine By similarity
Modified residue1921Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9C5C0 [UniParc].

Last modified May 31, 2011. Version 4.
Checksum: 1439ED0B3C82210E

FASTA61569,352
        10         20         30         40         50         60 
MQQNQVKKGT KEMEFFTEYG DANRYRILEV IGKGSYGVVC AAIDTHTGEK VAIKKINDVF 

        70         80         90        100        110        120 
EHISDALRIL REVKLLRLLR HPDIVEIKSI MLPPSKREFK DIYVVFELME SDLHQVIKAN 

       130        140        150        160        170        180 
DDLTREHHQF FLYQMLRALK FMHTANVYHR DLKPKNILAN ANCKLKVCDF GLARVAFNDT 

       190        200        210        220        230        240 
PTTVFWTDYV ATRWYRAPEL CGSFFSKYTP AIDVWSIGCI FAEVLTGKPL FPGKSVVHQL 

       250        260        270        280        290        300 
ELITDLLGTP KSETISGVRN DKARKYLTEM RKKNPVTFSQ KFSKADPLAL RLLQRLLAFD 

       310        320        330        340        350        360 
PKDRPTPAEA LADPYFKGLS KIEREPSSQQ ISKMEFEFER RRLTKDDIRE LIYREILEYH 

       370        380        390        400        410        420 
PQLLKDYMSG SEGSNFVYPS AIGHLRQQFT YLEENSSRNG PVIPLERKHA SLPRSTVHST 

       430        440        450        460        470        480 
VVHSTSQPNL GATDSRRVSF EPSKNGASSA GHPSTSAYPT KSIGPPPRVP PSGRPGRVVE 

       490        500        510        520        530        540 
SSVSYENGRN LKEAYFRSAV SSPHCYFRPN TMTNPENRNI EASSFPPKPQ NPVHQFSPTE 

       550        560        570        580        590        600 
PPAATTNQAD VETMNHPNPY FQPQLPKTDQ LNNNTHMAID AKLLQAQSQF GPAGAAAVAV 

       610 
AAHRNIGTIS YSAAS 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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. expand/collapse author list , 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] OF 13-615.
Strain: cv. Columbia.
[4]"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.
[5]"Ancient signals: comparative genomics of plant MAPK and MAPKK gene families."
Hamel L.P., Nicole M.C., Sritubtim S., Morency M.J., Ellis M., Ehlting J., Beaudoin N., Barbazuk B., Klessig D., Lee J., Martin G., Mundy J., Ohashi Y., Scheel D., Sheen J., Xing T., Zhang S., Seguin A., Ellis B.E.
Trends Plant Sci. 11:192-198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
[6]"Arabidopsis mitogen-activated protein kinase MPK18 mediates cortical microtubule functions in plant cells."
Walia A., Lee J.S., Wasteneys G., Ellis B.
Plant J. 59:565-575(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PHS1, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC018748 Genomic DNA. Translation: AAF78438.1. Sequence problems.
AC024260 Genomic DNA. Translation: AAG51978.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE32950.1.
AF360353 mRNA. Translation: AAK28649.2.
BT000870 mRNA. Translation: AAN41270.1.
PIRC96575.
RefSeqNP_175756.2. NM_104229.3.
UniGeneAt.25395.

3D structure databases

ProteinModelPortalQ9C5C0.
SMRQ9C5C0. Positions 18-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid27011. 6 interactions.
IntActQ9C5C0. 19 interactions.
STRING3702.AT1G53510.1-P.

Proteomic databases

PaxDbQ9C5C0.
PRIDEQ9C5C0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G53510.1; AT1G53510.1; AT1G53510.
GeneID841786.
KEGGath:AT1G53510.

Organism-specific databases

GeneFarm857. 89.
TAIRAT1G53510.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidQ9C5C0.
OMANTHMAID.

Enzyme and pathway databases

BioCycARA:AT1G53510-MONOMER.

Gene expression databases

GenevestigatorQ9C5C0.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ9C5C0.

Entry information

Entry nameMPK18_ARATH
AccessionPrimary (citable) accession number: Q9C5C0
Secondary accession number(s): Q9LPG7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 31, 2011
Last modified: June 11, 2014
This is version 84 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names