SUMOylation of DNA methylation proteins (Homo sapiens)

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4, 52, 31nucleoplasmPRC1 complexBMI1 UBE2I-G97-SUMO1 DNMT3BSUMO1-K-DNMT3B SUMO1:C93-UBE2IUBE2ICBX8 SUMO1:C93-UBE2IRNF2 DNMT1SCMH1-2 SUMO1:DNMT3BPHC1 UBE2I-G97-SUMO1 CBX2 SUMO1-K-DNMT3A SUMO1-C93-UBE2I DNMT1-G97-SUMO1 SUMO1:C93-UBE2ISUMO1-C93-UBE2I PHC3 SUMO1:DNMT1DNMT3B-G97-SUMO1 DNMT3ARING1 UBE2ICBX4 SUMO1-K-DNMT1 UBE2I-G97-SUMO1 PCGF2 SUMO1:DNMT3ASUMO1-C93-UBE2I PHC2 UBE2IDNMT3A-G97-SUMO1 13


Description

The known DNA methyltransferases (DNMT1, DNMT3A, and DNMT3B) can be SUMOylated (reviewed in Xu et al. 2010, Denis et al. 2011). SUMOylation affects the catalytic activity of DNMT1 and the protein interactions of DNMT3A. View original pathway at Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 4655427
Reactome-version 
Reactome version: 73
Reactome Author 
Reactome Author: May, Bruce

Quality Tags

Ontology Terms

 

Bibliography

  1. Park J, Kim TY, Jung Y, Song SH, Kim SH, Oh DY, Im SA, Bang YJ.; ''DNA methyltransferase 3B mutant in ICF syndrome interacts non-covalently with SUMO-1.''; PubMed Europe PMC Scholia
  2. Xu F, Mao C, Ding Y, Rui C, Wu L, Shi A, Zhang H, Zhang L, Xu Z.; ''Molecular and enzymatic profiles of mammalian DNA methyltransferases: structures and targets for drugs.''; PubMed Europe PMC Scholia
  3. Denis H, Ndlovu MN, Fuks F.; ''Regulation of mammalian DNA methyltransferases: a route to new mechanisms.''; PubMed Europe PMC Scholia
  4. Lee B, Muller MT.; ''SUMOylation enhances DNA methyltransferase 1 activity.''; PubMed Europe PMC Scholia
  5. Kang ES, Park CW, Chung JH.; ''Dnmt3b, de novo DNA methyltransferase, interacts with SUMO-1 and Ubc9 through its N-terminal region and is subject to modification by SUMO-1.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
113121view11:18, 2 November 2020ReactomeTeamReactome version 74
112355view15:28, 9 October 2020ReactomeTeamReactome version 73
101682view13:58, 1 November 2018DeSlOntology Term : 'pathway pertinent to DNA replication and repair, cell cycle, maintenance of genomic integrity, RNA and protein biosynthesis' added !
101681view13:56, 1 November 2018DeSlOntology Term : 'sumoylation pathway' added !
101256view11:14, 1 November 2018ReactomeTeamreactome version 66
101190view21:39, 31 October 2018ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
BMI1 ProteinP35226 (Uniprot-TrEMBL)
CBX2 ProteinQ14781 (Uniprot-TrEMBL)
CBX4 ProteinO00257 (Uniprot-TrEMBL)
CBX8 ProteinQ9HC52 (Uniprot-TrEMBL)
DNMT1-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
DNMT1ProteinP26358 (Uniprot-TrEMBL)
DNMT3A-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
DNMT3AProteinQ9Y6K1 (Uniprot-TrEMBL)
DNMT3B-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
DNMT3BProteinQ9UBC3 (Uniprot-TrEMBL)
PCGF2 ProteinP35227 (Uniprot-TrEMBL)
PHC1 ProteinP78364 (Uniprot-TrEMBL)
PHC2 ProteinQ8IXK0 (Uniprot-TrEMBL)
PHC3 ProteinQ8NDX5 (Uniprot-TrEMBL)
PRC1 complexComplexR-HSA-389114 (Reactome)
RING1 ProteinQ06587 (Uniprot-TrEMBL)
RNF2 ProteinQ99496 (Uniprot-TrEMBL)
SCMH1-2 ProteinQ96GD3-2 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-K-DNMT1 ProteinP26358 (Uniprot-TrEMBL)
SUMO1-K-DNMT3A ProteinQ9Y6K1 (Uniprot-TrEMBL)
SUMO1-K-DNMT3B ProteinQ9UBC3 (Uniprot-TrEMBL)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:DNMT1ComplexR-HSA-4655323 (Reactome)
SUMO1:DNMT3AComplexR-HSA-4655422 (Reactome)
SUMO1:DNMT3BComplexR-HSA-4655400 (Reactome)
UBE2I-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
UBE2IProteinP63279 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
DNMT1R-HSA-4655431 (Reactome)
DNMT3AR-HSA-4655440 (Reactome)
DNMT3BR-HSA-4655374 (Reactome)
PRC1 complexmim-catalysisR-HSA-4655440 (Reactome)
R-HSA-4655374 (Reactome) DNMT3B is SUMOylated with SUMO1 at unknown lysine residues (Kang et al. 2001, Park et al. 2008). SUMOylation relieves transcriptional repression by DNMT3B.
R-HSA-4655431 (Reactome) DNMT1 is SUMOyated at several unknown lysine residues with SUMO1 (Lee et al. 2009). SUMOylation increases the DNA methyltransferase activity of DNMT1.
R-HSA-4655440 (Reactome) As inferred from mouse homologs, CBX4 (Pc2) SUMOylates DNMT3A with SUMO1 at more than one lysine residue in the N-terminal (regulatory) domain. SUMOylation reduces the interaction of DNMT3A with HDAC1 and HDAC2.
SUMO1:C93-UBE2IR-HSA-4655374 (Reactome)
SUMO1:C93-UBE2IR-HSA-4655431 (Reactome)
SUMO1:C93-UBE2IR-HSA-4655440 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4655374 (Reactome)
SUMO1:C93-UBE2Imim-catalysisR-HSA-4655431 (Reactome)
SUMO1:DNMT1ArrowR-HSA-4655431 (Reactome)
SUMO1:DNMT3AArrowR-HSA-4655440 (Reactome)
SUMO1:DNMT3BArrowR-HSA-4655374 (Reactome)
UBE2IArrowR-HSA-4655374 (Reactome)
UBE2IArrowR-HSA-4655431 (Reactome)
UBE2IArrowR-HSA-4655440 (Reactome)
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