SUMOylation of intracellular receptors (Homo sapiens)

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6, 11, 24, 282, 22, 232951, 15, 312582516313, 21, 33264, 18, 32162534252, 22, 2331, 34359, 12, 277, 1410, 17nucleoplasmSUMO1-K50,K146,K443-THRB UBE2I-G93-SUMO2 RORASUMO1-C93-UBE2I SUMO1-C93-UBE2I PIAS2-2UBE2IPPARAK303-ESR1-G97-SUMO1 SUMO1-C93-UBE2I K520-AR-G97-SUMO1 SUMO1-K283,K389-THRA ARPIAS2-2 SUMO2,3-K409,K447-NR1H2 SUMO1-K132,K289-NR1H4 RARANR1H3:hydroxycholesterolSUMO3-C93-UBE2I SUMO3:UBE2ISUMO2-K240-RORASUMO1-C93-UBE2I K277-NR3C1-G97-SUMO1 SUMO2-C93-UBE2I SUMO1:RORASUMO3-K50,K146,K443-THRB2SUMO1:THRA-2SUMO1-K240-RORA UBE2I-G93-SUMO2 PIAS1 UBE2ICDCA UBE2I-G97-SUMO1 UBE2I-G92-SUMO3 NR2C1PIAS1,3THRBUBE2IK494-NR3C2-G97-SUMO1 UBE2ISUMO2-C93-UBE2I UBE2I-G93-SUMO2 SUMO1:C93-UBE2I22beta-hydroxycholesterol PIAS1 NR1H4-2 2SUMO1:AR2SUMO1:NR5A1DEXA SUMO1-C93-UBE2I SUMO1:C93-UBE2IPIAS3 K7-PGR-G97-SUMO1 UBE2I-G92-SUMO3 UBE2ISUMO3:UBE2INR3C1 UBE2ISUMO1:C93-UBE2IUBE2ISUMO2:UBE2Icis-bicyclo(3.3.0)oct-2-ene UBE2I-G92-SUMO3 THRA-2K389-THRA-G97-SUMO1 SUMO1-K89,K399,K428.K494-NR3C2 SUMO1-K107,K395-PPARG SUMO3-C93-UBE2I K132-NR1H4-G97-SUMO1 2SUMO1:PPARGSUMO1:PPARAK283-THRA-G97-SUMO1 UBE2I-G97-SUMO1 4SUMO1:NR3C2Rifampicin 24-hydroxycholesterol UBE2I-G92-SUMO3 PGRSUMO1-K108-RXRA SUMO1:C93-UBE2IUBE2I-G97-SUMO1 PPARA-G97-SUMO1 K388-PGR-G97-SUMO1 SUMO1:C93-UBE2INR5A2-2 SUMO2-C93-UBE2I PIAS1SUMO1:C93-UBE2ISUMO3:UBE2ISUMO3-NR1I2:rifampicinPPARG-G97-SUMO1 SUMO1-C93-UBE2I SUMO1-K277,K293-NR3C1 24-hydroxycholesterol UBE2I-G97-SUMO1 SUMO2-C93-UBE2I K194-NR5A1-G97-SUMO1 K302-ESR1-G97-SUMO1 UBE2IPPARGNR1H2 UBE2IK299-ESR1-G97-SUMO1 SUMO1-5K-ESR1 NR4A2DEXA 3SUMO1:PGRSUMO1:NR2C1K266-ESR1-G97-SUMO1 NR1I2-1 UBE2I-G97-SUMO1 UBE2IUBE2I-G97-SUMO1 SUMO2-K119,K194-NR5A1PIAS1,2-1SUMO1:C93-UBE2IESR1PIAS1,2-1UBE2I-G97-SUMO1 UBE2I:SUMO2,UBE2I:SUMO3NR5A1NR3C1:Dexamethasonecis-bicyclo(3.3.0)oct-2-ene K428-NR3C2-G97-SUMO1 NR5A2:cis-bicyclo(3.3.0)oct-2-enePIAS3 SUMO3-NR1I2 UBE2I-G97-SUMO1 K399-NR3C2-G97-SUMO1 SUMO2:UBE2ISUMO2-C93-UBE2I PIAS2-2 22beta-hydroxycholesterol VDRK119-NR5A1-G97-SUMO1 5SUMO1:ESR1PIAS2-1 UBE2I-G97-SUMO1 PIAS324-hydroxycholesterol NR3C2PIAS1 UBE2I-G93-SUMO2 SUMO2:UBE2ISUMO2:UBE2ISUMO2-C93-UBE2I NR1H4-G97-SUMO1 SUMO2,3-NR1H2:hydroxycholesterolK531-PGR-G97-SUMO1 PIAS1 UBE2I-G93-SUMO2 PIAS2-1 SUMO1-C93-UBE2I SUMO1-C93-UBE2I SUMO3-K283,K389-THRA-2SUMO2,3-K558,K577-NR4A2UBE2I-G93-SUMO2 SUMO2-K166,K171,K399-RARAK268-ESR1-G97-SUMO1 NR1I2:rifampicinRORA-G97-SUMO1 SUMO1:C93-UBE2INR1H3-1 SUMO1-K185-PPARA PIAS2-2,PIAS3,PIAS4K293-NR3C1-G97-SUMO1 PIAS4UBE2I:SUMO2,UBE2I:SUMO3PIAS1 K89-NR3C2-G97-SUMO1 SUMO2,3-NR1H3:hydroxysterolSUMO1:NR5A2:cis-bicyclo(3.3.0)oct-2-eneNR1H2:hydroxycholesterolUBE2I3SUMO1:THRBUBE2I-G97-SUMO1 UBE2I24-hydroxycholesterol SUMO1-C93-UBE2I 22beta-hydroxycholesterol UBE2I-G97-SUMO1 CDCA SUMO1-C93-UBE2I SUMO1:C93-UBE2INR1H4:chenodeoxycholateK146-THRB-G97-SUMO1 RXRA-G97-SUMO1 Rifampicin 2SUMO1:NR3C1:DEXAPIAS1,3K443-THRB-G97-SUMO1 UBE2IK395-PPARG-G97-SUMO1 PIAS4 SUMO2-VDRUBE2ISUMO1-C93-UBE2I NR2C1-G97-SUMO1 SUMO1-K386,520-AR SUMO1-K119,K194-NR5A1 SUMO1-K270-NR5A2-2 SUMO1-K7,K388,K531-PGR SUMO1:RXRAUBE2IHDAC4SUMO1:C93-UBE2ISUMO1:C93-UBE2ISUMO3-C93-UBE2I K50-THRB-G97-SUMO1 UBE2ISUMO2,3-NR1H3 SUMO1:C93-UBE2IUBE2I-G97-SUMO1 2SUMO1:NR1H4:chenodeoxycholatePIAS1,2-2SUMO3-C93-UBE2I PIAS3 K386-AR-G97-SUMO1 SUMO1-K250-NR2C1 NR5A2-G97-SUMO1 UBE2I-G92-SUMO3 22beta-hydroxycholesterol SUMO3-C93-UBE2I RXRASUMO1-C93-UBE2I 3030520, 30253417, 1434195343138353020, 301926179, 12, 2720, 3034420, 30313016302, 22, 2313, 21, 3310, 1720, 3025820, 301, 15, 3129343


At least 17 nuclear receptors have been discovered to be SUMOylated (reviewed in Treuter and Venteclef 2011, Wadosky et al. 2012, Knutson and Lange 2013). In all but a few cases (notably AR and RORA) SUMOylation causes transcriptional repression. Repression by SUMOylation is believed to occur through several mechanisms: interference with DNA binding, recruitment of corepressors, retention of corepressors at non-target promoters (transrepression), re-localization of nuclear receptors within the nucleus, interference with dimerization of receptors, and interference (crosstalk) with other post-translational modifications. SUMOylation of receptors affects inflammation and disease processes (Anbalagan et al. 2012). View original pathway at:Reactome.


Pathway is converted from Reactome ID: 4090294
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

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Ontology Terms



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  1. Ogawa H, Komatsu T, Hiraoka Y, Morohashi K.; ''Transcriptional Suppression by Transient Recruitment of ARIP4 to Sumoylated nuclear receptor Ad4BP/SF-1.''; PubMed
  2. Komatsu T, Mizusaki H, Mukai T, Ogawa H, Baba D, Shirakawa M, Hatakeyama S, Nakayama KI, Yamamoto H, Kikuchi A, Morohashi K.; ''Small ubiquitin-like modifier 1 (SUMO-1) modification of the synergy control motif of Ad4 binding protein/steroidogenic factor 1 (Ad4BP/SF-1) regulates synergistic transcription between Ad4BP/SF-1 and Sox9.''; PubMed
  3. Choi SJ, Chung SS, Rho EJ, Lee HW, Lee MH, Choi HS, Seol JH, Baek SH, Bang OS, Chung CH.; ''Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1.''; PubMed
  4. Poukka H, Karvonen U, Janne OA, Palvimo JJ.; ''Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1).''; PubMed
  5. Pourcet B, Pineda-Torra I, Derudas B, Staels B, Glineur C.; ''SUMOylation of human peroxisome proliferator-activated receptor alpha inhibits its trans-activity through the recruitment of the nuclear corepressor NCoR.''; PubMed
  6. Knutson TP, Lange CA.; ''Dynamic regulation of steroid hormone receptor transcriptional activity by reversible SUMOylation.''; PubMed
  7. Tian S, Poukka H, Palvimo JJ, Jänne OA.; ''Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor.''; PubMed
  8. Hu G, Xu C, Staudinger JL.; ''Pregnane X receptor is SUMOylated to repress the inflammatory response.''; PubMed
  9. Tirard M, Almeida OF, Hutzler P, Melchior F, Michaelidis TM.; ''Sumoylation and proteasomal activity determine the transactivation properties of the mineralocorticoid receptor.''; PubMed
  10. Balasubramaniyan N, Luo Y, Sun AQ, Suchy FJ.; ''SUMOylation of the farnesoid X receptor (FXR) regulates the expression of FXR target genes.''; PubMed
  11. Wadosky KM, Willis MS.; ''The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation.''; PubMed
  12. Tallec LP, Kirsh O, Lecomte MC, Viengchareun S, Zennaro MC, Dejean A, Lombès M.; ''Protein inhibitor of activated signal transducer and activator of transcription 1 interacts with the N-terminal domain of mineralocorticoid receptor and represses its transcriptional activity: implication of small ubiquitin-related modifier 1 modification.''; PubMed
  13. Man JH, Li HY, Zhang PJ, Zhou T, He K, Pan X, Liang B, Li AL, Zhao J, Gong WL, Jin BF, Xia Q, Yu M, Shen BF, Zhang XM.; ''PIAS3 induction of PRB sumoylation represses PRB transactivation by destabilizing its retention in the nucleus.''; PubMed
  14. Impens F, Radoshevich L, Cossart P, Ribet D.; ''Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.''; PubMed
  15. Chalkiadaki A, Talianidis I.; ''SUMO-dependent compartmentalization in promyelocytic leukemia protein nuclear bodies prevents the access of LRH-1 to chromatin.''; PubMed
  16. Hwang EJ, Lee JM, Jeong J, Park JH, Yang Y, Lim JS, Kim JH, Baek SH, Kim KI.; ''SUMOylation of RORalpha potentiates transcriptional activation function.''; PubMed
  17. Vavassori P, Mencarelli A, Renga B, Distrutti E, Fiorucci S.; ''The bile acid receptor FXR is a modulator of intestinal innate immunity.''; PubMed
  18. Kotaja N, Karvonen U, Jänne OA, Palvimo JJ.; ''PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases.''; PubMed
  19. Stankovic-Valentin N, Deltour S, Seeler J, Pinte S, Vergoten G, Guérardel C, Dejean A, Leprince D.; ''An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity.''; PubMed
  20. Kamitani T, Kito K, Nguyen HP, Fukuda-Kamitani T, Yeh ET.; ''Characterization of a second member of the sentrin family of ubiquitin-like proteins.''; PubMed
  21. Daniel AR, Faivre EJ, Lange CA.; ''Phosphorylation-dependent antagonism of sumoylation derepresses progesterone receptor action in breast cancer cells.''; PubMed
  22. Suda N, Shibata H, Kurihara I, Ikeda Y, Kobayashi S, Yokota K, Murai-Takeda A, Nakagawa K, Oya M, Murai M, Rainey WE, Saruta T, Itoh H.; ''Coactivation of SF-1-mediated transcription of steroidogenic enzymes by Ubc9 and PIAS1.''; PubMed
  23. Chen WY, Lee WC, Hsu NC, Huang F, Chung BC.; ''SUMO modification of repression domains modulates function of nuclear receptor 5A1 (steroidogenic factor-1).''; PubMed
  24. Treuter E, Venteclef N.; ''Transcriptional control of metabolic and inflammatory pathways by nuclear receptor SUMOylation.''; PubMed
  25. Liu YY, Kogai T, Schultz JJ, Mody K, Brent GA.; ''Thyroid hormone receptor isoform-specific modification by small ubiquitin-like modifier (SUMO) modulates thyroid hormone-dependent gene regulation.''; PubMed
  26. Sentis S, Le Romancer M, Bianchin C, Rostan MC, Corbo L.; ''Sumoylation of the estrogen receptor alpha hinge region regulates its transcriptional activity.''; PubMed
  27. Yokota K, Shibata H, Kurihara I, Kobayashi S, Suda N, Murai-Takeda A, Saito I, Kitagawa H, Kato S, Saruta T, Itoh H.; ''Coactivation of the N-terminal transactivation of mineralocorticoid receptor by Ubc9.''; PubMed
  28. Anbalagan M, Huderson B, Murphy L, Rowan BG.; ''Post-translational modifications of nuclear receptors and human disease.''; PubMed
  29. Zhu L, Santos NC, Kim KH.; ''Small ubiquitin-like modifier-2 modification of retinoic acid receptor-alpha regulates its subcellular localization and transcriptional activity.''; PubMed
  30. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed
  31. Venteclef N, Jakobsson T, Ehrlund A, Damdimopoulos A, Mikkonen L, Ellis E, Nilsson LM, Parini P, Jänne OA, Gustafsson JA, Steffensen KR, Treuter E.; ''GPS2-dependent corepressor/SUMO pathways govern anti-inflammatory actions of LRH-1 and LXRbeta in the hepatic acute phase response.''; PubMed
  32. Nishida T, Yasuda H.; ''PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription.''; PubMed
  33. Abdel-Hafiz H, Dudevoir ML, Horwitz KB.; ''Mechanisms underlying the control of progesterone receptor transcriptional activity by SUMOylation.''; PubMed
  34. Ghisletti S, Huang W, Ogawa S, Pascual G, Lin ME, Willson TM, Rosenfeld MG, Glass CK.; ''Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma.''; PubMed
  35. Jena S, Lee WP, Doherty D, Thompson PD.; ''PIAS4 represses vitamin D receptor-mediated signaling and acts as an E3-SUMO ligase towards vitamin D receptor.''; PubMed


101684view14:01, 1 November 2018DeSlOntology Term : 'receptor cell' added !
101683view14:00, 1 November 2018DeSlOntology Term : 'sumoylation pathway' added !
101275view11:16, 1 November 2018ReactomeTeamreactome version 66
101191view21:39, 31 October 2018ReactomeTeamNew pathway

External references


View all...
NameTypeDatabase referenceComment
22beta-hydroxycholesterol MetaboliteCHEBI:1301 (ChEBI)
24-hydroxycholesterol MetaboliteCHEBI:34310 (ChEBI)
2SUMO1:ARComplexR-HSA-4090282 (Reactome)
2SUMO1:NR1H4:chenodeoxycholateComplexR-HSA-4755409 (Reactome)
2SUMO1:NR3C1:DEXAComplexR-HSA-4341015 (Reactome)
2SUMO1:NR5A1ComplexR-HSA-4546374 (Reactome)
2SUMO1:PPARGComplexR-HSA-4717494 (Reactome)
2SUMO1:THRA-2ComplexR-HSA-4719400 (Reactome) PIAS2-2 SUMOylates THRA (alpha-1 isoform, THRA-2 in UniProt) with SUMO1 at lysine-283 and lysine-389. (A lysine residue corresponding to lysine-389 does not exist in the alpha-2 isoform.)
3SUMO1:PGRComplexR-HSA-4341081 (Reactome)
3SUMO1:THRBComplexR-HSA-4719435 (Reactome)
4SUMO1:NR3C2ComplexR-HSA-4341117 (Reactome)
5SUMO1:ESR1ComplexR-HSA-4090338 (Reactome)
ARProteinP10275 (Uniprot-TrEMBL)
CDCA MetaboliteCHEBI:16755 (ChEBI)
DEXA MetaboliteCHEBI:41879 (ChEBI)
ESR1ProteinP03372 (Uniprot-TrEMBL)
HDAC4ProteinP56524 (Uniprot-TrEMBL)
K119-NR5A1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K132-NR1H4-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K146-THRB-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K194-NR5A1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K266-ESR1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K268-ESR1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K277-NR3C1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K283-THRA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K293-NR3C1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K299-ESR1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K302-ESR1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K303-ESR1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K386-AR-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K388-PGR-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K389-THRA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K395-PPARG-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K399-NR3C2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K428-NR3C2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K443-THRB-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K494-NR3C2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K50-THRB-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K520-AR-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K531-PGR-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K7-PGR-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K89-NR3C2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NR1H2 ProteinP55055 (Uniprot-TrEMBL)
NR1H2:hydroxycholesterolComplexR-HSA-4720431 (Reactome)
NR1H3-1 ProteinQ13133-1 (Uniprot-TrEMBL)
NR1H3:hydroxycholesterolComplexR-HSA-4720438 (Reactome)
NR1H4-2 ProteinQ96RI1-2 (Uniprot-TrEMBL)
NR1H4-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NR1H4:chenodeoxycholateComplexR-HSA-4755440 (Reactome)
NR1I2-1 ProteinO75469-1 (Uniprot-TrEMBL)
NR1I2:rifampicinComplexR-HSA-4755506 (Reactome)
NR2C1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NR2C1ProteinP13056 (Uniprot-TrEMBL)
NR3C1 ProteinP04150 (Uniprot-TrEMBL)
NR3C1:DexamethasoneComplexR-HSA-879850 (Reactome)
NR3C2ProteinP08235 (Uniprot-TrEMBL)
NR4A2ProteinP43354 (Uniprot-TrEMBL)
NR5A1ProteinQ13285 (Uniprot-TrEMBL)
NR5A2-2 ProteinO00482-2 (Uniprot-TrEMBL)
NR5A2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
NR5A2:cis-bicyclo(3.3.0)oct-2-eneComplexR-HSA-4755467 (Reactome)
PGRProteinP06401 (Uniprot-TrEMBL)
PIAS1 ProteinO75925 (Uniprot-TrEMBL)
PIAS1,2-1ComplexR-HSA-4090382 (Reactome)
PIAS1,2-2ComplexR-HSA-4717502 (Reactome)
PIAS1,3ComplexR-HSA-4086016 (Reactome)
PIAS1ProteinO75925 (Uniprot-TrEMBL)
PIAS2-1 ProteinO75928-1 (Uniprot-TrEMBL)
PIAS2-2 ProteinO75928-2 (Uniprot-TrEMBL)
PIAS2-2,PIAS3,PIAS4ComplexR-HSA-9610513 (Reactome)
PIAS2-2ProteinO75928-2 (Uniprot-TrEMBL)
PIAS3 ProteinQ9Y6X2 (Uniprot-TrEMBL)
PIAS3ProteinQ9Y6X2 (Uniprot-TrEMBL)
PIAS4 ProteinQ8N2W9 (Uniprot-TrEMBL)
PIAS4ProteinQ8N2W9 (Uniprot-TrEMBL)
PPARA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
PPARAProteinQ07869 (Uniprot-TrEMBL)
PPARG-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
PPARGProteinP37231 (Uniprot-TrEMBL)
RARAProteinP10276 (Uniprot-TrEMBL)
RORA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
RORAProteinP35398 (Uniprot-TrEMBL)
RXRA-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
RXRAProteinP19793 (Uniprot-TrEMBL)
Rifampicin MetaboliteCHEBI:28077 (ChEBI)
SUMO1-5K-ESR1 ProteinP03372 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-K107,K395-PPARG ProteinP37231 (Uniprot-TrEMBL)
SUMO1-K108-RXRA ProteinP19793 (Uniprot-TrEMBL)
SUMO1-K119,K194-NR5A1 ProteinQ13285 (Uniprot-TrEMBL)
SUMO1-K132,K289-NR1H4 ProteinQ96RI1-2 (Uniprot-TrEMBL) Lysine-289 in NR1H4-1 corresponds to lysine-277 in NR1H4-2.
SUMO1-K185-PPARA ProteinQ07869 (Uniprot-TrEMBL)
SUMO1-K240-RORA ProteinP35398 (Uniprot-TrEMBL)
SUMO1-K250-NR2C1 ProteinP13056 (Uniprot-TrEMBL)
SUMO1-K270-NR5A2-2 ProteinO00482-2 (Uniprot-TrEMBL) Lysine-270 in the long isoform (isoform 2) corresponds to lysine-224 in the shorter isoform (isoform 1).
SUMO1-K277,K293-NR3C1 ProteinP04150 (Uniprot-TrEMBL)
SUMO1-K283,K389-THRA ProteinP10827-2 (Uniprot-TrEMBL)
SUMO1-K386,520-AR ProteinP10275 (Uniprot-TrEMBL)
SUMO1-K50,K146,K443-THRB ProteinP10828 (Uniprot-TrEMBL)
SUMO1-K7,K388,K531-PGR ProteinP06401 (Uniprot-TrEMBL)
SUMO1-K89,K399,K428.K494-NR3C2 ProteinP08235 (Uniprot-TrEMBL)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:NR2C1ComplexR-HSA-4717483 (Reactome)
SUMO1:NR5A2:cis-bicyclo(3.3.0)oct-2-eneComplexR-HSA-4755410 (Reactome)
SUMO1:PPARAComplexR-HSA-4341053 (Reactome)
SUMO1:RORAComplexR-HSA-4719452 (Reactome)
SUMO1:RXRAComplexR-HSA-4341089 (Reactome)
SUMO2,3-K409,K447-NR1H2 ProteinP55055 (Uniprot-TrEMBL)
SUMO2,3-K558,K577-NR4A2ProteinP43354 (Uniprot-TrEMBL)
SUMO2,3-NR1H2:hydroxycholesterolComplexR-HSA-4720444 (Reactome)
SUMO2,3-NR1H3 ProteinQ13133-1 (Uniprot-TrEMBL)
SUMO2,3-NR1H3:hydroxysterolComplexR-HSA-4720433 (Reactome)
SUMO2-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO2-K119,K194-NR5A1ProteinQ13285 (Uniprot-TrEMBL)
SUMO2-K166,K171,K399-RARAProteinP10276 (Uniprot-TrEMBL)
SUMO2-K240-RORAProteinP35398 (Uniprot-TrEMBL)
SUMO2-VDRProteinP11473 (Uniprot-TrEMBL)
SUMO2:UBE2IComplexR-HSA-2993778 (Reactome)
SUMO3-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO3-K283,K389-THRA-2ProteinP10827-2 (Uniprot-TrEMBL) PIAS2-2 SUMOylates THRA (alpha-1 isoform, THRA-2 in UniProt) with SUMO3 at lysine-283 and lysine-389. (A lysine residue corresponding to lysine-389 does not exist in the alpha-2 isoform.)
SUMO3-K50,K146,K443-THRBProteinP10828 (Uniprot-TrEMBL)
SUMO3-NR1I2 ProteinO75469-1 (Uniprot-TrEMBL)
SUMO3-NR1I2:rifampicinComplexR-HSA-4755441 (Reactome)
SUMO3:UBE2IComplexR-HSA-2993782 (Reactome)
THRA-2ProteinP10827-2 (Uniprot-TrEMBL)
THRBProteinP10828 (Uniprot-TrEMBL)
UBE2I-G92-SUMO3 ProteinP55854 (Uniprot-TrEMBL)
UBE2I-G93-SUMO2 ProteinP61956 (Uniprot-TrEMBL)
UBE2I-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
UBE2I:SUMO2,UBE2I:SUMO3ComplexR-HSA-3899312 (Reactome)
UBE2IProteinP63279 (Uniprot-TrEMBL)
VDRProteinP11473 (Uniprot-TrEMBL)
cis-bicyclo(3.3.0)oct-2-ene MetaboliteCHEBI:77361 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2SUMO1:ARArrowR-HSA-4090390 (Reactome)
2SUMO1:NR1H4:chenodeoxycholateArrowR-HSA-4755419 (Reactome)
2SUMO1:NR3C1:DEXAArrowR-HSA-4341025 (Reactome)
2SUMO1:NR5A1ArrowR-HSA-4546386 (Reactome)
2SUMO1:PPARGArrowR-HSA-4717461 (Reactome)
2SUMO1:THRA-2ArrowR-HSA-4719447 (Reactome)
3SUMO1:PGRArrowR-HSA-4341073 (Reactome)
3SUMO1:THRBArrowR-HSA-4719424 (Reactome)
4SUMO1:NR3C2ArrowR-HSA-4341016 (Reactome)
5SUMO1:ESR1ArrowR-HSA-4090408 (Reactome)
ARR-HSA-4090390 (Reactome)
ESR1R-HSA-4090408 (Reactome)
HDAC4mim-catalysisR-HSA-4720432 (Reactome)
HDAC4mim-catalysisR-HSA-4720446 (Reactome)
NR1H2:hydroxycholesterolR-HSA-4720432 (Reactome)
NR1H3:hydroxycholesterolR-HSA-4720446 (Reactome)
NR1H4:chenodeoxycholateR-HSA-4755419 (Reactome)
NR1I2:rifampicinR-HSA-4755524 (Reactome)
NR2C1R-HSA-4717521 (Reactome)
NR3C1:DexamethasoneR-HSA-4341025 (Reactome)
NR3C2R-HSA-4341016 (Reactome)
NR4A2R-HSA-4755526 (Reactome)
NR5A1R-HSA-4546385 (Reactome)
NR5A1R-HSA-4546386 (Reactome)
NR5A2:cis-bicyclo(3.3.0)oct-2-eneR-HSA-4755494 (Reactome)
PGRR-HSA-4341073 (Reactome)
PIAS1,2-1mim-catalysisR-HSA-4090390 (Reactome)
PIAS1,2-1mim-catalysisR-HSA-4755494 (Reactome)
PIAS1,2-2mim-catalysisR-HSA-4717461 (Reactome)
PIAS1,3mim-catalysisR-HSA-4090408 (Reactome)
PIAS1,3mim-catalysisR-HSA-4546385 (Reactome)
PIAS1,3mim-catalysisR-HSA-4546386 (Reactome)
PIAS1mim-catalysisR-HSA-4341016 (Reactome)
PIAS1mim-catalysisR-HSA-4717521 (Reactome)
PIAS1mim-catalysisR-HSA-4719424 (Reactome)
PIAS1mim-catalysisR-HSA-4719448 (Reactome)
PIAS2-2,PIAS3,PIAS4mim-catalysisR-HSA-4719413 (Reactome)
PIAS2-2,PIAS3,PIAS4mim-catalysisR-HSA-4719436 (Reactome)
PIAS2-2mim-catalysisR-HSA-4719423 (Reactome)
PIAS2-2mim-catalysisR-HSA-4719447 (Reactome)
PIAS3mim-catalysisR-HSA-4341073 (Reactome)
PIAS4mim-catalysisR-HSA-4341070 (Reactome)
PIAS4mim-catalysisR-HSA-4546387 (Reactome)
PIAS4mim-catalysisR-HSA-4755526 (Reactome)
PPARAR-HSA-4341070 (Reactome)
PPARGR-HSA-4717461 (Reactome)
R-HSA-4090390 (Reactome) PIAS1,2-1 SUMOylate AR at lysine-386 and lysine-520 with SUMO1 (Poukka et al. 2000, Kotaja et al. 2002, Nishida and Yasuda 2002). SUMOylation reduces transcription activation by AR.
R-HSA-4090408 (Reactome) PIAS1,3 SUMOylate ESR1 (Estrogen Receptor alpha, ER-alpha, ER, NR3A1) at lysines-266,268,299,302,303 with SUMO1 (Sentis et al. 2005). SUMOylation reduces transcription activation by ESR1.
R-HSA-4341016 (Reactome) PIAS1 SUMOylates NR3C2 (Mineralcorticoid receptor, MR) at lysine-89, lysine-399, lysine-428, and lysine 494 with SUMO1 (Tallec et al. 2003, Tirard et al. 2007, Yokota et al. 2007). SUMOylation represses the transcription activation activity of NR3C2.
R-HSA-4341025 (Reactome) NR3C1 (Glucocorticoid receptor, GR) is SUMOylated at lysine-277 and lysine-293 with SUMO1 (Tian et al. 2002, Impens et al. 2014). SUMOylation is enhanced when NR3C1 binds ligand (dexamethasone). SUMOylation reduces transcription activation by NR3C1.
R-HSA-4341048 (Reactome) RXRA (Retinoid X receptor alpha) is SUMOylated at lysine-108 with SUMO1 (Choi et al. 2006). SUMOylation represses transcription activation by RXRA.
R-HSA-4341070 (Reactome) PIAS4 SUMOylates PPARA at lysine-185 with SUMO1 (Pourcet et al. 2010). SUMOylation decreases the transactivation activity of PPARA. SUMOylation is decreased in the presence of ligand of PPARA.
R-HSA-4341072 (Reactome) RARA (Retinoic acid receptor alpha) is SUMOylated at lysine-166, lysine-171, and lysine-399 with SUMO2 (Zhu et al. 2009). SUMOylation at lysine-166 and lysine-171 is induced by all-trans retinoic acid and inhibits nuclear localization of RARA. SUMOylation at lysine-399 is observed in the absence of all-trans retinoic acid and enhances nuclear localization of RARA. SUMOylation of all 3 sites inhibits transcriptional activation by RARA.
R-HSA-4341073 (Reactome) PIAS3 SUMOylates PGR (Progesterone receptor, PR) at lysine-7, lysine-388, and lysine-531 with SUMO1 (Man et al. 2006, Daniel et al. 2007, Abdel-Hafiz et al. 2009). SUMOylation inhibits hormone-dependent transcription activation by PGR.
R-HSA-4546385 (Reactome) PIAS1,3 SUMOylate NR5A1 (Steroidogenic factor 1, SF1, SF-1) at lysine-119 and lysine-194 with SUMO2 (Chen et al. 2004, Komatsu et al. 2004, Suda et al. 2011). SUMOylation reduces synergistic activation of SOX9 by NR5A1.
R-HSA-4546386 (Reactome) PIAS1,3 SUMOylate NR5A1 (Steroidogenic factor 1, SF1, SF-1) at lysine-119 and lysine-194 with SUMO1 (Chen et al. 2004, Komatsu et al. 2004, Suda et al. 2011). SUMOylation reduces the synergistic activation of SOX9 by NR5A1.
R-HSA-4546387 (Reactome) E3 SUMO-protein ligase (PIAS4) SUMOylates Vitamin D3 receptor (VDR) with SUMO2 (Jena et al. 2012). SUMOylation inhibits transcriptional activation by VDR in response to vitamin D.
R-HSA-4717461 (Reactome) As inferred from mouse homologs, PIAS1,2-2 SUMOylate PPARG with SUMO1 at lysine-107 and lysine-395 (lysine-77 and lysine-365 of the shorter variant 1). SUMOylation decreases the transcriptional activation activity of PPARG. SUMOylation at lysine-395 is ligand-dependent and causes PPARG to recruit corepressors such as NCOR and HDAC3.
R-HSA-4717521 (Reactome) As inferred from mouse homologs, PIAS1 SUMOylates NR2C1 (TR2) with SUMO1 at lysine-250. UnSUMOylated NR2C1 is localized to PML bodies and activates expression of OCT4. SUMOylated NR2C1 delocalizes from PML bodies and acts as a repressor of transcription.
R-HSA-4719413 (Reactome) PIAS2-2 (PIASx-alpha, PIAS3, and PIAS4 SUMOylate RORA with SUMO2 at lysine-240 (Hwang et al. 2009). SUMOylation increases the transcriptional activity of RORA.
R-HSA-4719423 (Reactome) PIAS2-2 (PIasx-alpha) SUMOylates THRA (isoform alpha-1) with SUMO3 at lysine-283 and lysine-389 (Liu et al. 2012). (A lysine residue corresponding to lysine-389 does not exist in the alpha-2 isoform of THRA.) SUMOylation by SUMO3 enhances transcription in response to ligand binding.
R-HSA-4719424 (Reactome) PIAS1 SUMOylates THRB with SUMO1 at lysine-50, lysine-146, and lysine-443 (Liu et al. 2012). SUMOylation is required for induction of gene expression in response to ligand (triiodothyroxine). In the absence of SUMOylation the repressor NCOR is not dismissed in response to ligand binding.
R-HSA-4719436 (Reactome) PIAS2-2 (PIASx-alpha), PIAS3, and PIAS4 SUMOylate RORA with SUMO1 at lysine-240 (Hwang et al. 2009). SUMOylation increases transcriptional activation by RORA.
R-HSA-4719447 (Reactome) PIAS2-2 (PIASx-alpha) SUMOylates THRA (alpha-1 isoform) with SUMO1 at lysine-283 and lysine-389 (Liu et al. 2012). (A lysine residue corresponding to lysine-389 does not exist in the alpha-2 isoform.) SUMOylation by SUMO3 but not SUMO1 enhances induction of gene expression in response to the ligand triiodothyroxine.
R-HSA-4719448 (Reactome) PIAS1 SUMOylates THRB with SUMO3 at lysine-50, lysine-146, and lysine-443 (Liu et al. 2012). SUMOylation is required for induction of transcription in response to ligand binding.
R-HSA-4720432 (Reactome) HDAC4 SUMOylates NR1H2 (LXR-beta) with SUMO2,3 at lysine-409 and lysine-447 (lysine-410 and lysine-448 of the isoform used by Ghisletti et al. 2007) (Venteclef et al. 2010). SUMOylation is enhanced when NR1H2 binds specific oxysterols and causes NR1H2 to recruit the NCOR repressor and transrepress promoters such as iNOS.
R-HSA-4720446 (Reactome) HDAC4 SUMOylates NR1H3 with SUMO2,3 (Ghisletti et al. 2007). SUMOylation is enhanced when NR1H3 binds specific oxysterols. SUMOylation causes NR1H3 to recruit the NCOR repressor and act as a transrepressor at promoters such as iNOS.
R-HSA-4755419 (Reactome) NR1H4 (FXR, Bile Acid Receptor) is SUMOylated with SUMO1 at lysine-132 and lysine-289 (lysine-122 and lysine-275 of isoform 4, UniProt Q96RI1-2) (Vavassori et al. 2009, Balasubramaniyan et al. 2013). SUMOylation appears to be enhanced when NR1H4 binds ligands (Vavassori et al. 2009). SUMOylated NR1H4 transrepresses genes involved in inflammation (Vavassori et al. 2009) and inhibits ligand-induced activation of FXR targets: bile salt export pump (BSEP) and small heterodimer partner (SHP) (Balasubramaniya et al. 2013).
R-HSA-4755494 (Reactome) PIAS1,2-1 SUMOylate NR5A2 (LRH-1) with SUMO1 at lysine-270 (lysine-224 in the shorter isoform) (Chalkiadaki and Talianidis 2005, Ogawa et al. 2009, Venteclef et al. 2010). SUMOylation is enhanced when NR5A2 is bound to ligand. SUMOylated NR5A2 acts as a transrepressor of genes involved in inflammation such as haptoglobin, SAA, and CRP.
R-HSA-4755524 (Reactome) NR1I2 (Pregnane X Receptor, PXR) is SUMOylated with SUMO3 (Hu et al. 2010). SUMOylation is stimulated when NR1I2 binds ligand (rifampicin) and causes NR1I2 to transrepress genes encoding inflammatory cytokines.
R-HSA-4755526 (Reactome) As inferred from mouse homologs, PIAS4 SUMOylates NR4A2 (NUR1) with SUMO2,3 at lysine-558 and lysine-577. SUMOylation causes NR4A2 to interact as a monomer with the Co-REST complex and transrepress promoters of genes involved in inflammation.
RARAR-HSA-4341072 (Reactome)
RORAR-HSA-4719413 (Reactome)
RORAR-HSA-4719436 (Reactome)
RXRAR-HSA-4341048 (Reactome)
SUMO1:C93-UBE2IR-HSA-4090390 (Reactome)
SUMO1:C93-UBE2IR-HSA-4090408 (Reactome)
SUMO1:C93-UBE2IR-HSA-4341016 (Reactome)
SUMO1:C93-UBE2IR-HSA-4341025 (Reactome)
SUMO1:C93-UBE2IR-HSA-4341048 (Reactome)
SUMO1:C93-UBE2IR-HSA-4341070 (Reactome)
SUMO1:C93-UBE2IR-HSA-4341073 (Reactome)
SUMO1:C93-UBE2IR-HSA-4546386 (Reactome)
SUMO1:C93-UBE2IR-HSA-4717461 (Reactome)
SUMO1:C93-UBE2IR-HSA-4717521 (Reactome)
SUMO1:C93-UBE2IR-HSA-4719424 (Reactome)
SUMO1:C93-UBE2IR-HSA-4719436 (Reactome)
SUMO1:C93-UBE2IR-HSA-4719447 (Reactome)
SUMO1:C93-UBE2IR-HSA-4755419 (Reactome)
SUMO1:C93-UBE2IR-HSA-4755494 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4341025 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4341048 (Reactome)
SUMO1:NR2C1ArrowR-HSA-4717521 (Reactome)
SUMO1:NR5A2:cis-bicyclo(3.3.0)oct-2-eneArrowR-HSA-4755494 (Reactome)
SUMO1:PPARAArrowR-HSA-4341070 (Reactome)
SUMO1:RORAArrowR-HSA-4719436 (Reactome)
SUMO1:RXRAArrowR-HSA-4341048 (Reactome)
SUMO2,3-K558,K577-NR4A2ArrowR-HSA-4755526 (Reactome)
SUMO2,3-NR1H2:hydroxycholesterolArrowR-HSA-4720432 (Reactome)
SUMO2,3-NR1H3:hydroxysterolArrowR-HSA-4720446 (Reactome)
SUMO2-K119,K194-NR5A1ArrowR-HSA-4546385 (Reactome)
SUMO2-K166,K171,K399-RARAArrowR-HSA-4341072 (Reactome)
SUMO2-K240-RORAArrowR-HSA-4719413 (Reactome)
SUMO2-VDRArrowR-HSA-4546387 (Reactome)
SUMO2:UBE2IR-HSA-4341072 (Reactome)
SUMO2:UBE2IR-HSA-4546385 (Reactome)
SUMO2:UBE2IR-HSA-4546387 (Reactome)
SUMO2:UBE2IR-HSA-4719413 (Reactome)
SUMO2:UBE2Imim-catalysisR-HSA-4341072 (Reactome)
SUMO3-K283,K389-THRA-2ArrowR-HSA-4719423 (Reactome)
SUMO3-K50,K146,K443-THRBArrowR-HSA-4719448 (Reactome)
SUMO3-NR1I2:rifampicinArrowR-HSA-4755524 (Reactome)
SUMO3:UBE2IR-HSA-4719423 (Reactome)
SUMO3:UBE2IR-HSA-4719448 (Reactome)
SUMO3:UBE2IR-HSA-4755524 (Reactome)
THRA-2R-HSA-4719423 (Reactome)
THRA-2R-HSA-4719447 (Reactome)
THRBR-HSA-4719424 (Reactome)
THRBR-HSA-4719448 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4720432 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4720446 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4755526 (Reactome)
UBE2IArrowR-HSA-4090390 (Reactome)
UBE2IArrowR-HSA-4090408 (Reactome)
UBE2IArrowR-HSA-4341016 (Reactome)
UBE2IArrowR-HSA-4341025 (Reactome)
UBE2IArrowR-HSA-4341048 (Reactome)
UBE2IArrowR-HSA-4341070 (Reactome)
UBE2IArrowR-HSA-4341072 (Reactome)
UBE2IArrowR-HSA-4341073 (Reactome)
UBE2IArrowR-HSA-4546385 (Reactome)
UBE2IArrowR-HSA-4546386 (Reactome)
UBE2IArrowR-HSA-4546387 (Reactome)
UBE2IArrowR-HSA-4717461 (Reactome)
UBE2IArrowR-HSA-4717521 (Reactome)
UBE2IArrowR-HSA-4719413 (Reactome)
UBE2IArrowR-HSA-4719423 (Reactome)
UBE2IArrowR-HSA-4719424 (Reactome)
UBE2IArrowR-HSA-4719436 (Reactome)
UBE2IArrowR-HSA-4719447 (Reactome)
UBE2IArrowR-HSA-4719448 (Reactome)
UBE2IArrowR-HSA-4720432 (Reactome)
UBE2IArrowR-HSA-4720446 (Reactome)
UBE2IArrowR-HSA-4755419 (Reactome)
UBE2IArrowR-HSA-4755494 (Reactome)
UBE2IArrowR-HSA-4755524 (Reactome)
UBE2IArrowR-HSA-4755526 (Reactome)
VDRR-HSA-4546387 (Reactome)
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