ID CHKB_HUMAN Reviewed; 395 AA. AC Q9Y259; A0PJM6; Q13388; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 181. DE RecName: Full=Choline/ethanolamine kinase; DE AltName: Full=Choline kinase beta; DE Short=CK; DE Short=CKB; DE EC=2.7.1.32 {ECO:0000269|PubMed:19915674, ECO:0000269|PubMed:21665002}; DE AltName: Full=Choline kinase-like protein; DE AltName: Full=Ethanolamine kinase; DE Short=EK; DE EC=2.7.1.82 {ECO:0000269|PubMed:19915674}; DE AltName: Full=Ethanolamine kinase beta; DE Short=EKB; DE AltName: Full=choline/ethanolamine kinase beta; DE Short=CKEKB; GN Name=CHKB; Synonyms=CHETK, CHKL; 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 [GENOMIC DNA / MRNA] (ISOFORM 1). RX PubMed=10918069; DOI=10.1074/jbc.m006322200; RA Yamazaki N., Shinohara Y., Kajimoto K., Shindo M., Terada H.; RT "Novel expression of equivocal messages containing both regions of RT choline/ethanolamine kinase and muscle type carnitine palmitoyltransferase RT I."; RL J. Biol. Chem. 275:31739-31746(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Smink L.J., Huckle E.J.; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, and Lung; 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 [8] RP PROTEIN SEQUENCE OF 2-19, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [9] 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 [10] RP FUNCTION, CATALYTIC ACTIVITY, INVOLVEMENT IN MDCMC, VARIANTS MDCMC RP 39-SER--SER-395 DEL; 185-PRO--TRP-187 DEL; 270-TYR--SER-395 DEL; LYS-283; RP 308-GLN--SER-395 DEL AND LEU-377, CHARACTERIZATION OF VARIANTS MDCMC RP 39-SER--SER-395 DEL; 185-PRO--TRP-187 DEL; 270-TYR--SER-395 DEL; LYS-283 RP AND LEU-377, AND VARIANTS ILE-301 AND ARG-328. RX PubMed=21665002; DOI=10.1016/j.ajhg.2011.05.010; RA Mitsuhashi S., Ohkuma A., Talim B., Karahashi M., Koumura T., Aoyama C., RA Kurihara M., Quinlivan R., Sewry C., Mitsuhashi H., Goto K., Koksal B., RA Kale G., Ikeda K., Taguchi R., Noguchi S., Hayashi Y.K., Nonaka I., RA Sher R.B., Sugimoto H., Nakagawa Y., Cox G.A., Topaloglu H., Nishino I.; RT "A congenital muscular dystrophy with mitochondrial structural RT abnormalities caused by defective de novo phosphatidylcholine RT biosynthesis."; RL Am. J. Hum. Genet. 88:845-851(2011). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 14-395 IN COMPLEX WITH ADP; RP MAGNESIUM IONS AND HEMICHOLINIUM-3. RG Structural genomics consortium (SGC); RT "Crystal structure of human choline kinase beta in complex with RT phosphorylated hemicholinium-3 and adenosine nucleotide."; RL Submitted (SEP-2009) to the PDB data bank. RN [13] RP VARIANT MDCMC 292-GLU--SER-395 DEL. RX PubMed=22782513; DOI=10.1001/archneurol.2011.2333; RA Gutierrez Rios P., Kalra A.A., Wilson J.D., Tanji K., Akman H.O., RA Area Gomez E., Schon E.A., DiMauro S.; RT "Congenital megaconial myopathy due to a novel defect in the choline kinase RT beta gene."; RL Arch. Neurol. 69:657-661(2012). RN [14] RP VARIANT MDCMC 270-TYR--SER-395 DEL. RX PubMed=24997086; DOI=10.1016/j.ejpn.2014.06.005; RA Castro-Gago M., Dacruz-Alvarez D., Pintos-Martinez E., Beiras-Iglesias A., RA Delmiro A., Arenas J., Martin M.A., Martinez-Azorin F.; RT "Exome sequencing identifies a CHKB mutation in Spanish patient with RT megaconial congenital muscular dystrophy and mtDNA depletion."; RL Eur. J. Paediatr. Neurol. 18:796-800(2014). RN [15] RP VARIANTS MDCMC 159-ARG--SER-395 DEL AND 308-GLN--SER-395 DEL. RX PubMed=26067811; DOI=10.1007/s10545-015-9856-2; RA Haliloglu G., Talim B., Sel C.G., Topaloglu H.; RT "Clinical characteristics of megaconial congenital muscular dystrophy due RT to choline kinase beta gene defects in a series of 15 patients."; RL J. Inherit. Metab. Dis. 38:1099-1108(2015). RN [16] RP VARIANT MDCMC 216-TYR--SER-395 DEL. RX PubMed=25187204; DOI=10.1002/mus.24446; RA Cabrera-Serrano M., Junckerstorff R.C., Atkinson V., Sivadorai P., RA Allcock R.J., Lamont P., Laing N.G.; RT "Novel CHKB mutation expands the megaconial muscular dystrophy phenotype."; RL Muscle Nerve 51:140-143(2015). RN [17] RP VARIANT MDCMC 270-TYR--SER-395 DEL. RX PubMed=26006750; DOI=10.1016/j.braindev.2015.05.008; RA Castro-Gago M., Dacruz-Alvarez D., Pintos-Martinez E., Beiras-Iglesias A., RA Arenas J., Martin M.A., Martinez-Azorin F.; RT "Congenital neurogenic muscular atrophy in megaconial myopathy due to a RT mutation in CHKB gene."; RL Brain Dev. 38:167-172(2016). RN [18] RP ERRATUM OF PUBMED:26006750. RX PubMed=27138744; DOI=10.1016/j.braindev.2016.04.009; RA Castro-Gago M., Dacruz-Alvarez D., Pintos-Martinez E., Beiras-Iglesias A., RA Arenas J., Martin M.A., Martinez-Azorin F.; RL Brain Dev. 38:783-783(2016). CC -!- FUNCTION: Has a key role in phospholipid metabolism, and catalyzes the CC first step of phosphatidylethanolamine and phosphatidylcholine CC biosynthesis. {ECO:0000269|PubMed:19915674, CC ECO:0000269|PubMed:21665002}. 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:19915674, CC ECO:0000269|PubMed:21665002}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12838; CC Evidence={ECO:0000269|PubMed:21665002}; 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:19915674}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13070; CC Evidence={ECO:0000305|PubMed:19915674}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.57 mM for choline {ECO:0000269|PubMed:19915674}; CC KM=2.9 mM for ethanolamine {ECO:0000269|PubMed:19915674}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3. CC {ECO:0000305|PubMed:19915674}. CC -!- SUBUNIT: Homodimer, and heterodimer with CHKA. {ECO:0000269|Ref.12}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y259-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y259-2; Sequence=VSP_034248, VSP_034249; CC -!- DISEASE: Muscular dystrophy, congenital, megaconial type (MDCMC) CC [MIM:602541]: An autosomal recessive, congenital muscular dystrophy CC characterized by early-onset muscle wasting, intellectual disability, CC and dilated cardiomyopathy in half of affected individuals. Some CC patients may die from cardiomyopathy in the first or second decade of CC life. Muscle biopsy shows peculiar enlarged mitochondria that are CC prevalent toward the periphery of the fibers but are sparse in the CC center. {ECO:0000269|PubMed:21665002, ECO:0000269|PubMed:22782513, CC ECO:0000269|PubMed:24997086, ECO:0000269|PubMed:25187204, CC ECO:0000269|PubMed:26006750, ECO:0000269|PubMed:26067811}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which CC also produces the CPT1B protein from a non-overlapping reading frame. CC -!- SIMILARITY: Belongs to the choline/ethanolamine kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB03342.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB029885; BAA82511.1; -; Genomic_DNA. DR EMBL; AB029886; BAA82512.1; -; mRNA. DR EMBL; AL096780; CAB46629.1; -; mRNA. DR EMBL; AL096781; CAB46630.1; -; mRNA. DR EMBL; CR456419; CAG30305.1; -; mRNA. DR EMBL; AK314324; BAG36972.1; -; mRNA. DR EMBL; U62317; AAB03342.2; ALT_SEQ; Genomic_DNA. DR EMBL; CH471138; EAW73573.1; -; Genomic_DNA. DR EMBL; BC082263; AAH82263.1; -; mRNA. DR EMBL; BC101488; AAI01489.1; -; mRNA. DR EMBL; BC113521; AAI13522.2; -; mRNA. DR CCDS; CCDS14099.1; -. [Q9Y259-1] DR RefSeq; NP_005189.2; NM_005198.4. [Q9Y259-1] DR PDB; 2IG7; X-ray; 1.80 A; A/B=14-395. DR PDB; 3FEG; X-ray; 1.30 A; A=35-395. DR PDB; 3LQ3; X-ray; 1.42 A; A=14-395. DR PDBsum; 2IG7; -. DR PDBsum; 3FEG; -. DR PDBsum; 3LQ3; -. DR AlphaFoldDB; Q9Y259; -. DR SMR; Q9Y259; -. DR BioGRID; 107544; 3. DR IntAct; Q9Y259; 1. DR STRING; 9606.ENSP00000384400; -. DR BindingDB; Q9Y259; -. DR ChEMBL; CHEMBL3112385; -. DR DrugBank; DB00122; Choline. DR DrugBank; DB14006; Choline salicylate. DR SwissLipids; SLP:000001747; -. [Q9Y259-1] DR iPTMnet; Q9Y259; -. DR PhosphoSitePlus; Q9Y259; -. DR BioMuta; CHKB; -. DR DMDM; 6685604; -. DR EPD; Q9Y259; -. DR jPOST; Q9Y259; -. DR MassIVE; Q9Y259; -. DR MaxQB; Q9Y259; -. DR PaxDb; 9606-ENSP00000384400; -. DR PeptideAtlas; Q9Y259; -. DR ProteomicsDB; 85662; -. [Q9Y259-1] DR ProteomicsDB; 85663; -. [Q9Y259-2] DR Pumba; Q9Y259; -. DR Antibodypedia; 14556; 192 antibodies from 28 providers. DR DNASU; 1120; -. DR Ensembl; ENST00000406938.3; ENSP00000384400.3; ENSG00000100288.20. [Q9Y259-1] DR GeneID; 1120; -. DR KEGG; hsa:1120; -. DR MANE-Select; ENST00000406938.3; ENSP00000384400.3; NM_005198.5; NP_005189.2. DR UCSC; uc003bmv.4; human. [Q9Y259-1] DR AGR; HGNC:1938; -. DR CTD; 1120; -. DR DisGeNET; 1120; -. DR GeneCards; CHKB; -. DR GeneReviews; CHKB; -. DR HGNC; HGNC:1938; CHKB. DR HPA; ENSG00000100288; Low tissue specificity. DR MalaCards; CHKB; -. DR MIM; 602541; phenotype. DR MIM; 612395; gene. DR neXtProt; NX_Q9Y259; -. DR OpenTargets; ENSG00000100288; -. DR Orphanet; 280671; Megaconial congenital muscular dystrophy. DR Orphanet; 521305; Proximal myopathy with focal depletion of mitochondria. DR PharmGKB; PA26469; -. DR VEuPathDB; HostDB:ENSG00000100288; -. DR eggNOG; KOG2686; Eukaryota. DR GeneTree; ENSGT00950000182939; -. DR HOGENOM; CLU_012712_2_1_1; -. DR InParanoid; Q9Y259; -. DR OMA; HQWCREY; -. DR OrthoDB; 144299at2759; -. DR PhylomeDB; Q9Y259; -. DR TreeFam; TF313549; -. DR BRENDA; 2.7.1.32; 2681. DR PathwayCommons; Q9Y259; -. DR Reactome; R-HSA-1483191; Synthesis of PC. DR Reactome; R-HSA-1483213; Synthesis of PE. DR SABIO-RK; Q9Y259; -. DR SignaLink; Q9Y259; -. DR UniPathway; UPA00558; UER00741. DR BioGRID-ORCS; 1120; 13 hits in 1153 CRISPR screens. DR EvolutionaryTrace; Q9Y259; -. DR GeneWiki; CHKB_(gene); -. DR GenomeRNAi; 1120; -. DR Pharos; Q9Y259; Tbio. DR PRO; PR:Q9Y259; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q9Y259; Protein. DR Bgee; ENSG00000100288; Expressed in pituitary gland and 95 other cell types or tissues. DR ExpressionAtlas; Q9Y259; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004103; F:choline kinase activity; IDA:UniProtKB. DR GO; GO:0004305; F:ethanolamine kinase activity; IDA:UniProtKB. DR GO; GO:0006657; P:CDP-choline pathway; IBA:GO_Central. DR GO; GO:0007517; P:muscle organ development; IEA:Ensembl. DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IDA:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd05156; ChoK_euk; 1. DR Gene3D; 3.90.1200.10; -; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR PANTHER; PTHR22603; CHOLINE/ETHANOALAMINE KINASE; 1. DR PANTHER; PTHR22603:SF35; CHOLINE_ETHANOLAMINE KINASE; 1. DR Pfam; PF01633; Choline_kinase; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR Genevisible; Q9Y259; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Congenital muscular dystrophy; Direct protein sequencing; Disease variant; KW Kinase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding; KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895" FT CHAIN 2..395 FT /note="Choline/ethanolamine kinase" FT /id="PRO_0000206222" FT BINDING 75..81 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 77..79 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 104 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|Ref.12" FT BINDING 146..152 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|Ref.12" FT BINDING 244 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|Ref.12" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22223895" FT VAR_SEQ 75..127 FT /note="SGGLSNLLFRCSLPDHLPSVGEEPREVLLRLYGAILQGVDSLVLESVMFAIL FT A -> RWEVRGQPLRCADRGQGSAAGPSGCSMFSPPSCARAWGGAGPAWPGGGRGRGR FT (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_034248" FT VAR_SEQ 128..395 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_034249" FT VARIANT 39..395 FT /note="Missing (in MDCMC; loss of choline kinase activity; FT decreased amount of phosphatidylcholine in patients cells)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081791" FT VARIANT 159..395 FT /note="Missing (in MDCMC)" FT /evidence="ECO:0000269|PubMed:26067811" FT /id="VAR_081792" FT VARIANT 185..187 FT /note="Missing (in MDCMC; severely decreased choline kinase FT activity)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081793" FT VARIANT 216..395 FT /note="Missing (in MDCMC)" FT /evidence="ECO:0000269|PubMed:25187204" FT /id="VAR_081794" FT VARIANT 270..395 FT /note="Missing (in MDCMC; loss of choline kinase activity; FT decreased amount of phosphatidylcholine in patients cells)" FT /evidence="ECO:0000269|PubMed:21665002, FT ECO:0000269|PubMed:24997086, ECO:0000269|PubMed:26006750" FT /id="VAR_081795" FT VARIANT 283 FT /note="E -> K (in MDCMC; severely decreased choline kinase FT activity)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081796" FT VARIANT 292..395 FT /note="Missing (in MDCMC)" FT /evidence="ECO:0000269|PubMed:22782513" FT /id="VAR_081797" FT VARIANT 301 FT /note="T -> I (in dbSNP:rs147485527)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081798" FT VARIANT 308..395 FT /note="Missing (in MDCMC)" FT /evidence="ECO:0000269|PubMed:21665002, FT ECO:0000269|PubMed:26067811" FT /id="VAR_081799" FT VARIANT 328 FT /note="Q -> R (in dbSNP:rs141381896)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081800" FT VARIANT 377 FT /note="R -> L (in MDCMC; decreased choline kinase activity; FT dbSNP:rs772705206)" FT /evidence="ECO:0000269|PubMed:21665002" FT /id="VAR_081801" FT HELIX 43..57 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 59..63 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 70..74 FT /evidence="ECO:0007829|PDB:2IG7" FT TURN 77..79 FT /evidence="ECO:0007829|PDB:2IG7" FT STRAND 82..86 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:2IG7" FT STRAND 99..105 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:2IG7" FT HELIX 113..128 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 135..139 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 142..146 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 155..159 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 161..175 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 187..201 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 212..215 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 218..230 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 236..239 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 245..247 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 248..252 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:2IG7" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:2IG7" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 273..283 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 306..320 FT /evidence="ECO:0007829|PDB:3FEG" FT TURN 321..323 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 328..361 FT /evidence="ECO:0007829|PDB:3FEG" FT STRAND 365..368 FT /evidence="ECO:0007829|PDB:3FEG" FT HELIX 370..386 FT /evidence="ECO:0007829|PDB:3FEG" SQ SEQUENCE 395 AA; 45271 MW; 18367468B22FB9CE CRC64; MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY QWCREYLGGA WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE VLLRLYGAIL QGVDSLVLES VMFAILAERS LGPQLYGVFP EGRLEQYIPS RPLKTQELRE PVLSAAIATK MAQFHGMEMP FTKEPHWLFG TMERYLKQIQ DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH NDIQEGNILL LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH FFWGLWSILQ ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS //