CHKA_HUMAN
ID CHKA_HUMAN Reviewed; 457 AA.
AC P35790; Q8NE29;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Choline kinase alpha;
DE Short=CK;
DE EC=2.7.1.32 {ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:19915674};
DE AltName: Full=CHETK-alpha;
DE AltName: Full=Ethanolamine kinase;
DE Short=EK;
DE EC=2.7.1.82 {ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:19915674};
GN Name=CHKA; Synonyms=CHK, CKI {ECO:0000303|PubMed:1618328};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1618328; DOI=10.1016/0014-5793(92)80625-q;
RA Hosaka K., Tanaka S., Nikawa J., Yamashita S.;
RT "Cloning of a human choline kinase cDNA by complementation of the yeast cki
RT mutation.";
RL FEBS Lett. 304:229-232(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS GLY-220
RP AND GLN-422.
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=19915674; DOI=10.1371/journal.pone.0007819;
RA Gallego-Ortega D., Ramirez de Molina A., Ramos M.A., Valdes-Mora F.,
RA Barderas M.G., Sarmentero-Estrada J., Lacal J.C.;
RT "Differential role of human choline kinase alpha and beta enzymes in lipid
RT metabolism: implications in cancer onset and treatment.";
RL PLoS ONE 4:E7819-E7819(2009).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH PI4KA AND HCV NON-STRUCTURAL PROTEIN 5A
RP (MICROBIAL INFECTION).
RX PubMed=28566381; DOI=10.1128/jvi.00355-17;
RA Wong M.T., Chen S.S.;
RT "Hepatitis C Virus Subverts Human Choline Kinase-alpha To Bridge
RT Phosphatidylinositol-4-Kinase IIIalpha (PI4KIIIalpha) and NS5A and
RT Upregulates PI4KIIIalpha Activation, Thereby Promoting the Translocation of
RT the Ternary Complex to the Endoplasmic Reticulum for Viral Replication.";
RL J. Virol. 91:0-0(2017).
RN [6]
RP FUNCTION (ISOFORM 1), CATALYTIC ACTIVITY (ISOFORM 1), SUBCELLULAR LOCATION
RP (ISOFORM 1), SUBUNIT (ISOFORM 1), PHOSPHORYLATION AT SER-279, ACETYLATION
RP AT LYS-247, AND MUTAGENESIS OF GLU-175; 177-MET--LEU-179; 182-VAL--PHE-184;
RP 186-ILE-LEU-187; LYS-247 AND SER-279.
RX PubMed=34077757; DOI=10.1016/j.molcel.2021.05.005;
RA Liu R., Lee J.H., Li J., Yu R., Tan L., Xia Y., Zheng Y., Bian X.L.,
RA Lorenzi P.L., Chen Q., Lu Z.;
RT "Choline kinase alpha 2 acts as a protein kinase to promote lipolysis of
RT lipid droplets.";
RL Mol. Cell 81:2722-2735(2021).
RN [7] {ECO:0007744|PDB:2CKO, ECO:0007744|PDB:2CKP, ECO:0007744|PDB:2CKQ}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 50-439 IN COMPLEX WITH ADP AND
RP PHOSPHOCHOLINE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17007874; DOI=10.1016/j.jmb.2006.08.084;
RA Malito E., Sekulic N., Too W.C., Konrad M., Lavie A.;
RT "Elucidation of human choline kinase crystal structures in complex with the
RT products ADP or phosphocholine.";
RL J. Mol. Biol. 364:136-151(2006).
RN [8] {ECO:0007744|PDB:3G15}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 75-457 IN COMPLEX WITH
RP HEMICHOLINIUM-3 AND ADP.
RX PubMed=20299452; DOI=10.1074/jbc.m109.039024;
RA Hong B.S., Allali-Hassani A., Tempel W., Finerty P.J. Jr., Mackenzie F.,
RA Dimov S., Vedadi M., Park H.W.;
RT "Crystal structures of human choline kinase isoforms in complex with
RT hemicholinium-3: single amino acid near the active site influences
RT inhibitor sensitivity.";
RL J. Biol. Chem. 285:16330-16340(2010).
CC -!- FUNCTION: Plays a key role in phospholipid biosynthesis by catalyzing
CC the phosphorylation of free choline to phosphocholine, the first step
CC in phosphatidylcholine biosynthesis (PubMed:19915674, PubMed:34077757,
CC PubMed:17007874). Also phosphorylates ethanolamine, thereby
CC contributing to phosphatidylethanolamine biosynthesis (PubMed:19915674,
CC PubMed:17007874). Has higher activity with choline (PubMed:19915674,
CC PubMed:17007874). May contribute to tumor cell growth
CC (PubMed:19915674). {ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674, ECO:0000269|PubMed:34077757}.
CC -!- FUNCTION: [Isoform 1]: This isoform plays a key role in lipolysis of
CC lipid droplets following glucose deprivation (PubMed:34077757). In
CC response to glucose deprivation, phosphorylated by AMPK, promoting
CC localization to lipid droplets (PubMed:34077757). Phosphorylation is
CC followed by acetylation by KAT5, leading to dissociation of the
CC homodimer into a monomer (PubMed:34077757). Monomeric CHKA isoform 1 is
CC converted into a tyrosine-protein kinase, which phosphorylates lipid
CC droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of
CC lipid droplets (PubMed:34077757). {ECO:0000269|PubMed:34077757}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + choline = ADP + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:12837, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:295975, ChEBI:CHEBI:456216;
CC EC=2.7.1.32; Evidence={ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674, ECO:0000269|PubMed:34077757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838;
CC Evidence={ECO:0000269|PubMed:17007874, ECO:0000305|PubMed:19915674};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + ethanolamine = ADP + H(+) + phosphoethanolamine;
CC Xref=Rhea:RHEA:13069, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57603, ChEBI:CHEBI:58190, ChEBI:CHEBI:456216;
CC EC=2.7.1.82; Evidence={ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070;
CC Evidence={ECO:0000269|PubMed:17007874, ECO:0000305|PubMed:19915674};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:34077757};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC Evidence={ECO:0000269|PubMed:34077757};
CC -!- ACTIVITY REGULATION: Homodimerization or heterodimerization is required
CC for the choline and ethanolamine kinase activities.
CC {ECO:0000269|PubMed:34077757}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 mM for choline {ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674};
CC KM=0.4 mM for ATP {ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674};
CC KM=12 mM for ethanolamine {ECO:0000269|PubMed:17007874,
CC ECO:0000269|PubMed:19915674};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis;
CC phosphocholine from choline: step 1/1. {ECO:0000305|PubMed:17007874,
CC ECO:0000305|PubMed:19915674}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
CC {ECO:0000305|PubMed:17007874, ECO:0000305|PubMed:19915674}.
CC -!- SUBUNIT: Homodimer (PubMed:34077757, PubMed:17007874, PubMed:20299452).
CC Heterodimer with CHKB (By similarity). {ECO:0000250|UniProtKB:O54804,
CC ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:20299452,
CC ECO:0000269|PubMed:34077757}.
CC -!- SUBUNIT: [Isoform 1]: Monomer; acetylation by KAT5 promotes
CC dissociation of the homodimer and monomerization.
CC {ECO:0000269|PubMed:34077757}.
CC -!- SUBUNIT: (Microbial infection) Interacts with PI4KA/PI4KIIIalpha; CHKA
CC bridges PI4KA/PI4KIIIalpha and hepatitis C virus (HCV) non-structural
CC protein 5A (NS5A) and potentiates NS5A-stimulated PI4KA activity, which
CC then facilitates the targeting of the ternary complex to the ER for
CC viral replication. {ECO:0000269|PubMed:28566381}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:34077757}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Lipid droplet
CC {ECO:0000269|PubMed:34077757}. Note=Isoform 1 localizes to lipid
CC droplets following phosphorylation by AMPK.
CC {ECO:0000269|PubMed:34077757}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CHKalpha2 {ECO:0000303|PubMed:34077757}, alpha-2
CC {ECO:0000303|PubMed:34077757};
CC IsoId=P35790-1; Sequence=Displayed;
CC Name=2; Synonyms=CHKalpha1 {ECO:0000303|PubMed:34077757}, alpha-1
CC {ECO:0000303|PubMed:34077757};
CC IsoId=P35790-2; Sequence=VSP_009683;
CC -!- PTM: [Isoform 1]: Phosphorylated at Ser-279 by AMPK in response to
CC glucose deprivation, leading to localization to lipid droplets.
CC {ECO:0000269|PubMed:34077757}.
CC -!- PTM: [Isoform 1]: Acetylated by KAT5 at Lys-247 following
CC phosphorylation by AMPK, leading to monomerization and conversion into
CC a tyrosine-protein kinase. {ECO:0000269|PubMed:34077757}.
CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CHKAID44009ch11q13.html";
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DR EMBL; D10704; BAA01547.1; -; mRNA.
DR EMBL; AP002807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036471; AAH36471.1; -; mRNA.
DR CCDS; CCDS8178.1; -. [P35790-1]
DR CCDS; CCDS8179.1; -. [P35790-2]
DR PIR; S23104; S23104.
DR RefSeq; NP_001268.2; NM_001277.2. [P35790-1]
DR RefSeq; NP_997634.1; NM_212469.1. [P35790-2]
DR PDB; 2CKO; X-ray; 2.15 A; A/B=50-457.
DR PDB; 2CKP; X-ray; 3.10 A; A/B=50-457.
DR PDB; 2CKQ; X-ray; 2.40 A; A/B=50-457.
DR PDB; 2I7Q; X-ray; 1.90 A; A=75-457.
DR PDB; 3F2R; X-ray; 2.35 A; A/B=75-457.
DR PDB; 3G15; X-ray; 1.70 A; A/B=75-457.
DR PDB; 3ZM9; X-ray; 1.90 A; A/B=75-457.
DR PDB; 4BR3; X-ray; 2.20 A; A/B=75-457.
DR PDB; 4CG8; X-ray; 1.75 A; A=75-457.
DR PDB; 4CG9; X-ray; 1.83 A; A=75-457.
DR PDB; 4CGA; X-ray; 1.74 A; A=75-457.
DR PDB; 4DA5; X-ray; 2.40 A; A/B=1-457.
DR PDB; 5AFV; X-ray; 2.25 A; A/B=80-457.
DR PDB; 5EQE; X-ray; 2.40 A; A/B=75-457.
DR PDB; 5EQP; X-ray; 2.35 A; A/B=75-457.
DR PDB; 5EQY; X-ray; 2.50 A; A/B=75-457.
DR PDB; 5FTG; X-ray; 1.45 A; A=80-457.
DR PDB; 5FUT; X-ray; 1.60 A; A=80-457.
DR PDB; 5W6O; X-ray; 2.35 A; A/B=80-457.
DR PDB; 7A04; X-ray; 2.15 A; A/B=75-457.
DR PDB; 7A06; X-ray; 1.80 A; A=75-457.
DR PDB; 7NB1; X-ray; 2.30 A; AAA/BBB=75-457.
DR PDB; 7NB2; X-ray; 2.40 A; AAA/BBB=75-457.
DR PDB; 7NB3; X-ray; 2.00 A; AAA/BBB=75-457.
DR PDBsum; 2CKO; -.
DR PDBsum; 2CKP; -.
DR PDBsum; 2CKQ; -.
DR PDBsum; 2I7Q; -.
DR PDBsum; 3F2R; -.
DR PDBsum; 3G15; -.
DR PDBsum; 3ZM9; -.
DR PDBsum; 4BR3; -.
DR PDBsum; 4CG8; -.
DR PDBsum; 4CG9; -.
DR PDBsum; 4CGA; -.
DR PDBsum; 4DA5; -.
DR PDBsum; 5AFV; -.
DR PDBsum; 5EQE; -.
DR PDBsum; 5EQP; -.
DR PDBsum; 5EQY; -.
DR PDBsum; 5FTG; -.
DR PDBsum; 5FUT; -.
DR PDBsum; 5W6O; -.
DR PDBsum; 7A04; -.
DR PDBsum; 7A06; -.
DR PDBsum; 7NB1; -.
DR PDBsum; 7NB2; -.
DR PDBsum; 7NB3; -.
DR AlphaFoldDB; P35790; -.
DR SMR; P35790; -.
DR BioGRID; 107543; 7.
DR IntAct; P35790; 1.
DR STRING; 9606.ENSP00000265689; -.
DR BindingDB; P35790; -.
DR ChEMBL; CHEMBL3117; -.
DR DrugBank; DB00122; Choline.
DR DrugBank; DB14006; Choline salicylate.
DR SwissLipids; SLP:000001746; -. [P35790-1]
DR iPTMnet; P35790; -.
DR PhosphoSitePlus; P35790; -.
DR BioMuta; CHKA; -.
DR DMDM; 226694197; -.
DR EPD; P35790; -.
DR jPOST; P35790; -.
DR MassIVE; P35790; -.
DR MaxQB; P35790; -.
DR PaxDb; P35790; -.
DR PeptideAtlas; P35790; -.
DR PRIDE; P35790; -.
DR ProteomicsDB; 55154; -. [P35790-1]
DR ProteomicsDB; 55155; -. [P35790-2]
DR Antibodypedia; 16639; 234 antibodies from 29 providers.
DR CPTC; P35790; 3 antibodies.
DR DNASU; 1119; -.
DR Ensembl; ENST00000265689.9; ENSP00000265689.4; ENSG00000110721.12. [P35790-1]
DR Ensembl; ENST00000356135.9; ENSP00000348454.4; ENSG00000110721.12. [P35790-2]
DR GeneID; 1119; -.
DR KEGG; hsa:1119; -.
DR MANE-Select; ENST00000265689.9; ENSP00000265689.4; NM_001277.3; NP_001268.2.
DR UCSC; uc001onj.4; human. [P35790-1]
DR CTD; 1119; -.
DR DisGeNET; 1119; -.
DR GeneCards; CHKA; -.
DR HGNC; HGNC:1937; CHKA.
DR HPA; ENSG00000110721; Low tissue specificity.
DR MIM; 118491; gene.
DR neXtProt; NX_P35790; -.
DR OpenTargets; ENSG00000110721; -.
DR PharmGKB; PA26468; -.
DR VEuPathDB; HostDB:ENSG00000110721; -.
DR eggNOG; KOG2686; Eukaryota.
DR GeneTree; ENSGT00950000182939; -.
DR HOGENOM; CLU_012712_2_1_1; -.
DR InParanoid; P35790; -.
DR OMA; HEWTADY; -.
DR OrthoDB; 260340at2759; -.
DR PhylomeDB; P35790; -.
DR TreeFam; TF313549; -.
DR BioCyc; MetaCyc:HS03334-MON; -.
DR BRENDA; 2.7.1.32; 2681.
DR PathwayCommons; P35790; -.
DR Reactome; R-HSA-1483191; Synthesis of PC.
DR Reactome; R-HSA-1483213; Synthesis of PE.
DR SABIO-RK; P35790; -.
DR SignaLink; P35790; -.
DR SIGNOR; P35790; -.
DR UniPathway; UPA00558; UER00741.
DR UniPathway; UPA00753; UER00737.
DR BioGRID-ORCS; 1119; 130 hits in 1089 CRISPR screens.
DR ChiTaRS; CHKA; human.
DR EvolutionaryTrace; P35790; -.
DR GeneWiki; CHKA; -.
DR GenomeRNAi; 1119; -.
DR Pharos; P35790; Tchem.
DR PRO; PR:P35790; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; P35790; protein.
DR Bgee; ENSG00000110721; Expressed in left testis and 174 other tissues.
DR ExpressionAtlas; P35790; baseline and differential.
DR Genevisible; P35790; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004103; F:choline kinase activity; IDA:UniProtKB.
DR GO; GO:0004104; F:cholinesterase activity; IEA:Ensembl.
DR GO; GO:0004305; F:ethanolamine kinase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; TAS:ProtInc.
DR GO; GO:0006869; P:lipid transport; TAS:ProtInc.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Kinase; Lipid biosynthesis; Lipid droplet; Lipid metabolism;
KW Nucleotide-binding; Phospholipid biosynthesis; Phospholipid metabolism;
KW Phosphoprotein; Reference proteome; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..457
FT /note="Choline kinase alpha"
FT /id="PRO_0000206219"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 117..123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17007874,
FT ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP,
FT ECO:0007744|PDB:3G15"
FT BINDING 119..121
FT /ligand="phosphocholine"
FT /ligand_id="ChEBI:CHEBI:295975"
FT /evidence="ECO:0000269|PubMed:17007874,
FT ECO:0007744|PDB:2CKQ"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17007874,
FT ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP,
FT ECO:0007744|PDB:3G15"
FT BINDING 207..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17007874,
FT ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP,
FT ECO:0007744|PDB:3G15"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17007874,
FT ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP,
FT ECO:0007744|PDB:3G15"
FT MOD_RES 247
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:34077757"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:34077757"
FT VAR_SEQ 155..172
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009683"
FT VARIANT 220
FT /note="S -> G (in dbSNP:rs17853641)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054863"
FT VARIANT 422
FT /note="L -> Q (in dbSNP:rs17853642)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_054864"
FT MUTAGEN 175
FT /note="E->A: Does not affect interaction with PLIN2 and
FT PLIN3."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 177..179
FT /note="MVL->AAA: Does not affect interaction with PLIN2 and
FT PLIN3."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 182..184
FT /note="VMF->AAA: Does not affect interaction with PLIN2 and
FT PLIN3."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 186..187
FT /note="IL->AA: Abolished interaction with PLIN2 and PLIN3."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 247
FT /note="K->Q: Mimics acetylation; promoting monomerization,
FT leading to decreased choline kinase activity. Increased
FT lipolysis of lipid droplets."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 247
FT /note="K->R: Abolished acetylation by KAT5, leading to
FT prevent conversion into a tyrosine-protein kinase."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 279
FT /note="S->A: Abolished phosphorylation by AMPK, preventing
FT localization to lipid droplets and subsequent acetylation
FT by KAT5."
FT /evidence="ECO:0000269|PubMed:34077757"
FT MUTAGEN 279
FT /note="S->D: Mimics phosphorylation; promoting localization
FT to lipid droplets."
FT /evidence="ECO:0000269|PubMed:34077757"
FT CONFLICT 49..54
FT /note="GGQQPP -> APTAA (in Ref. 1; BAA01547)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="T -> A (in Ref. 1; BAA01547)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="M -> V (in Ref. 1; BAA01547)"
FT /evidence="ECO:0000305"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 101..105
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 119..128
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:5FUT"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 216..220
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 248..262
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 282..294
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:3G15"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:5FUT"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:3ZM9"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 372..386
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 388..392
FT /evidence="ECO:0007829|PDB:5FTG"
FT HELIX 395..430
FT /evidence="ECO:0007829|PDB:5FTG"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:3G15"
FT HELIX 437..455
FT /evidence="ECO:0007829|PDB:5FTG"
SQ SEQUENCE 457 AA; 52249 MW; 65F177ABE1AA3A12 CRC64;
MKTKFCTGGE AEPSPLGLLL SCGSGSAAPA PGVGQQRDAA SDLESKQLGG QQPPLALPPP
PPLPLPLPLP QPPPPQPPAD EQPEPRTRRR AYLWCKEFLP GAWRGLREDE FHISVIRGGL
SNMLFQCSLP DTTATLGDEP RKVLLRLYGA ILQMRSCNKE GSEQAQKENE FQGAEAMVLE
SVMFAILAER SLGPKLYGIF PQGRLEQFIP SRRLDTEELS LPDISAEIAE KMATFHGMKM
PFNKEPKWLF GTMEKYLKEV LRIKFTEESR IKKLHKLLSY NLPLELENLR SLLESTPSPV
VFCHNDCQEG NILLLEGREN SEKQKLMLID FEYSSYNYRG FDIGNHFCEW MYDYSYEKYP
FFRANIRKYP TKKQQLHFIS SYLPAFQNDF ENLSTEEKSI IKEEMLLEVN RFALASHFLW
GLWSIVQAKI SSIEFGYMDY AQARFDAYFH QKRKLGV
