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{{Infobox_gene}}
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'''Glycerol-3-phosphate acyltransferase 1, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''GPAM'' [[gene]].<ref name="pmid10997877">{{cite journal |vauthors=Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro | journal = DNA Res | volume = 7 | issue = 4 | pages = 273–81 |date=Dec 2000 | pmid = 10997877 | pmc =  | doi =  10.1093/dnares/7.4.271}}</ref><ref name="pmid8369314">{{cite journal |vauthors=Yet SF, Lee S, Hahm YT, Sul HS | title = Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase | journal = Biochemistry | volume = 32 | issue = 36 | pages = 9486–9491 |date=Oct 1993 | pmid = 8369314 | pmc =  | doi =10.1021/bi00087a029 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GPAM glycerol-3-phosphate acyltransferase, mitochondrial| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57678| accessdate = }}</ref>
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{{GNF_Protein_box
| image =
| image_source =
| PDB =  
| Name = Glycerol-3-phosphate acyltransferase, mitochondrial
| HGNCid = 24865
| Symbol = GPAM
| AltSymbols =; KIAA1560; GPAT1; MGC26846; RP11-426E5.2
| OMIM = 602395
| ECnumber =
  | Homologene = 7343
  | MGIid = 109162
| Function = {{GNF_GO|id=GO:0004366 |text = glycerol-3-phosphate O-acyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
  | Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008654 |text = phospholipid biosynthetic process}} {{GNF_GO|id=GO:0044255 |text = cellular lipid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 57678
    | Hs_Ensembl = ENSG00000119927
    | Hs_RefseqProtein = NP_065969
    | Hs_RefseqmRNA = NM_020918
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 113899614
    | Hs_GenLoc_end = 113933511
    | Hs_Uniprot = Q9HCL2
    | Mm_EntrezGene = 14732
    | Mm_Ensembl = ENSMUSG00000024978
    | Mm_RefseqmRNA = NM_008149
    | Mm_RefseqProtein = NP_032175
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 55122034
    | Mm_GenLoc_end = 55156365
    | Mm_Uniprot = Q69ZG4
  }}
}}
'''Glycerol-3-phosphate acyltransferase, mitochondrial''', also known as '''GPAM''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GPAM glycerol-3-phosphate acyltransferase, mitochondrial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57678| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15), which catalyzes the initial and committing step in glycerolipid biosynthesis, is predicted to play a pivotal role in the regulation of cellular triacylglycerol and phospholipid levels. Two mammalian forms of GPAT have been identified on the basis of localization to either the endoplasmic reticulum or mitochondria.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: GPAM glycerol-3-phosphate acyltransferase, mitochondrial| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57678| accessdate = }}</ref>
| summary_text = Glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15), which catalyzes the initial and committing step in glycerolipid biosynthesis, is predicted to play a pivotal role in the regulation of cellular triacylglycerol and phospholipid levels. Two mammalian forms of GPAT have been identified on the basis of localization to either the endoplasmic reticulum or mitochondria.[supplied by OMIM]<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Skorve J, Ruyter B, Rustan AC, ''et al.'' |title=Effect of 3- and 4-thia-substituted fatty acids on glycerolipid metabolism and mitochondrial beta-oxidation in rat liver. |journal=Biochem. Pharmacol. |volume=40 |issue= 9 |pages= 2005-12 |year= 1990 |pmid= 2242030 |doi=  }}
*{{cite journal  | author=Skorve J |title=Effect of 3- and 4-thia-substituted fatty acids on glycerolipid metabolism and mitochondrial beta-oxidation in rat liver |journal=Biochem. Pharmacol. |volume=40 |issue= 9 |pages= 2005–2012 |year= 1990 |pmid= 2242030 |doi=10.1016/0006-2952(90)90230-I  |name-list-format=vanc| author2=Ruyter B  | author3=Rustan AC  | display-authors=3  | last4=Christiansen  | first4=E  | last5=Drevon  | first5=C  | last6=Berge  | first6=R }}
*{{cite journal  | author=Thomas PD, Poznansky MJ |title=Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase. Effect of iron and copper salts and carbon tetrachloride. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2684-91 |year= 1990 |pmid= 2303421 |doi=  }}
*{{cite journal  |vauthors=Thomas PD, Poznansky MJ |title=Lipid peroxidation inactivates rat liver microsomal glycerol-3-phosphate acyl transferase. Effect of iron and copper salts and carbon tetrachloride |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2684–91 |year= 1990 |pmid= 2303421 |doi=  }}
*{{cite journal  | author=Yet SF, Lee S, Hahm YT, Sul HS |title=Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase. |journal=Biochemistry |volume=32 |issue= 36 |pages= 9486-91 |year= 1993 |pmid= 8369314 |doi=  }}
*{{cite journal  | author=Welch CL |title=Assignment of Gpam to distal mouse chromosome 19 by linkage analysis |journal=Mamm. Genome |volume=9 |issue= 1 |pages= 93–93 |year= 1998 |pmid= 9434961 |doi=10.1007/s003359900694 |name-list-format=vanc| author2=Xia YR  | author3=Edwards PA  | display-authors=3  | last4=Lusis  | first4=Aidons J.  | last5=Ericsson  | first5=Johan }}
*{{cite journal  | author=Welch CL, Xia YR, Edwards PA, ''et al.'' |title=Assignment of Gpam to distal mouse chromosome 19 by linkage analysis. |journal=Mamm. Genome |volume=9 |issue= 1 |pages= 93 |year= 1998 |pmid= 9434961 |doi= }}
*{{cite journal  |vauthors=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–1795 |year= 2001 |pmid= 11076863 |doi=10.1101/gr.143000  | pmc=310948 }}
*{{cite journal | author=Nagase T, Kikuno R, Nakayama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 4 |pages= 273-81 |year= 2001 |pmid= 10997877 |doi=  }}
*{{cite journal  | author=Wiemann S |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–435 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.GR1547R  | pmc=311072  |name-list-format=vanc| author2=Weil B  | author3=Wellenreuther R  | display-authors=3  | last4=Gassenhuber  | first4=J  | last5=Glassl  | first5=S  | last6=Ansorge  | first6=W  | last7=Böcher  | first7=M  | last8=Blöcker  | first8=H  | last9=Bauersachs  | first9=S }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  |vauthors=Igal RA, Wang S, Gonzalez-Baró M, Coleman RA |title=Mitochondrial glycerol phosphate acyltransferase directs the incorporation of exogenous fatty acids into triacylglycerol |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42205–42212 |year= 2001 |pmid= 11546763 |doi= 10.1074/jbc.M103386200 }}
*{{cite journal  | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal  | author=Strausberg RL |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= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Igal RA, Wang S, Gonzalez-Baró M, Coleman RA |title=Mitochondrial glycerol phosphate acyltransferase directs the incorporation of exogenous fatty acids into triacylglycerol. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42205-12 |year= 2001 |pmid= 11546763 |doi= 10.1074/jbc.M103386200 }}
*{{cite journal  | author=Deloukas P |title=The DNA sequence and comparative analysis of human chromosome 10 |journal=Nature |volume=429 |issue= 6990 |pages= 375–381 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 |name-list-format=vanc| author2=Earthrowl ME  | author3=Grafham DV  | display-authors=3  | last4=Rubenfield  | first4=M.  | last5=French  | first5=L.  | last6=Steward  | first6=C. A.  | last7=Sims  | first7=S. K.  | last8=Jones  | first8=M. C.  | last9=Searle  | first9=S. }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Wiemann S |title=From ORFeome to biology: a functional genomics pipeline |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–2144 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 | pmc=528930  |name-list-format=vanc| author2=Arlt D  | author3=Huber W  | display-authors=3  | last4=Wellenreuther  | first4=R  | last5=Schleeger  | first5=S  | last6=Mehrle  | first6=A  | last7=Bechtel  | first7=S  | last8=Sauermann  | first8=M  | last9=Korf  | first9=U }}
*{{cite journal  | author=Deloukas P, Earthrowl ME, Grafham DV, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375-81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462 }}
*{{cite journal  | author=Mehrle A |title=The LIFEdb database in 2006 |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–D418 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 | pmc=1347501  |name-list-format=vanc| author2=Rosenfelder H  | author3=Schupp I  | display-authors=3  | last4=Del Val  | first4=C  | last5=Arlt  | first5=D  | last6=Hahne  | first6=F  | last7=Bechtel  | first7=S  | last8=Simpson  | first8=J  | last9=Hofmann  | first9=O }}
*{{cite journal  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal  | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 08:55, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
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/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Glycerol-3-phosphate acyltransferase 1, mitochondrial is an enzyme that in humans is encoded by the GPAM gene.[1][2][3]

Glycerol-3-phosphate acyltransferase (GPAT; EC 2.3.1.15), which catalyzes the initial and committing step in glycerolipid biosynthesis, is predicted to play a pivotal role in the regulation of cellular triacylglycerol and phospholipid levels. Two mammalian forms of GPAT have been identified on the basis of localization to either the endoplasmic reticulum or mitochondria.[supplied by OMIM][3]

References

  1. ↑ Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O (Dec 2000). "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (4): 273–81. doi:10.1093/dnares/7.4.271. PMID 10997877.
  2. ↑ Yet SF, Lee S, Hahm YT, Sul HS (Oct 1993). "Expression and identification of p90 as the murine mitochondrial glycerol-3-phosphate acyltransferase". Biochemistry. 32 (36): 9486–9491. doi:10.1021/bi00087a029. PMID 8369314.
  3. ↑ 3.0 3.1 "Entrez Gene: GPAM glycerol-3-phosphate acyltransferase, mitochondrial".

Further reading



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