[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Umbilical vein endothelial cell; DOI=10.1074/jbc.271.17.10230; PubMed=8626589 [NCBI, ExPASy, EBI, Israel, Japan] Tang W., Bunting M., Zimmerman G.A., McIntyre T.M., Prescott S.M.; "Molecular cloning of a novel human diacylglycerol kinase highly selective for arachidonate-containing substrates."; J. Biol. Chem. 271:10237-10241(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-154. DOI=10.1016/S0378-1119(99)00345-5; PubMed=10571048 [NCBI, ExPASy, EBI, Israel, Japan] Tang W., Bardien S., Bhattacharya S.S., Prescott S.M.; "Characterization of the human diacylglycerol kinase epsilon gene and its assessment as a candidate for inherited retinitis pigmentosa."; Gene 239:185-192(1999).
[3]	VARIANT [LARGE SCALE ANALYSIS] ARG-99. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Highly selective for arachidonate-containing species of diacylglycerol (DAG). May terminate signals transmitted through arachidonoyl-DAG or may contribute to the synthesis of phospholipids with defined fatty acid composition.
CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate.
INTERACTION:
Q9Y266:NUDC; NbExp=1; IntAct=EBI-1057499, EBI-357298;
Q9BZD4:NUF2; NbExp=1; IntAct=EBI-1057499, EBI-999865;
P22234:PAICS; NbExp=1; IntAct=EBI-1057499, EBI-712261;
P08559:PDHA1; NbExp=1; IntAct=EBI-1057499, EBI-715747;
Q01105:SET; NbExp=1; IntAct=EBI-1057499, EBI-1053182;
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (Potential).
TISSUE SPECIFICITY: Expressed predominantly in testis.
SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase family.
SIMILARITY: Contains 1 DAGKc domain.
SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U49379; AAC50497.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF136745; AAD45666.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_003638.1; -.

UniGene

Hs.591179

3D structure databases

ModBase

P52429.

Protein-protein interaction databases

IntAct

P52429; 7.

PTM databases

PhosphoSite

P52429; -.

Organism-specific databases

GC17P052266; -.

HIX0039161; -.

HGNC:2852; DGKE.

HPA017167; -.

601440; gene. [NCBI / EBI]

PharmGKB

PA27313; -.

GeneCards

P52429.

Gene expression databases

ArrayExpress

P52429; -.

CleanEx

HS_DGKE; -.

GermOnline

ENSG00000153933; Homo sapiens.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005524;	Molecular function: ATP binding (traceable author statement from ProtInc).
GO:0019992;	Molecular function: diacylglycerol binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004143;	Molecular function: diacylglycerol kinase activity (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007205;	Biological process: activation of protein kinase C activity (inferred from electronic annotation from InterPro).
GO:0008654;	Biological process: phospholipid biosynthetic process (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR002219; DAG_PE_bd.
IPR000756; DAGKa.
IPR001206; DAGKc.
Graphical view of domain structure.

Pfam

PF00130; C1_1; 2.
PF00609; DAGK_acc; 1.
PF00781; DAGK_cat; 1.
Pfam graphical view of domain structure.

ProDom

PD002939; DAGKa; 1.
PD005043; DAGKc; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00109; C1; 2.
SM00045; DAGKa; 1.
SM00046; DAGKc; 1.
SMART graphical view of domain structure.

PROSITE

PS00479; ZF_DAG_PE_1; 2.
PS50081; ZF_DAG_PE_2; 2.
PROSITE graphical view of domain structure (profiles).

Proteomics databases

PRIDE

P52429; -.

Genome annotation databases

Ensembl

ENSG00000153933; Homo sapiens. [Contig view]

GeneID

8526; -.

KEGG

hsa:8526; -.

Phylogenomic databases

HOGENOM

P52429; -.

HOVERGEN

P52429; -.

Other

31924; -.

DGKE; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Kinase; Membrane; Metal-binding; Phorbol-ester binding; Polymorphism; Repeat; Transferase; Transmembrane; Zinc; Zinc-finger.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 567`	`567`	`Diacylglycerol kinase epsilon.`	`PRO_0000218464`
`TRANSMEM`	`22 42`	`21`	`Potential.`
`TRANSMEM`	`436 456`	`21`	`Potential.`
`DOMAIN`	`219 350`	`132`	`DAGKc.`
`ZN_FING`	`59 108`	`50`	`Phorbol-ester/DAG-type 1.`
`ZN_FING`	`124 177`	`54`	`Phorbol-ester/DAG-type 2.`
`VARIANT`	`99 99`	`1`	`L -> R (in a breast cancer sample; somatic mutation).`	`VAR_036120`

Sequence information

Length: 567 AA [This is the length of the unprocessed precursor]

Molecular weight: 63927 Da [This is the MW of the unprocessed precursor]

CRC64: BC334AD15FB4D0B4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEAERRPAPG SPSEGLFADG HLILWTLCSV LLPVFITFWC SLQRSRRQLH RRDIFRKSKH 

        70         80         90        100        110        120 
GWRDTDLFSQ PTYCCVCAQH ILQGAFCDCC GLRVDEGCLR KADKRFQCKE IMLKNDTKVL 

       130        140        150        160        170        180 
DAMPHHWIRG NVPLCSYCMV CKQQCGCQPK LCDYRCIWCQ KTVHDECMKN SLKNEKCDFG 

       190        200        210        220        230        240 
EFKNLIIPPS YLTSINQMRK DKKTDYEVLA SKLGKQWTPL IILANSRSGT NMGEGLLGEF 

       250        260        270        280        290        300 
RILLNPVQVF DVTKTPPIKA LQLCTLLPYY SARVLVCGGD GTVGWVLDAV DDMKIKGQEK 

       310        320        330        340        350        360 
YIPQVAVLPL GTGNDLSNTL GWGTGYAGEI PVAQVLRNVM EADGIKLDRW KVQVTNKGYY 

       370        380        390        400        410        420 
NLRKPKEFTM NNYFSVGPDA LMALNFHAHR EKAPSLFSSR ILNKAVYLFY GTKDCLVQEC 

       430        440        450        460        470        480 
KDLNKKVELE LDGERVALPS LEGIIVLNIG YWGGGCRLWE GMGDETYPLA RHDDGLLEVV 

       490        500        510        520        530        540 
GVYGSFHCAQ IQVKLANPFR IGQAHTVRLI LKCSMMPMQV DGEPWAQGPC TVTITHKTHA 

       550        560 
MMLYFSGEQT DDDISSTSDQ EDIKATE

P52429 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools