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Protein

CTP-dependent diacylglycerol kinase 1

Gene

DGK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in pre-tRNA splicing (By similarity). CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PAH1/SMP2. Involved in the resistance to nickel chloride and nalidixic acid. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus.By similarity3 Publications

Catalytic activityi

CTP + 1,2-diacyl-sn-glycerol = CDP + 1,2-diacyl-sn-glycerol 3-phosphate.2 Publications

Cofactori

Ca2+1 Publication, Mg2+1 Publication

Enzyme regulationi

Inhibited by N-ethylmaleimide, dCTP, and sphingoid bases including sphinganine, sphingosine and phytosphingosine. DAG pyrophosphate, cardiolipin, CDP-DAG, and lyso-PA inhibited activity by 23-66%. Also inhibited by Ca2+ concentrations of more than 1 mM, by addition of EDTA or EGTA at 5 mM, and by 5 mM Mn2+ and Zn2+. Stimulated by major membrane phospholipids including phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine, phosphatidylglycerol, and phosphatidate. Also stimulated to a maximum by addition of TritonX-100 at a concentration of 1 mM, followed by an apparent inhibition of activity at concentrations above 1 mM.1 Publication

Kineticsi

  1. KM=0.3 mM for CTP1 Publication
  2. KM=0.4 mM for dCTP1 Publication
  1. Vmax=0.018 nM/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.0-7.5.1 Publication

Temperature dependencei

Maximum activity at 30 degrees Celsius. Labile above 40 degrees Celsius.1 Publication

GO - Molecular functioni

  • diacylglycerol kinase activity Source: SGD

GO - Biological processi

  • phosphatidic acid biosynthetic process Source: SGD
  • vesicle-mediated transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

ER-Golgi transport, Transport

Keywords - Ligandi

Calcium, Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:G3O-33794-MONOMER.
YEAST:G3O-33794-MONOMER.
BRENDAi2.7.1.B4. 984.
SABIO-RKQ12382.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP-dependent diacylglycerol kinase 1 (EC:2.7.1.174)
Alternative name(s):
Diglyceride kinase 1
Short name:
DAG kinase 1
High-copy suppressor of SLY1 defect protein 1
Gene namesi
Name:DGK1
Synonyms:HSD1
Ordered Locus Names:YOR311C
ORF Names:O6111
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XV

Organism-specific databases

CYGDiYOR311c.
EuPathDBiFungiDB:YOR311C.
SGDiS000005838. DGK1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7777LumenalSequence AnalysisAdd
BLAST
Transmembranei78 – 9518HelicalSequence AnalysisAdd
BLAST
Topological domaini96 – 1038CytoplasmicSequence Analysis
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Topological domaini125 – 14016LumenalSequence AnalysisAdd
BLAST
Transmembranei141 – 16121HelicalSequence AnalysisAdd
BLAST
Topological domaini162 – 1632CytoplasmicSequence Analysis
Transmembranei164 – 18421HelicalSequence AnalysisAdd
BLAST
Topological domaini185 – 20319LumenalSequence AnalysisAdd
BLAST
Transmembranei204 – 22421HelicalSequence AnalysisAdd
BLAST
Topological domaini225 – 24420CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei245 – 26521HelicalSequence AnalysisAdd
BLAST
Topological domaini266 – 29025LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of endoplasmic reticulum membrane Source: SGD
  • integral component of membrane Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi76 – 761R → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. 1 Publication
Mutagenesisi77 – 771K → A: Loss of kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. 1 Publication
Mutagenesisi177 – 1771D → A: No kinase activity. Not temperature-sensitive for growth. Does not trigger nuclear membrane expansion. 2 Publications
Mutagenesisi184 – 1841G → A: 70% reduction in kinase activity. Not temperature-sensitive for growth. Regular shaped nuclear membrane structure. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290CTP-dependent diacylglycerol kinase 1PRO_0000240382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi11 – 111N-linked (GlcNAc...)Sequence Analysis
Modified residuei44 – 441Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei46 – 461Phosphoserine1 Publication
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ12382.
PaxDbiQ12382.

Interactioni

Protein-protein interaction databases

BioGridi34699. 222 interactions.
DIPiDIP-5021N.
MINTiMINT-561696.
STRINGi4932.YOR311C.

Structurei

3D structure databases

ProteinModelPortaliQ12382.
SMRiQ12382. Positions 146-221.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DGK1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0170.
HOGENOMiHOG000198978.
InParanoidiQ12382.
KOiK16368.
OMAiHLKSHEW.
OrthoDBiEOG7VX96V.

Sequencei

Sequence statusi: Complete.

Q12382-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTEDAIALP NSTLEPRTEA KQRLSSKSHQ VSAKVTIPAK EEISSSDDDA
60 70 80 90 100
HVPVTEIHLK SHEWFGDFIT KHEIPRKVFH SSIGFITLYL YTQGINYKNV
110 120 130 140 150
LWPLIYAFII LFILDLIRLN WPFFNMLYCR TVGALMRKKE IHTYNGVLWY
160 170 180 190 200
ILGLIFSFNF FSKDVTLISL FLLSWSDTAA ATIGRKYGHL TPKVARNKSL
210 220 230 240 250
AGSIAAFTVG VITCWVFYGY FVPAYSYVNK PGEIQWSPET SRLSLNMLSL
260 270 280 290
LGGVVAALSE GIDLFNWDDN FTIPVLSSLF MNAVIKTFKK
Length:290
Mass (Da):32,840
Last modified:November 1, 1996 - v1
Checksum:iF8A0EE6F1018025B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90565 Genomic DNA. Translation: CAA62166.1.
Z75219 Genomic DNA. Translation: CAA99631.1.
BK006948 Genomic DNA. Translation: DAA11076.1.
PIRiS58323.
RefSeqiNP_014956.3. NM_001183731.3.

Genome annotation databases

EnsemblFungiiYOR311C; YOR311C; YOR311C.
GeneIDi854488.
KEGGisce:YOR311C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90565 Genomic DNA. Translation: CAA62166.1.
Z75219 Genomic DNA. Translation: CAA99631.1.
BK006948 Genomic DNA. Translation: DAA11076.1.
PIRiS58323.
RefSeqiNP_014956.3. NM_001183731.3.

3D structure databases

ProteinModelPortaliQ12382.
SMRiQ12382. Positions 146-221.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34699. 222 interactions.
DIPiDIP-5021N.
MINTiMINT-561696.
STRINGi4932.YOR311C.

Proteomic databases

MaxQBiQ12382.
PaxDbiQ12382.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR311C; YOR311C; YOR311C.
GeneIDi854488.
KEGGisce:YOR311C.

Organism-specific databases

CYGDiYOR311c.
EuPathDBiFungiDB:YOR311C.
SGDiS000005838. DGK1.

Phylogenomic databases

eggNOGiCOG0170.
HOGENOMiHOG000198978.
InParanoidiQ12382.
KOiK16368.
OMAiHLKSHEW.
OrthoDBiEOG7VX96V.

Enzyme and pathway databases

BioCyciMetaCyc:G3O-33794-MONOMER.
YEAST:G3O-33794-MONOMER.
BRENDAi2.7.1.B4. 984.
SABIO-RKQ12382.

Miscellaneous databases

NextBioi976813.
PROiQ12382.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
    Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
    Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: FUNCTION.
  5. "Multicopy suppressors of the sly1 temperature-sensitive mutation in the ER-Golgi vesicular transport in Saccharomyces cerevisiae."
    Kosodo Y., Imai K., Hirata A., Noda Y., Takatsuki A., Adachi H., Yoda K.
    Yeast 18:1003-1014(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "An unconventional diacylglycerol kinase that regulates phospholipid synthesis and nuclear membrane growth."
    Han G.-S., O'Hara L., Carman G.M., Siniossoglou S.
    J. Biol. Chem. 283:20433-20442(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TRANSMEMBRANE DOMAINS, OVEREXPRESSION PHENOTYPE, KNOCKOUT, MUTAGENESIS OF ASP-177.
  11. "Characterization of the yeast DGK1-encoded CTP-dependent diacylglycerol kinase."
    Han G.-S., O'Hara L., Siniossoglou S., Carman G.M.
    J. Biol. Chem. 283:20443-20453(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS OF 133-145 AND 188-201, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF 1-MET--GLY-66; 1-MET--THR-70; 1-MET--LYS-77; ARG-76; LYS-77; ASP-177 AND GLY-184.
  12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-45 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDGK1_YEAST
AccessioniPrimary (citable) accession number: Q12382
Secondary accession number(s): D6W310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 784 molecules/cell in log phase SD medium.1 Publication
Rescues the lethality of dephosphorylated PAH1/SMP2. Overexpression causes the appearance of phosphatidate-enriched membranes around the nucleus, leading to expansion of the nuclear membrane without proliferation of the cortical endoplasmic reticulum membrane. Deletion restores normal nuclear structure in PAH1/SMP2 deleted cells and returns the level of INO1 mRNA to normal. Deletion does not affect the abnormal levels of phosphatidylinositol and major neutral lipid triacylglycerol seen in the PAH1/SMP2 deletion mutant.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.