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P52824

- DGKQ_HUMAN

UniProt

P52824 - DGKQ_HUMAN

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Protein

Diacylglycerol kinase theta

Gene

DGKQ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Inactivated by binding to RHOA. Not inhibited by phosphatidylserine.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 10849Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri121 – 16848Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23452Phorbol-ester/DAG-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. activating transcription factor binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. diacylglycerol kinase activity Source: UniProtKB
  4. kinase binding Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW
  6. NAD+ kinase activity Source: InterPro
  7. phospholipase binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. cAMP-mediated signaling Source: UniProtKB
  3. G-protein coupled receptor signaling pathway Source: UniProtKB
  4. platelet activation Source: Reactome
  5. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
  6. protein kinase C signaling Source: UniProtKB
  7. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  8. response to ATP Source: UniProtKB
  9. thrombin receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_2202. Effects of PIP2 hydrolysis.

Names & Taxonomyi

Protein namesi
Recommended name:
Diacylglycerol kinase theta (EC:2.7.1.107)
Short name:
DAG kinase theta
Alternative name(s):
Diglyceride kinase theta
Short name:
DGK-theta
Gene namesi
Name:DGKQ
Synonyms:DAGK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:2856. DGKQ.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. nuclear speck Source: UniProtKB
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi100 – 1001C → G: Abolishes translocation to the plasma membrane. 1 Publication
Mutagenesisi160 – 1601C → G: Abolishes translocation to the plasma membrane. 1 Publication
Mutagenesisi226 – 2261C → G: Abolishes translocation to the plasma membrane. 1 Publication
Mutagenesisi237 – 2371G → R: Abolishes enzymatic activity; no effect on translocation to the plasma membrane. 2 Publications
Mutagenesisi245 – 2451P → A or L: Greatly reduces enzymatic activity. 1 Publication
Mutagenesisi246 – 2461P → L: Abolishes enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA27317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 942942Diacylglycerol kinase thetaPRO_0000218467Add
BLAST

Post-translational modificationi

Phosphorylated by PRKCE and PRKCH in vitro.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP52824.
PaxDbiP52824.
PRIDEiP52824.

PTM databases

PhosphoSiteiP52824.

Expressioni

Gene expression databases

BgeeiP52824.
CleanExiHS_DGKQ.
ExpressionAtlasiP52824. baseline and differential.
GenevestigatoriP52824.

Organism-specific databases

HPAiCAB033835.
HPA026797.

Interactioni

Subunit structurei

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.5 Publications

Protein-protein interaction databases

BioGridi107979. 8 interactions.
STRINGi9606.ENSP00000273814.

Structurei

3D structure databases

ProteinModelPortaliP52824.
SMRiP52824. Positions 54-108, 184-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini395 – 494100Ras-associatingPROSITE-ProRule annotationAdd
BLAST
Domaini584 – 721138DAGKcPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi555 – 5595LXXLL motif 1
Motifi574 – 5785LXXLL motif 2

Domaini

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

Sequence similaritiesi

Contains 1 DAGKc domain.PROSITE-ProRule annotation
Contains 3 phorbol-ester/DAG-type zinc fingers.PROSITE-ProRule annotation
Contains 1 Ras-associating domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri60 – 10849Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri121 – 16848Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri183 – 23452Phorbol-ester/DAG-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG47311.
GeneTreeiENSGT00760000119050.
HOGENOMiHOG000007900.
HOVERGENiHBG094675.
InParanoidiP52824.
KOiK00901.
OMAiSDFIWGL.
OrthoDBiEOG71VSS6.
PhylomeDBiP52824.
TreeFamiTF312817.

Family and domain databases

InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. PE/DAG-bd.
IPR000159. Ras-assoc.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PfamiPF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF00788. RA. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 3 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50146. DAGK. 1 hit.
PS50200. RA. 1 hit.
PS00479. ZF_DAG_PE_1. 3 hits.
PS50081. ZF_DAG_PE_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52824-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAAEPGAR AWLGGGSPRP GSPACSPVLG SGGRARPGPG PGPGPERAGV
60 70 80 90 100
RAPGPAAAPG HSFRKVTLTK PTFCHLCSDF IWGLAGFLCD VCNFMSHEKC
110 120 130 140 150
LKHVRIPCTS VAPSLVRVPV AHCFGPRGLH KRKFCAVCRK VLEAPALHCE
160 170 180 190 200
VCELHLHPDC VPFACSDCRQ CHQDGHQDHD THHHHWREGN LPSGARCEVC
210 220 230 240 250
RKTCGSSDVL AGVRCEWCGV QAHSLCSAAL APECGFGRLR SLVLPPACVR
260 270 280 290 300
LLPGGFSKTQ SFRIVEAAEP GEGGDGADGS AAVGPGRETQ ATPESGKQTL
310 320 330 340 350
KIFDGDDAVR RSQFRLVTVS RLAGAEEVLE AALRAHHIPE DPGHLELCRL
360 370 380 390 400
PPSSQACDAW AGGKAGSAVI SEEGRSPGSG EATPEAWVIR ALPRAQEVLK
410 420 430 440 450
IYPGWLKVGV AYVSVRVTPK STARSVVLEV LPLLGRQAES PESFQLVEVA
460 470 480 490 500
MGCRHVQRTM LMDEQPLLDR LQDIRQMSVR QVSQTRFYVA ESRDVAPHVS
510 520 530 540 550
LFVGGLPPGL SPEEYSSLLH EAGATKATVV SVSHIYSSQG AVVLDVACFA
560 570 580 590 600
EAERLYMLLK DMAVRGRLLT ALVLPDLLHA KLPPDSCPLL VFVNPKSGGL
610 620 630 640 650
KGRDLLCSFR KLLNPHQVFD LTNGGPLPGL HLFSQVPCFR VLVCGGDGTV
660 670 680 690 700
GWVLGALEET RYRLACPEPS VAILPLGTGN DLGRVLRWGA GYSGEDPFSV
710 720 730 740 750
LLSVDEADAV LMDRWTILLD AHEAGSAEND TADAEPPKIV QMSNYCGIGI
760 770 780 790 800
DAELSLDFHQ AREEEPGKFT SRLHNKGVYV RVGLQKISHS RSLHKQIRLQ
810 820 830 840 850
VERQEVELPS IEGLIFINIP SWGSGADLWG SDSDTRFEKP RMDDGLLEVV
860 870 880 890 900
GVTGVVHMGQ VQGGLRSGIR IAQGSYFRVT LLKATPVQVD GEPWVQAPGH
910 920 930 940
MIISAAGPKV HMLRKAKQKP RRAGTTRDAR ADAAPAPESD PR
Length:942
Mass (Da):101,155
Last modified:September 1, 2009 - v2
Checksum:i836D4FCBC208A5B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 462PE → RD in AAA98749. (PubMed:7607687)Curated
Sequence conflicti50 – 567VRAPGPA → GVRARAR in AAA98749. (PubMed:7607687)Curated
Sequence conflicti933 – 9331A → R in AAA98749. (PubMed:7607687)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271P → L.1 Publication
Corresponds to variant rs17855876 [ dbSNP | Ensembl ].
VAR_058478

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L38707 mRNA. Translation: AAA98749.1.
AC019103 Genomic DNA. No translation available.
BC063801 mRNA. Translation: AAH63801.1.
CCDSiCCDS3342.1.
RefSeqiNP_001338.2. NM_001347.3.
UniGeneiHs.584858.

Genome annotation databases

EnsembliENST00000273814; ENSP00000273814; ENSG00000145214.
ENST00000621998; ENSP00000482164; ENSG00000145214.
GeneIDi1609.
KEGGihsa:1609.
UCSCiuc003gbw.4. human.

Polymorphism databases

DMDMi257051005.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L38707 mRNA. Translation: AAA98749.1 .
AC019103 Genomic DNA. No translation available.
BC063801 mRNA. Translation: AAH63801.1 .
CCDSi CCDS3342.1.
RefSeqi NP_001338.2. NM_001347.3.
UniGenei Hs.584858.

3D structure databases

ProteinModelPortali P52824.
SMRi P52824. Positions 54-108, 184-234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107979. 8 interactions.
STRINGi 9606.ENSP00000273814.

PTM databases

PhosphoSitei P52824.

Polymorphism databases

DMDMi 257051005.

Proteomic databases

MaxQBi P52824.
PaxDbi P52824.
PRIDEi P52824.

Protocols and materials databases

DNASUi 1609.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000273814 ; ENSP00000273814 ; ENSG00000145214 .
ENST00000621998 ; ENSP00000482164 ; ENSG00000145214 .
GeneIDi 1609.
KEGGi hsa:1609.
UCSCi uc003gbw.4. human.

Organism-specific databases

CTDi 1609.
GeneCardsi GC04M000942.
HGNCi HGNC:2856. DGKQ.
HPAi CAB033835.
HPA026797.
MIMi 601207. gene.
neXtProti NX_P52824.
PharmGKBi PA27317.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47311.
GeneTreei ENSGT00760000119050.
HOGENOMi HOG000007900.
HOVERGENi HBG094675.
InParanoidi P52824.
KOi K00901.
OMAi SDFIWGL.
OrthoDBi EOG71VSS6.
PhylomeDBi P52824.
TreeFami TF312817.

Enzyme and pathway databases

Reactomei REACT_2202. Effects of PIP2 hydrolysis.

Miscellaneous databases

GeneWikii DGKQ.
GenomeRNAii 1609.
NextBioi 6614.
PROi P52824.
SOURCEi Search...

Gene expression databases

Bgeei P52824.
CleanExi HS_DGKQ.
ExpressionAtlasi P52824. baseline and differential.
Genevestigatori P52824.

Family and domain databases

InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. PE/DAG-bd.
IPR000159. Ras-assoc.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
Pfami PF00130. C1_1. 2 hits.
PF00609. DAGK_acc. 1 hit.
PF00781. DAGK_cat. 1 hit.
PF00788. RA. 1 hit.
[Graphical view ]
SMARTi SM00109. C1. 3 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view ]
SUPFAMi SSF111331. SSF111331. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEi PS50146. DAGK. 1 hit.
PS50200. RA. 1 hit.
PS00479. ZF_DAG_PE_1. 3 hits.
PS50081. ZF_DAG_PE_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PLCB1.
  6. 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.

Entry informationi

Entry nameiDGKQ_HUMAN
AccessioniPrimary (citable) accession number: P52824
Secondary accession number(s): Q6P3W4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: September 1, 2009
Last modified: October 29, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3