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P52824 (DGKQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Diacylglycerol kinase theta

Short name=DAG kinase theta
EC=2.7.1.107
Alternative name(s):
Diglyceride kinase theta
Short name=DGK-theta
Gene names
Name:DGKQ
Synonyms:DAGK4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length942 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylates diacylglycerol (DAG) to generate phosphatidic acid (PA). May regulate the activity of protein kinase C by controlling the balance between these two signaling lipids. Activated in the nucleus in response to alpha-thrombin and nerve growth factor By similarity. May be involved in cAMP-induced activation of NR5A1 and subsequent steroidogenic gene transcription by delivering PA as ligand for NR5A1. Acts synergistically with NR5A1 on CYP17 transcriptional activity. Ref.8

Catalytic activity

ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.4

Enzyme regulation

Inactivated by binding to RHOA. Not inhibited by phosphatidylserine.

Subunit structure

Interacts with RHOA (constitutively activated, GTP-bound); the interaction inhibits DGKQ. Interacts with PRKCE. Interacts with PRKCH. Interacts with PLCB1. Interacts with NR5A1; the interaction requires the LXXLL motif 1 and LXXLL motif 2 in DGKQ. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm. Cell membrane. Cytoplasmcytoskeleton. Nucleus. Nucleus speckle. Note: Translocates to the nucleus in response to thrombin stimulation By similarity. Translocates to the plasma membrane in response to steroid hormone receptor stimulation. Translocation to the plasma membrane is dependent on G-protein coupled receptor stimulation and subsequent activation of PRKCE and probably PRKCH. Ref.4 Ref.5 Ref.7

Domain

The L-X-X-L-L repeats are implicated in binding to the nuclear receptor NR5A1.

Post-translational modification

Phosphorylated by PRKCE and PRKCH in vitro.

Sequence similarities

Belongs to the eukaryotic diacylglycerol kinase family.

Contains 1 DAGKc domain.

Contains 3 phorbol-ester/DAG-type zinc fingers.

Contains 1 Ras-associating domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from mutant phenotype Ref.7. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cAMP-mediated signaling

Inferred from direct assay Ref.8. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

protein kinase C signaling

Inferred from direct assay Ref.7. Source: UniProtKB

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: InterPro

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.8. Source: UniProtKB

response to ATP

Inferred from direct assay Ref.7. Source: UniProtKB

thrombin receptor signaling pathway

Inferred from direct assay Ref.7. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytoskeleton

Inferred from direct assay Ref.4. Source: UniProtKB

cytosol

Inferred from direct assay Ref.4. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.5. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7Ref.8. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.4Ref.7. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NAD+ kinase activity

Inferred from electronic annotation. Source: InterPro

activating transcription factor binding

Inferred from physical interaction Ref.8. Source: UniProtKB

diacylglycerol kinase activity

Inferred from direct assay Ref.4Ref.7. Source: UniProtKB

kinase binding

Inferred from physical interaction Ref.7. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase binding

Inferred from physical interaction Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 942942Diacylglycerol kinase theta
PRO_0000218467

Regions

Domain395 – 494100Ras-associating
Domain584 – 721138DAGKc
Zinc finger60 – 10849Phorbol-ester/DAG-type 1
Zinc finger121 – 16848Phorbol-ester/DAG-type 2
Zinc finger183 – 23452Phorbol-ester/DAG-type 3
Motif555 – 5595LXXLL motif 1
Motif574 – 5785LXXLL motif 2

Natural variations

Natural variant271P → L. Ref.3
Corresponds to variant rs17855876 [ dbSNP | Ensembl ].
VAR_058478

Experimental info

Mutagenesis1001C → G: Abolishes translocation to the plasma membrane. Ref.7
Mutagenesis1601C → G: Abolishes translocation to the plasma membrane. Ref.7
Mutagenesis2261C → G: Abolishes translocation to the plasma membrane. Ref.7
Mutagenesis2371G → R: Abolishes enzymatic activity; no effect on translocation to the plasma membrane. Ref.6 Ref.7
Mutagenesis2451P → A or L: Greatly reduces enzymatic activity. Ref.6
Mutagenesis2461P → L: Abolishes enzymatic activity. Ref.6
Sequence conflict45 – 462PE → RD in AAA98749. Ref.1
Sequence conflict50 – 567VRAPGPA → GVRARAR in AAA98749. Ref.1
Sequence conflict9331A → R in AAA98749. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P52824 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: 836D4FCBC208A5B6

FASTA942101,155
        10         20         30         40         50         60 
MAAAAEPGAR AWLGGGSPRP GSPACSPVLG SGGRARPGPG PGPGPERAGV RAPGPAAAPG 

        70         80         90        100        110        120 
HSFRKVTLTK PTFCHLCSDF IWGLAGFLCD VCNFMSHEKC LKHVRIPCTS VAPSLVRVPV 

       130        140        150        160        170        180 
AHCFGPRGLH KRKFCAVCRK VLEAPALHCE VCELHLHPDC VPFACSDCRQ CHQDGHQDHD 

       190        200        210        220        230        240 
THHHHWREGN LPSGARCEVC RKTCGSSDVL AGVRCEWCGV QAHSLCSAAL APECGFGRLR 

       250        260        270        280        290        300 
SLVLPPACVR LLPGGFSKTQ SFRIVEAAEP GEGGDGADGS AAVGPGRETQ ATPESGKQTL 

       310        320        330        340        350        360 
KIFDGDDAVR RSQFRLVTVS RLAGAEEVLE AALRAHHIPE DPGHLELCRL PPSSQACDAW 

       370        380        390        400        410        420 
AGGKAGSAVI SEEGRSPGSG EATPEAWVIR ALPRAQEVLK IYPGWLKVGV AYVSVRVTPK 

       430        440        450        460        470        480 
STARSVVLEV LPLLGRQAES PESFQLVEVA MGCRHVQRTM LMDEQPLLDR LQDIRQMSVR 

       490        500        510        520        530        540 
QVSQTRFYVA ESRDVAPHVS LFVGGLPPGL SPEEYSSLLH EAGATKATVV SVSHIYSSQG 

       550        560        570        580        590        600 
AVVLDVACFA EAERLYMLLK DMAVRGRLLT ALVLPDLLHA KLPPDSCPLL VFVNPKSGGL 

       610        620        630        640        650        660 
KGRDLLCSFR KLLNPHQVFD LTNGGPLPGL HLFSQVPCFR VLVCGGDGTV GWVLGALEET 

       670        680        690        700        710        720 
RYRLACPEPS VAILPLGTGN DLGRVLRWGA GYSGEDPFSV LLSVDEADAV LMDRWTILLD 

       730        740        750        760        770        780 
AHEAGSAEND TADAEPPKIV QMSNYCGIGI DAELSLDFHQ AREEEPGKFT SRLHNKGVYV 

       790        800        810        820        830        840 
RVGLQKISHS RSLHKQIRLQ VERQEVELPS IEGLIFINIP SWGSGADLWG SDSDTRFEKP 

       850        860        870        880        890        900 
RMDDGLLEVV GVTGVVHMGQ VQGGLRSGIR IAQGSYFRVT LLKATPVQVD GEPWVQAPGH 

       910        920        930        940 
MIISAAGPKV HMLRKAKQKP RRAGTTRDAR ADAAPAPESD PR 

« Hide

References

« Hide 'large scale' references
[1]"Chromosomal localization of three mouse diacylglycerol kinase (DAGK) genes: genes sharing sequence homology to the Drosophila retinal degeneration A (rdgA) gene."
Pilz A., Schaap D., Hunt D., Fitzgibbon J.
Genomics 26:599-601(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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], VARIANT LEU-27.
Tissue: Uterus.
[4]"Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA."
Houssa B., de Widt J., Kranenburg O., Moolenaar W.H., van Blitterswijk W.J.
J. Biol. Chem. 274:6820-6822(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
[5]"Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus."
Tabellini G., Bortul R., Santi S., Riccio M., Baldini G., Cappellini A., Billi A.M., Berezney R., Ruggeri A., Cocco L., Martelli A.M.
Exp. Cell Res. 287:143-154(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PLCB1.
[6]"Structure-activity relationship of diacylglycerol kinase theta."
Los A.P., van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.
Biochim. Biophys. Acta 1636:169-174(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHOA, MUTAGENESIS OF GLY-237; PRO-245 AND PRO-246.
[7]"Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C."
van Baal J., de Widt J., Divecha N., van Blitterswijk W.J.
J. Biol. Chem. 280:9870-9878(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRKCE AND PRKCH, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-100; CYS-160; CYS-226 AND GLY-237.
[8]"Cyclic AMP-stimulated interaction between steroidogenic factor 1 and diacylglycerol kinase theta facilitates induction of CYP17."
Li D., Urs A.N., Allegood J., Leon A., Merrill A.H. Jr., Sewer M.B.
Mol. Cell. Biol. 27:6669-6685(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NR5A1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L38707 mRNA. Translation: AAA98749.1.
AC019103 Genomic DNA. No translation available.
BC063801 mRNA. Translation: AAH63801.1.
RefSeqNP_001338.2. NM_001347.3.
UniGeneHs.584858.

3D structure databases

ProteinModelPortalP52824.
SMRP52824. Positions 54-108, 120-169, 184-234, 397-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107979. 8 interactions.
STRING9606.ENSP00000273814.

PTM databases

PhosphoSiteP52824.

Polymorphism databases

DMDM257051005.

Proteomic databases

PaxDbP52824.
PRIDEP52824.

Protocols and materials databases

DNASU1609.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273814; ENSP00000273814; ENSG00000145214.
GeneID1609.
KEGGhsa:1609.
UCSCuc003gbw.4. human.

Organism-specific databases

CTD1609.
GeneCardsGC04M000942.
HGNCHGNC:2856. DGKQ.
HPACAB033835.
HPA026797.
MIM601207. gene.
neXtProtNX_P52824.
PharmGKBPA27317.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47311.
HOGENOMHOG000007900.
HOVERGENHBG094675.
InParanoidP52824.
KOK00901.
OMASDFIWGL.
OrthoDBEOG71VSS6.
PhylomeDBP52824.
TreeFamTF312817.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP52824.
BgeeP52824.
CleanExHS_DGKQ.
GenevestigatorP52824.

Family and domain databases

InterProIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000159. Ras-assoc.
[Graphical view]
PfamPF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTSM00109. C1. 3 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMSSF111331. SSF111331. 1 hit.
PROSITEPS50146. DAGK. 1 hit.
PS50200. RA. 1 hit.
PS00479. ZF_DAG_PE_1. 3 hits.
PS50081. ZF_DAG_PE_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDGKQ.
GenomeRNAi1609.
NextBio6614.
PROP52824.
SOURCESearch...

Entry information

Entry nameDGKQ_HUMAN
AccessionPrimary (citable) accession number: P52824
Secondary accession number(s): Q6P3W4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM