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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

1-acylglycerol-3-phosphate O-acyltransferase 5

This gene encodes a member of the 1-acylglycerol-3-phosphate O-acyltransferase family. This integral membrane protein converts lysophosphatidic acid to phosphatidic acid, the second step in de novo phospholipid biosynthesis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, LPAAT3, AGPAT4, AMMECR1, SRP1
Papers on AGPAT5
Identification of miR-26 as a key mediator of estrogen stimulated cell proliferation by targeting CHD1, GREB1 and KPNA2.
Zhu et al., In Breast Cancer Res, 2013
Screening of estrogen responsive genes, which were also predicted to be targeted by miR-26, identified GREB1 and nine other genes (AGPAT5, AMMECR1, CHD1, ERLIN1, HSPA8, KPNA2, MREG, NARG1, and PLOD2).
Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria.
Agarwal et al., Dallas, United States. In J Lipid Res, 2011
enzymatic properties, tissue distribution, and subcellular localization of human AGPAT3 and AGPAT5
Lipid defect underlies selective skin barrier impairment of an epidermal-specific deletion of Gata-3.
Segre et al., Bethesda, United States. In J Cell Biol, 2006
Genomic analysis identifies highly conserved GATA-3 binding sites bound in vivo by GATA-3 in the first intron of the lipid acyltransferase gene AGPAT5.
Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity.
Garg et al., Dallas, United States. In Arch Biochem Biophys, 2006
AGPAT8 is most closely related to AGPAT5, and its cDNA is expressed most in the heart, while AGPAT5 is expressed more in the prostate and testis.
Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart.
Choy et al., Winnipeg, Canada. In Biochem J, 2005
This publication describes the molecular cloning, tissue distribution, and enzyme characterization of the mouse homolog, mAGPAT5.
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