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Q12382

- DGK1_YEAST

UniProt

Q12382 - DGK1_YEAST

Protein

CTP-dependent diacylglycerol kinase 1

Gene

DGK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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+ or 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

    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

    1. diacylglycerol kinase activity Source: SGD

    GO - Biological processi

    1. phosphatidic acid biosynthetic process Source: SGD
    2. vesicle-mediated transport Source: UniProtKB-KW

    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.
    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: Chromosome XV

    Organism-specific databases

    CYGDiYOR311c.
    SGDiS000005838. DGK1.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of endoplasmic reticulum membrane Source: SGD
    3. integral component of membrane Source: SGD
    4. nuclear membrane Source: UniProtKB-SubCell

    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.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12382.

    Interactioni

    Protein-protein interaction databases

    BioGridi34699. 223 interactions.
    DIPiDIP-5021N.
    MINTiMINT-561696.
    STRINGi4932.YOR311C.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12382.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 7777LumenalSequence AnalysisAdd
    BLAST
    Topological domaini96 – 1038CytoplasmicSequence Analysis
    Topological domaini125 – 14016LumenalSequence AnalysisAdd
    BLAST
    Topological domaini162 – 1632CytoplasmicSequence Analysis
    Topological domaini185 – 20319LumenalSequence AnalysisAdd
    BLAST
    Topological domaini225 – 24420CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini266 – 29025LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei78 – 9518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei141 – 16121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei164 – 18421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei204 – 22421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei245 – 26521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DGK1 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0170.
    HOGENOMiHOG000198978.
    KOiK16368.
    OMAiHLKSHEW.
    OrthoDBiEOG7VX96V.

    Family and domain databases

    InterProiIPR000374. PC_trans.
    [Graphical view]
    PfamiPF01148. CTP_transf_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12382-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGTEDAIALP NSTLEPRTEA KQRLSSKSHQ VSAKVTIPAK EEISSSDDDA    50
    HVPVTEIHLK SHEWFGDFIT KHEIPRKVFH SSIGFITLYL YTQGINYKNV 100
    LWPLIYAFII LFILDLIRLN WPFFNMLYCR TVGALMRKKE IHTYNGVLWY 150
    ILGLIFSFNF FSKDVTLISL FLLSWSDTAA ATIGRKYGHL TPKVARNKSL 200
    AGSIAAFTVG VITCWVFYGY FVPAYSYVNK PGEIQWSPET SRLSLNMLSL 250
    LGGVVAALSE GIDLFNWDDN FTIPVLSSLF MNAVIKTFKK 290
    Length:290
    Mass (Da):32,840
    Last modified:November 1, 1996 - v1
    Checksum:iF8A0EE6F1018025B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X90565 Genomic DNA. Translation: CAA62166.1 .
    Z75219 Genomic DNA. Translation: CAA99631.1 .
    BK006948 Genomic DNA. Translation: DAA11076.1 .
    PIRi S58323.
    RefSeqi NP_014956.3. NM_001183731.3.

    3D structure databases

    ProteinModelPortali Q12382.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34699. 223 interactions.
    DIPi DIP-5021N.
    MINTi MINT-561696.
    STRINGi 4932.YOR311C.

    Proteomic databases

    MaxQBi Q12382.
    PaxDbi Q12382.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR311C ; YOR311C ; YOR311C .
    GeneIDi 854488.
    KEGGi sce:YOR311C.

    Organism-specific databases

    CYGDi YOR311c.
    SGDi S000005838. DGK1.

    Phylogenomic databases

    eggNOGi COG0170.
    HOGENOMi HOG000198978.
    KOi K16368.
    OMAi HLKSHEW.
    OrthoDBi EOG7VX96V.

    Enzyme and pathway databases

    BioCyci MetaCyc:G3O-33794-MONOMER.
    YEAST:G3O-33794-MONOMER.
    SABIO-RK Q12382.

    Miscellaneous databases

    NextBioi 976813.

    Gene expression databases

    Genevestigatori Q12382.

    Family and domain databases

    InterProi IPR000374. PC_trans.
    [Graphical view ]
    Pfami PF01148. CTP_transf_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 92 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