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Q9Y259 (CHKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Choline/ethanolamine kinase
Alternative name(s):
Choline kinase beta
Short name=CK
Short name=CKB
EC=2.7.1.32
Choline kinase-like protein
Ethanolamine kinase
Short name=EK
EC=2.7.1.82
Ethanolamine kinase beta
Short name=EKB
choline/ethanolamine kinase beta
Short name=CKEKB
Gene names
Name:CHKB
Synonyms:CHETK, CHKL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9

Catalytic activity

ATP + choline = ADP + phosphocholine. Ref.9

ATP + ethanolamine = ADP + O-phosphoethanolamine. Ref.9

Pathway

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

Subunit structure

Homodimer, and heterodimer with CHKA.

Miscellaneous

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

Sequence similarities

Belongs to the choline/ethanolamine kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.57 mM for choline Ref.9

KM=2.9 mM for ethanolamine

Sequence caution

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y259-1)

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: Q9Y259-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 395394Choline/ethanolamine kinase
PRO_0000206222

Regions

Nucleotide binding75 – 817ATP By similarity
Nucleotide binding146 – 1527ATP
Region77 – 793Substrate binding By similarity

Sites

Binding site1041ATP
Binding site2441ATP By similarity
Binding site2641ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.10

Natural variations

Alternative sequence75 – 12753SGGLS…FAILA → RWEVRGQPLRCADRGQGSAA GPSGCSMFSPPSCARAWGGA GPAWPGGGRGRGR in isoform 2.
VSP_034248
Alternative sequence128 – 395268Missing in isoform 2.
VSP_034249

Secondary structure

............................................................ 395
Helix Strand Turn

Details...

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 18367468B22FB9CE

FASTA39545,271
        10         20         30         40         50         60 
MAAEATAVAG SGAVGGCLAK DGLQQSKCPD TTPKRRRASS LSRDAERRAY QWCREYLGGA 

        70         80         90        100        110        120 
WRRVQPEELR VYPVSGGLSN LLFRCSLPDH LPSVGEEPRE VLLRLYGAIL QGVDSLVLES 

       130        140        150        160        170        180 
VMFAILAERS LGPQLYGVFP EGRLEQYIPS RPLKTQELRE PVLSAAIATK MAQFHGMEMP 

       190        200        210        220        230        240 
FTKEPHWLFG TMERYLKQIQ DLPPTGLPEM NLLEMYSLKD EMGNLRKLLE STPSPVVFCH 

       250        260        270        280        290        300 
NDIQEGNILL LSEPENADSL MLVDFEYSSY NYRGFDIGNH FCEWVYDYTH EEWPFYKARP 

       310        320        330        340        350        360 
TDYPTQEQQL HFIRHYLAEA KKGETLSQEE QRKLEEDLLV EVSRYALASH FFWGLWSILQ 

       370        380        390 
ASMSTIEFGY LDYAQSRFQF YFQQKGQLTS VHSSS 

« Hide

Isoform 2 [UniParc].

Checksum: 1C3DBAB66A5D1637
Show »

FASTA12713,506

References

« Hide 'large scale' references
[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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS14099.1. [Q9Y259-1]
RefSeqNP_005189.2. NM_005198.4. [Q9Y259-1]
UniGeneHs.654827.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IG7X-ray1.80A/B14-395[»]
3FEGX-ray1.30A35-395[»]
3LQ3X-ray1.42A14-395[»]
ProteinModelPortalQ9Y259.
SMRQ9Y259. Positions 42-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107544. 2 interactions.
IntActQ9Y259. 1 interaction.
STRING9606.ENSP00000384400.

Chemistry

DrugBankDB00122. Choline.

PTM databases

PhosphoSiteQ9Y259.

Polymorphism databases

DMDM6685604.

Proteomic databases

MaxQBQ9Y259.
PaxDbQ9Y259.
PRIDEQ9Y259.

Protocols and materials databases

DNASU1120.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000406938; ENSP00000384400; ENSG00000100288. [Q9Y259-1]
GeneID1120.
KEGGhsa:1120.
UCSCuc003bmu.3. human. [Q9Y259-1]

Organism-specific databases

CTD1120.
GeneCardsGC22M051017.
GeneReviewsCHKB.
HGNCHGNC:1938. CHKB.
HPAHPA018797.
MIM612395. gene.
neXtProtNX_Q9Y259.
Orphanet280671. Congenital muscular dystrophy due to phosphatidylcholine biosynthesis defect.
PharmGKBPA26469.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0510.
HOGENOMHOG000041274.
HOVERGENHBG050943.
InParanoidQ9Y259.
KOK14156.
OMAYKAQPAN.
OrthoDBEOG72VH68.
PhylomeDBQ9Y259.
TreeFamTF313549.

Enzyme and pathway databases

BRENDA2.7.1.32. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ9Y259.
UniPathwayUPA00558; UER00741.

Gene expression databases

BgeeQ9Y259.
CleanExHS_CHKB.
GenevestigatorQ9Y259.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y259.
GeneWikiCHKB_(gene).
GenomeRNAi1120.
NextBio4648.
PROQ9Y259.
SOURCESearch...

Entry information

Entry nameCHKB_HUMAN
AccessionPrimary (citable) accession number: Q9Y259
Secondary accession number(s): A0PJM6, Q13388
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 118 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 chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM