SUMOylation of chromatin organization proteins (Homo sapiens)

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1713, 152223152611, 14, 18242220, 292, 5, 10, 1512, 16, 283, 6, 8, 191, 1612, 28nucleoplasmK-CBX5-G97-SUMO1 SUMO2,3-K559-HDAC4NDC1 NUPL2 AAAS SUMO1:C93-UBE2ICBX8 BMI1-G97-SUMO1 PHC1 BMI1 SUMO1-K84,K-CBX5 HDAC2-G97-SUMO1 CBX4 NUP107 NUP155 NUP93 SEH1L-2 SUMO1-K75-SUZ12 HDAC2UBE2I-G97-SUMO1 PCGF2 SUMO1-C93-UBE2I SUMO3-C93-UBE2I POM121C SUZ12PHC2 SUMO1-C93-UBE2I UBE2IUBE2I-G93-SUMO2 NUP214 SCMH1-2 UBE2I-G93-SUMO2 SUMO1:C93-UBE2ISUMO2-C93-UBE2I HDAC4-G97-SUMO1 NUP205 SUMO3:UBE2IUBE2I-G92-SUMO3 CBX5UBE2IPHC3 HDAC4UBE2I-G97-SUMO1 NUP133 Nuclear Pore Complex(NPC)CBX4-G97-SUMO1 SUMO3-HIST1H4SUMO2:UBE2IUBE2I-G93-SUMO2 SUMO1:CBX5UBE2I-G92-SUMO3 NUP188 SUMO1:HDAC4UBE2I-G97-SUMO1 BMI1 SATB1-G97-SUMO1 PCGF2 NUP98-4 UBE2IUBE2ISUMO1:C93-UBE2INUP50 UBE2I-G97-SUMO1 UBE2ISUMO1:CBX4:PRC1UBE2I-G97-SUMO1 SUMO3:UBE2INUP43 UBE2ICBX4 PHC3 HDAC1UBE2I:SUMO2,UBE2I:SUMO3SUMO3-C93-UBE2I NUP160 NUP85 SUMO1-C93-UBE2I SUMO1:BMI1:PRC1RING1 SUMO1:HDAC2UBE2IK444-HDAC1-G97-SUMO1 CBX2 UBE2ITPR SUMO3-C93-UBE2I SUMO3-K233,K350-SATB2HIST1H4-G97-SUMO1 UBE2I-G97-SUMO1 NUP54 NUP153 SUMO3-C93-UBE2I SUMO1:SUZ12SUMO1:C93-UBE2ISUMO1-K1971-CHD3 PHC3 L3MBTL2SUMO1-K744-SATB1 PCGF2 RNF2 SUMO1-K462-HDAC2 SUMO1:CHD3CBX8 SUMO2,3-K744-SATB1NUP35 SUMO1:C93-UBE2I2SUMO1:HDAC1CHD3PHC2 RANBP2 CBX2 SUMO1-K559-HDAC4 SUMO1-C93-UBE2I SUMO1:HIST1H4SUMO1-K88-BMI1 NUP98-3 SATB2K84-CBX5-G97-SUMO1 RNF2 PIAS1SUMO1:C93-UBE2IUBE2I-G92-SUMO3 Nup45 CBX2 K1971-CHD3-G97-SUMO1 SUMO1-C93-UBE2I NUPL1-2 SUMO2-C93-UBE2I NUP37 RAE1 NUP88 UBE2I-G97-SUMO1 NUP210 SCMH1-2 PHC2 NUP98-5 SUMO1-C93-UBE2I PRC1 complexPHC1 UBE2I:SUMO2,UBE2I:SUMO3SUMO1:SATB1POM121 SUZ12-G97-SUMO1 SATB1CBX8 RING1 PHC1 UBE2I-G92-SUMO3 RNF2 UBE2ISUMO2-K675,K700-L3MBTL2SUMO1-C93-UBE2I SUMO1-K494-CBX4 RING1 SUMO1:C93-UBE2ISUMO2-C93-UBE2I K476-HDAC1-G97-SUMO1 HIST1H4UBE2I-G97-SUMO1 PIAS2-2SCMH1-2 SUMO1-HIST1H4 SUMO1-K444,K476-HDAC1 SUMO1-C93-UBE2I ZBED1SUMO1:C93-UBE2INUP62 2412, 16, 289, 272227233, 6, 81512, 2830279, 2711, 18201527274, 7, 21, 255, 10, 159, 27


Description

SUMOylation of proteins involved in chromatin organization regulates gene expression in several ways: direct influence on catalytic activity of enzymes that modify chromatin, recruitment of proteins that form repressive (e.g. PRC1) or activating complexes on chromatin, recruitment of proteins to larger bodies (e.g PML bodies) in the nucleus (reviewed in Cubenas-Potts and Matunis 2013). View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 4551638
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Stielow C, Stielow B, Finkernagel F, Scharfe M, Jarek M, Suske G.; ''SUMOylation of the polycomb group protein L3MBTL2 facilitates repression of its target genes.''; PubMed
  2. Citro S, Jaffray E, Hay RT, Seiser C, Chiocca S.; ''A role for paralog-specific sumoylation in histone deacetylase 1 stability.''; PubMed
  3. Kagey MH, Melhuish TA, Powers SE, Wotton D.; ''Multiple activities contribute to Pc2 E3 function.''; PubMed
  4. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed
  5. David G, Neptune MA, DePinho RA.; ''SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities.''; PubMed
  6. Roscic A, Möller A, Calzado MA, Renner F, Wimmer VC, Gresko E, Lüdi KS, Schmitz ML.; ''Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2.''; PubMed
  7. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed
  8. Merrill JC, Melhuish TA, Kagey MH, Yang SH, Sharrocks AD, Wotton D.; ''A role for non-covalent SUMO interaction motifs in Pc2/CBX4 E3 activity.''; PubMed
  9. 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
  10. Cheng J, Wang D, Wang Z, Yeh ET.; ''SENP1 enhances androgen receptor-dependent transcription through desumoylation of histone deacetylase 1.''; PubMed
  11. Lamoliatte F, Bonneil E, Durette C, Caron-Lizotte O, Wildemann D, Zerweck J, Wenshuk H, Thibault P.; ''Targeted identification of SUMOylation sites in human proteins using affinity enrichment and paralog-specific reporter ions.''; PubMed
  12. Tan JA, Sun Y, Song J, Chen Y, Krontiris TG, Durrin LK.; ''SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage.''; PubMed
  13. Knipscheer P, Flotho A, Klug H, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK, Pichler A.; ''Ubc9 sumoylation regulates SUMO target discrimination.''; PubMed
  14. Lamoliatte F, Caron D, Durette C, Mahrouche L, Maroui MA, Caron-Lizotte O, Bonneil E, Chelbi-Alix MK, Thibault P.; ''Large-scale analysis of lysine SUMOylation by SUMO remnant immunoaffinity profiling.''; PubMed
  15. Kirsh O, Seeler JS, Pichler A, Gast A, Müller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T, Melchior F, Dejean A.; ''The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.''; PubMed
  16. Tammsalu T, Matic I, Jaffray EG, Ibrahim AFM, Tatham MH, Hay RT.; ''Proteome-wide identification of SUMO2 modification sites.''; PubMed
  17. Cubeñas-Potts C, Matunis MJ.; ''SUMO: a multifaceted modifier of chromatin structure and function.''; PubMed
  18. Dobreva G, Dambacher J, Grosschedl R.; ''SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression.''; PubMed
  19. Kang X, Qi Y, Zuo Y, Wang Q, Zou Y, Schwartz RJ, Cheng J, Yeh ET.; ''SUMO-specific protease 2 is essential for suppression of polycomb group protein-mediated gene silencing during embryonic development.''; PubMed
  20. Brandl A, Wagner T, Uhlig KM, Knauer SK, Stauber RH, Melchior F, Schneider G, Heinzel T, Krämer OH.; ''Dynamically regulated sumoylation of HDAC2 controls p53 deacetylation and restricts apoptosis following genotoxic stress.''; PubMed
  21. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed
  22. Shiio Y, Eisenman RN.; ''Histone sumoylation is associated with transcriptional repression.''; PubMed
  23. Ismail IH, Gagné JP, Caron MC, McDonald D, Xu Z, Masson JY, Poirier GG, Hendzel MJ.; ''CBX4-mediated SUMO modification regulates BMI1 recruitment at sites of DNA damage.''; PubMed
  24. Riising EM, Boggio R, Chiocca S, Helin K, Pasini D.; ''The polycomb repressive complex 2 is a potential target of SUMO modifications.''; PubMed
  25. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed
  26. Yamashita D, Moriuchi T, Osumi T, Hirose F.; ''Transcription Factor hDREF Is a Novel SUMO E3 Ligase of Mi2α.''; PubMed
  27. Su HL, Li SS.; ''Molecular features of human ubiquitin-like SUMO genes and their encoded proteins.''; PubMed
  28. Tan JA, Song J, Chen Y, Durrin LK.; ''Phosphorylation-dependent interaction of SATB1 and PIAS1 directs SUMO-regulated caspase cleavage of SATB1.''; PubMed
  29. Wagner T, Kiweler N, Wolff K, Knauer SK, Brandl A, Hemmerich P, Dannenberg JH, Heinzel T, Schneider G, Krämer OH.; ''Sumoylation of HDAC2 promotes NF-κB-dependent gene expression.''; PubMed
  30. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed

History

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CompareRevisionActionTimeUserComment
101563view11:43, 1 November 2018ReactomeTeamreactome version 66
101099view21:26, 31 October 2018ReactomeTeamreactome version 65
100628view20:00, 31 October 2018ReactomeTeamreactome version 64
100178view16:45, 31 October 2018ReactomeTeamreactome version 63
99728view15:12, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93785view13:36, 16 August 2017ReactomeTeamreactome version 61
93318view11:20, 9 August 2017ReactomeTeamreactome version 61
88417view11:53, 5 August 2016FehrhartOntology Term : 'sumoylation pathway' added !
86403view09:17, 11 July 2016ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2SUMO1:HDAC1ComplexR-HSA-4615845 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
BMI1 ProteinP35226 (Uniprot-TrEMBL)
BMI1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
CBX2 ProteinQ14781 (Uniprot-TrEMBL)
CBX4 ProteinO00257 (Uniprot-TrEMBL)
CBX4-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
CBX5ProteinP45973 (Uniprot-TrEMBL)
CBX8 ProteinQ9HC52 (Uniprot-TrEMBL)
CHD3ProteinQ12873 (Uniprot-TrEMBL)
HDAC1ProteinQ13547 (Uniprot-TrEMBL)
HDAC2-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
HDAC2ProteinQ92769 (Uniprot-TrEMBL)
HDAC4-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
HDAC4ProteinP56524 (Uniprot-TrEMBL)
HIST1H4-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
HIST1H4ProteinP62805 (Uniprot-TrEMBL)
K-CBX5-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K1971-CHD3-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K444-HDAC1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K476-HDAC1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K84-CBX5-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
L3MBTL2ProteinQ969R5 (Uniprot-TrEMBL)
NDC1 ProteinQ9BTX1 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
PCGF2 ProteinP35227 (Uniprot-TrEMBL)
PHC1 ProteinP78364 (Uniprot-TrEMBL)
PHC2 ProteinQ8IXK0 (Uniprot-TrEMBL)
PHC3 ProteinQ8NDX5 (Uniprot-TrEMBL)
PIAS1ProteinO75925 (Uniprot-TrEMBL)
PIAS2-2ProteinO75928-2 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
PRC1 complexComplexR-HSA-389114 (Reactome)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
RING1 ProteinQ06587 (Uniprot-TrEMBL)
RNF2 ProteinQ99496 (Uniprot-TrEMBL)
SATB1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
SATB1ProteinQ01826 (Uniprot-TrEMBL)
SATB2ProteinQ9UPW6 (Uniprot-TrEMBL)
SCMH1-2 ProteinQ96GD3-2 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-HIST1H4 ProteinP62805 (Uniprot-TrEMBL)
SUMO1-K1971-CHD3 ProteinQ12873 (Uniprot-TrEMBL)
SUMO1-K444,K476-HDAC1 ProteinQ13547 (Uniprot-TrEMBL)
SUMO1-K462-HDAC2 ProteinQ92769 (Uniprot-TrEMBL)
SUMO1-K494-CBX4 ProteinO00257 (Uniprot-TrEMBL)
SUMO1-K559-HDAC4 ProteinP56524 (Uniprot-TrEMBL)
SUMO1-K744-SATB1 ProteinQ01826 (Uniprot-TrEMBL)
SUMO1-K75-SUZ12 ProteinQ15022 (Uniprot-TrEMBL)
SUMO1-K84,K-CBX5 ProteinP45973 (Uniprot-TrEMBL)
SUMO1-K88-BMI1 ProteinP35226 (Uniprot-TrEMBL)
SUMO1:BMI1:PRC1ComplexR-HSA-4551667 (Reactome)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:CBX4:PRC1ComplexR-HSA-4551608 (Reactome)
SUMO1:CBX5ComplexR-HSA-4615966 (Reactome)
SUMO1:CHD3ComplexR-HSA-8956369 (Reactome)
SUMO1:HDAC2ComplexR-HSA-4615975 (Reactome)
SUMO1:HDAC4ComplexR-HSA-4615848 (Reactome)
SUMO1:HIST1H4ComplexR-HSA-4570562 (Reactome)
SUMO1:SATB1ComplexR-HSA-4616004 (Reactome)
SUMO1:SUZ12ComplexR-HSA-4615968 (Reactome)
SUMO2,3-K559-HDAC4ProteinP56524 (Uniprot-TrEMBL)
SUMO2,3-K744-SATB1ProteinQ01826 (Uniprot-TrEMBL)
SUMO2-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO2-K675,K700-L3MBTL2ProteinQ969R5 (Uniprot-TrEMBL)
SUMO2:UBE2IComplexR-HSA-2993778 (Reactome)
SUMO3-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO3-HIST1H4ProteinP62805 (Uniprot-TrEMBL)
SUMO3-K233,K350-SATB2ProteinQ9UPW6 (Uniprot-TrEMBL)
SUMO3:UBE2IComplexR-HSA-2993782 (Reactome)
SUZ12-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
SUZ12ProteinQ15022 (Uniprot-TrEMBL)
TPR ProteinP12270 (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)
ZBED1ProteinO96006 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2SUMO1:HDAC1ArrowR-HSA-4615889 (Reactome)
CBX5R-HSA-4615933 (Reactome)
CHD3R-HSA-8956365 (Reactome)
HDAC1R-HSA-4615889 (Reactome)
HDAC2R-HSA-4616015 (Reactome)
HDAC4R-HSA-4615872 (Reactome)
HDAC4R-HSA-4615987 (Reactome)
HIST1H4R-HSA-4570485 (Reactome)
HIST1H4R-HSA-4570496 (Reactome)
L3MBTL2R-HSA-6804485 (Reactome)
Nuclear Pore Complex (NPC)mim-catalysisR-HSA-4615872 (Reactome)
Nuclear Pore Complex (NPC)mim-catalysisR-HSA-4615987 (Reactome)
PIAS1mim-catalysisR-HSA-4615839 (Reactome)
PIAS1mim-catalysisR-HSA-4615900 (Reactome)
PIAS1mim-catalysisR-HSA-4615905 (Reactome)
PIAS1mim-catalysisR-HSA-6804485 (Reactome)
PIAS2-2mim-catalysisR-HSA-4615873 (Reactome)
PRC1 complexR-HSA-4551655 (Reactome)
PRC1 complexR-HSA-4551727 (Reactome)
PRC1 complexmim-catalysisR-HSA-4551655 (Reactome)
PRC1 complexmim-catalysisR-HSA-4551727 (Reactome)
R-HSA-4551655 (Reactome) CBX4 SUMOylates BMI1 in Polycomb Repressive Complex 1 (PRC1) at lysine-88 (Ismail et al. 2012). SUMOylation of BMI1 is necessary for its accumulation at sites of DNA damage. CBX4 directly binds poly(ADP-ribose) synthesized by PARP1 at sites of damage.
R-HSA-4551727 (Reactome) CBX4 in Polycomb Repressive Complex 1 (PRC1) autoSUMOylates with SUMO1 (Kagey et al.2005, Roscic et al. 2006, Merrill et al. 2010). As inferred from mouse homologs, SUMOylation of CBX4 appears to be essential for recruitment of the PRC1 complex to histone H3 trimethylated at lysine-27 (H3K27me3) (Kang et al. 2010).
R-HSA-4570485 (Reactome) Histone H4 (HIST1H4) is SUMOylated at an unknown residue with SUMO3 (Shiio and Eisenman 2003). SUMOylation of histone H4 is associated with repression of transcription.
R-HSA-4570496 (Reactome) Histone H4 (HIST1H4) is SUMOylated at an unknown residue with SUMO1 (Shiio and Eisenman 2003). SUMOylated histone H4 is associated with repression of transcription.
R-HSA-4615839 (Reactome) PIAS1 SUMOylates SATB1 at lysine-744 with SUMO2,3 (Tan et al. 2008, Tan et al. 2010, Tammsalu et al. 2014). SUMOylation targets SATB1 to PML bodies where it is cleaved by caspase.
R-HSA-4615872 (Reactome) RANBP2 SUMOylates HDAC4 at lysine-559 with SUMO1 (Kirsh et al. 2002, Knipscheer et al. 2008). SUMOylation increases transcription repression by HDAC4.
R-HSA-4615873 (Reactome) PIAS2-2 (PIASxbeta) SUMOylates SUZ12, a subunit of the Polycomb Repressive Complex 2 (PRC2), at lysine-75 with SUMO1 (Riising et al. 2008). SUMOyation does not affect the repression of transcription by PRC2. The effect of SUMOylation on PRC2 function is unknown. The EZH2 subunit of PRC2 can also be SUMOylated at multiple positions.
R-HSA-4615889 (Reactome) HDAC1 is SUMOylated at lysine-444 and lysine-476 with SUMO1 (Kirsh et al. 2002, David et al. 2002, Cheng et al. 2004, Citro et al. 2013). SUMOylation with SUMO1 enhances transcription repression by HDAC1 and promotes degradation of HDAC1 (Citro et al. 2013). HDAC1 can also be SUMOylated with SUMO2, which enhances stability of HDAC1 (Citro et al. 2013).
R-HSA-4615900 (Reactome) PIAS1 SUMOylates SATB2 at lysine-233 and lysine-350 with SUMO3 (Dobreva et al. 2003, Lamoliatte et al. 2013, Lamoliatte et al. 2014). SUMOylation reduces binding of SATB2 to matrix attachment regions and reduces activation of transcription by SATB2. SUMOylated SATB2 is localized to the nuclear periphery.
R-HSA-4615905 (Reactome) PIAS1 SUMOylates SATB1 at lysine-744 with SUMO1 (Tan et al. 2008, Tan et al. 2010). SUMOylation targets SATB1 to PML bodies where it is cleaved by caspase.
R-HSA-4615933 (Reactome) As inferred from mouse homologs, CBX5 (HP1 alpha) is SUMOylated at lysine-84 and other lysine residues with SUMO1. SUMOylated CBX5 associates with long non-coding transcripts in pericentric heterochromatin and SUMOylation is required for initial targeting of CBX5 to pericentric domains.
R-HSA-4615987 (Reactome) RANBP2 SUMOylates HDAC4 at lysine-559 with SUMO2,3 (Kirsh et al. 2002). SUMOylation increases transcription repression by HDAC4.
R-HSA-4616015 (Reactome) HDAC2 is SUMOylated at lysine-462 with SUMO1 (Brandl et al. 2012). SUMOylation of HDAC2 blocks TP53-dependent (p53-dependent) expression of genes but is required for induction of NF-kB-dependent gene expression (Wagner et al. 2015).
R-HSA-6804485 (Reactome) PIAS1 and possibly other SUMO E3 ligases SUMOylates L3MBTL2 with SUMO2 at lysine-675 and lysine-700 near the C-terminus (Stielow et al. 2014, Tammsalu et al. 2014). SUMOylation of L3MBTL2 does not appear to affect its chromatin binding activity, however SUMOylation does enhance transcriptional repression of a subset of L3MBTL2-target genes, particularly those with low L3MBTL2 occupancy including pro-inflammatory genes (Stielow et al. 2014). SUMOylated L3MBTL2 appears to increase the level of local ubiquitinated histone H2A (Stielow et al. 2014).
R-HSA-8956365 (Reactome) ZBED1 (hDREF) SUMOylates CHD3 (Mi2alpha) at lysine-1971 with SUMO1 (Yamashita et al. 2016). SUMOylation leads to dissociation of CHD3 from chromatin and suppresses transcriptional repression by CHD3.
SATB1R-HSA-4615839 (Reactome)
SATB1R-HSA-4615905 (Reactome)
SATB2R-HSA-4615900 (Reactome)
SUMO1:BMI1:PRC1ArrowR-HSA-4551655 (Reactome)
SUMO1:C93-UBE2IR-HSA-4551655 (Reactome)
SUMO1:C93-UBE2IR-HSA-4551727 (Reactome)
SUMO1:C93-UBE2IR-HSA-4570496 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615872 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615873 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615889 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615905 (Reactome)
SUMO1:C93-UBE2IR-HSA-4615933 (Reactome)
SUMO1:C93-UBE2IR-HSA-4616015 (Reactome)
SUMO1:C93-UBE2IR-HSA-8956365 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4570496 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4615889 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4615933 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4616015 (Reactome)
SUMO1:CBX4:PRC1ArrowR-HSA-4551727 (Reactome)
SUMO1:CBX5ArrowR-HSA-4615933 (Reactome)
SUMO1:CHD3ArrowR-HSA-8956365 (Reactome)
SUMO1:HDAC2ArrowR-HSA-4616015 (Reactome)
SUMO1:HDAC4ArrowR-HSA-4615872 (Reactome)
SUMO1:HIST1H4ArrowR-HSA-4570496 (Reactome)
SUMO1:SATB1ArrowR-HSA-4615905 (Reactome)
SUMO1:SUZ12ArrowR-HSA-4615873 (Reactome)
SUMO2,3-K559-HDAC4ArrowR-HSA-4615987 (Reactome)
SUMO2,3-K744-SATB1ArrowR-HSA-4615839 (Reactome)
SUMO2-K675,K700-L3MBTL2ArrowR-HSA-6804485 (Reactome)
SUMO2:UBE2IR-HSA-6804485 (Reactome)
SUMO3-HIST1H4ArrowR-HSA-4570485 (Reactome)
SUMO3-K233,K350-SATB2ArrowR-HSA-4615900 (Reactome)
SUMO3:UBE2IR-HSA-4570485 (Reactome)
SUMO3:UBE2IR-HSA-4615900 (Reactome)
SUMO3:UBE2Imim-catalysisR-HSA-4570485 (Reactome)
SUZ12R-HSA-4615873 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4615839 (Reactome)
UBE2I:SUMO2,UBE2I:SUMO3R-HSA-4615987 (Reactome)
UBE2IArrowR-HSA-4551655 (Reactome)
UBE2IArrowR-HSA-4551727 (Reactome)
UBE2IArrowR-HSA-4570485 (Reactome)
UBE2IArrowR-HSA-4570496 (Reactome)
UBE2IArrowR-HSA-4615839 (Reactome)
UBE2IArrowR-HSA-4615872 (Reactome)
UBE2IArrowR-HSA-4615873 (Reactome)
UBE2IArrowR-HSA-4615889 (Reactome)
UBE2IArrowR-HSA-4615900 (Reactome)
UBE2IArrowR-HSA-4615905 (Reactome)
UBE2IArrowR-HSA-4615933 (Reactome)
UBE2IArrowR-HSA-4615987 (Reactome)
UBE2IArrowR-HSA-4616015 (Reactome)
UBE2IArrowR-HSA-6804485 (Reactome)
UBE2IArrowR-HSA-8956365 (Reactome)
ZBED1mim-catalysisR-HSA-8956365 (Reactome)
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