Q9LZW4 · CIPKE_ARATH
- ProteinCBL-interacting serine/threonine-protein kinase 14
- GeneCIPK14
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids442 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner (By similarity).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Cofactor
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | plant-type vacuole | |
Cellular Component | plasmodesma | |
Molecular Function | ATP binding | |
Molecular Function | kinase binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | response to abscisic acid | |
Biological Process | response to cold | |
Biological Process | response to glucose | |
Biological Process | response to heat | |
Biological Process | response to oxidative stress | |
Biological Process | response to salt stress | |
Biological Process | response to water deprivation | |
Biological Process | signal transduction |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCBL-interacting serine/threonine-protein kinase 14
- 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 accessionQ9LZW4
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Disruption phenotype
Increased sensitivity to glucose.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 311 | No effect on binding to CBL2. | ||||
Sequence: N → A | ||||||
Mutagenesis | 313 | Loss of binding to CBL2. | ||||
Sequence: F → A | ||||||
Mutagenesis | 316 | No effect on binding to CBL2. | ||||
Sequence: I → A | ||||||
Mutagenesis | 319 | No effect on binding to CBL2. | ||||
Sequence: S → A or D | ||||||
Mutagenesis | 322 | Loss of binding to CBL2. | ||||
Sequence: F → A | ||||||
Mutagenesis | 324 | No effect on binding to CBL2. | ||||
Sequence: L → A | ||||||
Mutagenesis | 327 | No effect on binding to CBL2. | ||||
Sequence: L → A | ||||||
Mutagenesis | 328 | No effect on binding to CBL2. | ||||
Sequence: F → A | ||||||
Mutagenesis | 336 | No effect on binding to CBL2. | ||||
Sequence: R → A | ||||||
Mutagenesis | 339 | No effect on binding to CBL2. | ||||
Sequence: R → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 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_0000337216 | 1-442 | CBL-interacting serine/threonine-protein kinase 14 | |||
Sequence: MVDSDPVEFPPENRRGQLFGKYEVGKLVGCGAFAKVYHGRSTATGQSVAIKVVSKQRLQKGGLNGNIQREIAIMHRLRHPSIVRLFEVLATKSKIFFVMEFAKGGELFAKVSKGRFCEDLSRRYFQQLISAVGYCHSRGIFHRDLKPENLLLDEKLDLKISDFGLSALTDQIRPDGLLHTLCGTPAYVAPEVLAKKGYDGAKIDIWSCGIILFVLNAGYLPFNDHNLMVMYRKIYKGEFRIPKWTSPDLRRLLTRLLDTNPQTRITIEEIIHDPWFKQGYDDRMSKFHLEDSDMKLPADETDSEMGARRMNAFDIISGSPGFNLSGLFGDARKYDRVERFVSAWTAERVVERLEEIVSAENLTVAKKETWGMKIEGQKGNFAMVVEINQLTDELVMIEVRKRQRAAASGRDLWTDTLRPFFVELVHESDQTDPEPTQVHTTS | ||||||
Modified residue | 166 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 180 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Predominant in roots, cauline leaves, and flowers (PubMed:11577192).
Ubiquitous with highest expression in 7-day-old seedlings and flower buds, followed by that in cauline leaves and young siliques (PubMed:25058458).
Ubiquitous with highest expression in 7-day-old seedlings and flower buds, followed by that in cauline leaves and young siliques (PubMed:25058458).
Induction
By light in a cytokinin-dependent manner and N6-benzylaminopurine (BA). Also induced by sucrose, glucose and fructose. Induced by several abiotic stresses like salt, cold, heat, oxidative, drought, PEG8000, glucose treatments as well exogenous abscisic acid (ABA) application (PubMed:25058458).
Developmental stage
First observed in imbibed seeds. Mostly localized in hypocotyls during germination and in seedlings. In mature plants, confined to vascular tissues of leaves and roots. In flowers, expressed in the vascular bundle of the stamen filament and in the stigma, where the filament joins the pistil.
Gene expression databases
Interaction
Subunit
Interacts with CBL2 (PubMed:11577192, PubMed:18237745, PubMed:19832944, PubMed:25058458).
Interacts with CBL3 (PubMed:19832944, PubMed:25058458).
Interacts with CBL8 (PubMed:19832944).
Interacts with CBL9 (PubMed:25058458).
Interacts with KIN10 and KIN11 (PubMed:25058458).
Interacts with CBL3 (PubMed:19832944, PubMed:25058458).
Interacts with CBL8 (PubMed:19832944).
Interacts with CBL9 (PubMed:25058458).
Interacts with KIN10 and KIN11 (PubMed:25058458).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9LZW4 | At2g44050 O80575 | 4 | EBI-307576, EBI-4473692 | |
BINARY | Q9LZW4 | BZIP18 O22873 | 3 | EBI-307576, EBI-4438646 | |
BINARY | Q9LZW4 | CBL2 Q8LAS7 | 9 | EBI-307576, EBI-485991 | |
BINARY | Q9LZW4 | MYC2 Q39204 | 5 | EBI-307576, EBI-1792336 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-276 | Protein kinase | ||||
Sequence: YEVGKLVGCGAFAKVYHGRSTATGQSVAIKVVSKQRLQKGGLNGNIQREIAIMHRLRHPSIVRLFEVLATKSKIFFVMEFAKGGELFAKVSKGRFCEDLSRRYFQQLISAVGYCHSRGIFHRDLKPENLLLDEKLDLKISDFGLSALTDQIRPDGLLHTLCGTPAYVAPEVLAKKGYDGAKIDIWSCGIILFVLNAGYLPFNDHNLMVMYRKIYKGEFRIPKWTSPDLRRLLTRLLDTNPQTRITIEEIIHDPWF | ||||||
Region | 162-191 | Activation loop | ||||
Sequence: DFGLSALTDQIRPDGLLHTLCGTPAYVAPE | ||||||
Domain | 305-329 | NAF | ||||
Sequence: MGARRMNAFDIISGSPGFNLSGLFG | ||||||
Region | 335-365 | PPI | ||||
Sequence: DRVERFVSAWTAERVVERLEEIVSAENLTVA |
Domain
The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases (By similarity).
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length442
- Mass (Da)50,298
- Last updated2000-10-01 v1
- Checksum319532FEFB7244C8
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF295669 EMBL· GenBank· DDBJ | AAK16689.1 EMBL· GenBank· DDBJ | mRNA | ||
AB035147 EMBL· GenBank· DDBJ | BAB11737.1 EMBL· GenBank· DDBJ | mRNA | ||
AL162351 EMBL· GenBank· DDBJ | CAB82752.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED90397.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF360189 EMBL· GenBank· DDBJ | AAK25899.1 EMBL· GenBank· DDBJ | mRNA | ||
AY142684 EMBL· GenBank· DDBJ | AAN13222.1 EMBL· GenBank· DDBJ | mRNA |