Choline kinase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P20485 (KICH_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Choline kinase
EC=2.7.1.32

Gene names

Name:	CKI1
Synonyms:	CKI
Ordered Locus Names:	YLR133W
ORF Names:	L3130, L9606.8

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Responsible for phosphatidylcholine synthesis via the CDP-choline pathway. Also exhibits ethanolamine kinase activity but at 14% efficiency compared with choline.
Catalytic activity	ATP + choline = ADP + phosphocholine.
Pathway	Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphocholine from choline: step 1/1.
Subunit structure	Monomer. Interacts with NAP1. Ref.9
Subcellular location	Cytoplasm.
Miscellaneous	Present with 3930 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the choline/ethanolamine kinase family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	phosphatidylethanolamine biosynthetic process Inferred from mutant phenotype PubMed 10329685. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay PubMed 14562095. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW choline kinase activity Inferred from direct assay Ref.1. Source: SGD ethanolamine kinase activity Inferred from mutant phenotype PubMed 10329685. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAP1	P25293	5	EBI-9699,EBI-11850

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 582

582

Choline kinase

PRO_0000206226

Amino acid modifications

Modified residue

Phosphoserine Ref.7

Modified residue

Phosphoserine; by PKA Ref.5

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphothreonine Ref.10

Modified residue

Phosphoserine; by PKA Ref.5 Ref.7 Ref.8 Ref.10

Modified residue

Phosphothreonine Ref.8

Modified residue

Phosphoserine Ref.8

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphothreonine Ref.10

Modified residue

Phosphoserine Ref.10

Modified residue

Phosphoserine Ref.10

Experimental info

Mutagenesis

S → A: Decrease in activity and in phosphorylation by PKA. No phosphorylation by PKA, and strong decrease in activity; when associated with A-85. Ref.5

Mutagenesis

S → A: No phosphorylation by PKA, and strong decrease in activity; when associated with A-30. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P20485 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 68C395B9CC120A0E
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FASTA

582

66,317

        10         20         30         40         50         60 
MVQESRPGSV RSYSVGYQAR SRSSSQRRHS LTRQRSSQRL IRTISIESDV SNITDDDDLR 

        70         80         90        100        110        120 
AVNEGVAGVQ LDVSETANKG PRRASATDVT DSLGSTSSEY IEIPFVKETL DASLPSDYLK 

       130        140        150        160        170        180 
QDILNLIQSL KISKWYNNKK IQPVAQDMNL VKISGAMTNA IFKVEYPKLP SLLLRIYGPN 

       190        200        210        220        230        240 
IDNIIDREYE LQILARLSLK NIGPSLYGCF VNGRFEQFLE NSKTLTKDDI RNWKNSQRIA 

       250        260        270        280        290        300 
RRMKELHVGV PLLSSERKNG SACWQKINQW LRTIEKVDQW VGDPKNIENS LLCENWSKFM 

       310        320        330        340        350        360 
DIVDRYHKWL ISQEQGIEQV NKNLIFCHND AQYGNLLFTA PVMNTPSLYT APSSTSLTSQ 

       370        380        390        400        410        420 
SSSLFPSSSN VIVDDIINPP KQEQSQDSKL VVIDFEYAGA NPAAYDLANH LSEWMYDYNN 

       430        440        450        460        470        480 
AKAPHQCHAD RYPDKEQVLN FLYSYVSHLR GGAKEPIDEE VQRLYKSIIQ WRPTVQLFWS 

       490        500        510        520        530        540 
LWAILQSGKL EKKEASTAIT REEIGPNGKK YIIKTEPESP EEDFVENDDE PEAGVSIDTF 

       550        560        570        580 
DYMAYGRDKI AVFWGDLIGL GIITEEECKN FSSFKFLDTS YL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of the yeast CKI gene encoding choline kinase and its expression in Escherichia coli." Hosaka K., Kodaki T., Yamashita S. J. Biol. Chem. 264:2053-2059(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Phosphorylation of Saccharomyces cerevisiae choline kinase on Ser30 and Ser85 by protein kinase A regulates phosphatidylcholine synthesis by the CDP-choline pathway." Yu Y., Sreenivas A., Ostrander D.B., Carman G.M. J. Biol. Chem. 277:34978-34986(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-30 AND SER-85, MUTAGENESIS OF SER-30 AND SER-85.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-85, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; THR-90 AND SER-92, MASS SPECTROMETRY.
[9]	"Phosphorylation by casein kinase 2 regulates Nap1 localization and function." Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F. Mol. Cell. Biol. 28:1313-1325(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-51; THR-54; SER-85; SER-95; THR-96; SER-97 AND SER-98, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04454 Genomic DNA. Translation: AAA34499.1. X91258 Genomic DNA. Translation: CAA62646.1. Z73305 Genomic DNA. Translation: CAA97704.1. U53881 Genomic DNA. Translation: AAB82396.1. AY692779 Genomic DNA. Translation: AAT92798.1. BK006945 Genomic DNA. Translation: DAA09444.1.
PIR	A32034.
RefSeq	NP_013234.1. NM_001182020.1.
3D structure databases
ProteinModelPortal	P20485.
SMR	P20485. Positions 159-487.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2617N.
IntAct	P20485. 5 interactions.
MINT	MINT-422889.
STRING	4932.YLR133W.
Proteomic databases
PaxDb	P20485.
PeptideAtlas	P20485.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YLR133W; YLR133W; YLR133W.
GeneID	850824.
KEGG	sce:YLR133W.
Organism-specific databases
CYGD	YLR133w.
SGD	S000004123. CKI1.
Phylogenomic databases
eggNOG	COG0510.
GeneTree	ENSGT00530000062991.
HOGENOM	HOG000246747.
KO	K00866.
OMA	CHNDTQY.
OrthoDB	EOG466ZW1.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13669.
UniPathway	UPA00753; UER00737.
Gene expression databases
Genevestigator	P20485.
GermOnline	YLR133W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR026712. Cho/Etha_kinase. IPR007521. Choline_kin_N. IPR011009. Kinase-like_dom. [Graphical view]
PANTHER	PTHR22603. PTHR22603. 1 hit.
Pfam	PF04428. Choline_kin_N. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
ProtoNet	Search...
Other
NextBio	967079.

Entry information

Entry name

KICH_YEAST

Accession

Primary (citable) accession number: P20485
Secondary accession number(s): D6VYC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents