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P35790

- CHKA_HUMAN

UniProt

P35790 - CHKA_HUMAN

Protein

Choline kinase alpha

Gene

CHKA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (14 Apr 2009)
      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.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=0.2 mM for choline2 Publications
    2. KM=0.4 mM for ATP2 Publications
    3. KM=12 mM for ethanolamine2 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei146 – 1461ATP
    Binding sitei308 – 3081ATPCurated
    Binding sitei330 – 3301ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi117 – 1237ATP
    Nucleotide bindingi207 – 2137ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. choline binding Source: Ensembl
    3. choline kinase activity Source: UniProtKB
    4. cholinesterase activity Source: Ensembl
    5. drug binding Source: UniProtKB
    6. ethanolamine kinase activity Source: UniProtKB
    7. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. CDP-choline pathway Source: GOC
    2. choline metabolic process Source: Ensembl
    3. glycerophospholipid biosynthetic process Source: Reactome
    4. lipid metabolic process Source: ProtInc
    5. lipid transport Source: ProtInc
    6. phosphatidylcholine biosynthetic process Source: UniProtKB
    7. phosphatidylethanolamine biosynthetic process Source: UniProtKB
    8. phospholipid metabolic process Source: Reactome
    9. signal transduction Source: GOC
    10. 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

    ReactomeiREACT_120919. Synthesis of PE.
    REACT_121238. Synthesis of PC.
    SABIO-RKP35790.
    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, CKI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1937. CHKA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26468.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457Choline kinase alphaPRO_0000206219Add
    BLAST

    Proteomic databases

    MaxQBiP35790.
    PaxDbiP35790.
    PRIDEiP35790.

    PTM databases

    PhosphoSiteiP35790.

    Expressioni

    Gene expression databases

    ArrayExpressiP35790.
    BgeeiP35790.
    CleanExiHS_CHKA.
    GenevestigatoriP35790.

    Organism-specific databases

    HPAiHPA024153.

    Interactioni

    Subunit structurei

    Heterodimer with CHKB By similarity. Homodimer.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi107543. 6 interactions.
    IntActiP35790. 1 interaction.
    STRINGi9606.ENSP00000265689.

    Structurei

    Secondary structure

    1
    457
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 9814
    Helixi101 – 1033
    Helixi108 – 1103
    Beta strandi112 – 1176
    Beta strandi119 – 12810
    Beta strandi136 – 1383
    Beta strandi141 – 1499
    Helixi175 – 18915
    Beta strandi196 – 2005
    Beta strandi203 – 2075
    Beta strandi211 – 2133
    Helixi216 – 2205
    Helixi222 – 23615
    Helixi248 – 26215
    Helixi268 – 27811
    Helixi282 – 29413
    Beta strandi300 – 3034
    Helixi309 – 3113
    Beta strandi312 – 3154
    Helixi318 – 3203
    Beta strandi322 – 3243
    Beta strandi326 – 3283
    Beta strandi335 – 3384
    Helixi339 – 34911
    Beta strandi352 – 3543
    Helixi366 – 3683
    Helixi372 – 38615
    Helixi388 – 3925
    Helixi395 – 43036
    Beta strandi433 – 4353
    Helixi437 – 45620

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CKOX-ray2.15A/B50-457[»]
    2CKPX-ray3.10A/B50-457[»]
    2CKQX-ray2.40A/B50-457[»]
    2I7QX-ray1.90A75-457[»]
    3F2RX-ray2.35A/B75-457[»]
    3G15X-ray1.70A/B75-457[»]
    3ZM9X-ray1.90A/B75-457[»]
    4BR3X-ray2.20A/B75-457[»]
    4CG8X-ray1.75A75-457[»]
    4CG9X-ray1.83A75-457[»]
    4CGAX-ray1.74A75-457[»]
    4DA5X-ray2.40A/B1-457[»]
    ProteinModelPortaliP35790.
    SMRiP35790. Positions 81-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35790.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 1213Substrate binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi50 – 8536Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the choline/ethanolamine kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0510.
    HOGENOMiHOG000041274.
    HOVERGENiHBG050943.
    InParanoidiP35790.
    KOiK14156.
    OMAiRAYLWCK.
    OrthoDBiEOG72VH68.
    PhylomeDBiP35790.
    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: P35790-1) [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

    MKTKFCTGGE AEPSPLGLLL SCGSGSAAPA PGVGQQRDAA SDLESKQLGG    50
    QQPPLALPPP PPLPLPLPLP QPPPPQPPAD EQPEPRTRRR AYLWCKEFLP 100
    GAWRGLREDE FHISVIRGGL SNMLFQCSLP DTTATLGDEP RKVLLRLYGA 150
    ILQMRSCNKE GSEQAQKENE FQGAEAMVLE SVMFAILAER SLGPKLYGIF 200
    PQGRLEQFIP SRRLDTEELS LPDISAEIAE KMATFHGMKM PFNKEPKWLF 250
    GTMEKYLKEV LRIKFTEESR IKKLHKLLSY NLPLELENLR SLLESTPSPV 300
    VFCHNDCQEG NILLLEGREN SEKQKLMLID FEYSSYNYRG FDIGNHFCEW 350
    MYDYSYEKYP FFRANIRKYP TKKQQLHFIS SYLPAFQNDF ENLSTEEKSI 400
    IKEEMLLEVN RFALASHFLW GLWSIVQAKI SSIEFGYMDY AQARFDAYFH 450
    QKRKLGV 457
    Length:457
    Mass (Da):52,249
    Last modified:April 14, 2009 - v3
    Checksum:i65F177ABE1AA3A12
    GO
    Isoform 2 (identifier: P35790-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-172: Missing.

    Show »
    Length:439
    Mass (Da):50,155
    Checksum:i73507D716F15F9E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 546GGQQPP → APTAA in BAA01547. (PubMed:1618328)Curated
    Sequence conflicti87 – 871T → A in BAA01547. (PubMed:1618328)Curated
    Sequence conflicti154 – 1541M → V in BAA01547. (PubMed:1618328)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti220 – 2201S → G.1 Publication
    Corresponds to variant rs17853641 [ dbSNP | Ensembl ].
    VAR_054863
    Natural varianti422 – 4221L → Q.1 Publication
    Corresponds to variant rs17853642 [ dbSNP | Ensembl ].
    VAR_054864

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei155 – 17218Missing in isoform 2. 1 PublicationVSP_009683Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10704 mRNA. Translation: BAA01547.1.
    AP002807 Genomic DNA. No translation available.
    AP002992 Genomic DNA. No translation available.
    BC036471 mRNA. Translation: AAH36471.1.
    CCDSiCCDS8178.1. [P35790-1]
    CCDS8179.1. [P35790-2]
    PIRiS23104.
    RefSeqiNP_001268.2. NM_001277.2. [P35790-1]
    NP_997634.1. NM_212469.1. [P35790-2]
    UniGeneiHs.77221.

    Genome annotation databases

    EnsembliENST00000265689; ENSP00000265689; ENSG00000110721. [P35790-1]
    ENST00000356135; ENSP00000348454; ENSG00000110721. [P35790-2]
    GeneIDi1119.
    KEGGihsa:1119.
    UCSCiuc001onj.3. human. [P35790-1]
    uc001onk.3. human. [P35790-2]

    Polymorphism databases

    DMDMi226694197.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10704 mRNA. Translation: BAA01547.1 .
    AP002807 Genomic DNA. No translation available.
    AP002992 Genomic DNA. No translation available.
    BC036471 mRNA. Translation: AAH36471.1 .
    CCDSi CCDS8178.1. [P35790-1 ]
    CCDS8179.1. [P35790-2 ]
    PIRi S23104.
    RefSeqi NP_001268.2. NM_001277.2. [P35790-1 ]
    NP_997634.1. NM_212469.1. [P35790-2 ]
    UniGenei Hs.77221.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CKO X-ray 2.15 A/B 50-457 [» ]
    2CKP X-ray 3.10 A/B 50-457 [» ]
    2CKQ X-ray 2.40 A/B 50-457 [» ]
    2I7Q X-ray 1.90 A 75-457 [» ]
    3F2R X-ray 2.35 A/B 75-457 [» ]
    3G15 X-ray 1.70 A/B 75-457 [» ]
    3ZM9 X-ray 1.90 A/B 75-457 [» ]
    4BR3 X-ray 2.20 A/B 75-457 [» ]
    4CG8 X-ray 1.75 A 75-457 [» ]
    4CG9 X-ray 1.83 A 75-457 [» ]
    4CGA X-ray 1.74 A 75-457 [» ]
    4DA5 X-ray 2.40 A/B 1-457 [» ]
    ProteinModelPortali P35790.
    SMRi P35790. Positions 81-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107543. 6 interactions.
    IntActi P35790. 1 interaction.
    STRINGi 9606.ENSP00000265689.

    Chemistry

    BindingDBi P35790.
    ChEMBLi CHEMBL3117.
    DrugBanki DB00122. Choline.

    PTM databases

    PhosphoSitei P35790.

    Polymorphism databases

    DMDMi 226694197.

    Proteomic databases

    MaxQBi P35790.
    PaxDbi P35790.
    PRIDEi P35790.

    Protocols and materials databases

    DNASUi 1119.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265689 ; ENSP00000265689 ; ENSG00000110721 . [P35790-1 ]
    ENST00000356135 ; ENSP00000348454 ; ENSG00000110721 . [P35790-2 ]
    GeneIDi 1119.
    KEGGi hsa:1119.
    UCSCi uc001onj.3. human. [P35790-1 ]
    uc001onk.3. human. [P35790-2 ]

    Organism-specific databases

    CTDi 1119.
    GeneCardsi GC11M067820.
    H-InvDB HIX0017419.
    HGNCi HGNC:1937. CHKA.
    HPAi HPA024153.
    MIMi 118491. gene.
    neXtProti NX_P35790.
    PharmGKBi PA26468.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0510.
    HOGENOMi HOG000041274.
    HOVERGENi HBG050943.
    InParanoidi P35790.
    KOi K14156.
    OMAi RAYLWCK.
    OrthoDBi EOG72VH68.
    PhylomeDBi P35790.
    TreeFami TF313549.

    Enzyme and pathway databases

    UniPathwayi UPA00558 ; UER00741 .
    UPA00753 ; UER00737 .
    Reactomei REACT_120919. Synthesis of PE.
    REACT_121238. Synthesis of PC.
    SABIO-RK P35790.

    Miscellaneous databases

    ChiTaRSi CHKA. human.
    EvolutionaryTracei P35790.
    GeneWikii CHKA.
    GenomeRNAii 1119.
    NextBioi 4642.
    PROi P35790.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35790.
    Bgeei P35790.
    CleanExi HS_CHKA.
    Genevestigatori P35790.

    Family and domain databases

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

    Publicationsi

    1. "Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation."
      Hosaka K., Tanaka S., Nikawa J., Yamashita S.
      FEBS Lett. 304:229-232(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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 2), VARIANTS GLY-220 AND GLN-422.
      Tissue: Testis.
    4. "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.
    5. "Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine."
      Malito E., Sekulic N., Too W.C., Konrad M., Lavie A.
      J. Mol. Biol. 364:136-151(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 50-439 IN COMPLEX WITH ADP AND PHOSPHOCHOLINE, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Crystal structures of human choline kinase isoforms in complex with hemicholinium-3: single amino acid near the active site influences inhibitor sensitivity."
      Hong B.S., Allali-Hassani A., Tempel W., Finerty P.J. Jr., Mackenzie F., Dimov S., Vedadi M., Park H.W.
      J. Biol. Chem. 285:16330-16340(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 75-457 IN COMPLEX WITH HEMICHOLINIUM-3 AND ADP.

    Entry informationi

    Entry nameiCHKA_HUMAN
    AccessioniPrimary (citable) accession number: P35790
    Secondary accession number(s): Q8NE29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 133 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3