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O54804

- CHKA_MOUSE

UniProt

O54804 - CHKA_MOUSE

Protein

Choline kinase alpha

Gene

Chka

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (03 Oct 2012)
      Previous versions | rss
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    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.

    Pathwayi

    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

    1. ATP binding Source: UniProtKB-KW
    2. choline binding Source: Ensembl
    3. choline kinase activity Source: UniProtKB
    4. cholinesterase activity Source: MGI
    5. drug binding Source: UniProtKB
    6. ethanolamine kinase activity Source: UniProtKB
    7. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. CDP-choline pathway Source: GOC
    2. choline metabolic process Source: Ensembl
    3. phosphatidylcholine biosynthetic process Source: UniProtKB
    4. phosphatidylethanolamine biosynthetic process Source: UniProtKB

    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

    BRENDAi2.7.1.82. 3474.
    ReactomeiREACT_199009. Synthesis of PE.
    REACT_207335. Synthesis of PC.
    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: Chromosome 19

    Organism-specific databases

    MGIiMGI:107760. Chka.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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

    PaxDbiO54804.
    PRIDEiO54804.

    PTM databases

    PhosphoSiteiO54804.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously with the highest level in testis.

    Gene expression databases

    ArrayExpressiO54804.
    CleanExiMM_CHKA.
    GenevestigatoriO54804.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with CHKB.1 Publication

    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. Align

    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

    MKTKFCTGGE AEPSPLGLLL SCGGNAAPTP GVGQQRDAAG ELESKQLGGR    50
    TQPLALPPPP PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR 100
    GLREDQFHIS VIRGGLSNML FQCSLPDSIA SVGDEPRKVL LRLYGAILKM 150
    RSCNKEGSEQ AQNENEFQGA EAMVLESVMF AILAERSLGP KLFGIFPQGR 200
    LEQFIPSRRL DTEELRLPDI SAEIAEKMAT FHGMKMPFNK EPKWLFGTME 250
    KYLNQVLRLK FSREARVQQL HKILSYNLPL ELENLRSLLQ YTRSPVVFCH 300
    NDCQEGNILL LEGQENSERR KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY 350
    TYEKYPFFRA NIQKYPSRKQ QLHFISSYLT TFQNDFESLS SEEQFATKED 400
    MLLEVNRFAL ASHFLWGLWS IVQAKISSIE FGYMEYAQAR FEAYFDQKRK 450
    LGV 453
    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. Reason: Intron retention.
    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.
    The sequence BAA88154.1 differs from that shown. Reason: Erroneous gene model prediction.

    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:
    EMBL
    GenBank
    DDBJ
    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.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS29400.1. [O54804-2 ]
    CCDS70913.1. [O54804-1 ]
    RefSeqi NP_001258425.1. NM_001271496.1. [O54804-1 ]
    NP_038518.2. NM_013490.4. [O54804-2 ]
    UniGenei Mm.225505.

    3D structure databases

    ProteinModelPortali O54804.
    SMRi O54804. Positions 77-453.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei O54804.

    Proteomic databases

    PaxDbi O54804.
    PRIDEi O54804.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000025760 ; ENSMUSP00000025760 ; ENSMUSG00000024843 . [O54804-1 ]
    ENSMUST00000072055 ; ENSMUSP00000071933 ; ENSMUSG00000024843 . [O54804-2 ]
    GeneIDi 12660.
    KEGGi mmu:12660.

    Organism-specific databases

    CTDi 1119.
    MGIi MGI:107760. Chka.

    Phylogenomic databases

    eggNOGi COG0510.
    GeneTreei ENSGT00530000062991.
    HOGENOMi HOG000041274.
    HOVERGENi HBG050943.
    InParanoidi O54804.
    KOi K14156.
    OMAi RAYLWCK.
    TreeFami TF313549.

    Enzyme and pathway databases

    UniPathwayi UPA00558 ; UER00741 .
    UPA00753 ; UER00737 .
    BRENDAi 2.7.1.82. 3474.
    Reactomei REACT_199009. Synthesis of PE.
    REACT_207335. Synthesis of PC.

    Miscellaneous databases

    ChiTaRSi CHKA. mouse.
    NextBioi 281884.
    PROi O54804.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O54804.
    CleanExi MM_CHKA.
    Genevestigatori O54804.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 113 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