O54804 (CHKA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Choline kinase alpha
Short name=CK
EC=2.7.1.32

Alternative name(s):
CHETK-alpha
Ethanolamine kinase
Short name=EK
EC=2.7.1.82

Gene names

Name:	Chka
Synonyms:	Chk

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	453 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline By similarity.
Catalytic activity	ATP + choline = ADP + phosphocholine. ATP + ethanolamine = ADP + O-phosphoethanolamine.
Pathway	Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1. Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.
Subunit structure	Homodimer, and heterodimer with CHKB. Ref.7
Subcellular location	Cytoplasm.
Tissue specificity	Expressed ubiquitously with the highest level in testis.
Disruption phenotype	Death at an early embryonic stage. Embryos die after 3 to 5 days of development. Ref.8
Sequence similarities	Belongs to the choline/ethanolamine kinase family.
Sequence caution	The sequence AAH56758.1 differs from that shown. Reason: Intron retention. The sequence BAA88154.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence BAB29191.1 differs from that shown. Reason: Intron retention. The sequence BAC34841.1 differs from that shown. Reason: Intron retention. The sequence BAC35539.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	choline metabolic process Inferred from electronic annotation. Source: Compara phosphatidylethanolamine biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW choline binding Inferred from electronic annotation. Source: Compara choline kinase activity Inferred from sequence or structural similarity. Source: UniProtKB cholinesterase activity Inferred from direct assay PubMed 16371353. Source: MGI drug binding Inferred from sequence or structural similarity. Source: UniProtKB ethanolamine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: O54804-1)

Also known as: CHETK-alpha2;

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: O54804-2)

Also known as: CHETK-alpha1;

The sequence of this isoform differs from the canonical sequence as follows:
     151-168: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 453	453	Choline kinase alpha		PRO_0000206220
Regions
	Nucleotide binding	113 – 119	7	ATP By similarity
	Nucleotide binding	203 – 209	7	ATP By similarity
	Region	115 – 117	3	Substrate binding By similarity
	Compositional bias	53 – 81	29	Pro-rich
Sites
	Binding site	142	1	ATP By similarity
	Binding site	304	1	ATP By similarity
	Binding site	326	1	ATP By similarity
Natural variations
	Alternative sequence	151 – 168	18	Missing in isoform 2.		VSP_009684
Experimental info
	Sequence conflict	193	1	F → Y in BAA24898. Ref.1
	Sequence conflict	193	1	F → Y in BAA88154. Ref.2
	Sequence conflict	193	1	F → Y in BAA88153. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CHETK-alpha2) [UniParc]. Last modified October 3, 2012. Version 3. Checksum: 66042FEE92C333D4	FASTA	453	51,985
	10 20 30 40 50 60 MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR TQPLALPPPP 70 80 90 100 110 120 PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR GLREDQFHIS VIRGGLSNML 130 140 150 160 170 180 FQCSLPDSIA SVGDEPRKVL LRLYGAILKM RSCNKEGSEQ AQNENEFQGA EAMVLESVMF 190 200 210 220 230 240 AILAERSLGP KLFGIFPQGR LEQFIPSRRL DTEELRLPDI SAEIAEKMAT FHGMKMPFNK 250 260 270 280 290 300 EPKWLFGTME KYLNQVLRLK FSREARVQQL HKILSYNLPL ELENLRSLLQ YTRSPVVFCH 310 320 330 340 350 360 NDCQEGNILL LEGQENSERR KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY TYEKYPFFRA 370 380 390 400 410 420 NIQKYPSRKQ QLHFISSYLT TFQNDFESLS SEEQFATKED MLLEVNRFAL ASHFLWGLWS 430 440 450 IVQAKISSIE FGYMEYAQAR FEAYFDQKRK LGV
	Isoform 2 (CHETK-alpha1) [UniParc]. Checksum: DC7377434296F68A	FASTA	435	49,904
	10 20 30 40 50 60 MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR TQPLALPPPP 70 80 90 100 110 120 PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR GLREDQFHIS VIRGGLSNML 130 140 150 160 170 180 FQCSLPDSIA SVGDEPRKVL LRLYGAILKM GAEAMVLESV MFAILAERSL GPKLFGIFPQ 190 200 210 220 230 240 GRLEQFIPSR RLDTEELRLP DISAEIAEKM ATFHGMKMPF NKEPKWLFGT MEKYLNQVLR 250 260 270 280 290 300 LKFSREARVQ QLHKILSYNL PLELENLRSL LQYTRSPVVF CHNDCQEGNI LLLEGQENSE 310 320 330 340 350 360 RRKLMLIDFE YSSYNYRGFD IGNHFCEWMY DYTYEKYPFF RANIQKYPSR KQQLHFISSY 370 380 390 400 410 420 LTTFQNDFES LSSEEQFATK EDMLLEVNRF ALASHFLWGL WSIVQAKISS IEFGYMEYAQ 430 ARFEAYFDQK RKLGV

References

	« Hide 'large scale' referencesShow 'large scale' 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] (ISOFORM 2). Strain: Swiss Webster / NIH.
[2]	"Structure and characterization of the genes for murine choline/ethanolamine kinase isozymes alpha and beta." Aoyama C., Yamazaki N., Terada H., Ishidate K. J. Lipid Res. 41:452-464(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2). Strain: 129/Sv. Tissue: Liver.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-371 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-150 (ISOFORM 1). Strain: C57BL/6. Tissue: Brain and Limb.
[6]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168 (ISOFORM 1). Strain: C57BL/6J. Tissue: Embryonic eye, Embryonic head and Eye.
[7]	"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.
[8]	"Early embryonic lethality caused by disruption of the gene for choline kinase alpha, the first enzyme in phosphatidylcholine biosynthesis." Wu G., Aoyama C., Young S.G., Vance D.E. J. Biol. Chem. 283:1456-1462(2008) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011002 mRNA. Translation: BAA24898.1. AB030621 Genomic DNA. Translation: BAA88153.1. AB030621 Genomic DNA. Translation: BAA88154.1. Sequence problems. AC133523 Genomic DNA. No translation available. CH466612 Genomic DNA. Translation: EDL32956.1. BC056758 mRNA. Translation: AAH56758.1. Sequence problems. BC060218 mRNA. No translation available. AK014174 mRNA. Translation: BAB29191.1. Sequence problems. AK052056 mRNA. Translation: BAC34841.1. Sequence problems. AK053818 mRNA. Translation: BAC35539.1. Sequence problems.
IPI	IPI00118685. IPI00409960.
RefSeq	NP_001258425.1. NM_001271496.1. NP_038518.2. NM_013490.4.
UniGene	Mm.225505.
3D structure databases
ProteinModelPortal	O54804.
SMR	O54804. Positions 77-453.
ModBase	Search...
PTM databases
PhosphoSite	O54804.
Proteomic databases
PaxDb	O54804.
PRIDE	O54804.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025760; ENSMUSP00000025760; ENSMUSG00000024843. ENSMUST00000072055; ENSMUSP00000071933; ENSMUSG00000024843.
GeneID	12660.
KEGG	mmu:12660.
UCSC	uc008fxg.1. mouse.
Organism-specific databases
CTD	1119.
MGI	MGI:107760. Chka.
Phylogenomic databases
eggNOG	COG0510.
GeneTree	ENSGT00530000062991.
HOGENOM	HOG000041274.
HOVERGEN	HBG050943.
InParanoid	O54804.
KO	K14156.
OMA	TRRRAYL.
OrthoDB	EOG49GKH0.
Enzyme and pathway databases
BRENDA	2.7.1.82. 3474.
UniPathway	UPA00558; UER00741. UPA00753; UER00737.
Gene expression databases
CleanEx	MM_CHKA.
Genevestigator	O54804.
GermOnline	ENSMUSG00000024843. 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
ChiTaRS	CHKA. mouse.
NextBio	281884.
SOURCE	Search...

Entry information

Entry name

CHKA_MOUSE

Accession

Primary (citable) accession number: O54804
Secondary accession number(s): G5E853 , Q8BPL3, Q8BPW6, Q9CXP3, Q9QX56

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	October 3, 2012
Last modified:	May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program