P20485 · KICH_YEAST
- ProteinCholine kinase
- GeneCKI1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids582 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the committed step in the synthesis of phosphatidylcholine by the CDP-choline pathway (PubMed:10329685, PubMed:2536698, PubMed:9506987).
Also exhibits ethanolamine kinase activity but it is a poor substrate at 14% efficiency compared with choline (PubMed:2536698, PubMed:9506987).
Also exhibits ethanolamine kinase activity but it is a poor substrate at 14% efficiency compared with choline (PubMed:2536698, PubMed:9506987).
Miscellaneous
Present with 3930 molecules/cell in log phase SD medium.
Catalytic activity
- choline + ATP = phosphocholine + ADP + H+This reaction proceeds in the forward direction.
- ethanolamine + ATP = phosphoethanolamine + ADP + H+This reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
90 μM | ATP | |||||
0.27 mM | choline |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
138.7 μmol/min/mg | for choline |
pH Dependence
Optimum pH is 9.5-12.
Temperature Dependence
Optimum temperature is 30 degrees Celsius.
Pathway
Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | choline kinase activity | |
Molecular Function | ethanolamine kinase activity | |
Biological Process | phosphatidylcholine biosynthetic process | |
Biological Process | phosphatidylethanolamine biosynthetic process | |
Biological Process | phosphorylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameCholine kinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP20485
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30 | Decrease in activity and in phosphorylation by PKA. No phosphorylation by PKA, and strong decrease in activity; when associated with A-85. | ||||
Sequence: S → A | ||||||
Mutagenesis | 85 | No phosphorylation by PKA, and strong decrease in activity; when associated with A-30. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 10 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000206226 | 2-582 | Choline kinase | |||
Sequence: VQESRPGSVRSYSVGYQARSRSSSQRRHSLTRQRSSQRLIRTISIESDVSNITDDDDLRAVNEGVAGVQLDVSETANKGPRRASATDVTDSLGSTSSEYIEIPFVKETLDASLPSDYLKQDILNLIQSLKISKWYNNKKIQPVAQDMNLVKISGAMTNAIFKVEYPKLPSLLLRIYGPNIDNIIDREYELQILARLSLKNIGPSLYGCFVNGRFEQFLENSKTLTKDDIRNWKNSQRIARRMKELHVGVPLLSSERKNGSACWQKINQWLRTIEKVDQWVGDPKNIENSLLCENWSKFMDIVDRYHKWLISQEQGIEQVNKNLIFCHNDAQYGNLLFTAPVMNTPSLYTAPSSTSLTSQSSSLFPSSSNVIVDDIINPPKQEQSQDSKLVVIDFEYAGANPAAYDLANHLSEWMYDYNNAKAPHQCHADRYPDKEQVLNFLYSYVSHLRGGAKEPIDEEVQRLYKSIIQWRPTVQLFWSLWAILQSGKLEKKEASTAITREEIGPNGKKYIIKTEPESPEEDFVENDDEPEAGVSIDTFDYMAYGRDKIAVFWGDLIGLGIITEEECKNFSSFKFLDTSYL | ||||||
Modified residue | 30 | Phosphoserine; by PKA | ||||
Sequence: S | ||||||
Modified residue | 48 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 51 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 54 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 85 | Phosphoserine; by PKA | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Monomer. Interacts with NAP1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P20485 | NAP1 P25293 | 5 | EBI-9699, EBI-11850 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-25 | Polar residues | ||||
Sequence: MVQESRPGSVRSYSVGYQARSRSSS | ||||||
Region | 1-36 | Disordered | ||||
Sequence: MVQESRPGSVRSYSVGYQARSRSSSQRRHSLTRQRS |
Sequence similarities
Belongs to the choline/ethanolamine kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length582
- Mass (Da)66,317
- Last updated1991-02-01 v1
- Checksum68C395B9CC120A0E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-25 | Polar residues | ||||
Sequence: MVQESRPGSVRSYSVGYQARSRSSS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J04454 EMBL· GenBank· DDBJ | AAA34499.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X91258 EMBL· GenBank· DDBJ | CAA62646.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z73305 EMBL· GenBank· DDBJ | CAA97704.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U53881 EMBL· GenBank· DDBJ | AAB82396.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692779 EMBL· GenBank· DDBJ | AAT92798.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09444.1 EMBL· GenBank· DDBJ | Genomic DNA |