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Q6P5E8

- DGKQ_MOUSE

UniProt

Q6P5E8 - DGKQ_MOUSE

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Protein

Diacylglycerol kinase theta

Gene
Dgkq
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 similarity.

Catalytic activityi

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

Enzyme regulationi

Inactivated by binding to RHOA. Not inhibited by phosphatidylserine By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri54 – 10249Phorbol-ester/DAG-type 1Add
BLAST
Zinc fingeri115 – 16248Phorbol-ester/DAG-type 2Add
BLAST
Zinc fingeri177 – 22852Phorbol-ester/DAG-type 3Add
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. diacylglycerol kinase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW
  4. NAD+ kinase activity Source: InterPro

GO - Biological processi

  1. cAMP-mediated signaling Source: Ensembl
  2. protein kinase C-activating G-protein coupled receptor signaling pathway Source: InterPro
  3. protein kinase C signaling Source: Ensembl
  4. response to ATP Source: Ensembl
  5. thrombin receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_219232. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:102918. Dgkq.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity. Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Nucleus speckle By similarity
Note: Translocates to the nucleus in response to thrombin stimulation By similarity. Translocates to the plasma membrane in response to steroid hormone receptor stimulation By similarity. 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. cytoskeleton Source: UniProtKB-SubCell
  2. cytosol Source: Ensembl
  3. nuclear speck Source: UniProtKB-SubCell
  4. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 934934Diacylglycerol kinase thetaPRO_0000381763Add
BLAST

Post-translational modificationi

Phosphorylated by PRKCE and PRKCH in vitro By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ6P5E8.
PRIDEiQ6P5E8.

PTM databases

PhosphoSiteiQ6P5E8.

Expressioni

Gene expression databases

BgeeiQ6P5E8.
GenevestigatoriQ6P5E8.

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 By similarity.

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000057859.

Structurei

3D structure databases

ProteinModelPortaliQ6P5E8.
SMRiQ6P5E8. Positions 50-102, 178-229.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini387 – 486100Ras-associatingAdd
BLAST
Domaini576 – 713138DAGKcAdd
BLAST

Sequence similaritiesi

Contains 1 DAGKc domain.

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG47311.
GeneTreeiENSGT00750000117493.
HOGENOMiHOG000007900.
InParanoidiQ6P5E8.
KOiK00901.
OMAiSDFIWGL.
OrthoDBiEOG71VSS6.
PhylomeDBiQ6P5E8.
TreeFamiTF312817.

Family and domain databases

InterProiIPR016064. ATP-NAD_kinase_PpnK-typ.
IPR020454. DAG/PE-bd.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. Prot_Kinase_C-like_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. 2 hits.
[Graphical view]
PRINTSiPR00008. DAGPEDOMAIN.
SMARTiSM00109. C1. 3 hits.
SM00045. DAGKa. 1 hit.
SM00046. DAGKc. 1 hit.
SM00314. RA. 1 hit.
[Graphical view]
SUPFAMiSSF111331. SSF111331. 1 hit.
SSF54236. SSF54236. 2 hits.
PROSITEiPS50146. DAGK. 1 hit.
PS50200. RA. 1 hit.
PS00479. ZF_DAG_PE_1. 3 hits.
PS50081. ZF_DAG_PE_2. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6P5E8-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAAAAEPGAR TWPGSGSPRL GSPAGSPVLG ISGRTRPGSG PERTSRAIGS    50
AAPGHSFRKV TLTKPTFCHL CSDFIWGLAG FLCDVCNFMS HEKCLKQVKT 100
PCTSIAPSLV RVPVAHCFGS LGLYKRKFCV VCRKSLEVPA FRCEVCELHV 150
HPDCVPFACS DCRQCHQDGQ QDYDTYHHHW REGNLPSGAR CEVCRKTCGS 200
SDVLAGVRCE WCGVQAHSVC STALAPECTF GRLRSMVLPP SCVRLLSRNF 250
SKMHCFRIPE TMVLELGDGD DGVDGSAAIG TGREVLTATE STKQTLKIFD 300
GNDSMRKNQF RLVTVSRLAR NEEVMEAALR AYYISEDPKD FQLQALPLSG 350
NAQALGKAGT TEEEASKGSC PRDSVPEAWV IRSLPRTQEI LKIYPGWLKV 400
GVAYVSIRVN SQSTARSVVQ EVLPLFGQQV EDKERFQLIE VLMSSRQVQR 450
TVLADEEPLL DRLWDIRQTS VRQVSQTRFY VAETRATAPR VSLFVGGLPP 500
GLSPQDYSNL LHEAMATKAA VVSVSHVYSL QGAVILDVTC FAEAERLYML 550
ARDTAVHGRP LTALVLPDVL HTKLPPDCCP LLVFVNPKSG GLKGRELLCS 600
FRKLLNPHQV FELTNGGPLP GFHLFSQVPS FRVLVCGGDG TVGWVLAALE 650
ETRRHLACPE PSVAILPLGT GNDLGRVLRW GAGYSGEDPF SVLVSVDEAD 700
AVLMDRWTIL LDAHEIDSTE NNVVETEPPK IVQMNNYCGI GIDAELSLDF 750
HQAREEEPGK FTSRFHNKGV YVRVGLQKIS HSRSLHKEIR LQVEQQEVEL 800
PSIEGLIFIN IPSWGSGADL WGSDNDSRFE KPRIDDGLLE VVGVTGVVHM 850
GQVQGGLRSG IRIAQGSYFR VTLLKATPVQ VDGEPWVQAP GHMIISATAP 900
KVHMLRKAKQ KPRKAGANRD TRVDTLPAPE GNPL 934
Length:934
Mass (Da):102,254
Last modified:July 5, 2004 - v1
Checksum:iC7FA90936443818E
GO
Isoform 2 (identifier: Q6P5E8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-548: Missing.

Note: No experimental confirmation available.

Show »
Length:386
Mass (Da):42,209
Checksum:i8430D1C19674B841
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 548548Missing in isoform 2. VSP_037832Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK134745 mRNA. Translation: BAE22264.1.
BC062929 mRNA. Translation: AAH62929.1.
CCDSiCCDS19515.1. [Q6P5E8-1]
RefSeqiNP_950176.1. NM_199011.1. [Q6P5E8-1]
UniGeneiMm.260921.

Genome annotation databases

EnsembliENSMUST00000053913; ENSMUSP00000057859; ENSMUSG00000004815. [Q6P5E8-1]
GeneIDi110524.
KEGGimmu:110524.
UCSCiuc008yot.1. mouse. [Q6P5E8-1]
uc012eau.1. mouse. [Q6P5E8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK134745 mRNA. Translation: BAE22264.1 .
BC062929 mRNA. Translation: AAH62929.1 .
CCDSi CCDS19515.1. [Q6P5E8-1 ]
RefSeqi NP_950176.1. NM_199011.1. [Q6P5E8-1 ]
UniGenei Mm.260921.

3D structure databases

ProteinModelPortali Q6P5E8.
SMRi Q6P5E8. Positions 50-102, 178-229.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000057859.

PTM databases

PhosphoSitei Q6P5E8.

Proteomic databases

PaxDbi Q6P5E8.
PRIDEi Q6P5E8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053913 ; ENSMUSP00000057859 ; ENSMUSG00000004815 . [Q6P5E8-1 ]
GeneIDi 110524.
KEGGi mmu:110524.
UCSCi uc008yot.1. mouse. [Q6P5E8-1 ]
uc012eau.1. mouse. [Q6P5E8-2 ]

Organism-specific databases

CTDi 1609.
MGIi MGI:102918. Dgkq.

Phylogenomic databases

eggNOGi NOG47311.
GeneTreei ENSGT00750000117493.
HOGENOMi HOG000007900.
InParanoidi Q6P5E8.
KOi K00901.
OMAi SDFIWGL.
OrthoDBi EOG71VSS6.
PhylomeDBi Q6P5E8.
TreeFami TF312817.

Enzyme and pathway databases

Reactomei REACT_219232. Effects of PIP2 hydrolysis.

Miscellaneous databases

NextBioi 364149.
PROi Q6P5E8.
SOURCEi Search...

Gene expression databases

Bgeei Q6P5E8.
Genevestigatori Q6P5E8.

Family and domain databases

InterProi IPR016064. ATP-NAD_kinase_PpnK-typ.
IPR020454. DAG/PE-bd.
IPR000756. Diacylglycerol_kin_accessory.
IPR001206. Diacylglycerol_kinase_cat_dom.
IPR002219. Prot_Kinase_C-like_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. 2 hits.
[Graphical view ]
PRINTSi PR00008. DAGPEDOMAIN.
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. 2 hits.
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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  2. "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] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiDGKQ_MOUSE
AccessioniPrimary (citable) accession number: Q6P5E8
Secondary accession number(s): Q3UYE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 1, 2009
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi