Signaling by Nuclear Receptors
Holzer G, Markov GV, Laudet V. Evolution of Nuclear Receptors and Ligand Signaling: Toward a Soft Key-Lock Model? Curr Top Dev Biol. 2017;125():1–38. doi: 10.1016/bs.ctdb.2017.02.003. PMID: 28527568.; Levin ER, Hammes SR. Nuclear receptors outside the nucleus: extranuclear signalling by steroid receptors. Nature Reviews Molecular Cell Biology. 2016 Oct 12;17(12):783–97. doi: 10.1038/nrm.2016.122.; Schwartz N, Verma A, Bivens CB, Schwartz Z, Boyan BD. Rapid steroid hormone actions via membrane receptors. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2016 Sep;1863(9):2289–98. doi: 10.1016/j.bbamcr.2016.06.004.; Simons SS, Edwards DP, Kumar R. Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges. Mol Endocrinol. 2014 Feb;28(2):173–82. PMID: 24284822; PMCID: PMC3896641.; Hah N, Kraus WL. Hormone-regulated transcriptomes: Lessons learned from estrogen signaling pathways in breast cancer cells. Molecular and Cellular Endocrinology. 2014 Jan;382(1):652–64. doi: 10.1016/j.mce.2013.06.021.; Echeverria PC, Picard D. Molecular chaperones, essential partners of steroid hormone receptors for activity and mobility. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2010 Jun;1803(6):641–9. doi: 10.1016/j.bbamcr.2009.11.012.; Beato M, Chávez S, Truss M. Transcriptional regulation by steroid hormones. Steroids. 1996 Apr;61(4):240–51. doi: 10.1016/0039-128x(96)00030-x. PMID: 8733009.
Metabolites
Enzyme
| EC Number | name | full name | note |
|---|---|---|---|
| 1.1.1.- | |||
| 1.1.1.1 | alcohol dehydrogenase | alcohol:NAD+ oxidoreductase | |
| 1.1.1.284 | S-(hydroxymethyl)glutathione dehydrogenase | S-(hydroxymethyl)glutathione:NAD+ oxidoreductase | |
| 1.2.4.1 | pyruvate dehydrogenase (acetyl-transferring) | pyruvate:[dihydrolipoyllysine-residue acetyltransferase]-lipoyllysine 2-oxidoreductase (decarboxylating, acceptor-acetylating) | |
| 1.8.1.4 | dihydrolipoyl dehydrogenase | protein-N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase | |
| 2.1.1.319 | type I protein arginine methyltransferase | S-adenosyl-L-methionine:[protein]-L-arginine N-methyltransferase ([protein]-Nomega,Nomega-dimethyl-L-arginine-forming) | |
| 2.7.1.137 | phosphatidylinositol 3-kinase | ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase | |
| 2.7.1.91 | sphingosine kinase | ATP:sphingoid base 1-phosphotransferase | |
| 2.7.10.1 | receptor protein-tyrosine kinase | ATP:[protein]-L-tyrosine O-phosphotransferase (receptor-type) | |
| 2.7.10.2 | non-specific protein-tyrosine kinase | ATP:[protein]-L-tyrosine O-phosphotransferase (non-specific) | |
| 2.7.11.13 | protein kinase C | ATP:protein phosphotransferase (diacylglycerol-dependent) | |
| 2.7.11.2 | [pyruvate dehydrogenase (acetyl-transferring)] kinase | ATP:[pyruvate dehydrogenase (acetyl-transferring)] phosphotransferase | |
| 2.7.11.24 | mitogen-activated protein kinase | ATP:protein phosphotransferase (MAPKK-activated) | |
| 2.7.7.6 | DNA-directed RNA polymerase | nucleoside-triphosphate:RNA nucleotidyltransferase (DNA-directed) | |
| 3.6.5.2 | small monomeric GTPase | GTP phosphohydrolase (cell-regulating) |
Proteins
| Protein ID | name | full name |
|---|