UniProtKB - Q01134 (CHKA_RAT)
Choline kinase alpha
Chka
Functioni
Plays a key role in phospholipid biosynthesis by catalyzing the phosphorylation of free choline to phosphocholine, the first step in phosphatidylcholine biosynthesis. Also phosphorylates ethanolamine, thereby contributing to phosphatidylethanolamine biosynthesis. Has higher activity with choline. May contribute to tumor cell growth.
By similarityThis isoform plays a key role in lipolysis of lipid droplets following glucose deprivation (By similarity).
In response to glucose deprivation, phosphorylated by AMPK, promoting localization to lipid droplets (By similarity).
Phosphorylation is followed by acetylation by KAT5, leading to dissociation of the homodimer into a monomer (By similarity).
Monomeric CHKA isoform 1 is converted into a tyrosine-protein kinase, which phosphorylates lipid droplet structural proteins PLIN2 and PLIN3, leading to lipolysis of lipid droplets (By similarity).
By similarityCatalytic activityi
- EC:2.7.1.32By similarityThis reaction proceeds in the forwardBy similarity direction.
- EC:2.7.1.82By similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.This reaction proceeds in the forwardBy similarity direction.
: phosphatidylcholine biosynthesis Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes phosphocholine from choline.By similarity This subpathway is part of the pathway phosphatidylcholine biosynthesis, which is itself part of Phospholipid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphocholine from choline, the pathway phosphatidylcholine biosynthesis and in Phospholipid metabolism.
Pathwayi: phosphatidylethanolamine biosynthesis
This protein is involved in step 1 of the subpathway that synthesizes phosphatidylethanolamine from ethanolamine.By similarity This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from ethanolamine, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 142 | ATPBy similarity | 1 | |
Binding sitei | 304 | ATPBy similarity | 1 | |
Binding sitei | 326 | ATPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 113 – 119 | ATPBy similarity | 7 | |
Nucleotide bindingi | 203 – 209 | ATPBy similarity | 7 |
GO - Molecular functioni
- ATP binding Source: RGD
- choline binding Source: RGD
- choline kinase activity Source: RGD
- cholinesterase activity Source: RGD
- ethanolamine kinase activity Source: RGD
- identical protein binding Source: RGD
GO - Biological processi
- CDP-choline pathway Source: GO_Central
- choline metabolic process Source: RGD
- ethanolamine metabolic process Source: RGD
- phosphatidylcholine biosynthetic process Source: UniProtKB
- phosphatidylethanolamine biosynthetic process Source: UniProtKB
- response to 3-methylcholanthrene Source: RGD
- response to toxic substance Source: RGD
Keywordsi
Molecular function | Kinase, Transferase |
Biological process | Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
Reactomei | R-RNO-1483191, Synthesis of PC R-RNO-1483213, Synthesis of PE |
SABIO-RKi | Q01134 |
UniPathwayi | UPA00558;UER00741 UPA00753;UER00737 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:Chka Synonyms:Chk, Ckr |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 61944, Chka |
Subcellular locationi
Cytoplasm and Cytosol
- cytosol By similarity
Other locations
- Lipid droplet By similarity
Note: Isoform 1 localizes to lipid droplets following phosphorylation by AMPK.By similarity
Other locations
- cytoplasm Source: GO_Central
Keywords - Cellular componenti
Cytoplasm, Lipid dropletPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000206221 | 1 – 453 | Choline kinase alphaAdd BLAST | 453 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 71 | PhosphoserineCombined sources | 1 | |
Modified residuei | 243 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 275 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | Q01134 |
PRIDEi | Q01134 |
PTM databases
iPTMneti | Q01134 |
PhosphoSitePlusi | Q01134 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000016791, Expressed in liver and 21 other tissues |
ExpressionAtlasi | Q01134, baseline and differential |
Genevisiblei | Q01134, RN |
Interactioni
Subunit structurei
Heterodimer with CHKB (By similarity). Homodimer (By similarity).
By similarityMonomer; acetylation by KAT5 promotes dissociation of the homodimer and monomerization.
By similarityGO - Molecular functioni
- identical protein binding Source: RGD
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000023020 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 22 – 81 | DisorderedSequence analysisAdd BLAST | 60 | |
Regioni | 115 – 117 | Phosphocholine bindingBy similarity | 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 53 – 77 | Pro residuesSequence analysisAdd BLAST | 25 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2686, Eukaryota |
GeneTreei | ENSGT00950000182939 |
HOGENOMi | CLU_012712_2_1_1 |
InParanoidi | Q01134 |
OMAi | HEWTADY |
OrthoDBi | 1469912at2759 |
PhylomeDBi | Q01134 |
TreeFami | TF313549 |
Family and domain databases
InterProi | View protein in InterPro IPR011009, Kinase-like_dom_sf |
SUPFAMi | SSF56112, SSF56112, 1 hit |
s (2)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MKTKFCTGGE AEPSPLGLLL SCGGSAAPTP GVGQQRDAAG ELESKQLGGR
60 70 80 90 100
SQPLALPPPP PPPLPLPPPP SPPLADEQPE PRTRRRAYLW CKEFLPGAWR
110 120 130 140 150
GLREDQFHIS VIRGGLSNML FQCSLPDSIA SVGDEPRKVL LRLYGAILKM
160 170 180 190 200
RSCNKEGSEQ AQNENEFQGA EAMVLESVMF AILAERSLGP KLYGIFPQGR
210 220 230 240 250
LEQFIPSRRL DTEELCLPDI SAEIAEKMAT FHGMKMPFNK EPKWLFGTME
260 270 280 290 300
KYLNQVLRLK FSREARVQQL HKFLSYNLPL ELENLRSLLQ YTRSPVVFCH
310 320 330 340 350
NDCQEGNILL LEGQENSEKQ KLMLIDFEYS SYNYRGFDIG NHFCEWMYDY
360 370 380 390 400
TYEKYPFFRA NIQKYPTRKQ QLHFISSYLT TFQNDFESLS SEEQSATKED
410 420 430 440 450
MLLEVNRFAL ASHFLWGLWS IVQAKISSIE FGYMEYAQAR FDAYFDQKRK
LGV
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_001067 | 151 – 168 | Missing in isoform 2. CuratedAdd BLAST | 18 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10261 mRNA Translation: BAA01102.1 D37884 Genomic DNA Translation: BAA07126.1 D37885 mRNA Translation: BAA07127.1 |
PIRi | A42672 JX0342 |
RefSeqi | NP_058823.1, NM_017127.1 [Q01134-2] XP_006230770.1, XM_006230708.3 [Q01134-1] |
Genome annotation databases
Ensembli | ENSRNOT00000022824; ENSRNOP00000022824; ENSRNOG00000016791 [Q01134-2] ENSRNOT00000023020; ENSRNOP00000023020; ENSRNOG00000016791 [Q01134-1] |
GeneIDi | 29194 |
KEGGi | rno:29194 |
UCSCi | RGD:61944, rat [Q01134-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D10261 mRNA Translation: BAA01102.1 D37884 Genomic DNA Translation: BAA07126.1 D37885 mRNA Translation: BAA07127.1 |
PIRi | A42672 JX0342 |
RefSeqi | NP_058823.1, NM_017127.1 [Q01134-2] XP_006230770.1, XM_006230708.3 [Q01134-1] |
3D structure databases
SMRi | Q01134 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 10116.ENSRNOP00000023020 |
PTM databases
iPTMneti | Q01134 |
PhosphoSitePlusi | Q01134 |
Proteomic databases
PaxDbi | Q01134 |
PRIDEi | Q01134 |
Genome annotation databases
Ensembli | ENSRNOT00000022824; ENSRNOP00000022824; ENSRNOG00000016791 [Q01134-2] ENSRNOT00000023020; ENSRNOP00000023020; ENSRNOG00000016791 [Q01134-1] |
GeneIDi | 29194 |
KEGGi | rno:29194 |
UCSCi | RGD:61944, rat [Q01134-1] |
Organism-specific databases
CTDi | 1119 |
RGDi | 61944, Chka |
Phylogenomic databases
eggNOGi | KOG2686, Eukaryota |
GeneTreei | ENSGT00950000182939 |
HOGENOMi | CLU_012712_2_1_1 |
InParanoidi | Q01134 |
OMAi | HEWTADY |
OrthoDBi | 1469912at2759 |
PhylomeDBi | Q01134 |
TreeFami | TF313549 |
Enzyme and pathway databases
UniPathwayi | UPA00558;UER00741 UPA00753;UER00737 |
Reactomei | R-RNO-1483191, Synthesis of PC R-RNO-1483213, Synthesis of PE |
SABIO-RKi | Q01134 |
Miscellaneous databases
PROi | PR:Q01134 |
Gene expression databases
Bgeei | ENSRNOG00000016791, Expressed in liver and 21 other tissues |
ExpressionAtlasi | Q01134, baseline and differential |
Genevisiblei | Q01134, RN |
Family and domain databases
InterProi | View protein in InterPro IPR011009, Kinase-like_dom_sf |
SUPFAMi | SSF56112, SSF56112, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CHKA_RAT | |
Accessioni | Q01134Primary (citable) accession number: Q01134 Secondary accession number(s): Q63114 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1993 |
Last sequence update: | May 30, 2000 | |
Last modified: | February 23, 2022 | |
This is version 145 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families