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Q9Y259

- CHKB_HUMAN

UniProt

Q9Y259 - CHKB_HUMAN

Protein

Choline/ethanolamine kinase

Gene

CHKB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW
    2. choline kinase activity Source: UniProtKB
    3. ethanolamine kinase activity Source: UniProtKB

    GO - Biological processi

    1. CDP-choline pathway Source: GOC
    2. glycerophospholipid biosynthetic process Source: Reactome
    3. phosphatidylcholine biosynthetic process Source: Reactome
    4. phosphatidylethanolamine biosynthetic process Source: UniProtKB
    5. phospholipid metabolic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:1938. CHKB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Pathology & Biotechi

    Organism-specific databases

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

    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.
    GenevestigatoriQ9Y259.

    Organism-specific databases

    HPAiHPA018797.

    Interactioni

    Subunit structurei

    Homodimer, and heterodimer with CHKA.1 Publication

    Protein-protein interaction databases

    BioGridi107544. 2 interactions.
    IntActiQ9Y259. 1 interaction.
    STRINGi9606.ENSP00000384400.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000041274.
    HOVERGENiHBG050943.
    InParanoidiQ9Y259.
    KOiK14156.
    OMAiYKAQPAN.
    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. Align

    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

    MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY    50
    QWCREYLGGA WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE 100
    VLLRLYGAIL QGVDSLVLES VMFAILAERS LGPQLYGVFP EGRLEQYIPS 150
    RPLKTQELRE PVLSAAIATK MAQFHGMEMP FTKEPHWLFG TMERYLKQIQ 200
    DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH NDIQEGNILL 250
    LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP 300
    TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH 350
    FFWGLWSILQ ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS 395
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi6685604.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14099.1. [Q9Y259-1 ]
    RefSeqi NP_005189.2. NM_005198.4. [Q9Y259-1 ]
    UniGenei Hs.654827.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IG7 X-ray 1.80 A/B 14-395 [» ]
    3FEG X-ray 1.30 A 35-395 [» ]
    3LQ3 X-ray 1.42 A 14-395 [» ]
    ProteinModelPortali Q9Y259.
    SMRi Q9Y259. Positions 42-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107544. 2 interactions.
    IntActi Q9Y259. 1 interaction.
    STRINGi 9606.ENSP00000384400.

    Chemistry

    DrugBanki DB00122. Choline.

    PTM databases

    PhosphoSitei Q9Y259.

    Polymorphism databases

    DMDMi 6685604.

    Proteomic databases

    MaxQBi Q9Y259.
    PaxDbi Q9Y259.
    PRIDEi Q9Y259.

    Protocols and materials databases

    DNASUi 1120.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000406938 ; ENSP00000384400 ; ENSG00000100288 . [Q9Y259-1 ]
    GeneIDi 1120.
    KEGGi hsa:1120.
    UCSCi uc003bmu.3. human. [Q9Y259-1 ]

    Organism-specific databases

    CTDi 1120.
    GeneCardsi GC22M051017.
    GeneReviewsi CHKB.
    HGNCi HGNC:1938. CHKB.
    HPAi HPA018797.
    MIMi 612395. gene.
    neXtProti NX_Q9Y259.
    Orphaneti 280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
    PharmGKBi PA26469.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0510.
    HOGENOMi HOG000041274.
    HOVERGENi HBG050943.
    InParanoidi Q9Y259.
    KOi K14156.
    OMAi YKAQPAN.
    OrthoDBi EOG72VH68.
    PhylomeDBi Q9Y259.
    TreeFami TF313549.

    Enzyme and pathway databases

    UniPathwayi UPA00558 ; UER00741 .
    BRENDAi 2.7.1.32. 2681.
    Reactomei REACT_120919. Synthesis of PE.
    REACT_121238. Synthesis of PC.
    SABIO-RK Q9Y259.

    Miscellaneous databases

    EvolutionaryTracei Q9Y259.
    GeneWikii CHKB_(gene).
    GenomeRNAii 1120.
    NextBioi 4648.
    PROi Q9Y259.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y259.
    CleanExi HS_CHKB.
    Genevestigatori Q9Y259.

    Family and domain databases

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

    Publicationsi

    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].
    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: October 1, 2014
    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
    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