Q2MHE4 · HT1_ARATH
- ProteinSerine/threonine/tyrosine-protein kinase HT1
- GeneHT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids390 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine/threonine/tyrosine kinase involved in the control of stomatal movement in response to CO2 (PubMed:16518390, PubMed:27694184, PubMed:27923039, PubMed:29101334, PubMed:30361234).
Functions as a major negative regulator of CO2-induced stomatal closing (PubMed:16518390).
Does not seem to be involved in stomatal closure in response to abscisic acid (ABA) or light (PubMed:16518390).
Involved in the control of red light-induced stomatal opening (PubMed:26192339).
Is epistatic to SRK2E/OST1 function during stomatal responses to red light and altered CO2 (PubMed:26192339).
Phosphorylates SRK2E/OST1 and GHR1 to prevents SRK2E/OST1- and GHR1-induced activation of SLAC1, thus preventing stomatal closure (PubMed:25599916, PubMed:27694184, PubMed:30361234).
Mediates the phosphorylation of CBC1 and CBC2 (PubMed:29101334).
Functions as a major negative regulator of CO2-induced stomatal closing (PubMed:16518390).
Does not seem to be involved in stomatal closure in response to abscisic acid (ABA) or light (PubMed:16518390).
Involved in the control of red light-induced stomatal opening (PubMed:26192339).
Is epistatic to SRK2E/OST1 function during stomatal responses to red light and altered CO2 (PubMed:26192339).
Phosphorylates SRK2E/OST1 and GHR1 to prevents SRK2E/OST1- and GHR1-induced activation of SLAC1, thus preventing stomatal closure (PubMed:25599916, PubMed:27694184, PubMed:30361234).
Mediates the phosphorylation of CBC1 and CBC2 (PubMed:29101334).
Miscellaneous
'Suu' means 'mouth' in both Estonian and Finnish.
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Inhibited by MPK4 and MPK12.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | transmembrane receptor protein tyrosine kinase activity | |
Biological Process | cellular response to carbon dioxide | |
Biological Process | protein autophosphorylation | |
Biological Process | regulation of response to red or far red light | |
Biological Process | regulation of stomatal closure | |
Biological Process | regulation of stomatal movement | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine/tyrosine-protein kinase HT1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ2MHE4
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Suppressed low CO2-induced stomatal opening and impaired CO2-triggered stomatal closure.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 109 | In suu/ht1-8D; dominant mutation leading to constitutively open stomata and subsequent high stomatal conductance, and impaired stomatal CO2 responses. Reduced binding and inhibition by MPK4 and MPK12. | ||||
Sequence: A → V | ||||||
Mutagenesis | 113 | Loss of kinase activity. Impaired MPK12-mediated phosphorylation. | ||||
Sequence: K → M | ||||||
Mutagenesis | 113 | Loss of kinase activity, induces a disrupted CO2 response. | ||||
Sequence: K → W | ||||||
Mutagenesis | 136-149 | In ht1-2; loss of kinase activity. Impaired ability to control stomatal movements in response to CO2 but normal responses to blue light, fusicoccin and abscisic acid (ABA). Tightly closed stomata. | ||||
Sequence: Missing | ||||||
Mutagenesis | 211 | In ht1-1; impairs the ability to control stomatal movements in response to CO2 probably due to loss of protein kinase activity. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 15 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000235238 | 1-390 | Serine/threonine/tyrosine-protein kinase HT1 | |||
Sequence: MSGLCFNPFRLRWSLRSKLPLEPSLPNLPCNPSSSKTNRYAEAETMEKKRFDSMESWSMILESENVETWEASKGEREEWTADLSQLFIGNKFASGAHSRIYRGIYKQRAVAVKMVRIPTHKEETRAKLEQQFKSEVALLSRLFHPNIVQFIAACKKPPVYCIITEYMSQGNLRMYLNKKEPYSLSIETVLRLALDISRGMEYLHSQGVIHRDLKSNNLLLNDEMRVKVADFGTSCLETQCREAKGNMGTYRWMAPEMIKEKPYTRKVDVYSFGIVLWELTTALLPFQGMTPVQAAFAVAEKNERPPLPASCQPALAHLIKRCWSENPSKRPDFSNIVAVLEKYDECVKEGLPLTSHASLTKTKKAILDHLKGCVTSISSPFSSSSVPVNA |
Post-translational modification
Autophosphorylated.
Keywords
- PTM
Proteomic databases
Expression
Tissue specificity
Mainly localizes in guard cells. Expressed at low level in leaves, stems, roots and flowers.
Gene expression databases
Interaction
Subunit
Interacts with DTX56 (PubMed:25599916).
Binds to MPK4 and MPK12 (PubMed:27694184, PubMed:27923039).
Associates to CBC1 and CBC2 (PubMed:29101334).
Binds to MPK4 and MPK12 (PubMed:27694184, PubMed:27923039).
Associates to CBC1 and CBC2 (PubMed:29101334).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q2MHE4 | SRK2E Q940H6 | 2 | EBI-11174828, EBI-782514 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 86-359 | Protein kinase | ||||
Sequence: LFIGNKFASGAHSRIYRGIYKQRAVAVKMVRIPTHKEETRAKLEQQFKSEVALLSRLFHPNIVQFIAACKKPPVYCIITEYMSQGNLRMYLNKKEPYSLSIETVLRLALDISRGMEYLHSQGVIHRDLKSNNLLLNDEMRVKVADFGTSCLETQCREAKGNMGTYRWMAPEMIKEKPYTRKVDVYSFGIVLWELTTALLPFQGMTPVQAAFAVAEKNERPPLPASCQPALAHLIKRCWSENPSKRPDFSNIVAVLEKYDECVKEGLPLTSHASL |
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length390
- Mass (Da)44,281
- Last updated2006-02-21 v1
- Checksum8198FDAC936DC573
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB221045 EMBL· GenBank· DDBJ | BAE75921.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC003113 EMBL· GenBank· DDBJ | AAF70839.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE33962.2 EMBL· GenBank· DDBJ | Genomic DNA |