Diacylglycerol kinase theta - Homo sapiens (Human)

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P52824 (DGKQ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 109. History...

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

Documents (5) |

Third-party data

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

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	942 AA.
Sequence status	Complete.
Protein existence	Evidence 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-diacylglycerol = 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. Cytoplasm › cytoskeleton. 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 component	Cell membrane Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cAMP-mediated signaling Inferred from direct assay Ref.8. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome protein kinase C signaling cascade Inferred from direct assay Ref.7. Source: UniProtKB protein kinase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro response to ATP Inferred from direct assay Ref.7. Source: UniProtKB thrombin receptor signaling pathway Inferred from direct assay Ref.7. Source: UniProtKB
Cellular_component	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 plasma membrane Inferred from direct assay Ref.4 Ref.7. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW diacylglycerol kinase activity Inferred from direct assay Ref.4 Ref.7. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 942

942

Diacylglycerol kinase theta

PRO_0000218467

Regions

Domain

395 – 494

100

Ras-associating

Domain

584 – 721

138

DAGKc

Zinc finger

60 – 108

Phorbol-ester/DAG-type 1

Zinc finger

121 – 168

Phorbol-ester/DAG-type 2

Zinc finger

183 – 234

Phorbol-ester/DAG-type 3

Motif

555 – 559

LXXLL motif 1

Motif

574 – 578

LXXLL motif 2

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Natural variations

Natural variant

P → L. Ref.3
Corresponds to variant rs17855876 [ dbSNP | Ensembl ].

VAR_058478

Experimental info

Mutagenesis

100

C → G: Abolishes translocation to the plasma membrane. Ref.7

Mutagenesis

160

C → G: Abolishes translocation to the plasma membrane. Ref.7

Mutagenesis

226

C → G: Abolishes translocation to the plasma membrane. Ref.7

Mutagenesis

237

G → R: Abolishes enzymatic activity; no effect on translocation to the plasma membrane. Ref.6 Ref.7

Mutagenesis

245

P → A or L: Greatly reduces enzymatic activity. Ref.6

Mutagenesis

246

P → L: Abolishes enzymatic activity. Ref.6

Sequence conflict

45 – 46

PE → RD in AAA98749. Ref.1

Sequence conflict

50 – 56

VRAPGPA → GVRARAR in AAA98749. Ref.1

Sequence conflict

933

A → R in AAA98749. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P52824 [UniParc].

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

FASTA

942

101,155

        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' referencesShow '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. 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.
IPI	IPI00005565.
RefSeq	NP_001338.2. NM_001347.3.
UniGene	Hs.584858.
3D structure databases
ProteinModelPortal	P52824.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000273814.
PTM databases
PhosphoSite	P52824.
Polymorphism databases
DMDM	257051005.
Proteomic databases
PaxDb	P52824.
PRIDE	P52824.
Protocols and materials databases
DNASU	1609.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273814; ENSP00000273814; ENSG00000145214.
GeneID	1609.
KEGG	hsa:1609.
UCSC	uc003gbw.3. human.
Organism-specific databases
CTD	1609.
GeneCards	GC04M000942.
HGNC	HGNC:2856. DGKQ.
HPA	HPA026797.
MIM	601207. gene.
neXtProt	NX_P52824.
PharmGKB	PA27317.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG47311.
HOGENOM	HOG000007900.
HOVERGEN	HBG094675.
InParanoid	P52824.
KO	K00901.
OMA	TKPTFCH.
OrthoDB	EOG49KFPV.
PhylomeDB	P52824.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P52824.
Bgee	P52824.
CleanEx	HS_DGKQ.
Genevestigator	P52824.
GermOnline	ENSG00000145214. Homo sapiens.
Family and domain databases
InterPro	IPR000756. Diacylglycerol_kin_accessory. IPR001206. Diacylglycerol_kinase_cat_dom. IPR002219. Prot_Kinase_C-like_PE/DAG-bd. IPR000159. Ras-assoc. [Graphical view]
Pfam	PF00130. C1_1. 2 hits. PF00609. DAGK_acc. 1 hit. PF00781. DAGK_cat. 1 hit. PF00788. RA. 1 hit. [Graphical view]
SMART	SM00109. C1. 3 hits. SM00045. DAGKa. 1 hit. SM00046. DAGKc. 1 hit. SM00314. RA. 1 hit. [Graphical view]
PROSITE	PS50146. DAGK. 1 hit. PS50200. RA. 1 hit. PS00479. ZF_DAG_PE_1. 3 hits. PS50081. ZF_DAG_PE_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	1609.
NextBio	6614.
SOURCE	Search...

Entry information

Entry name

DGKQ_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism 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