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Protein

Choline kinase alpha

Gene

Chka

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + choline = ADP + phosphocholine.
ATP + ethanolamine = ADP + O-phosphoethanolamine.

Pathway:iphosphatidylcholine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphocholine from choline.
Proteins known to be involved in this subpathway in this organism are:
  1. Choline kinase alpha (Chka)
This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphocholine from choline, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.

Pathway:iphosphatidylethanolamine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes phosphatidylethanolamine from ethanolamine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Choline/ethanolamine kinase (Chkb), Ethanolamine kinase 2 (Etnk2), Ethanolamine kinase 1 (Etnk1), Choline kinase alpha (Chka)
  2. Ethanolamine-phosphate cytidylyltransferase (Pcyt2)
  3. Choline/ethanolaminephosphotransferase 1 (Cept1), Ethanolaminephosphotransferase 1 (Ept1)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from ethanolamine, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421ATPBy similarity
Binding sitei304 – 3041ATPBy similarity
Binding sitei326 – 3261ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi113 – 1197ATPBy similarity
Nucleotide bindingi203 – 2097ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • choline binding Source: Ensembl
  • choline kinase activity Source: UniProtKB
  • cholinesterase activity Source: MGI
  • drug binding Source: UniProtKB
  • ethanolamine kinase activity Source: UniProtKB
  • protein homodimerization activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_271919. Synthesis of PC.
REACT_354254. Synthesis of PE.
UniPathwayiUPA00558; UER00741.
UPA00753; UER00737.

Names & Taxonomyi

Protein namesi
Recommended name:
Choline kinase alpha (EC:2.7.1.32)
Short name:
CK
Alternative name(s):
CHETK-alpha
Ethanolamine kinase (EC:2.7.1.82)
Short name:
EK
Gene namesi
Name:Chka
Synonyms:Chk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:107760. Chka.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Death at an early embryonic stage. Embryos die after 3 to 5 days of development.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 453453Choline kinase alphaPRO_0000206220Add
BLAST

Proteomic databases

MaxQBiO54804.
PaxDbiO54804.
PRIDEiO54804.

PTM databases

PhosphoSiteiO54804.

Expressioni

Tissue specificityi

Expressed ubiquitously with the highest level in testis.

Gene expression databases

CleanExiMM_CHKA.
ExpressionAtlasiO54804. baseline and differential.
GenevisibleiO54804. MM.

Interactioni

Subunit structurei

Homodimer, and heterodimer with CHKB.1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071933.

Structurei

3D structure databases

ProteinModelPortaliO54804.
SMRiO54804. Positions 77-453.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 1173Substrate bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi53 – 8129Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the choline/ethanolamine kinase family.Curated

Phylogenomic databases

eggNOGiCOG0510.
GeneTreeiENSGT00530000062991.
HOGENOMiHOG000041274.
HOVERGENiHBG050943.
InParanoidiO54804.
KOiK14156.
OMAiRAYLWCK.
TreeFamiTF313549.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O54804-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR
60 70 80 90 100
TQPLALPPPP PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR
110 120 130 140 150
GLREDQFHIS VIRGGLSNML FQCSLPDSIA SVGDEPRKVL LRLYGAILKM
160 170 180 190 200
RSCNKEGSEQ AQNENEFQGA EAMVLESVMF AILAERSLGP KLFGIFPQGR
210 220 230 240 250
LEQFIPSRRL DTEELRLPDI SAEIAEKMAT FHGMKMPFNK EPKWLFGTME
260 270 280 290 300
KYLNQVLRLK FSREARVQQL HKILSYNLPL ELENLRSLLQ YTRSPVVFCH
310 320 330 340 350
NDCQEGNILL LEGQENSERR KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY
360 370 380 390 400
TYEKYPFFRA NIQKYPSRKQ QLHFISSYLT TFQNDFESLS SEEQFATKED
410 420 430 440 450
MLLEVNRFAL ASHFLWGLWS IVQAKISSIE FGYMEYAQAR FEAYFDQKRK

LGV
Length:453
Mass (Da):51,985
Last modified:October 3, 2012 - v3
Checksum:i66042FEE92C333D4
GO
Isoform 2 (identifier: O54804-2) [UniParc]FASTAAdd to basket

Also known as: CHETK-alpha1

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

Show »
Length:435
Mass (Da):49,904
Checksum:iDC7377434296F68A
GO

Sequence cautioni

The sequence AAH56758.1 differs from that shown.Intron retention.Curated
The sequence BAA88154.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence BAB29191.1 differs from that shown.Intron retention.Curated
The sequence BAC34841.1 differs from that shown.Intron retention.Curated
The sequence BAC35539.1 differs from that shown.Intron retention.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti193 – 1931F → Y in BAA24898 (PubMed:9714798).Curated
Sequence conflicti193 – 1931F → Y in BAA88154 (PubMed:10706593).Curated
Sequence conflicti193 – 1931F → Y in BAA88153 (PubMed:10706593).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei151 – 16818Missing in isoform 2. 2 PublicationsVSP_009684Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29400.1. [O54804-2]
CCDS70913.1. [O54804-1]
RefSeqiNP_001258425.1. NM_001271496.1. [O54804-1]
NP_038518.2. NM_013490.4. [O54804-2]
UniGeneiMm.225505.

Genome annotation databases

EnsembliENSMUST00000025760; ENSMUSP00000025760; ENSMUSG00000024843. [O54804-1]
ENSMUST00000072055; ENSMUSP00000071933; ENSMUSG00000024843. [O54804-2]
GeneIDi12660.
KEGGimmu:12660.
UCSCiuc008fxg.2. mouse. [O54804-2]
uc008fxh.2. mouse. [O54804-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS29400.1. [O54804-2]
CCDS70913.1. [O54804-1]
RefSeqiNP_001258425.1. NM_001271496.1. [O54804-1]
NP_038518.2. NM_013490.4. [O54804-2]
UniGeneiMm.225505.

3D structure databases

ProteinModelPortaliO54804.
SMRiO54804. Positions 77-453.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071933.

PTM databases

PhosphoSiteiO54804.

Proteomic databases

MaxQBiO54804.
PaxDbiO54804.
PRIDEiO54804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025760; ENSMUSP00000025760; ENSMUSG00000024843. [O54804-1]
ENSMUST00000072055; ENSMUSP00000071933; ENSMUSG00000024843. [O54804-2]
GeneIDi12660.
KEGGimmu:12660.
UCSCiuc008fxg.2. mouse. [O54804-2]
uc008fxh.2. mouse. [O54804-1]

Organism-specific databases

CTDi1119.
MGIiMGI:107760. Chka.

Phylogenomic databases

eggNOGiCOG0510.
GeneTreeiENSGT00530000062991.
HOGENOMiHOG000041274.
HOVERGENiHBG050943.
InParanoidiO54804.
KOiK14156.
OMAiRAYLWCK.
TreeFamiTF313549.

Enzyme and pathway databases

UniPathwayiUPA00558; UER00741.
UPA00753; UER00737.
ReactomeiREACT_271919. Synthesis of PC.
REACT_354254. Synthesis of PE.

Miscellaneous databases

ChiTaRSiChka. mouse.
NextBioi281884.
PROiO54804.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CHKA.
ExpressionAtlasiO54804. baseline and differential.
GenevisibleiO54804. MM.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCHKA_MOUSE
AccessioniPrimary (citable) accession number: O54804
Secondary accession number(s): G5E853
, Q8BPL3, Q8BPW6, Q9CXP3, Q9QX56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: October 3, 2012
Last modified: July 22, 2015
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.