CHKB_HUMAN
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 03-AUG-2022, entry version 172.
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};
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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; 2.
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; Q9Y259; -.
DR PeptideAtlas; Q9Y259; -.
DR PRIDE; Q9Y259; -.
DR ProteomicsDB; 85662; -. [Q9Y259-1]
DR ProteomicsDB; 85663; -. [Q9Y259-2]
DR Antibodypedia; 14556; 167 antibodies from 27 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 CTD; 1120; -.
DR DisGeNET; 1120; -.
DR GeneCards; 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; CKPRLLE; -.
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 1076 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 93 other tissues.
DR ExpressionAtlas; Q9Y259; baseline and differential.
DR Genevisible; Q9Y259; HS.
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:0006656; P:phosphatidylcholine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR026712; Cho/Etha_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR22603:SF35; PTHR22603:SF35; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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
