DGKQ

DGKQ
Identifiers
Aliases DGKQ, DAGK, DAGK4, DAGK7, diacylglycerol kinase theta
External IDs MGI: 102918 HomoloGene: 20352 GeneCards: DGKQ
Genetically Related Diseases
Parkinson's disease[1]
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

1609

110524

Ensembl

ENSG00000145214

ENSMUSG00000004815

UniProt

P52824

Q6P5E8

RefSeq (mRNA)

NM_001347

NM_199011

RefSeq (protein)

NP_001338.2

NP_950176.1

Location (UCSC) Chr 4: 0.96 – 0.99 Mb Chr 5: 108.65 – 108.67 Mb
PubMed search [2] [3]
Wikidata
View/Edit HumanView/Edit Mouse

Diacylglycerol kinase theta is an enzyme that in humans is encoded by the DGKQ gene.[4][5][6]

The protein encoded by this gene contains three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain. It is localized in the speckle domains of the nucleus, and mediates the regeneration of phosphatidylinositol (PI) from diacylglycerol in the PI-cycle during cell signal transduction.[6]

Interactions

DGKQ has been shown to interact with RHOA.[7]

References

  1. "Diseases that are genetically associated with DGKQ view/edit references on wikidata".
  2. "Human PubMed Reference:".
  3. "Mouse PubMed Reference:".
  4. Endele S, Zabel B, Winterpacht A (Jun 1996). "Assignment of the human diacylglycerol kinase 4 (DAGK4) gene to chromosome 4p16.3". Genomics. 33 (1): 145–6. doi:10.1006/geno.1996.0174. PMID 8617502.
  5. Houssa B, Schaap D, van der Wal J, Goto K, Kondo H, Yamakawa A, Shibata M, Takenawa T, van Blitterswijk WJ (May 1997). "Cloning of a novel human diacylglycerol kinase (DGKtheta) containing three cysteine-rich domains, a proline-rich region, and a pleckstrin homology domain with an overlapping Ras-associating domain". J Biol Chem. 272 (16): 10422–8. doi:10.1074/jbc.272.16.10422. PMID 9099683.
  6. 1 2 "Entrez Gene: DGKQ diacylglycerol kinase, theta 110kDa".
  7. Houssa, B; de Widt J; Kranenburg O; Moolenaar W H; van Blitterswijk W J (Mar 1999). "Diacylglycerol kinase theta binds to and is negatively regulated by active RhoA". J. Biol. Chem. UNITED STATES. 274 (11): 6820–2. doi:10.1074/jbc.274.11.6820. ISSN 0021-9258. PMID 10066731.

Further reading


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