GenomeNet

Database: UniProt
Entry: CHKB_HUMAN
LinkDB: CHKB_HUMAN
Original site: 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   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   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: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.
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
//
DBGET integrated database retrieval system