UniProtKB - O75907 (DGAT1_HUMAN)
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>sp|O75907|DGAT1_HUMAN Diacylglycerol O-acyltransferase 1 OS=Homo sapiens OX=9606 GN=DGAT1 PE=1 SV=2 MGDRGSSRRRRTGSRPSSHGGGGPAAAEEEVRDAAAGPDVGAAGDAPAPAPNKDGDAGVG SGHWELRCHRLQDSLFSSDSGFSNYRGILNWCVVMLILSNARLFLENLIKYGILVDPIQV VSLFLKDPYSWPAPCLVIAANVFAVAAFQVEKRLAVGALTEQAGLLLHVANLATILCFPA AVVLLVESITPVGSLLALMAHTILFLKLFSYRDVNSWCRRARAKAASAGKKASSAAAPHT VSYPDNLTYRDLYYFLFAPTLCYELNFPRSPRIRKRFLLRRILEMLFFTQLQVGLIQQWM VPTIQNSMKPFKDMDYSRIIERLLKLAVPNHLIWLIFFYWLFHSCLNAVAELMQFGDREF YRDWWNSESVTYFWQNWNIPVHKWCIRHFYKPMLRRGSSKWMARTGVFLASAFFHEYLVS VPLRMFRLWAFTGMMAQIPLAWFVGRFFQGNYGNAAVWLSLIIGQPIAVLMYVHDYYVLN YEAPAAEACommunity curation ()Add a publicationFeedback
Diacylglycerol O-acyltransferase 1
DGAT1
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
6 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes."
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.
J. Biol. Chem. 273:26765-26771(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. - Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION. - Ref.6"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption."
Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R., Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.
J. Biol. Chem. 283:29802-29811(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- a 1,2-diacyl-sn-glycerolEC:2.3.1.20
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Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
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Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion based on experiment ini
- Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
Source: Rhea- Search for this reaction in UniProtKB.
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a 1,2-diacyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+an acyl-CoA- Search proteins in UniProtKB for this molecule.
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=a triacyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- all-trans-retinolEC:2.3.1.76
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Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Source: Rhea- Search for this reaction in UniProtKB.
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all-trans-retinol- Search proteins in UniProtKB for this molecule.
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+an acyl-CoA- Search proteins in UniProtKB for this molecule.
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=an all-trans-retinyl ester- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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Manual assertion based on experiment ini
- Ref.6"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption."
Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R., Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.
J. Biol. Chem. 283:29802-29811(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.6"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption."
Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R., Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.
J. Biol. Chem. 283:29802-29811(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+2-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2-di-(9Z-octadecenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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Manual assertion based on experiment ini
- Ref.6"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption."
Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R., Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.
J. Biol. Chem. 283:29802-29811(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion inferred by curator fromi
- Ref.6"Acylation of acylglycerols by acyl coenzyme A:diacylglycerol acyltransferase 1 (DGAT1). Functional importance of DGAT1 in the intestinal fat absorption."
Cheng D., Iqbal J., Devenny J., Chu C.H., Chen L., Dong J., Seethala R., Keim W.J., Azzara A.V., Lawrence R.M., Pelleymounter M.A., Hussain M.M.
J. Biol. Chem. 283:29802-29811(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY.
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1,2-di-(9Z-octadecenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2,3-tri-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- all-trans-retinol
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Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion inferred by curator fromi
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
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all-trans-retinol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=all-trans-retinyl hexadecanoate- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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Manual assertion based on experiment ini
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1-O-(9Z-octadecenyl)-glycerol- Search proteins in UniProtKB for this molecule.
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=1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
- Search proteins in UniProtKB for this molecule.
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Manual assertion based on experiment ini
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1-O-(9Z-octadecenyl)-mono-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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=1-O-(9Z-octadecenyl)-2,3-di-(9Z-octadecenoyl)glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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Manual assertion based on experiment ini
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2-di-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoate
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred by curator fromi
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoate- Search proteins in UniProtKB for this molecule.
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+1,2-di-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+H+- Search proteins in UniProtKB for this molecule.
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=1,2,3-tri-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+H2O- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-3-(9Z)-octadecenoyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- hexadecane-1,2-diol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
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hexadecane-1,2-diol- Search proteins in UniProtKB for this molecule.
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+2hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=1,2-O,O-dihexadecanoyl-1,2-hexadecanediol- Search proteins in UniProtKB for this molecule.
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+2CoA- Search proteins in UniProtKB for this molecule.
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- hexadecane-1,2-diol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
hexadecane-1,2-diol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=2-hydroxyhexadecyl hexadecanoate- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- 2-(9Z-octadecenoyl)-glycerol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
2-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- 1,2-di-(9Z-octadecenoyl)-sn-glycerol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
1,2-di-(9Z-octadecenoyl)-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- hexadecan-1-ol
- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
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hexadecan-1-ol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=CoA- Search proteins in UniProtKB for this molecule.
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+hexadecanyl hexadecanoate- Search proteins in UniProtKB for this molecule.
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- 13-cis-retinol
- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
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Manual assertion inferred from sequence similarity toi
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13-cis-retinol- Search proteins in UniProtKB for this molecule.
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+hexadecanoyl-CoA- Search proteins in UniProtKB for this molecule.
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=13-cis-retinyl hexadecanoate- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
- Search proteins in UniProtKB for this molecule.
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+1,3-di-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2,3-tri-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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- (9Z)-octadecenoyl-CoA
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Manual assertion inferred from sequence similarity toi
This reaction proceeds in the forward- Search for this reaction in UniProtKB.
- See the description of this reaction in Rhea.
Manual assertion inferred from sequence similarity toi
direction.Source: Rhea- Search for this reaction in UniProtKB.
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(9Z)-octadecenoyl-CoA- Search proteins in UniProtKB for this molecule.
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+2,3-di-(9Z)-octadecenoyl-sn-glycerol- Search proteins in UniProtKB for this molecule.
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=1,2,3-tri-(9Z-octadecenoyl)-glycerol- Search proteins in UniProtKB for this molecule.
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+CoA- Search proteins in UniProtKB for this molecule.
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<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=25.9 µM for retinol1 Publication
Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
- KM=13.9 µM for palmitoyl coenzyme A1 Publication
Manual assertion based on experiment ini
- Ref.5"Acyl coenzyme A dependent retinol esterification by acyl coenzyme A: diacylglycerol acyltransferase 1."
Orland M.D., Anwar K., Cromley D., Chu C.H., Chen L., Billheimer J.T., Hussain M.M., Cheng D.
Biochim. Biophys. Acta 1737:76-82(2005) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, FUNCTION.
- KM=14.6 µM for (9Z)-octadecenoyl-CoA1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- KM=8.6 µM for octadecanoyl-CoA1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- KM=6.4 µM for hexadecanoyl-coA1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- KM=6.2 µM for (9Z)-hexadecenoyl-CoA1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- KM=597.1 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer)1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- KM=497.5 µM for 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer)1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=956.6 pmol/min/µg enzyme with (9Z)-octadecenoyl-CoA as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=839.4 pmol/min/µg enzyme with octadecanoyl-CoA as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=767.8 pmol/min/µg enzyme with hexadecanoyl-coA as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=838.6 pmol/min/µg enzyme with (9Z)-hexadecenoyl-CoA as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=3310 pmol/min/µg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homodimer) as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Vmax=3628 pmol/min/µg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycerol (with DGAT1 as homotetramer) as substrate1 Publication
Manual assertion based on experiment ini
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycerolipid metabolism
This protein is involved in the pathway glycerolipid metabolism, which is part of Lipid metabolism.View all proteins of this organism that are known to be involved in the pathway glycerolipid metabolism and in Lipid metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 390 | Acyl-CoACombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
Binding sitei | 404 | Acyl-CoACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 415 | 1 Publication Manual assertion based on experiment ini
| 1 | |
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 416 | Important for catalytic activity1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 477 | Acyl-CoACombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 2-acylglycerol O-acyltransferase activity Source: Ensembl
- diacylglycerol O-acyltransferase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469.
- identical protein binding Source: IntAct
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- O-acyltransferase activity Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- retinol O-fatty-acyltransferase activity Source: UniProtKB-EC
- transferase activity, transferring acyl groups Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.1"Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes."
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.
J. Biol. Chem. 273:26765-26771(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
GO - Biological processi
- acylglycerol acyl-chain remodeling Source: Reactome
- diacylglycerol metabolic process Source: UniProtKBInferred from direct assayi
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469.
- fatty acid homeostasis Source: Ensembl
- lipid storage Source: BHF-UCL
- long-chain fatty-acyl-CoA metabolic process Source: BHF-UCL
- monoacylglycerol biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.7"Synthesis of neutral ether lipid monoalkyl-diacylglycerol by lipid acyltransferases."
Ma Z., Onorato J.M., Chen L., Nelson D.W., Yen C.E., Cheng D.
J. Lipid Res. 58:1091-1099(2017) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, FUNCTION.
- neutrophil degranulation Source: Reactome
- triglyceride biosynthetic process Source: UniProtKBInferred from direct assayi
- "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase."
Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E., Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E., Konrad R.J., Beigneux A.P., Young S.G., Cao G.
J. Biol. Chem. 283:10048-10057(2008) [PubMed] [Europe PMC] [Abstract] - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469.
- triglyceride metabolic process Source: ProtIncTraceable author statementi
- Ref.1"Characterization of two human genes encoding acyl coenzyme A:cholesterol acyltransferase-related enzymes."
Oelkers P., Behari A., Cromley D., Billheimer J.T., Sturley S.L.
J. Biol. Chem. 273:26765-26771(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- very-low-density lipoprotein particle assembly Source: BHF-UCL
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- "Overexpression of human diacylglycerol acyltransferase 1, acyl-coa:cholesterol acyltransferase 1, or acyl-CoA:cholesterol acyltransferase 2 stimulates secretion of apolipoprotein B-containing lipoproteins in McA-RH7777 cells."
Liang J.J., Oelkers P., Guo C., Chu P.C., Dixon J.L., Ginsberg H.N., Sturley S.L.
J Biol Chem 279:44938-44944(2004) [PubMed] [Europe PMC] [Abstract]
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Molecular function | Acyltransferase, Transferase |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.3.1.20, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | O75907 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1482883, Acyl chain remodeling of DAG and TAG R-HSA-6798695, Neutrophil degranulation R-HSA-75109, Triglyceride biosynthesis |
SIGNOR Signaling Network Open Resource More...SIGNORi | O75907 |
UniPathway: a resource for the exploration and annotation of metabolic pathways More...UniPathwayi | UPA00230 |
Protein family/group databases
Transport Classification Database More...TCDBi | 2.A.50.4.1, the glycerol uptake (gup) or membrane-bound acyl transfeerase (mboat) family |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000000308 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Diacylglycerol O-acyltransferase 1Curated (EC:2.3.1.20
Manual assertion based on experiment ini
Alternative name(s): ACAT-related gene product 1 Acyl-CoA retinol O-fatty-acyltransferase1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Manual assertion based on experiment ini
Short name: ARAT1 Publication Manual assertion based on opinion ini
Short name: Retinol O-fatty-acyltransferase1 Publication Manual assertion based on opinion ini
Diglyceride acyltransferase |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:DGAT11 Publication Manual assertion based on opinion ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:AGRP11 Publication Manual assertion based on opinion ini
|
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen and Host Database Resources More...EuPathDBi | HostDB:ENSG00000185000.9 |
Human Gene Nomenclature Database More...HGNCi | HGNC:2843, DGAT1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604900, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O75907 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Endoplasmic reticulum
- Endoplasmic reticulum membrane By similarity
Manual assertion inferred from sequence similarity toi
; Multi-pass membrane protein 2 PublicationsManual assertion based on experiment ini
- Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
- Endoplasmic reticulum membrane By similarity
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- endoplasmic reticulum membrane Source: GO_CentralInferred from biological aspect of ancestori
Plasma Membrane
- plasma membrane Source: Reactome
Other locations
- integral component of membrane Source: UniProtKBInferred from direct assayi
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416. - Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469.
- specific granule membrane Source: Reactome
- integral component of membrane Source: UniProtKBInferred from direct assayi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 83 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 83 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 84 – 118 | Helical; Name=1Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 35 | |
Topological domaini | 119 – 130 | Lumenal2 Publications Manual assertion based on experiment ini
| 12 | |
Transmembranei | 131 – 156 | Helical; Name=2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 26 | |
Topological domaini | 157 – 161 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 5 | |
Transmembranei | 162 – 184 | Helical; Name=3Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 23 | |
Topological domaini | 185 – 191 | Lumenal2 Publications Manual assertion based on experiment ini
| 7 | |
Transmembranei | 192 – 223 | Helical; Name=4Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 32 | |
Topological domaini | 224 – 273 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 50 | |
Transmembranei | 274 – 308 | Helical; Name=5Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 35 | |
Topological domaini | 309 – 315 | Lumenal2 Publications Manual assertion based on experiment ini
| 7 | |
Transmembranei | 316 – 353 | Helical; Name=6Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 38 | |
Topological domaini | 354 – 399 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 46 | |
Transmembranei | 400 – 420 | Helical; Name=7Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 21 | |
Topological domaini | 421 – 428 | Lumenal2 Publications Manual assertion based on experiment ini
| 8 | |
Transmembranei | 429 – 447 | Helical; Name=8Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 19 | |
Topological domaini | 448 – 449 | Cytoplasmic2 Publications Manual assertion based on experiment ini
| 2 | |
Transmembranei | 450 – 481 | Helical; Name=9Combined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 32 | |
Topological domaini | 482 – 488 | Lumenal2 Publications Manual assertion based on experiment ini
| 7 |
Keywords - Cellular componenti
Endoplasmic reticulum, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Diarrhea 7, protein-losing enteropathy type (DIAR7)2 PublicationsManual assertion based on experiment ini
- Ref.8"DGAT1 mutation is linked to a congenital diarrheal disorder."
Haas J.T., Winter H.S., Lim E., Kirby A., Blumenstiel B., DeFelice M., Gabriel S., Jalas C., Branski D., Grueter C.A., Toporovski M.S., Walther T.C., Daly M.J., Farese R.V. Jr.
J. Clin. Invest. 122:4680-4684(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN DIAR7. - Ref.12"Autozygome and high throughput confirmation of disease genes candidacy."
Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R., AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A., El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O., Al-Mureikhi M., Jasser A.A., Alsaif H.S. , Alluhaydan I., Seidahmed M.Z., Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M., Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B., Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E., Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S., Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.
Genet. Med. 21:736-742(2019) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT DIAR7 458-TRP--ALA-488 DEL.
Haas J.T., Winter H.S., Lim E., Kirby A., Blumenstiel B., DeFelice M., Gabriel S., Jalas C., Branski D., Grueter C.A., Toporovski M.S., Walther T.C., Daly M.J., Farese R.V. Jr.
J. Clin. Invest. 122:4680-4684(2012) [PubMed] [Europe PMC] [Abstract]
Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R., AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A., El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O., Al-Mureikhi M., Jasser A.A., Alsaif H.S. , Alluhaydan I., Seidahmed M.Z., Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M., Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B., Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E., Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S., Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.
Genet. Med. 21:736-742(2019) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 346 | L → W: Strongly reduced diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 371 | T → A: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 375 | Q → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 377 | W → F: Abolished diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 378 | N → A or L: Abolished diacylglycerol O-acyltransferase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 381 | V → A: Does not affect diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 381 | V → W: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 382 | H → A: Decreased diacylglycerol O-acyltransferase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 385 | C → W: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 386 | I → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 390 | Y → A: Decreased diacylglycerol O-acyltransferase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 391 | K → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 400 | K → L: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 404 | R → A: Does not affect diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 404 | R → L: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 407 | V → F: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 411 | S → A or W: Abolished diacylglycerol O-acyltransferase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 411 | S → I: Decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 415 | H → A: Abolished diacylglycerol O-acyltransferase activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 416 | E → A: Abolished diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 434 | M → A or I: Reduced diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 437 | Q → A: Reduced diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 465 | Q → A: Reduced diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 469 | V → A: Slightly decreased diacylglycerol O-acyltransferase activity. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNET More...DisGeNETi | 8694 |
MalaCards human disease database More...MalaCardsi | DGAT1 |
MIMi | 615863, phenotype |
Open Targets More...OpenTargetsi | ENSG00000185000 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 329242, Congenital chronic diarrhea with protein-losing enteropathy |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27303 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | O75907, Tclin |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL6009 |
DrugCentral More...DrugCentrali | O75907 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2821 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | DGAT1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000207654 | 1 – 488 | Diacylglycerol O-acyltransferase 1Add BLAST | 488 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 17 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
Modified residuei | 18 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O75907 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | O75907 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | O75907 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O75907 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O75907 |
PeptideAtlas More...PeptideAtlasi | O75907 |
PRoteomics IDEntifications database More...PRIDEi | O75907 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 50257 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O75907 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O75907 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000185000, Expressed in small intestine and 114 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O75907, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O75907, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000185000, Tissue enriched (intestine) |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer or homotetramer; both forms have similar enzymatic activities.
2 PublicationsManual assertion based on experiment ini
- Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsO75907
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-3906527,EBI-3906527 |
Non-structural protein 5A (PRO_0000045602) from Hepatitis C virus genotype 2a (isolate JFH-1). | 2 | EBI-3906527,EBI-6927873 |
GO - Molecular functioni
- identical protein binding Source: IntActInferred from physical interactioni
- Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 114241, 15 interactors |
Protein interaction database and analysis system More...IntActi | O75907, 13 interactors |
Molecular INTeraction database More...MINTi | O75907 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000482264 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O75907 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | O75907, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 78 – 80 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 88 – 112 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 113 – 115 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 116 – 126 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 128 – 130 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 132 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 23 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 155 – 157 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 161 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 24 | |
Helixi | 191 – 225 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 35 | |
Helixi | 244 – 246 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 249 – 256 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 275 – 299 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 25 | |
Helixi | 301 – 306 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Turni | 311 – 313 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 316 – 342 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 27 | |
Helixi | 344 – 352 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 364 – 366 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 370 – 374 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 379 – 388 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 391 – 395 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 400 – 419 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
Turni | 420 – 423 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 429 – 447 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
Helixi | 450 – 462 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Turni | 463 – 465 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 466 – 478 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O75907 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 91 | Involved in homomerizationBy similarity Manual assertion inferred from sequence similarity toi Add BLAST | 91 | |
Regioni | 1 – 57 | Disordered1 Publication Manual assertion inferred by curator fromi
| 57 | |
Regioni | 119 – 130 | Extracellular loop 1 (EL1)1 Publication Manual assertion based on experiment ini
| 12 | |
Regioni | 131 – 488 | MBOAT fold1 Publication Manual assertion based on experiment ini
| 358 | |
Regioni | 224 – 276 | Intracellular loop 1 (IL1)1 Publication Manual assertion based on experiment ini
| 53 | |
Regioni | 354 – 399 | Intracellular loop 2 (IL2)1 Publication Manual assertion based on experiment ini
| 46 | |
Regioni | 374 – 382 | Acyl-CoA bindingCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 9 | |
Regioni | 380 – 394 | Amphipathic helix (AH)1 Publication Manual assertion based on experiment ini
| 15 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 360 – 366 | FYXDWWN motif1 Publication Manual assertion based on opinion ini
| 7 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Manual assertion inferred by curator fromi
- Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
Manual assertion based on experiment ini
- Ref.10"Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme."
Sui X., Wang K., Gluchowski N.L., Elliott S.D., Liao M., Walther T.C., Farese R.V. Jr.
Nature 581:323-328(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS)IN COMPLEX WITH (9Z)-OCTADECENOYL-COA, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, MUTAGENESIS OF GLN-375; ASN-378; VAL-381; HIS-382; CYS-385; ILE-386; TYR-390; LYS-391; ARG-404; VAL-407; SER-411; HIS-415; MET-434; GLN-437; GLN-465 AND VAL-469. - Ref.11"Structure and mechanism of human diacylglycerol O-acyltransferase 1."
Wang L., Qian H., Nian Y., Han Y., Ren Z., Zhang H., Hu L., Prasad B.V.V., Laganowsky A., Yan N., Zhou M.
Nature 581:329-332(2020) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) IN COMPLEX WITH (9Z)-OCTADECENOYL-COA AND 1,2-DI-(9Z-OCTADECENOYL)-SN-GLYCEROL, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBUNIT, DOMAIN, MUTAGENESIS OF LEU-346; THR-371; TRP-377; ASN-378; HIS-382; TYR-390; LYS-400; ARG-404; SER-411; HIS-415 AND GLU-416.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0380, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00950000183081 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_018190_0_0_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O75907 |
Identification of Orthologs from Complete Genome Data More...OMAi | RSKYRHV |
Database of Orthologous Groups More...OrthoDBi | 1275897at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O75907 |
TreeFam database of animal gene trees More...TreeFami | TF314921 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR027251, Diacylglycerol_acylTrfase1 IPR004299, MBOAT_fam IPR014371, Oat_ACAT_DAG_ARE |
The PANTHER Classification System More...PANTHERi | PTHR10408, PTHR10408, 1 hit PTHR10408:SF7, PTHR10408:SF7, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF03062, MBOAT, 1 hit |
PIRSF; a whole-protein classification database More...PIRSFi | PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit PIRSF500231, Oat_dag, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
10 20 30 40 50
MGDRGSSRRR RTGSRPSSHG GGGPAAAEEE VRDAAAGPDV GAAGDAPAPA
60 70 80 90 100
PNKDGDAGVG SGHWELRCHR LQDSLFSSDS GFSNYRGILN WCVVMLILSN
110 120 130 140 150
ARLFLENLIK YGILVDPIQV VSLFLKDPYS WPAPCLVIAA NVFAVAAFQV
160 170 180 190 200
EKRLAVGALT EQAGLLLHVA NLATILCFPA AVVLLVESIT PVGSLLALMA
210 220 230 240 250
HTILFLKLFS YRDVNSWCRR ARAKAASAGK KASSAAAPHT VSYPDNLTYR
260 270 280 290 300
DLYYFLFAPT LCYELNFPRS PRIRKRFLLR RILEMLFFTQ LQVGLIQQWM
310 320 330 340 350
VPTIQNSMKP FKDMDYSRII ERLLKLAVPN HLIWLIFFYW LFHSCLNAVA
360 370 380 390 400
ELMQFGDREF YRDWWNSESV TYFWQNWNIP VHKWCIRHFY KPMLRRGSSK
410 420 430 440 450
WMARTGVFLA SAFFHEYLVS VPLRMFRLWA FTGMMAQIPL AWFVGRFFQG
460 470 480
NYGNAAVWLS LIIGQPIAVL MYVHDYYVLN YEAPAAEA
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
A0A0A0MR74 | A0A0A0MR74_HUMAN | Acyl-CoA retinol O-fatty-acyltransf... Acyl-CoA retinol O-fatty-acyltransferase, EC 2.3.1.20, EC 2.3.1.76 (Diacylglycerol O-acyltransferase 1) (Diglyceride acyltransferase) | DGAT1 | 315 | Annotation score: Annotation score:5 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 129 | Y → H in AAC63997 (PubMed:9756920).Curated | 1 |
Natural variant
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF059202 mRNA Translation: AAC63997.1 AB057815 mRNA Translation: BAC66170.1 CH471162 Genomic DNA Translation: EAW82127.1 CH471162 Genomic DNA Translation: EAW82129.1 BC015762 mRNA Translation: AAH15762.1 BC023565 mRNA Translation: AAH23565.1 BC150649 mRNA Translation: AAI50650.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS6420.1 |
NCBI Reference Sequences More...RefSeqi | NP_036211.2, NM_012079.5 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000528718; ENSP00000482264; ENSG00000185000 ENST00000644790; ENSP00000495489; ENSG00000285482 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 8694 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:8694 |
UCSC genome browser More...UCSCi | uc003zbv.5, human |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
O75907 | O-acyltransferase | 488 | UniRef100_O75907 | |||
O-acyltransferase | 488 | |||||
Acyl-CoA retinol O-fatty-acyltransferase (Fragment) | 400 | |||||
O-acyltransferase | 488 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
O75907 | Diacylglycerol O-acyltransferase 1 | 491 | UniRef90_O75907 | |||
O-acyltransferase | 488 | |||||
O-acyltransferase | 488 | |||||
Acyl-CoA retinol O-fatty-acyltransferase (Fragment) | 400 | |||||
O-acyltransferase | 496 | |||||
+40 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
O75907 | Diacylglycerol O-acyltransferase 1 | 491 | UniRef50_O75907 | |||
O-acyltransferase | 488 | |||||
O-acyltransferase | 488 | |||||
Acyl-CoA retinol O-fatty-acyltransferase (Fragment) | 400 | |||||
O-acyltransferase | 496 | |||||
+67 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF059202 mRNA Translation: AAC63997.1 AB057815 mRNA Translation: BAC66170.1 CH471162 Genomic DNA Translation: EAW82127.1 CH471162 Genomic DNA Translation: EAW82129.1 BC015762 mRNA Translation: AAH15762.1 BC023565 mRNA Translation: AAH23565.1 BC150649 mRNA Translation: AAI50650.1 |
CCDSi | CCDS6420.1 |
RefSeqi | NP_036211.2, NM_012079.5 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
6VP0 | electron microscopy | 3.10 | C/E | 1-488 | [»] | |
6VYI | electron microscopy | 3.00 | A/B | 1-488 | [»] | |
6VZ1 | electron microscopy | 3.20 | A/B | 1-488 | [»] | |
SMRi | O75907 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 114241, 15 interactors |
IntActi | O75907, 13 interactors |
MINTi | O75907 |
STRINGi | 9606.ENSP00000482264 |
Chemistry databases
BindingDBi | O75907 |
ChEMBLi | CHEMBL6009 |
DrugCentrali | O75907 |
GuidetoPHARMACOLOGYi | 2821 |
SwissLipidsi | SLP:000000308 |
Protein family/group databases
TCDBi | 2.A.50.4.1, the glycerol uptake (gup) or membrane-bound acyl transfeerase (mboat) family |
PTM databases
iPTMneti | O75907 |
PhosphoSitePlusi | O75907 |
Polymorphism and mutation databases
BioMutai | DGAT1 |
Proteomic databases
EPDi | O75907 |
jPOSTi | O75907 |
MassIVEi | O75907 |
MaxQBi | O75907 |
PaxDbi | O75907 |
PeptideAtlasi | O75907 |
PRIDEi | O75907 |
ProteomicsDBi | 50257 |
Protocols and materials databases
Antibodypedia a portal for validated antibodies More...Antibodypediai | 28443, 306 antibodies |
The DNASU plasmid repository More...DNASUi | 8694 |
Genome annotation databases
Ensembli | ENST00000528718; ENSP00000482264; ENSG00000185000 ENST00000644790; ENSP00000495489; ENSG00000285482 |
GeneIDi | 8694 |
KEGGi | hsa:8694 |
UCSCi | uc003zbv.5, human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 8694 |
DisGeNETi | 8694 |
EuPathDBi | HostDB:ENSG00000185000.9 |
GeneCards: human genes, protein and diseases More...GeneCardsi | DGAT1 |
HGNCi | HGNC:2843, DGAT1 |
HPAi | ENSG00000185000, Tissue enriched (intestine) |
MalaCardsi | DGAT1 |
MIMi | 604900, gene 615863, phenotype |
neXtProti | NX_O75907 |
OpenTargetsi | ENSG00000185000 |
Orphaneti | 329242, Congenital chronic diarrhea with protein-losing enteropathy |
PharmGKBi | PA27303 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0380, Eukaryota |
GeneTreei | ENSGT00950000183081 |
HOGENOMi | CLU_018190_0_0_1 |
InParanoidi | O75907 |
OMAi | RSKYRHV |
OrthoDBi | 1275897at2759 |
PhylomeDBi | O75907 |
TreeFami | TF314921 |
Enzyme and pathway databases
UniPathwayi | UPA00230 |
BRENDAi | 2.3.1.20, 2681 |
PathwayCommonsi | O75907 |
Reactomei | R-HSA-1482883, Acyl chain remodeling of DAG and TAG R-HSA-6798695, Neutrophil degranulation R-HSA-75109, Triglyceride biosynthesis |
SIGNORi | O75907 |
Miscellaneous databases
BioGRID ORCS database of CRISPR phenotype screens More...BioGRID-ORCSi | 8694, 7 hits in 842 CRISPR screens |
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | DGAT1, human |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 8694 |
Pharosi | O75907, Tclin |
Protein Ontology More...PROi | PR:O75907 |
RNActi | O75907, protein |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000185000, Expressed in small intestine and 114 other tissues |
ExpressionAtlasi | O75907, baseline and differential |
Genevisiblei | O75907, HS |
Family and domain databases
InterProi | View protein in InterPro IPR027251, Diacylglycerol_acylTrfase1 IPR004299, MBOAT_fam IPR014371, Oat_ACAT_DAG_ARE |
PANTHERi | PTHR10408, PTHR10408, 1 hit PTHR10408:SF7, PTHR10408:SF7, 1 hit |
Pfami | View protein in Pfam PF03062, MBOAT, 1 hit |
PIRSFi | PIRSF000439, Oat_ACAT_DAG_ARE, 1 hit PIRSF500231, Oat_dag, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | DGAT1_HUMAN | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | O75907Primary (citable) accession number: O75907 Secondary accession number(s): B2RWQ2, D3DWL6, Q96BB8 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 18, 2001 |
Last sequence update: | July 25, 2003 | |
Last modified: | December 2, 2020 | |
This is version 171 of the entry and version 2 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations