Q9Y259 (CHKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Choline/ethanolamine kinase

Alternative name(s):
Choline kinase beta
Short name=CK
Short name=CKB
EC=2.7.1.32
Choline kinase-like protein
Ethanolamine kinase
Short name=EK
EC=2.7.1.82
Ethanolamine kinase beta
Short name=EKB
choline/ethanolamine kinase beta
Short name=CKEKB

Gene names

Name:	CHKB
Synonyms:	CHETK, CHKL

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	395 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a key role in phospholipid biosynthesis. Catalyzes the first step in phosphatidylethanolamine biosynthesis. Phosphorylates ethanolamine, and can also act on choline (in vitro). Has higher activity with ethanolamine. May not significantly contribute to in vivo phosphatidylcholine biosynthesis. Ref.8
Catalytic activity	ATP + choline = ADP + O-phosphocholine. Ref.8 ATP + ethanolamine = ADP + O-phosphoethanolamine. Ref.8
Pathway	Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
Subunit structure	Homodimer, and heterodimer with CHKA.
Miscellaneous	This protein is produced by a bicistronic gene which also produces the CPT1B protein from a non-overlapping reading frame.
Sequence similarities	Belongs to the choline/ethanolamine kinase family.
Biophysicochemical properties	Kinetic parameters: KM=0.57 mM for choline Ref.8 KM=2.9 mM for ethanolamine
Sequence caution	The sequence AAB03342.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	phosphatidylethanolamine biosynthetic process Inferred from direct assay Ref.8. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW choline kinase activity Inferred from direct assay Ref.8. Source: UniProtKB ethanolamine kinase activity Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y259-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9Y259-2)

The sequence of this isoform differs from the canonical sequence as follows:
     75-127: SGGLSNLLFR...LESVMFAILA → RWEVRGQPLR...WPGGGRGRGR
     128-395: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 395

394

Choline/ethanolamine kinase

PRO_0000206222

Regions

Nucleotide binding

75 – 81

7

ATP By similarity

Nucleotide binding

146 – 152

7

ATP

Region

77 – 79

3

Substrate binding By similarity

Sites

Binding site

104

1

ATP

Binding site

244

1

ATP By similarity

Binding site

264

1

ATP

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Modified residue

39

1

Phosphoserine Ref.7

Modified residue

42

1

Phosphoserine Ref.7

Natural variations

Alternative sequence

75 – 127

53

SGGLS…FAILA → RWEVRGQPLRCADRGQGSAA GPSGCSMFSPPSCARAWGGA GPAWPGGGRGRGR in isoform 2.

VSP_034248

Alternative sequence

128 – 395

268

Missing in isoform 2.

VSP_034249

Secondary structure

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395

Helix Strand Turn

Details...

Helix

44 – 56

13

Helix

59 – 62

4

Turn

66 – 68

3

Beta strand

70 – 74

5

Turn

77 – 79

3

Beta strand

81 – 86

6

Beta strand

94 – 96

3

Beta strand

99 – 105

7

Helix

108 – 110

3

Helix

113 – 128

16

Beta strand

135 – 139

5

Beta strand

142 – 146

5

Helix

155 – 159

5

Helix

161 – 175

15

Helix

187 – 200

14

Helix

212 – 215

4

Helix

218 – 230

13

Beta strand

236 – 239

4

Helix

245 – 247

3

Beta strand

248 – 250

3

Beta strand

260 – 262

3

Helix

265 – 267

3

Beta strand

269 – 272

4

Helix

273 – 282

10

Helix

283 – 285

3

Helix

300 – 302

3

Helix

306 – 320

15

Turn

321 – 323

3

Helix

328 – 363

36

Helix

370 – 388

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 18367468B22FB9CE	FASTA	395	45,271
	10 20 30 40 50 60 MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY QWCREYLGGA 70 80 90 100 110 120 WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE VLLRLYGAIL QGVDSLVLES 130 140 150 160 170 180 VMFAILAERS LGPQLYGVFP EGRLEQYIPS RPLKTQELRE PVLSAAIATK MAQFHGMEMP 190 200 210 220 230 240 FTKEPHWLFG TMERYLKQIQ DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH 250 260 270 280 290 300 NDIQEGNILL LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP 310 320 330 340 350 360 TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH FFWGLWSILQ 370 380 390 ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS
	Isoform 2 [UniParc]. Checksum: 1C3DBAB66A5D1637	FASTA	127	13,506
	10 20 30 40 50 60 MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY QWCREYLGGA 70 80 90 100 110 120 WRRVQPEELR VYPVRWEVRG QPLRCADRGQ GSAAGPSGCS MFSPPSCARA WGGAGPAWPG GGRGRGR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel expression of equivocal messages containing both regions of choline/ethanolamine kinase and muscle type carnitine palmitoyltransferase I." Yamazaki N., Shinohara Y., Kajimoto K., Shindo M., Terada H. J. Biol. Chem. 275:31739-31746(2000) [PubMed: 10918069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]	Smink L.J., Huckle E.J. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[6]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-19, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-42, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment." Gallego-Ortega D., Ramirez de Molina A., Ramos M.A., Valdes-Mora F., Barderas M.G., Sarmentero-Estrada J., Lacal J.C. PLoS ONE 4:E7819-E7819(2009) [PubMed: 19915674] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[9]	"Crystal structure of human choline kinase beta in complex with phosphorylated hemicholinium-3 and adenosine nucleotide." Structural genomics consortium (SGC) Submitted (SEP-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 14-395 IN COMPLEX WITH ADP; MAGNESIUM IONS AND HEMICHOLINIUM-3.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB029885 Genomic DNA. Translation: BAA82511.1.
AB029886 mRNA. Translation: BAA82512.1.
AL096780 mRNA. Translation: CAB46629.1.
AL096781 mRNA. Translation: CAB46630.1.
CR456419 mRNA. Translation: CAG30305.1.
U62317 Genomic DNA. Translation: AAB03342.2. Sequence problems.
BC082263 mRNA. Translation: AAH82263.1.

IPI

IPI00031758.
IPI00376947.

RefSeq

NP_005189.2. NM_005198.4.

UniGene

Hs.654827.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IG7	X-ray	1.80	A/B	14-395	[»]
3FEG	X-ray	1.30	A	35-395	[»]
3LQ3	X-ray	1.42	A	14-395	[»]

ProteinModelPortal

Q9Y259.

SMR

Q9Y259. Positions 42-388.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y259. 1 interaction.

STRING

Q9Y259.

PTM databases

PhosphoSite

Q9Y259.

Polymorphism databases

DMDM

6685604.

Proteomic databases

PRIDE

Q9Y259.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000406938; ENSP00000384400; ENSG00000100288.

GeneID

1120.

KEGG

hsa:1120.

UCSC

uc003bmq.1. human.
uc003bms.1. human.

Organism-specific databases

CTD

1120.

GeneCards

GC22M051017.

H-InvDB

HIX0138765.

HGNC

HGNC:1938. CHKB.

HPA

HPA018797.

MIM

612395. gene.

neXtProt

NX_Q9Y259.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00530000062991.

HOGENOM

HBG384775.

HOVERGEN

HBG050943.

InParanoid

Q9Y259.

OMA

EMNLLEM.

OrthoDB

EOG49GKH0.

PhylomeDB

Q9Y259.

Enzyme and pathway databases

BRENDA

2.7.1.32. 2681.

Gene expression databases

Bgee

Q9Y259.

CleanEx

HS_CHKB.

Genevestigator

Q9Y259.

GermOnline

ENSG00000205560. Homo sapiens.

Family and domain databases

InterPro

IPR002573. Choline/ethanolamine_kinase.
IPR011009. Kinase-like_dom.
[Graphical view]

KO

K14156.

Pfam

PF01633. Choline_kinase. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00122. Choline.

NextBio

4648.

SOURCE

Search...

Entry information

Entry name

CHKB_HUMAN

Accession

Primary (citable) accession number: Q9Y259
Secondary accession number(s): Q13388

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.