Skip Header

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

P35790

- CHKA_HUMAN

UniProt

P35790 - CHKA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Choline kinase alpha

Gene

CHKA

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

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
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

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
Complete GO annotation...

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

BgeeiP35790.
CleanExiHS_CHKA.
ExpressionAtlasiP35790. baseline and differential.
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 – 9814Combined sources
Helixi101 – 1033Combined sources
Helixi108 – 1103Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi119 – 12810Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi141 – 1499Combined sources
Helixi175 – 18915Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi211 – 2133Combined sources
Helixi216 – 2205Combined sources
Helixi222 – 23615Combined sources
Helixi248 – 26215Combined sources
Helixi268 – 27811Combined sources
Helixi282 – 29413Combined sources
Beta strandi300 – 3034Combined sources
Helixi309 – 3113Combined sources
Beta strandi312 – 3154Combined sources
Helixi318 – 3203Combined sources
Beta strandi322 – 3243Combined sources
Beta strandi326 – 3283Combined sources
Beta strandi335 – 3384Combined sources
Helixi339 – 34911Combined sources
Beta strandi352 – 3543Combined sources
Helixi366 – 3683Combined sources
Helixi372 – 38615Combined sources
Helixi388 – 3925Combined sources
Helixi395 – 43036Combined sources
Beta strandi433 – 4353Combined sources
Helixi437 – 45620Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000062991.
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

        10         20         30         40         50
MKTKFCTGGE AEPSPLGLLL SCGSGSAAPA PGVGQQRDAA SDLESKQLGG
60 70 80 90 100
QQPPLALPPP PPLPLPLPLP QPPPPQPPAD EQPEPRTRRR AYLWCKEFLP
110 120 130 140 150
GAWRGLREDE FHISVIRGGL SNMLFQCSLP DTTATLGDEP RKVLLRLYGA
160 170 180 190 200
ILQMRSCNKE GSEQAQKENE FQGAEAMVLE SVMFAILAER SLGPKLYGIF
210 220 230 240 250
PQGRLEQFIP SRRLDTEELS LPDISAEIAE KMATFHGMKM PFNKEPKWLF
260 270 280 290 300
GTMEKYLKEV LRIKFTEESR IKKLHKLLSY NLPLELENLR SLLESTPSPV
310 320 330 340 350
VFCHNDCQEG NILLLEGREN SEKQKLMLID FEYSSYNYRG FDIGNHFCEW
360 370 380 390 400
MYDYSYEKYP FFRANIRKYP TKKQQLHFIS SYLPAFQNDF ENLSTEEKSI
410 420 430 440 450
IKEEMLLEVN RFALASHFLW GLWSIVQAKI SSIEFGYMDY AQARFDAYFH

QKRKLGV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00530000062991.
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

Bgeei P35790.
CleanExi HS_CHKA.
ExpressionAtlasi P35790. baseline and differential.
Genevestigatori P35790.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: November 26, 2014
This is version 135 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