O55229 (CHKB_MOUSE) 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
Ethanolamine kinase
Short name=EK
EC=2.7.1.82
choline/ethanolamine kinase beta
Short name=CKEKB

Gene names

Name:	Chkb
Synonyms:	Chetk, Chkl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	394 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 By similarity.
Catalytic activity	ATP + choline = ADP + phosphocholine. ATP + ethanolamine = ADP + O-phosphoethanolamine.
Pathway	Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
Subunit structure	Homodimer, and heterodimer with CHKA. Ref.2
Tissue specificity	Expressed ubiquitously with the highest level in testis.
Involvement in disease	Defects in Chkb are a cause of rostrocaudal muscular dystrophy (rmd). The disease is characterized by rapidly progressive muscular dystrophy and neonatal forelimb bone deformity. The dystrophy is only evident in skeletal muscle tissues in an unusual rostral-to-caudal gradient. Ref.3
Disruption phenotype	Hindlimb muscular dystrophy. Hindlimb skeletal muscle tissue exhibits impaired phosphatidylcholine biosynthesis and increased phosphatidylcholine catabolism, with concomitant accumulation of choline. Mitochondria are abnormally large and exhibit decreased inner membrane potential. Ref.4
Sequence similarities	Belongs to the choline/ethanolamine kinase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	muscle organ development Inferred from mutant phenotype Ref.3. Source: MGI phosphatidylethanolamine biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW choline kinase activity Inferred from sequence or structural similarity. Source: UniProtKB ethanolamine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 394	393	Choline/ethanolamine kinase		PRO_0000206223
Regions
	Nucleotide binding	75 – 81	7	ATP By similarity
	Nucleotide binding	146 – 152	7	ATP By similarity
	Region	77 – 79	3	Substrate binding By similarity
Sites
	Binding site	104	1	ATP By similarity
	Binding site	244	1	ATP By similarity
	Binding site	264	1	ATP By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity

Sequences

	Sequence		Length	Mass (Da)
	O55229 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A5EE79EC551D07A2	FASTA	394	45,126
	10 20 30 40 50 60 MAADGTGVVG GGAVGGGLPK DGLQDAKCPE PIPNRRRASS LSRDAQRRAY QWCREYLGGA 70 80 90 100 110 120 WRRARPEELS VCPVSGGLSN LLFRCSLPNH VPSVGGEPRE VLLRLYGAIL QGVDSLVLES 130 140 150 160 170 180 VMFAILAERS LGPQLYGVFP EGRLEQYLPS RPLKTQELRD PVLSGAIATR MARFHGMEMP 190 200 210 220 230 240 FTKEPRWLFG TMERYLKQIQ DLPSTSLPQM NLVEMYSLKD EMNSLRKLLD DTPSPVVFCH 250 260 270 280 290 300 NDIQEGNILL LSEPDSDDNL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTY EEWPFYKARP 310 320 330 340 350 360 TDYPTREQQL HFIRHYLAEV QKGEILSEEE QKKREEELLL EISRYSLASH FFWGLWSTLQ 370 380 390 ASMSTIEFGY LEYAQSRFQF YFQQKGQLTS SPSS

References

[1]	"Molecular cloning of mouse choline kinase and choline/ethanolamine kinase: their sequence comparison to the respective rat homologs." Aoyama C., Nakashima K., Ishidate K. Biochim. Biophys. Acta 1393:179-185(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss Webster / NIH.
[2]	"Deletion and alanine mutation analyses for the formation of active homo-or hetero-dimer complexes of mouse choline kinase-alpha and -beta." Liao H., Aoyama C., Ishidate K., Teraoka H. Biochim. Biophys. Acta 1761:111-120(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[3]	"A rostrocaudal muscular dystrophy caused by a defect in choline kinase beta, the first enzyme in phosphatidylcholine biosynthesis." Sher R.B., Aoyama C., Huebsch K.A., Ji S., Kerner J., Yang Y., Frankel W.N., Hoppel C.L., Wood P.A., Vance D.E., Cox G.A. J. Biol. Chem. 281:4938-4948(2006) [PubMed] [Europe PMC] [Abstract] Cited for: DISEASE.
[4]	"Understanding the muscular dystrophy caused by deletion of choline kinase beta in mice." Wu G., Sher R.B., Cox G.A., Vance D.E. Biochim. Biophys. Acta 1791:347-356(2009) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011001 Transcribed RNA. Translation: BAA24897.1. AB011000 mRNA. Translation: BAA24896.1.
IPI	IPI00116681.
RefSeq	NP_031718.1. NM_007692.6.
UniGene	Mm.485045.
3D structure databases
ProteinModelPortal	O55229.
SMR	O55229. Positions 42-390.
ModBase	Search...
PTM databases
PhosphoSite	O55229.
Proteomic databases
PaxDb	O55229.
PRIDE	O55229.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023289; ENSMUSP00000023289; ENSMUSG00000022617.
GeneID	12651.
KEGG	mmu:12651.
Organism-specific databases
CTD	1120.
MGI	MGI:1328313. Chkb.
Phylogenomic databases
eggNOG	COG0510.
HOGENOM	HOG000041274.
HOVERGEN	HBG050943.
InParanoid	O55229.
KO	K14156.
OMA	FTKEPRW.
OrthoDB	EOG49GKH0.
Enzyme and pathway databases
UniPathway	UPA00558; UER00741.
Gene expression databases
ArrayExpress	O55229.
Bgee	O55229.
CleanEx	MM_CHKB.
Genevestigator	O55229.
GermOnline	ENSMUSG00000022618. Mus musculus.
Family and domain databases
InterPro	IPR026712. Cho/Etha_kinase. IPR011009. Kinase-like_dom. [Graphical view]
PANTHER	PTHR22603. PTHR22603. 1 hit.
SUPFAM	SSF56112. Kinase_like. 1 hit.
ProtoNet	Search...
Other
NextBio	281860.
SOURCE	Search...

Entry information

Entry name

CHKB_MOUSE

Accession

Primary (citable) accession number: O55229

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
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