Q8GYQ5 · MPK12_ARATH
- ProteinMitogen-activated protein kinase 12
- GeneMPK12
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids372 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Negative regulator of the auxin transduction signaling pathway (PubMed:19000167).
Involved in stomatal movement regulation by phosphorylating and repressing HT1 and HT1-mediated GHR1 phosphorylation (PubMed:27694184, PubMed:27923039).
Required for CO2-mediated stomatal movements (e.g. closure) (PubMed:27923039).
Involved in stomatal movement regulation by phosphorylating and repressing HT1 and HT1-mediated GHR1 phosphorylation (PubMed:27694184, PubMed:27923039).
Required for CO2-mediated stomatal movements (e.g. closure) (PubMed:27923039).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Activated by threonine and tyrosine phosphorylation.
Features
Showing features for binding site, site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | kinase activity | |
Molecular Function | MAP kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein tyrosine kinase activity | |
Biological Process | auxin-activated signaling pathway | |
Biological Process | cellular response to carbon dioxide | |
Biological Process | intracellular signal transduction | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of stomatal closure | |
Biological Process | regulation of stomatal movement | |
Biological Process | response to auxin | |
Biological Process | response to indolebutyric acid |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitogen-activated protein kinase 12
- EC number
- Short namesAtMPK12 ; MAP kinase 12
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8GYQ5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Seems to translocate at the plasma membrane upon interaction with HT1.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Lethal in homozygous plants (PubMed:27923039).
Abolished CO2-mediated stomatal closure (PubMed:27694184, PubMed:27923039).
Increased stomatal opening (PubMed:27923039).
Abolished CO2-mediated stomatal closure (PubMed:27694184, PubMed:27923039).
Increased stomatal opening (PubMed:27923039).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 53 | Increased stomatal opening and altered CO2 and ozone (O3) responses. Weaker interaction with HT1. Strongly suppressed inhibition of HT1 activity. Loss of autophosphorylation. | ||||
Sequence: G → R | ||||||
Mutagenesis | 70 | Loss of kinase activity. Reduced inhibition of HT1 activity. Loss of autophosphorylation. | ||||
Sequence: K → R | ||||||
Mutagenesis | 122 | Hyperactive kinase, can inhibit HT1 activity. | ||||
Sequence: Y → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000245812 | 1-372 | Mitogen-activated protein kinase 12 | |||
Sequence: MSGESSSGSTEHCIKVVPTHGGRYVQYNVYGQLFEVSRKYVPPIRPIGRGACGIVCAAVNSVTGEKVAIKKIGNAFDNIIDAKRTLREIKLLRHMDHENVITIKDIVRPPQRDIFNDVYIVYELMDTDLQRILRSNQTLTSDQCRFLVYQLLRGLKYVHSANILHRDLRPSNVLLNSKNELKIGDFGLARTTSDTDFMTEYVVTRWYRAPELLLNCSEYTAAIDIWSVGCILGEIMTGQPLFPGKDYVHQLRLITELVGSPDNSSLGFLRSDNARRYVRQLPRYPKQQFAARFPKMPTTAIDLLERMLVFDPNRRISVDEALGHAYLSPHHDVAKEPVCSTPFSFDFEHPSCTEEHIKELIYKESVKFNPDH | ||||||
Modified residue | 199 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 201 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 204 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylated (PubMed:27923039).
Dually phosphorylated on Thr-199 and Tyr-201, which activates the enzyme (By similarity).
Activated by auxin. Dephosphorylated and inactivated by IBR5
Dually phosphorylated on Thr-199 and Tyr-201, which activates the enzyme (By similarity).
Activated by auxin. Dephosphorylated and inactivated by IBR5
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in seedlings, roots, stems, leaves, flowers and siliques, mostly around stomata.
Gene expression databases
Interaction
Subunit
Interacts with IBR5/SKIP33 (PubMed:19000167, PubMed:27923039).
Binds to HT1 (PubMed:27694184, PubMed:27923039).
Binds to HT1 (PubMed:27694184, PubMed:27923039).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8GYQ5 | IBR5 Q84JU4 | 8 | EBI-2128461, EBI-604555 | |
BINARY | Q8GYQ5 | MKK1 Q94A06 | 2 | EBI-2128461, EBI-994464 | |
BINARY | Q8GYQ5 | MKK6 Q9FJV0 | 2 | EBI-2128461, EBI-1238868 | |
BINARY | Q8GYQ5 | MKK9 Q9FX43 | 2 | EBI-2128461, EBI-2128545 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 41-327 | Protein kinase | ||||
Sequence: VPPIRPIGRGACGIVCAAVNSVTGEKVAIKKIGNAFDNIIDAKRTLREIKLLRHMDHENVITIKDIVRPPQRDIFNDVYIVYELMDTDLQRILRSNQTLTSDQCRFLVYQLLRGLKYVHSANILHRDLRPSNVLLNSKNELKIGDFGLARTTSDTDFMTEYVVTRWYRAPELLLNCSEYTAAIDIWSVGCILGEIMTGQPLFPGKDYVHQLRLITELVGSPDNSSLGFLRSDNARRYVRQLPRYPKQQFAARFPKMPTTAIDLLERMLVFDPNRRISVDEALGHAYL | ||||||
Motif | 199-201 | TXY | ||||
Sequence: TEY | ||||||
Region | 210-372 | IBR5 binding | ||||
Sequence: PELLLNCSEYTAAIDIWSVGCILGEIMTGQPLFPGKDYVHQLRLITELVGSPDNSSLGFLRSDNARRYVRQLPRYPKQQFAARFPKMPTTAIDLLERMLVFDPNRRISVDEALGHAYLSPHHDVAKEPVCSTPFSFDFEHPSCTEEHIKELIYKESVKFNPDH |
Domain
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similarities
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q8GYQ5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length372
- Mass (Da)42,475
- Last updated2003-03-01 v1
- Checksum1A8FF099D1DC80B9
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4IH84 | F4IH84_ARATH | MPK12 | 324 | ||
A0A178VX75 | A0A178VX75_ARATH | MPK12 | 406 |
Sequence caution
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC005397 EMBL· GenBank· DDBJ | AAC62906.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002685 EMBL· GenBank· DDBJ | AEC10639.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK117449 EMBL· GenBank· DDBJ | BAC42114.1 EMBL· GenBank· DDBJ | mRNA | ||
BT024898 EMBL· GenBank· DDBJ | ABD85169.1 EMBL· GenBank· DDBJ | mRNA |