CHKA
entrez
1119
canonical
uniprot
P35790
canonical
ensembl
ENSG00000110721
resolver
ensp
ENSP00000265689
resolver
ensp
ENSP00000348454
resolver
ensp
ENSP00000538508
resolver
ensp
ENSP00000538509
resolver
ensp
ENSP00000745246
resolver
ensp
ENSP00000745249
resolver
genesymbol
CHKA
resolver
genesymbol_syn
CHK
resolver
genesymbol_syn
CKI
resolver
hgnc
HGNC:1937
resolver
uniprot
Q8NE29
resolver
uniprot_entry
CHKA_HUMAN
resolver
uniprot_sec
Q8NE29
resolver
activity_regulation
ACTIVITY REGULATION: Homodimerization or heterodimerization is required for the choline and ethanolamine kinase activities. {ECO:0000269|PubMed:34077757}.
uniprot
proteins
amino_acid_sequence
MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPPPPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGLSNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLESVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKMPFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPVVFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYPFFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLWGLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with microcephaly, movement abnormalities, and seizures (NEDMIMS) [MIM:620023]: An autosomal recessive neurodevelopmental disorder characterized by severe global developmental delay, impaired intellectual development, microcephaly, early-onset seizures, and movement abnormalities. {ECO:0000269|PubMed:35202461}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.32
uniprot
proteins
ec_number
2.7.1.82
uniprot
proteins
function
FUNCTION: Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis (PubMed:17007874, PubMed:19915674, PubMed:23416529, PubMed:34077757). Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis (PubMed:17007874, PubMed:19915674). Has higher activity with choline (PubMed:17007874, PubMed:19915674). May contribute to tumor cell growth (PubMed:19915674). {ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:19915674, ECO:0000269|PubMed:23416529, ECO:0000269|PubMed:34077757}.; FUNCTION: [Isoform 1]: This isoform plays a key role in lipolysis of lipid droplets following glucose deprivation (PubMed:34077757). In response to glucose deprivation, phosphorylated by AMPK, promoting localization to lipid droplets (PubMed:34077757). Phosphorylation is followed by acetylation by KAT5, leading to dissociation of the homodimer into a monomer (PubMed:34077757). Monomeric CHKA isoform 1 is converted into a tyrosine-protein kinase, which phosphorylates lipid droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of lipid droplets (PubMed:34077757). {ECO:0000269|PubMed:34077757}.
uniprot
proteins
mass_dalton
52249
uniprot
proteins
mutagenesis
MUTAGEN 175; /note="E->A: Does not affect interaction with PLIN2 and PLIN3."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 177..179; /note="MVL->AAA: Does not affect interaction with PLIN2 and PLIN3."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 182..184; /note="VMF->AAA: Does not affect interaction with PLIN2 and PLIN3."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 186..187; /note="IL->AA: Abolished interaction with PLIN2 and PLIN3."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 247; /note="K->Q: Mimics acetylation; promoting monomerization, leading to decreased choline kinase activity. Increased lipolysis of lipid droplets."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 247; /note="K->R: Abolished acetylation by KAT5, leading to prevent conversion into a tyrosine-protein kinase."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 279; /note="S->A: Abolished phosphorylation by AMPK, preventing localization to lipid droplets and subsequent acetylation by KAT5."; /evidence="ECO:0000269|PubMed:34077757"; MUTAGEN 279; /note="S->D: Mimics phosphorylation; promoting localization to lipid droplets."; /evidence="ECO:0000269|PubMed:34077757
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1. {ECO:0000269|PubMed:23416529, ECO:0000305|PubMed:17007874, ECO:0000305|PubMed:19915674}.; PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. {ECO:0000305|PubMed:17007874, ECO:0000305|PubMed:19915674}.
uniprot
proteins
post_translational_modification
PTM: [Isoform 1]: Phosphorylated at Ser-279 by AMPK in response to glucose deprivation, leading to localization to lipid droplets. {ECO:0000269|PubMed:34077757}.; PTM: [Isoform 1]: Acetylated by KAT5 at Lys-247 following phosphorylation by AMPK, leading to monomerization and conversion into a tyrosine-protein kinase. {ECO:0000269|PubMed:34077757}.
uniprot
proteins
protein_family
Choline/ethanolamine kinase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1618328
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17007874
uniprot
proteins
pubmed
19915674
uniprot
proteins
pubmed
20299452
uniprot
proteins
pubmed
23416529
uniprot
proteins
pubmed
28566381
uniprot
proteins
pubmed
34077757
uniprot
proteins
pubmed
35202461
uniprot
proteins
sequence_length
457
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:34077757}.; SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet {ECO:0000269|PubMed:34077757}. Note=Isoform 1 localizes to lipid droplets following phosphorylation by AMPK. {ECO:0000269|PubMed:34077757}.
uniprot
proteins