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Q39021 (MPK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 123. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitogen-activated protein kinase 1

Short name=AtMPK1
Short name=MAP kinase 1
EC=2.7.11.24
Gene names
Name:MPK1
Ordered Locus Names:At1g10210
ORF Names:F14N23.9
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

Activated by threonine and tyrosine phosphorylation Probable. Ref.1

Subunit structure

Interacts with MKK3. Ref.7

Tissue specificity

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

Domain

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

Post-translational modification

Dually phosphorylated on Thr-191 and Tyr-193, which activates the enzyme By similarity. Autophosphorylated on threonine and tyrosine residues Probable. Phosphorylated on Ser residue. Ref.1

Sequence similarities

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

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Mitogen-activated protein kinase 1
PRO_0000186310

Regions

Domain32 – 319288Protein kinase
Nucleotide binding38 – 469ATP By similarity
Motif191 – 1933TXY

Sites

Active site1581Proton acceptor By similarity
Binding site611ATP By similarity

Amino acid modifications

Modified residue1911Phosphothreonine By similarity
Modified residue1931Phosphotyrosine By similarity
Modified residue1961Phosphothreonine By similarity

Experimental info

Sequence conflict1291V → R in BAA03535. Ref.1
Sequence conflict2501L → I in BAA03535. Ref.1
Sequence conflict2621D → V in BAA03535. Ref.1
Sequence conflict2871G → C in BAA03535. Ref.1
Sequence conflict3101V → A in BAA03535. Ref.1
Sequence conflict3521M → I in BAA03535. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q39021 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: F2962D7881C87A1B

FASTA37042,644
        10         20         30         40         50         60 
MATLVDPPNG IRNEGKHYFS MWQTLFEIDT KYMPIKPIGR GAYGVVCSSV NSDTNEKVAI 

        70         80         90        100        110        120 
KKIHNVYENR IDALRTLREL KLLRHLRHEN VIALKDVMMP IHKMSFKDVY LVYELMDTDL 

       130        140        150        160        170        180 
HQIIKSSQVL SNDHCQYFLF QLLRGLKYIH SANILHRDLK PGNLLVNANC DLKICDFGLA 

       190        200        210        220        230        240 
RASNTKGQFM TEYVVTRWYR APELLLCCDN YGTSIDVWSV GCIFAELLGR KPIFQGTECL 

       250        260        270        280        290        300 
NQLKLIVNIL GSQREEDLEF IDNPKAKRYI RSLPYSPGMS LSRLYPGAHV LAIDLLQKML 

       310        320        330        340        350        360 
VFDPSKRISV SEALQHPYMA PLYDPNANPP AQVPIDLDVD EDLREEMIRE MMWNEMLHYH 

       370 
PQASTLNTEL 

« Hide

References

« Hide 'large scale' references
[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. 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.
[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. 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].
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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D14713 mRNA. Translation: BAA03535.1.
AC005489 Genomic DNA. Translation: AAD32871.1.
CP002684 Genomic DNA. Translation: AEE28553.1.
CP002684 Genomic DNA. Translation: AEE28554.1.
AY059937 mRNA. Translation: AAL24419.1.
BT000062 mRNA. Translation: AAN15381.1.
PIRF86236.
RefSeqNP_001031017.1. NM_001035940.1.
NP_172492.1. NM_100895.2.
UniGeneAt.261.

3D structure databases

ProteinModelPortalQ39021.
SMRQ39021. Positions 25-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid22799. 3 interactions.
IntActQ39021. 3 interactions.
STRING3702.AT1G10210.1-P.

Proteomic databases

PaxDbQ39021.
PRIDEQ39021.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G10210.1; AT1G10210.1; AT1G10210.
AT1G10210.2; AT1G10210.2; AT1G10210.
GeneID837559.
KEGGath:AT1G10210.

Organism-specific databases

GeneFarm855. 89.
TAIRAT1G10210.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233024.
InParanoidQ39021.
KOK04371.
OMAQGLSNDH.
PhylomeDBQ39021.

Enzyme and pathway databases

BioCycARA:AT1G10210-MONOMER.
ARA:GQT-430-MONOMER.
BRENDA2.7.11.24. 399.

Gene expression databases

ArrayExpressQ39021.
GenevestigatorQ39021.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMPK1_ARATH
AccessionPrimary (citable) accession number: Q39021
Secondary accession number(s): Q9SY63
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 6, 2002
Last modified: June 11, 2014
This is version 123 of the entry and version 2 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