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{{ | '''1-acyl-sn-glycerol-3-phosphate acyltransferase alpha''' is an [[enzyme]] that in humans is encoded by the ''AGPAT1'' [[gene]].<ref name="pmid9461603">{{cite journal | vauthors = Aguado B, Campbell RD | title = Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex | journal = J Biol Chem | volume = 273 | issue = 7 | pages = 4096–105 |date=Mar 1998 | pmid = 9461603 | pmc = | doi =10.1074/jbc.273.7.4096 }}</ref><ref name="pmid9291118">{{cite journal | vauthors = Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ | title = A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases | series = 326 | journal = Biochem J | volume = ( Pt 2) | issue = | pages = 455–61 |date=Sep 1997 | pmid = 9291118 | pmc = 1218691 | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: AGPAT1 1-acylglycerol-3-phosphate O-acyltransferase 1 (lysophosphatidic acid acyltransferase, alpha)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10554| accessdate = }}</ref> | ||
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| summary_text = This gene encodes an enzyme that converts lysophosphatidic acid (LPA) into phosphatidic acid (PA). LPA and PA are two | | summary_text = This gene encodes an enzyme that converts [[lysophosphatidic acid]] (LPA) into [[phosphatidic acid]] (PA). LPA and PA are two [[phospholipid]]s involved in [[signal transduction]] and in [[lipid biosynthesis]] in cells. This enzyme localizes to the [[endoplasmic reticulum]]. This gene is located in the [[class III region]] of the [[human major histocompatibility complex]]. [[Alternative splicing]] results in two [[Transcription (genetics)|transcript]] variants [[encoding]] the same protein.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|AGPAT1}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | author=Leung DW |title=The structure and functions of human lysophosphatidic acid acyltransferases. |journal=Front. Biosci. |volume=6 |issue= |pages= | *{{cite journal | author=Leung DW |title=The structure and functions of human lysophosphatidic acid acyltransferases. |journal=Front. Biosci. |volume=6 |issue= 1|pages= D944–53 |year= 2001 |pmid= 11487472 |doi=10.2741/Leung }} | ||
*{{cite journal | | *{{cite journal | vauthors=Andersson B, Wentland MA, Ricafrente JY |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107–13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Yu W, Andersson B, Worley KC |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353–8 |year= 1997 |pmid= 9110174 |doi= 10.1101/gr.7.4.353| pmc=139146 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=West J, Tompkins CK, Balantac N |title=Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells. |journal=DNA Cell Biol. |volume=16 |issue= 6 |pages= 691–701 |year= 1997 |pmid= 9212163 |doi= 10.1089/dna.1997.16.691|display-authors=etal}} | ||
*{{cite journal | vauthors=Aguado B, Campbell RD |title=Human lysophosphatidic acid acyltransferase is encoded by a gene located in the major histocompatibility complex. |journal=Biochem. Soc. Trans. |volume=25 |issue= 4 |pages= S597 |year= 1998 |pmid= 9450025 |doi= }} | |||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Mungall AJ, Palmer SA, Sims SK |title=The DNA sequence and analysis of human chromosome 6. |journal=Nature |volume=425 |issue= 6960 |pages= 805–11 |year= 2003 |pmid= 14574404 |doi= 10.1038/nature02055 |display-authors=etal}} | ||
*{{cite journal | vauthors=Xie T, Rowen L, Aguado B |title=Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. |journal=Genome Res. |volume=13 |issue= 12 |pages= 2621–36 |year= 2004 |pmid= 14656967 |doi= 10.1101/gr.1736803 | pmc=403804 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Ota T, Suzuki Y, Nishikawa T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Gerhard DS, Wagner L, Feingold EA |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Servillo L, Balestrieri C, Giovane A |title=Lysophospholipid transacetylase in the regulation of PAF levels in human monocytes and macrophages. |journal=FASEB J. |volume=20 |issue= 7 |pages= 1015–7 |year= 2006 |pmid= 16571775 |doi= 10.1096/fj.05-5059fje |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Lloyd EE, Gaubatz JW, Burns AR, Pownall HJ |title=Sustained elevations in NEFA induce cyclooxygenase-2 activity and potentiate THP-1 macrophage foam cell formation. |journal=Atherosclerosis |volume=192 |issue= 1 |pages= 49–55 |year= 2007 |pmid= 16870193 |doi= 10.1016/j.atherosclerosis.2006.06.014 }} | ||
*{{cite journal | | |||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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{{gene-6-stub}} |
Latest revision as of 17:52, 29 August 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Ensembl |
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UniProt |
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RefSeq (mRNA) |
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RefSeq (protein) |
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Location (UCSC) | n/a | n/a | |||||
PubMed search | n/a | n/a | |||||
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1-acyl-sn-glycerol-3-phosphate acyltransferase alpha is an enzyme that in humans is encoded by the AGPAT1 gene.[1][2][3]
This gene encodes an enzyme that converts lysophosphatidic acid (LPA) into phosphatidic acid (PA). LPA and PA are two phospholipids involved in signal transduction and in lipid biosynthesis in cells. This enzyme localizes to the endoplasmic reticulum. This gene is located in the class III region of the human major histocompatibility complex. Alternative splicing results in two transcript variants encoding the same protein.[3]
References
- ↑ Aguado B, Campbell RD (Mar 1998). "Characterization of a human lysophosphatidic acid acyltransferase that is encoded by a gene located in the class III region of the human major histocompatibility complex". J Biol Chem. 273 (7): 4096–105. doi:10.1074/jbc.273.7.4096. PMID 9461603.
- ↑ Stamps AC, Elmore MA, Hill ME, Kelly K, Makda AA, Finnen MJ (Sep 1997). "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid acyltransferases". Biochem J. 326. ( Pt 2): 455–61. PMC 1218691. PMID 9291118.
- ↑ 3.0 3.1 "Entrez Gene: AGPAT1 1-acylglycerol-3-phosphate O-acyltransferase 1 (lysophosphatidic acid acyltransferase, alpha)".
External links
- Human AGPAT1 genome location and AGPAT1 gene details page in the UCSC Genome Browser.
Further reading
- Leung DW (2001). "The structure and functions of human lysophosphatidic acid acyltransferases". Front. Biosci. 6 (1): D944–53. doi:10.2741/Leung. PMID 11487472.
- Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
- Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- West J, Tompkins CK, Balantac N, et al. (1997). "Cloning and expression of two human lysophosphatidic acid acyltransferase cDNAs that enhance cytokine-induced signaling responses in cells". DNA Cell Biol. 16 (6): 691–701. doi:10.1089/dna.1997.16.691. PMID 9212163.
- Aguado B, Campbell RD (1998). "Human lysophosphatidic acid acyltransferase is encoded by a gene located in the major histocompatibility complex". Biochem. Soc. Trans. 25 (4): S597. PMID 9450025.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. doi:10.1038/nature02055. PMID 14574404.
- Xie T, Rowen L, Aguado B, et al. (2004). "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse". Genome Res. 13 (12): 2621–36. doi:10.1101/gr.1736803. PMC 403804. PMID 14656967.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Servillo L, Balestrieri C, Giovane A, et al. (2006). "Lysophospholipid transacetylase in the regulation of PAF levels in human monocytes and macrophages". FASEB J. 20 (7): 1015–7. doi:10.1096/fj.05-5059fje. PMID 16571775.
- Lloyd EE, Gaubatz JW, Burns AR, Pownall HJ (2007). "Sustained elevations in NEFA induce cyclooxygenase-2 activity and potentiate THP-1 macrophage foam cell formation". Atherosclerosis. 192 (1): 49–55. doi:10.1016/j.atherosclerosis.2006.06.014. PMID 16870193.
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