P24100 · CDKA1_ARATH
- ProteinCyclin-dependent kinase A-1
- GeneCDKA-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids294 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the control of the cell cycle. Essential for both G1/S and G2/M (mitosis) phase transitions. Functions in cell morphogenesis as well as cell proliferation. Required for cell division (entry into mitosis) of the generative cell in male gametogenesis. Required to trigger guard mother cells (GMC) symmetric divisions at the late stage of stomatal development, probably via the regulation of G1 to S transition in the cell cycle. Required for the function of SPCH in entering the stomatal lineage (PubMed:25680231).
Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division when in the presence of CYCD3-2 via the phosphorylation of SPCH (PubMed:24687979, PubMed:25680231).
Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division when in the presence of CYCD3-2 via the phosphorylation of SPCH (PubMed:24687979, PubMed:25680231).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
CDK kinase activated by CDKF-1. CDK kinase activity inhibited by KRP1/ICK1, KRP2/ICK2, KRP3/ICK6, KRP4/ICK7, KRP5/ICK3, KRP6/ICK4 and KRP7/ICK5. Down-regulated by phosphorylation by WEE1.
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclin-dependent kinase A-1
- EC number
- Short namesCDKA;1
- 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 accessionP24100
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Phenotypes & Variants
Disruption phenotype
Plants display lethal male gametophyte (PubMed:16460514, PubMed:25680231).
Impaired stomata formation with arrested guard mother cells (GMC) divisions (PubMed:25680231).
Impaired last mitotic division in the male gametophyte, leading to 50 percent of pollen with two gametes (PubMed:25680231).
The double mutant flp-1 myb88 displays an enhanced stomatal phenotype with more and larger stomatal clusters. Triple mutants cdka;1 flp-1 myb88 don't have guard cells stacks but accumulates sGCs (PubMed:24687979).
Impaired stomata formation with arrested guard mother cells (GMC) divisions (PubMed:25680231).
Impaired last mitotic division in the male gametophyte, leading to 50 percent of pollen with two gametes (PubMed:25680231).
The double mutant flp-1 myb88 displays an enhanced stomatal phenotype with more and larger stomatal clusters. Triple mutants cdka;1 flp-1 myb88 don't have guard cells stacks but accumulates sGCs (PubMed:24687979).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 14 | Increased kinase activity; when associated with F-15. | ||||
Sequence: T → A | ||||||
Mutagenesis | 15 | Abolishes phosphorylation by WEE1. Increased kinase activity; when associated with A-14. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 146 | Decreased kinase activity and disturbed cell cycle. Reduced frequency of cell division during embryo development. Altered stomatal production. Interacts with SPCH. | ||||
Sequence: D → N | ||||||
Mutagenesis | 156 | Decreased kinase activity and disturbed cell cycle. | ||||
Sequence: P → L | ||||||
Mutagenesis | 161 | Strong reduction in kinase activity and ability to bind substrate. Strong reduction in plant growth. Sterile plants. | ||||
Sequence: T → D | ||||||
Mutagenesis | 161 | Strong reduction in kinase activity and ability to bind substrate. | ||||
Sequence: T → V | ||||||
Mutagenesis | 166 | Decreased kinase activity and disturbed cell cycle. | ||||
Sequence: T → I | ||||||
Mutagenesis | 234-236 | No change in kinase activity, but disturbed cell cycle. Loss of interaction with CKS1. | ||||
Sequence: Missing |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 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_0000085749 | 1-294 | Cyclin-dependent kinase A-1 | |||
Sequence: MDQYEKVEKIGEGTYGVVYKARDKVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHSNIVKLQDVVHSEKRLYLVFEYLDLDLKKHMDSTPDFSKDLHMIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNSLKLADFGLARAFGIPVRTFTHEVVTLWYRAPEILLGSHHYSTPVDIWSVGCIFAEMISQKPLFPGDSEIDQLFKIFRIMGTPYEDTWRGVTSLPDYKSAFPKWKPTDLETFVPNLDPDGVDLLSKMLLMDPTKRINARAALEHEYFKDLGGMP | ||||||
Modified residue | 15 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 161 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated at Tyr-15 by WEE1. Phosphorylation at Thr-161 is important for the kinase activity and substrate binding. Binding to the anti-phosphatase PAS2 prevents dephosphorylation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, stems, flowers and siliques.
Induction
By nematode infection in roots. Down-regulated by salt stress in root meristem and replication blocking agents (hydroxyurea and aphidicolin).
Developmental stage
Expressed throughout the cell cycle. Expressed in actively dividing cells: root and shoot apical meristems, leaf primordia and emerging lateral root meristem. Expressed in light-grown seedlings from 1 up to 7 days after germination with a peak at 2 and 3 days.
Gene expression databases
Interaction
Subunit
Interacts with CDT1A, CYCA2-3, CYCD2-1, CYCD3-1, CYCD4-1, CYCD4-2, CYCH1-1, CYCU1-1, CYCU2-1, CYCU2-2, CYCU3-1, CYCU4-1, CYCU4-2, CYCU4-3, CKS1, KRP2/ICK2, KRP3/ICK6, KRP4/ICK7, KRP6/ICK4, KRP7/ICK5, and C-terminal domain of KRP1/ICK1. Interacts with WEE1 and TIF4A-1/EIF4A-1. Interacts with PAS2; when phosphorylated at Tyr-15. Interacts with SMR3, SMR4, SMR5, SMR6, SMR8 and At4g14310. Binds to CYCD3-2 (PubMed:24687979).
Component of a DREAM-like complex which modulates a variety of developmentally regulated genes and of the mitotic genes in proliferating and differentiated cells. Interacts with MYB3R3 at later and with MYB3R4 at earlier stages of leaf development (PubMed:26069325).
May interact with SPCH (PubMed:25680231).
Component of a DREAM-like complex which modulates a variety of developmentally regulated genes and of the mitotic genes in proliferating and differentiated cells. Interacts with MYB3R3 at later and with MYB3R4 at earlier stages of leaf development (PubMed:26069325).
May interact with SPCH (PubMed:25680231).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P24100 | CKS1 O23249 | 9 | EBI-371713, EBI-1253127 | |
BINARY | P24100 | CYCD2-1 P42752 | 4 | EBI-371713, EBI-1253160 | |
BINARY | P24100 | CYCD3-1 P42753 | 5 | EBI-371713, EBI-1253610 | |
BINARY | P24100 | CYCD4-1 Q8LGA1 | 4 | EBI-371713, EBI-1253202 | |
BINARY | P24100 | CYCU1-1 Q9LJ45 | 2 | EBI-371713, EBI-1773749 | |
BINARY | P24100 | CYCU4-1 O80513 | 2 | EBI-371713, EBI-1773819 | |
BINARY | P24100 | CYCU4-3 Q9FKF6 | 2 | EBI-371713, EBI-1773829 | |
BINARY | P24100 | EIF4A1 P41376 | 2 | EBI-371713, EBI-371706 | |
BINARY | P24100 | KRP1 Q67Y93 | 10 | EBI-371713, EBI-1636730 | |
BINARY | P24100 | KRP2 Q9SCR2 | 6 | EBI-371713, EBI-1636748 | |
BINARY | P24100 | KRP3 Q9FKB5 | 4 | EBI-371713, EBI-1773302 | |
BINARY | P24100 | KRP4 Q8GYJ3 | 4 | EBI-371713, EBI-1253225 | |
BINARY | P24100 | KRP5 Q9LRY0 | 3 | EBI-371713, EBI-1636764 | |
BINARY | P24100 | KRP6 Q0WNX9 | 3 | EBI-371713, EBI-1253171 | |
BINARY | P24100 | KRP7 Q94CL9 | 3 | EBI-371713, EBI-1773344 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-287 | Protein kinase | ||||
Sequence: YEKVEKIGEGTYGVVYKARDKVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHSNIVKLQDVVHSEKRLYLVFEYLDLDLKKHMDSTPDFSKDLHMIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNSLKLADFGLARAFGIPVRTFTHEVVTLWYRAPEILLGSHHYSTPVDIWSVGCIFAEMISQKPLFPGDSEIDQLFKIFRIMGTPYEDTWRGVTSLPDYKSAFPKWKPTDLETFVPNLDPDGVDLLSKMLLMDPTKRINARAALEHEYF |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length294
- Mass (Da)34,030
- Last updated1992-03-01 v1
- ChecksumB5FAE55FA9EC366E
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M59198 EMBL· GenBank· DDBJ | AAA32831.1 EMBL· GenBank· DDBJ | mRNA | ||
S45387 EMBL· GenBank· DDBJ | AAB23643.1 EMBL· GenBank· DDBJ | mRNA | ||
X57839 EMBL· GenBank· DDBJ | CAA40971.1 EMBL· GenBank· DDBJ | mRNA | ||
D10850 EMBL· GenBank· DDBJ | BAA01623.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL132963 EMBL· GenBank· DDBJ | CAB87903.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002686 EMBL· GenBank· DDBJ | AEE78452.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY090353 EMBL· GenBank· DDBJ | AAL91258.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
BT024706 EMBL· GenBank· DDBJ | ABD59044.1 EMBL· GenBank· DDBJ | mRNA | ||
AK226373 EMBL· GenBank· DDBJ | BAE98520.1 EMBL· GenBank· DDBJ | mRNA | ||
AY085153 EMBL· GenBank· DDBJ | AAM61706.1 EMBL· GenBank· DDBJ | mRNA |