Pathways Knowlegdes

Necessitatibus eius consequatur ex aliquid fuga eum quidem sint consectetur velit

Pathway DOIs Note
Post-translational protein modification

Accession ID: Reactome:R-BTA-597592		 -
SUMOylation

Accession ID: Reactome:R-BTA-2990846
  • 10.1016/j.tcb.2007.08.002
  • 10.1016/j.tox.2010.07.013
  • 10.1038/nrm3011
  • 10.1042/bj20100158
  • 10.1042/bst20130015
  • 10.1242/jcs.050542
 Hay RT. Decoding the SUMO signal. Biochem Soc Trans. 2013 Apr;41(2):463–73. doi: 10.1042/bst20130015. PMID: 23514139.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein SUMOylation. Biochem J. 2010 May 13;428(2):133–45. PMID: 20462400; PMCID: PMC3310159.; Wang Y, Dasso M. SUMOylation and deSUMOylation at a glance. J Cell Sci. 2009 Dec 01;122(Pt 23):4249–52. PMID: 19923268; PMCID: PMC2779127.; Hay RT. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007 Aug;17(8):370–6. doi: 10.1016/j.tcb.2007.08.002. PMID: 17768054.
SUMOylation of intracellular receptors

Accession ID: Reactome:R-BTA-4090294
  • 10.1016/b978-0-12-416673-8.00008-3
  • 10.1016/j.bbadis.2010.12.008
  • 10.1152/ajpheart.00703.2011
  • 10.1621/nrs.10001
 Knutson TP, Lange CA. Dynamic regulation of steroid hormone receptor transcriptional activity by reversible SUMOylation. Vitam Horm. 2013;93():227–61. doi: 10.1016/b978-0-12-416673-8.00008-3. PMID: 23810010.; Wadosky KM, Willis MS. The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation. American Journal of Physiology-Heart and Circulatory Physiology. 2012 Feb;302(3):H515–26. doi: 10.1152/ajpheart.00703.2011.; Anbalagan M, Huderson B, Murphy L, Rowan BG. Post-translational modifications of nuclear receptors and human disease. Nucl Recept Signal. 2012;10():e001. PMID: 22438791; PMCID: PMC3309075.; Treuter E, Venteclef N. Transcriptional control of metabolic and inflammatory pathways by nuclear receptor SUMOylation. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 2011 Aug;1812(8):909–18. doi: 10.1016/j.bbadis.2010.12.008.
Metabolism of proteins

Accession ID: Reactome:R-DRE-392499
  • 10.1016/j.bbalip.2012.09.010
  • 10.1083/jcb.200708199
  • 10.1210/edrv-2-2-137
  • 10.32607/20758251-2009-1-3-29-51
 Agassandian M, Mallampalli RK. Surfactant phospholipid metabolism. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2013 Mar;1831(3):612–25. doi: 10.1016/j.bbalip.2012.09.010.; Knorre DG, Kudryashova NV, Godovikova TS. Chemical and Functional Aspects of Posttranslational Modification of Proteins. Acta Naturae. 2009 Dec 15;1(3):29–51. doi: 10.32607/20758251-2009-1-3-29-51.; Kutik S, Guiard B, Meyer HE, Wiedemann N, Pfanner N. Cooperation of translocase complexes in mitochondrial protein import. J Cell Biol. 2007 Nov 19;179(4):585–91. PMID: 17998403; PMCID: PMC2080918.; Chertow BS. The role of lysosomes and proteases in hormone secretion and degradation. Endocr Rev. 1981;2(2):137–73. doi: 10.1210/edrv-2-2-137. PMID: 6117463.
Post-translational protein modification

Accession ID: Reactome:R-DME-597592		 -
SUMO E3 ligases SUMOylate target proteins

Accession ID: Reactome:R-DME-3108232
  • 10.1007/s00018-007-7137-4
  • 10.1016/j.tox.2010.07.013
  • 10.1038/embor.2010.206
  • 10.1038/nrm3011
  • 10.1038/nsmb.2526
  • 10.1074/mcp.m600212-mcp200
  • 10.1126/scisignal.2000282
  • 10.1126/scisignal.2001484
  • 10.1146/annurev-biochem-061909-093311
  • 10.1146/annurev-genet-111212-133453
  • 10.1155/2012/875148
  • 10.12703/p5-45
  • 10.2741/s388
 Jentsch S, Psakhye I. Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu Rev Genet. 2013;47():167–86. doi: 10.1146/annurev-genet-111212-133453. PMID: 24016193.; Yang XJ, Chiang CM. Sumoylation in gene regulation, human disease, and therapeutic action. F1000Prime Rep. 2013;5():45. PMID: 24273646; PMCID: PMC3816760.; Flotho A, Melchior F. Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem. 2013;82():357–85. doi: 10.1146/annurev-biochem-061909-093311. PMID: 23746258.; Becker J, Barysch SV, Karaca S, Dittner C, Hsiao HH, Berriel Diaz M, Herzig S, Urlaub H, Melchior F. Detecting endogenous SUMO targets in mammalian cells and tissues. Nat Struct Mol Biol. 2013 Apr;20(4):525–31. doi: 10.1038/nsmb.2526. PMID: 23503365.; Citro S, Chiocca S. Sumo paralogs: redundancy and divergencies. Front Biosci (Schol Ed). 2013 Jan 01;5(2):544–53. doi: 10.2741/s388. PMID: 23277067.; Da Silva-Ferrada E, Lopitz-Otsoa F, Lang V, Rodríguez MS, Matthiesen R. Strategies to Identify Recognition Signals and Targets of SUMOylation. Biochemistry Research International. 2012;2012():1–16. doi: 10.1155/2012/875148.; Tatham MH, Matic I, Mann M, Hay RT. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal. 2011 Jun 21;4(178):rs4. doi: 10.1126/scisignal.2001484. PMID: 21693764.; Bruderer R, Tatham MH, Plechanovova A, Matic I, Garg AK, Hay RT. Purification and identification of endogenous polySUMO conjugates. EMBO Reports. 2011 Jan 21;12(2):142–8. doi: 10.1038/embor.2010.206.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT. System-wide changes to SUMO modifications in response to heat shock. Sci Signal. 2009 May 26;2(72):ra24. doi: 10.1126/scisignal.2000282. PMID: 19471022.; Zhao J. Sumoylation regulates diverse biological processes. Cellular and Molecular Life Sciences. 2007 Sep 04;64(23):3017–33. doi: 10.1007/s00018-007-7137-4.; Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, Lamond AI. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics. 2006 Dec;5(12):2298–310. doi: 10.1074/mcp.m600212-mcp200. PMID: 17000644.
Metabolism of proteins

Accession ID: Reactome:R-HSA-392499
  • 10.1016/j.bbalip.2012.09.010
  • 10.1083/jcb.200708199
  • 10.1210/edrv-2-2-137
  • 10.32607/20758251-2009-1-3-29-51
 Agassandian M, Mallampalli RK. Surfactant phospholipid metabolism. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2013 Mar;1831(3):612–25. doi: 10.1016/j.bbalip.2012.09.010.; Knorre DG, Kudryashova NV, Godovikova TS. Chemical and Functional Aspects of Posttranslational Modification of Proteins. Acta Naturae. 2009 Dec 15;1(3):29–51. doi: 10.32607/20758251-2009-1-3-29-51.; Kutik S, Guiard B, Meyer HE, Wiedemann N, Pfanner N. Cooperation of translocase complexes in mitochondrial protein import. J Cell Biol. 2007 Nov 19;179(4):585–91. PMID: 17998403; PMCID: PMC2080918.; Chertow BS. The role of lysosomes and proteases in hormone secretion and degradation. Endocr Rev. 1981;2(2):137–73. doi: 10.1210/edrv-2-2-137. PMID: 6117463.
Post-translational protein modification

Accession ID: Reactome:R-HSA-597592		 -
SUMOylation

Accession ID: Reactome:R-HSA-2990846
  • 10.1016/j.tcb.2007.08.002
  • 10.1016/j.tox.2010.07.013
  • 10.1038/nrm3011
  • 10.1042/bj20100158
  • 10.1042/bst20130015
  • 10.1242/jcs.050542
 Hay RT. Decoding the SUMO signal. Biochem Soc Trans. 2013 Apr;41(2):463–73. doi: 10.1042/bst20130015. PMID: 23514139.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein SUMOylation. Biochem J. 2010 May 13;428(2):133–45. PMID: 20462400; PMCID: PMC3310159.; Wang Y, Dasso M. SUMOylation and deSUMOylation at a glance. J Cell Sci. 2009 Dec 01;122(Pt 23):4249–52. PMID: 19923268; PMCID: PMC2779127.; Hay RT. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007 Aug;17(8):370–6. doi: 10.1016/j.tcb.2007.08.002. PMID: 17768054.
SUMOylation of intracellular receptors

Accession ID: Reactome:R-HSA-4090294
  • 10.1016/b978-0-12-416673-8.00008-3
  • 10.1016/j.bbadis.2010.12.008
  • 10.1152/ajpheart.00703.2011
  • 10.1621/nrs.10001
 Knutson TP, Lange CA. Dynamic regulation of steroid hormone receptor transcriptional activity by reversible SUMOylation. Vitam Horm. 2013;93():227–61. doi: 10.1016/b978-0-12-416673-8.00008-3. PMID: 23810010.; Wadosky KM, Willis MS. The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation. American Journal of Physiology-Heart and Circulatory Physiology. 2012 Feb;302(3):H515–26. doi: 10.1152/ajpheart.00703.2011.; Anbalagan M, Huderson B, Murphy L, Rowan BG. Post-translational modifications of nuclear receptors and human disease. Nucl Recept Signal. 2012;10():e001. PMID: 22438791; PMCID: PMC3309075.; Treuter E, Venteclef N. Transcriptional control of metabolic and inflammatory pathways by nuclear receptor SUMOylation. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 2011 Aug;1812(8):909–18. doi: 10.1016/j.bbadis.2010.12.008.
Post-translational protein modification

Accession ID: Reactome:R-RNO-597592		 -
SUMOylation

Accession ID: Reactome:R-RNO-2990846
  • 10.1016/j.tcb.2007.08.002
  • 10.1016/j.tox.2010.07.013
  • 10.1038/nrm3011
  • 10.1042/bj20100158
  • 10.1042/bst20130015
  • 10.1242/jcs.050542
 Hay RT. Decoding the SUMO signal. Biochem Soc Trans. 2013 Apr;41(2):463–73. doi: 10.1042/bst20130015. PMID: 23514139.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein SUMOylation. Biochem J. 2010 May 13;428(2):133–45. PMID: 20462400; PMCID: PMC3310159.; Wang Y, Dasso M. SUMOylation and deSUMOylation at a glance. J Cell Sci. 2009 Dec 01;122(Pt 23):4249–52. PMID: 19923268; PMCID: PMC2779127.; Hay RT. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007 Aug;17(8):370–6. doi: 10.1016/j.tcb.2007.08.002. PMID: 17768054.
SUMOylation of intracellular receptors

Accession ID: Reactome:R-RNO-4090294
  • 10.1016/b978-0-12-416673-8.00008-3
  • 10.1016/j.bbadis.2010.12.008
  • 10.1152/ajpheart.00703.2011
  • 10.1621/nrs.10001
 Knutson TP, Lange CA. Dynamic regulation of steroid hormone receptor transcriptional activity by reversible SUMOylation. Vitam Horm. 2013;93():227–61. doi: 10.1016/b978-0-12-416673-8.00008-3. PMID: 23810010.; Wadosky KM, Willis MS. The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation. American Journal of Physiology-Heart and Circulatory Physiology. 2012 Feb;302(3):H515–26. doi: 10.1152/ajpheart.00703.2011.; Anbalagan M, Huderson B, Murphy L, Rowan BG. Post-translational modifications of nuclear receptors and human disease. Nucl Recept Signal. 2012;10():e001. PMID: 22438791; PMCID: PMC3309075.; Treuter E, Venteclef N. Transcriptional control of metabolic and inflammatory pathways by nuclear receptor SUMOylation. Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 2011 Aug;1812(8):909–18. doi: 10.1016/j.bbadis.2010.12.008.
SUMO E3 ligases SUMOylate target proteins

Accession ID: Reactome:R-XTR-3108232
  • 10.1007/s00018-007-7137-4
  • 10.1016/j.tox.2010.07.013
  • 10.1038/embor.2010.206
  • 10.1038/nrm3011
  • 10.1038/nsmb.2526
  • 10.1074/mcp.m600212-mcp200
  • 10.1126/scisignal.2000282
  • 10.1126/scisignal.2001484
  • 10.1146/annurev-biochem-061909-093311
  • 10.1146/annurev-genet-111212-133453
  • 10.1155/2012/875148
  • 10.12703/p5-45
  • 10.2741/s388
 Jentsch S, Psakhye I. Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu Rev Genet. 2013;47():167–86. doi: 10.1146/annurev-genet-111212-133453. PMID: 24016193.; Yang XJ, Chiang CM. Sumoylation in gene regulation, human disease, and therapeutic action. F1000Prime Rep. 2013;5():45. PMID: 24273646; PMCID: PMC3816760.; Flotho A, Melchior F. Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem. 2013;82():357–85. doi: 10.1146/annurev-biochem-061909-093311. PMID: 23746258.; Becker J, Barysch SV, Karaca S, Dittner C, Hsiao HH, Berriel Diaz M, Herzig S, Urlaub H, Melchior F. Detecting endogenous SUMO targets in mammalian cells and tissues. Nat Struct Mol Biol. 2013 Apr;20(4):525–31. doi: 10.1038/nsmb.2526. PMID: 23503365.; Citro S, Chiocca S. Sumo paralogs: redundancy and divergencies. Front Biosci (Schol Ed). 2013 Jan 01;5(2):544–53. doi: 10.2741/s388. PMID: 23277067.; Da Silva-Ferrada E, Lopitz-Otsoa F, Lang V, Rodríguez MS, Matthiesen R. Strategies to Identify Recognition Signals and Targets of SUMOylation. Biochemistry Research International. 2012;2012():1–16. doi: 10.1155/2012/875148.; Tatham MH, Matic I, Mann M, Hay RT. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal. 2011 Jun 21;4(178):rs4. doi: 10.1126/scisignal.2001484. PMID: 21693764.; Bruderer R, Tatham MH, Plechanovova A, Matic I, Garg AK, Hay RT. Purification and identification of endogenous polySUMO conjugates. EMBO Reports. 2011 Jan 21;12(2):142–8. doi: 10.1038/embor.2010.206.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT. System-wide changes to SUMO modifications in response to heat shock. Sci Signal. 2009 May 26;2(72):ra24. doi: 10.1126/scisignal.2000282. PMID: 19471022.; Zhao J. Sumoylation regulates diverse biological processes. Cellular and Molecular Life Sciences. 2007 Sep 04;64(23):3017–33. doi: 10.1007/s00018-007-7137-4.; Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, Lamond AI. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics. 2006 Dec;5(12):2298–310. doi: 10.1074/mcp.m600212-mcp200. PMID: 17000644.
Metabolism of proteins

Accession ID: Reactome:R-RNO-392499
  • 10.1016/j.bbalip.2012.09.010
  • 10.1083/jcb.200708199
  • 10.1210/edrv-2-2-137
  • 10.32607/20758251-2009-1-3-29-51
 Agassandian M, Mallampalli RK. Surfactant phospholipid metabolism. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2013 Mar;1831(3):612–25. doi: 10.1016/j.bbalip.2012.09.010.; Knorre DG, Kudryashova NV, Godovikova TS. Chemical and Functional Aspects of Posttranslational Modification of Proteins. Acta Naturae. 2009 Dec 15;1(3):29–51. doi: 10.32607/20758251-2009-1-3-29-51.; Kutik S, Guiard B, Meyer HE, Wiedemann N, Pfanner N. Cooperation of translocase complexes in mitochondrial protein import. J Cell Biol. 2007 Nov 19;179(4):585–91. PMID: 17998403; PMCID: PMC2080918.; Chertow BS. The role of lysosomes and proteases in hormone secretion and degradation. Endocr Rev. 1981;2(2):137–73. doi: 10.1210/edrv-2-2-137. PMID: 6117463.
Metabolism of proteins

Accession ID: Reactome:R-SSC-392499
  • 10.1016/j.bbalip.2012.09.010
  • 10.1083/jcb.200708199
  • 10.1210/edrv-2-2-137
  • 10.32607/20758251-2009-1-3-29-51
 Agassandian M, Mallampalli RK. Surfactant phospholipid metabolism. Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids. 2013 Mar;1831(3):612–25. doi: 10.1016/j.bbalip.2012.09.010.; Knorre DG, Kudryashova NV, Godovikova TS. Chemical and Functional Aspects of Posttranslational Modification of Proteins. Acta Naturae. 2009 Dec 15;1(3):29–51. doi: 10.32607/20758251-2009-1-3-29-51.; Kutik S, Guiard B, Meyer HE, Wiedemann N, Pfanner N. Cooperation of translocase complexes in mitochondrial protein import. J Cell Biol. 2007 Nov 19;179(4):585–91. PMID: 17998403; PMCID: PMC2080918.; Chertow BS. The role of lysosomes and proteases in hormone secretion and degradation. Endocr Rev. 1981;2(2):137–73. doi: 10.1210/edrv-2-2-137. PMID: 6117463.
SUMO E3 ligases SUMOylate target proteins

Accession ID: Reactome:R-SSC-3108232
  • 10.1007/s00018-007-7137-4
  • 10.1016/j.tox.2010.07.013
  • 10.1038/embor.2010.206
  • 10.1038/nrm3011
  • 10.1038/nsmb.2526
  • 10.1074/mcp.m600212-mcp200
  • 10.1126/scisignal.2000282
  • 10.1126/scisignal.2001484
  • 10.1146/annurev-biochem-061909-093311
  • 10.1146/annurev-genet-111212-133453
  • 10.1155/2012/875148
  • 10.12703/p5-45
  • 10.2741/s388
 Jentsch S, Psakhye I. Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu Rev Genet. 2013;47():167–86. doi: 10.1146/annurev-genet-111212-133453. PMID: 24016193.; Yang XJ, Chiang CM. Sumoylation in gene regulation, human disease, and therapeutic action. F1000Prime Rep. 2013;5():45. PMID: 24273646; PMCID: PMC3816760.; Flotho A, Melchior F. Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem. 2013;82():357–85. doi: 10.1146/annurev-biochem-061909-093311. PMID: 23746258.; Becker J, Barysch SV, Karaca S, Dittner C, Hsiao HH, Berriel Diaz M, Herzig S, Urlaub H, Melchior F. Detecting endogenous SUMO targets in mammalian cells and tissues. Nat Struct Mol Biol. 2013 Apr;20(4):525–31. doi: 10.1038/nsmb.2526. PMID: 23503365.; Citro S, Chiocca S. Sumo paralogs: redundancy and divergencies. Front Biosci (Schol Ed). 2013 Jan 01;5(2):544–53. doi: 10.2741/s388. PMID: 23277067.; Da Silva-Ferrada E, Lopitz-Otsoa F, Lang V, Rodríguez MS, Matthiesen R. Strategies to Identify Recognition Signals and Targets of SUMOylation. Biochemistry Research International. 2012;2012():1–16. doi: 10.1155/2012/875148.; Tatham MH, Matic I, Mann M, Hay RT. Comparative proteomic analysis identifies a role for SUMO in protein quality control. Sci Signal. 2011 Jun 21;4(178):rs4. doi: 10.1126/scisignal.2001484. PMID: 21693764.; Bruderer R, Tatham MH, Plechanovova A, Matic I, Garg AK, Hay RT. Purification and identification of endogenous polySUMO conjugates. EMBO Reports. 2011 Jan 21;12(2):142–8. doi: 10.1038/embor.2010.206.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Golebiowski F, Matic I, Tatham MH, Cole C, Yin Y, Nakamura A, Cox J, Barton GJ, Mann M, Hay RT. System-wide changes to SUMO modifications in response to heat shock. Sci Signal. 2009 May 26;2(72):ra24. doi: 10.1126/scisignal.2000282. PMID: 19471022.; Zhao J. Sumoylation regulates diverse biological processes. Cellular and Molecular Life Sciences. 2007 Sep 04;64(23):3017–33. doi: 10.1007/s00018-007-7137-4.; Vertegaal AC, Andersen JS, Ogg SC, Hay RT, Mann M, Lamond AI. Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Mol Cell Proteomics. 2006 Dec;5(12):2298–310. doi: 10.1074/mcp.m600212-mcp200. PMID: 17000644.
Post-translational protein modification

Accession ID: Reactome:R-XTR-597592		 -
SUMOylation

Accession ID: Reactome:R-XTR-2990846
  • 10.1016/j.tcb.2007.08.002
  • 10.1016/j.tox.2010.07.013
  • 10.1038/nrm3011
  • 10.1042/bj20100158
  • 10.1042/bst20130015
  • 10.1242/jcs.050542
 Hay RT. Decoding the SUMO signal. Biochem Soc Trans. 2013 Apr;41(2):463–73. doi: 10.1042/bst20130015. PMID: 23514139.; Hannoun Z, Greenhough S, Jaffray E, Hay RT, Hay DC. Post-translational modification by SUMO. Toxicology. 2010 Dec 30;278(3):288–93. doi: 10.1016/j.tox.2010.07.013. PMID: 20674646.; Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. 2010 Nov 23;11(12):861–71. doi: 10.1038/nrm3011.; Wilkinson KA, Henley JM. Mechanisms, regulation and consequences of protein SUMOylation. Biochem J. 2010 May 13;428(2):133–45. PMID: 20462400; PMCID: PMC3310159.; Wang Y, Dasso M. SUMOylation and deSUMOylation at a glance. J Cell Sci. 2009 Dec 01;122(Pt 23):4249–52. PMID: 19923268; PMCID: PMC2779127.; Hay RT. SUMO-specific proteases: a twist in the tail. Trends Cell Biol. 2007 Aug;17(8):370–6. doi: 10.1016/j.tcb.2007.08.002. PMID: 17768054.
SUMOylation of intracellular receptors

Accession ID: Reactome:R-XTR-4090294
  • 10.1016/b978-0-12-416673-8.00008-3
  • 10.1016/j.bbadis.2010.12.008
  • 10.1152/ajpheart.00703.2011
  • 10.1621/nrs.10001
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