Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Choline/ethanolamine kinase

Gene

CHKB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + choline = ADP + phosphocholine.1 Publication
ATP + ethanolamine = ADP + O-phosphoethanolamine.1 Publication

Kineticsi

  1. KM=0.57 mM for choline1 Publication
  2. KM=2.9 mM for ethanolamine1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041ATP
    Binding sitei244 – 2441ATPBy similarity
    Binding sitei264 – 2641ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi75 – 817ATPBy similarity
    Nucleotide bindingi146 – 1527ATP

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • choline kinase activity Source: UniProtKB
    • ethanolamine kinase activity Source: UniProtKB

    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

    BRENDAi2.7.1.32. 2681.
    ReactomeiREACT_120919. Synthesis of PE.
    REACT_121238. Synthesis of PC.
    SABIO-RKQ9Y259.
    UniPathwayiUPA00558; UER00741.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Choline/ethanolamine kinase
    Alternative name(s):
    Choline kinase beta (EC:2.7.1.32)
    Short name:
    CK
    Short name:
    CKB
    Choline kinase-like protein
    Ethanolamine kinase (EC:2.7.1.82)
    Short name:
    EK
    Ethanolamine kinase beta
    Short name:
    EKB
    choline/ethanolamine kinase beta
    Short name:
    CKEKB
    Gene namesi
    Name:CHKB
    Synonyms:CHETK, CHKL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1938. CHKB.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
    PharmGKBiPA26469.

    Chemistry

    DrugBankiDB00122. Choline.

    Polymorphism and mutation databases

    BioMutaiCHKB.
    DMDMi6685604.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 395394Choline/ethanolamine kinasePRO_0000206222Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y259.
    PaxDbiQ9Y259.
    PRIDEiQ9Y259.

    PTM databases

    PhosphoSiteiQ9Y259.

    Expressioni

    Gene expression databases

    BgeeiQ9Y259.
    CleanExiHS_CHKB.
    ExpressionAtlasiQ9Y259. baseline.
    GenevestigatoriQ9Y259.

    Organism-specific databases

    HPAiHPA018797.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with CHKA.1 Publication

    Protein-protein interaction databases

    BioGridi107544. 1 interaction.
    IntActiQ9Y259. 1 interaction.
    STRINGi9606.ENSP00000384400.

    Structurei

    Secondary structure

    1
    395
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi43 – 5715Combined sources
    Helixi59 – 635Combined sources
    Helixi66 – 683Combined sources
    Beta strandi70 – 745Combined sources
    Turni77 – 793Combined sources
    Beta strandi82 – 865Combined sources
    Beta strandi94 – 963Combined sources
    Beta strandi99 – 1057Combined sources
    Helixi108 – 1103Combined sources
    Helixi113 – 12816Combined sources
    Beta strandi135 – 1395Combined sources
    Beta strandi142 – 1465Combined sources
    Beta strandi149 – 1524Combined sources
    Helixi155 – 1595Combined sources
    Helixi161 – 17515Combined sources
    Helixi187 – 20115Combined sources
    Helixi212 – 2154Combined sources
    Helixi218 – 23013Combined sources
    Beta strandi236 – 2394Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi248 – 2525Combined sources
    Beta strandi260 – 2623Combined sources
    Helixi265 – 2673Combined sources
    Beta strandi269 – 2724Combined sources
    Helixi273 – 28311Combined sources
    Helixi300 – 3023Combined sources
    Helixi306 – 32015Combined sources
    Turni321 – 3233Combined sources
    Helixi328 – 36134Combined sources
    Beta strandi365 – 3684Combined sources
    Helixi370 – 38617Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IG7X-ray1.80A/B14-395[»]
    3FEGX-ray1.30A35-395[»]
    3LQ3X-ray1.42A14-395[»]
    ProteinModelPortaliQ9Y259.
    SMRiQ9Y259. Positions 42-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y259.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni77 – 793Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the choline/ethanolamine kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0510.
    GeneTreeiENSGT00530000062991.
    HOGENOMiHOG000041274.
    HOVERGENiHBG050943.
    InParanoidiQ9Y259.
    KOiK14156.
    OMAiCLAKDGL.
    OrthoDBiEOG72VH68.
    PhylomeDBiQ9Y259.
    TreeFamiTF313549.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

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

    Isoform 1 (identifier: Q9Y259-1) [UniParc]FASTAAdd to basket

    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
    MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY
    60 70 80 90 100
    QWCREYLGGA WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE
    110 120 130 140 150
    VLLRLYGAIL QGVDSLVLES VMFAILAERS LGPQLYGVFP EGRLEQYIPS
    160 170 180 190 200
    RPLKTQELRE PVLSAAIATK MAQFHGMEMP FTKEPHWLFG TMERYLKQIQ
    210 220 230 240 250
    DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH NDIQEGNILL
    260 270 280 290 300
    LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP
    310 320 330 340 350
    TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH
    360 370 380 390
    FFWGLWSILQ ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS
    Length:395
    Mass (Da):45,271
    Last modified:January 23, 2007 - v3
    Checksum:i18367468B22FB9CE
    GO
    Isoform 2 (identifier: Q9Y259-2) [UniParc]FASTAAdd to basket

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

    Show »
    Length:127
    Mass (Da):13,506
    Checksum:i1C3DBAB66A5D1637
    GO

    Sequence cautioni

    The sequence AAB03342.2 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei75 – 12753SGGLS…FAILA → RWEVRGQPLRCADRGQGSAA GPSGCSMFSPPSCARAWGGA GPAWPGGGRGRGR in isoform 2. CuratedVSP_034248Add
    BLAST
    Alternative sequencei128 – 395268Missing in isoform 2. CuratedVSP_034249Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    AK314324 mRNA. Translation: BAG36972.1.
    U62317 Genomic DNA. Translation: AAB03342.2. Sequence problems.
    CH471138 Genomic DNA. Translation: EAW73573.1.
    BC082263 mRNA. Translation: AAH82263.1.
    BC101488 mRNA. Translation: AAI01489.1.
    BC113521 mRNA. Translation: AAI13522.2.
    CCDSiCCDS14099.1. [Q9Y259-1]
    RefSeqiNP_005189.2. NM_005198.4. [Q9Y259-1]
    UniGeneiHs.654827.

    Genome annotation databases

    EnsembliENST00000406938; ENSP00000384400; ENSG00000100288. [Q9Y259-1]
    GeneIDi1120.
    KEGGihsa:1120.
    UCSCiuc003bmu.3. human. [Q9Y259-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    AK314324 mRNA. Translation: BAG36972.1.
    U62317 Genomic DNA. Translation: AAB03342.2. Sequence problems.
    CH471138 Genomic DNA. Translation: EAW73573.1.
    BC082263 mRNA. Translation: AAH82263.1.
    BC101488 mRNA. Translation: AAI01489.1.
    BC113521 mRNA. Translation: AAI13522.2.
    CCDSiCCDS14099.1. [Q9Y259-1]
    RefSeqiNP_005189.2. NM_005198.4. [Q9Y259-1]
    UniGeneiHs.654827.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IG7X-ray1.80A/B14-395[»]
    3FEGX-ray1.30A35-395[»]
    3LQ3X-ray1.42A14-395[»]
    ProteinModelPortaliQ9Y259.
    SMRiQ9Y259. Positions 42-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107544. 1 interaction.
    IntActiQ9Y259. 1 interaction.
    STRINGi9606.ENSP00000384400.

    Chemistry

    BindingDBiQ9Y259.
    ChEMBLiCHEMBL3112385.
    DrugBankiDB00122. Choline.

    PTM databases

    PhosphoSiteiQ9Y259.

    Polymorphism and mutation databases

    BioMutaiCHKB.
    DMDMi6685604.

    Proteomic databases

    MaxQBiQ9Y259.
    PaxDbiQ9Y259.
    PRIDEiQ9Y259.

    Protocols and materials databases

    DNASUi1120.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000406938; ENSP00000384400; ENSG00000100288. [Q9Y259-1]
    GeneIDi1120.
    KEGGihsa:1120.
    UCSCiuc003bmu.3. human. [Q9Y259-1]

    Organism-specific databases

    CTDi1120.
    GeneCardsiGC22M051017.
    GeneReviewsiCHKB.
    HGNCiHGNC:1938. CHKB.
    HPAiHPA018797.
    MIMi612395. gene.
    neXtProtiNX_Q9Y259.
    Orphaneti280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
    PharmGKBiPA26469.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0510.
    GeneTreeiENSGT00530000062991.
    HOGENOMiHOG000041274.
    HOVERGENiHBG050943.
    InParanoidiQ9Y259.
    KOiK14156.
    OMAiCLAKDGL.
    OrthoDBiEOG72VH68.
    PhylomeDBiQ9Y259.
    TreeFamiTF313549.

    Enzyme and pathway databases

    UniPathwayiUPA00558; UER00741.
    BRENDAi2.7.1.32. 2681.
    ReactomeiREACT_120919. Synthesis of PE.
    REACT_121238. Synthesis of PC.
    SABIO-RKQ9Y259.

    Miscellaneous databases

    EvolutionaryTraceiQ9Y259.
    GeneWikiiCHKB_(gene).
    GenomeRNAii1120.
    NextBioi4648.
    PROiQ9Y259.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y259.
    CleanExiHS_CHKB.
    ExpressionAtlasiQ9Y259. baseline.
    GenevestigatoriQ9Y259.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    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] [Europe PMC] [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain and Lung.
    8. 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, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "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.

    Entry informationi

    Entry nameiCHKB_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y259
    Secondary accession number(s): A0PJM6, Q13388
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2007
    Last modified: May 27, 2015
    This is version 126 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Miscellaneous

    This protein is produced by a bicistronic gene which also produces the CPT1B protein from a non-overlapping reading frame.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. 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.