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P35790 (CHKA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline kinase alpha

Short name=CK
EC=2.7.1.32
Alternative name(s):
CHETK-alpha
Ethanolamine kinase
Short name=EK
EC=2.7.1.82
Gene names
Name:CHKA
Synonyms:CHK, CKI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Catalytic activity

ATP + choline = ADP + phosphocholine. Ref.4

ATP + ethanolamine = ADP + O-phosphoethanolamine. Ref.4

Pathway

Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1.

Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from ethanolamine: step 1/3.

Subunit structure

Heterodimer with CHKB By similarity. Homodimer. Ref.5

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the choline/ethanolamine kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.2 mM for choline Ref.4 Ref.5

KM=0.4 mM for ATP

KM=12 mM for ethanolamine

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCDP-choline pathway

Inferred from direct assay Ref.4. Source: GOC

choline metabolic process

Inferred from electronic annotation. Source: Ensembl

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

lipid metabolic process

Traceable author statement PubMed 10363580. Source: ProtInc

lipid transport

Traceable author statement PubMed 10363580. Source: ProtInc

phosphatidylcholine biosynthetic process

Inferred from direct assay Ref.4. Source: UniProtKB

phosphatidylethanolamine biosynthetic process

Inferred from direct assay Ref.4. Source: UniProtKB

phospholipid metabolic process

Traceable author statement. Source: Reactome

signal transduction

Traceable author statement PubMed 10363580. Source: GOC

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

choline binding

Inferred from electronic annotation. Source: Ensembl

choline kinase activity

Inferred from direct assay Ref.4. Source: UniProtKB

cholinesterase activity

Inferred from electronic annotation. Source: Ensembl

drug binding

Inferred from direct assay Ref.4. Source: UniProtKB

ethanolamine kinase activity

Inferred from direct assay Ref.4. Source: UniProtKB

signal transducer activity

Traceable author statement PubMed 10363580. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35790-1)

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.
Isoform 2 (identifier: P35790-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Choline kinase alpha
PRO_0000206219

Regions

Nucleotide binding117 – 1237ATP
Nucleotide binding207 – 2137ATP
Region119 – 1213Substrate binding
Compositional bias50 – 8536Pro-rich

Sites

Binding site1461ATP
Binding site3081ATP Probable
Binding site3301ATP

Natural variations

Alternative sequence155 – 17218Missing in isoform 2.
VSP_009683
Natural variant2201S → G. Ref.3
Corresponds to variant rs17853641 [ dbSNP | Ensembl ].
VAR_054863
Natural variant4221L → Q. Ref.3
Corresponds to variant rs17853642 [ dbSNP | Ensembl ].
VAR_054864

Experimental info

Sequence conflict49 – 546GGQQPP → APTAA in BAA01547. Ref.1
Sequence conflict871T → A in BAA01547. Ref.1
Sequence conflict1541M → V in BAA01547. Ref.1

Secondary structure

............................................................. 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 14, 2009. Version 3.
Checksum: 65F177ABE1AA3A12

FASTA45752,249
        10         20         30         40         50         60 
MKTKFCTGGE AEPSPLGLLL SCGSGSAAPA PGVGQQRDAA SDLESKQLGG QQPPLALPPP 

        70         80         90        100        110        120 
PPLPLPLPLP QPPPPQPPAD EQPEPRTRRR AYLWCKEFLP GAWRGLREDE FHISVIRGGL 

       130        140        150        160        170        180 
SNMLFQCSLP DTTATLGDEP RKVLLRLYGA ILQMRSCNKE GSEQAQKENE FQGAEAMVLE 

       190        200        210        220        230        240 
SVMFAILAER SLGPKLYGIF PQGRLEQFIP SRRLDTEELS LPDISAEIAE KMATFHGMKM 

       250        260        270        280        290        300 
PFNKEPKWLF GTMEKYLKEV LRIKFTEESR IKKLHKLLSY NLPLELENLR SLLESTPSPV 

       310        320        330        340        350        360 
VFCHNDCQEG NILLLEGREN SEKQKLMLID FEYSSYNYRG FDIGNHFCEW MYDYSYEKYP 

       370        380        390        400        410        420 
FFRANIRKYP TKKQQLHFIS SYLPAFQNDF ENLSTEEKSI IKEEMLLEVN RFALASHFLW 

       430        440        450 
GLWSIVQAKI SSIEFGYMDY AQARFDAYFH QKRKLGV 

« Hide

Isoform 2 [UniParc].

Checksum: 73507D716F15F9E4
Show »

FASTA43950,155

References

« Hide 'large scale' references
[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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10704 mRNA. Translation: BAA01547.1.
AP002807 Genomic DNA. No translation available.
AP002992 Genomic DNA. No translation available.
BC036471 mRNA. Translation: AAH36471.1.
PIRS23104.
RefSeqNP_001268.2. NM_001277.2.
NP_997634.1. NM_212469.1.
UniGeneHs.77221.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKOX-ray2.15A/B50-439[»]
2CKPX-ray3.10A/B50-439[»]
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[»]
ProteinModelPortalP35790.
SMRP35790. Positions 81-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107543. 6 interactions.
IntActP35790. 1 interaction.
STRING9606.ENSP00000265689.

Chemistry

BindingDBP35790.
ChEMBLCHEMBL3117.
DrugBankDB00122. Choline.

PTM databases

PhosphoSiteP35790.

Polymorphism databases

DMDM226694197.

Proteomic databases

PaxDbP35790.
PRIDEP35790.

Protocols and materials databases

DNASU1119.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265689; ENSP00000265689; ENSG00000110721. [P35790-1]
ENST00000356135; ENSP00000348454; ENSG00000110721. [P35790-2]
GeneID1119.
KEGGhsa:1119.
UCSCuc001onj.3. human. [P35790-1]
uc001onk.3. human. [P35790-2]

Organism-specific databases

CTD1119.
GeneCardsGC11M067820.
H-InvDBHIX0017419.
HGNCHGNC:1937. CHKA.
HPAHPA024153.
MIM118491. gene.
neXtProtNX_P35790.
PharmGKBPA26468.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0510.
HOGENOMHOG000041274.
HOVERGENHBG050943.
InParanoidP35790.
KOK14156.
OMARAYLWCK.
OrthoDBEOG72VH68.
PhylomeDBP35790.
TreeFamTF313549.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SABIO-RKP35790.
UniPathwayUPA00558; UER00741.
UPA00753; UER00737.

Gene expression databases

ArrayExpressP35790.
BgeeP35790.
CleanExHS_CHKA.
GenevestigatorP35790.

Family and domain databases

InterProIPR026712. Cho/Etha_kinase.
IPR011009. Kinase-like_dom.
[Graphical view]
PANTHERPTHR22603:SF7. PTHR22603:SF7. 1 hit.
SUPFAMSSF56112. SSF56112. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCHKA. human.
EvolutionaryTraceP35790.
GeneWikiCHKA.
GenomeRNAi1119.
NextBio4642.
PROP35790.
SOURCESearch...

Entry information

Entry nameCHKA_HUMAN
AccessionPrimary (citable) accession number: P35790
Secondary accession number(s): Q8NE29
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 14, 2009
Last modified: April 16, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM