SUMOylation of ubiquitinylation proteins (Homo sapiens)

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364, 5, 101, 6nucleoplasmNUP62 NUP205 NUP50 SUMO1-C93-UBE2I RAE1 NUP98-3 POM121C NUP107 TRIM27 UBE2IPML,TRIM27,PIAS1,2-1MDM-G97-SUMO1 NUP88 SUMO1-C93-UBE2I NDC1 SUMO1-K159,171,196-VHL K196-VHL-G97-SUMO1 UBE2IUBE2I-G97-SUMO1 SUMO1-K182-MDM2 NUP37 RANBP2 PML POM121 NUP43 PIAS1 SUMO1:C93-UBE2INup45 K159-VHL-G97-SUMO1 NUP98-5 NUP210 MDM2UBE2I-G97-SUMO1 3SUMO1:VHLNUPL2 VHLNuclear Pore Complex(NPC)PIAS4NUP35 SUMO1:MDM2SUMO1:C93-UBE2INUP188 NUP155 NUP93 PIAS2-1 NUP160 NUP98-4 NUP54 NUP153 NUP133 NUPL1-2 AAAS K171-VHL-G97-SUMO1 TPR NUP85 NUP214 SEH1L-2 2, 7-91, 64, 5, 1011


Description

Several ubiquitin E3 ligases are regulated by SUMOylation (reviewed in Wilson and Heaton 2008). SUMOylation appears to be necessary for nuclear import of MDM2, the E3 ligase that ubiquitinylates TP53 (p53). SUMOylation of VHL abolishes its ubiquitin ligase activity. HERC2, RNF168, and BRCA1 are ubiquitin ligases that are SUMOylated during DNA damage response and repair. View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 3232142
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

Quality Tags

Ontology Terms

 

Bibliography

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  1. Chu Y, Yang X.; ''SUMO E3 ligase activity of TRIM proteins.''; PubMed Europe PMC
  2. 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 Europe PMC
  3. Wilson VG, Heaton PR.; ''Ubiquitin proteolytic system: focus on SUMO.''; PubMed Europe PMC
  4. Cai Q, Verma SC, Kumar P, Ma M, Robertson ES.; ''Hypoxia inactivates the VHL tumor suppressor through PIASy-mediated SUMO modification.''; PubMed Europe PMC
  5. Chien W, Lee KL, Ding LW, Wuensche P, Kato H, Doan NB, Poellinger L, Said JW, Koeffler HP.; ''PIAS4 is an activator of hypoxia signalling via VHL suppression during growth of pancreatic cancer cells.''; PubMed Europe PMC
  6. Miyauchi Y, Yogosawa S, Honda R, Nishida T, Yasuda H.; ''Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes.''; PubMed Europe PMC
  7. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed Europe PMC
  8. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed Europe PMC
  9. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed Europe PMC
  10. Cai Q, Robertson ES.; ''Ubiquitin/SUMO modification regulates VHL protein stability and nucleocytoplasmic localization.''; PubMed Europe PMC
  11. 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 Europe PMC

History

CompareRevisionActionTimeUserComment
101677view13:55, 1 November 2018DeSlOntology Term : 'sumoylation pathway' added !
101502view11:37, 1 November 2018ReactomeTeamreactome version 66
101194view21:39, 31 October 2018ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
3SUMO1:VHLComplexR-HSA-4551704 (Reactome)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
K159-VHL-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K171-VHL-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
K196-VHL-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
MDM-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
MDM2ProteinQ00987 (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)
PIAS1 ProteinO75925 (Uniprot-TrEMBL)
PIAS2-1 ProteinO75928-1 (Uniprot-TrEMBL)
PIAS4ProteinQ8N2W9 (Uniprot-TrEMBL)
PML ProteinP29590 (Uniprot-TrEMBL)
PML,TRIM27,PIAS1,2-1ComplexR-HSA-3000441 (Reactome)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SUMO1-C93-UBE2I ProteinP63279 (Uniprot-TrEMBL)
SUMO1-K159,171,196-VHL ProteinP40337 (Uniprot-TrEMBL)
SUMO1-K182-MDM2 ProteinQ00987 (Uniprot-TrEMBL)
SUMO1:C93-UBE2IComplexR-HSA-2993783 (Reactome)
SUMO1:MDM2ComplexR-HSA-3730855 (Reactome)
TPR ProteinP12270 (Uniprot-TrEMBL)
TRIM27 ProteinP14373 (Uniprot-TrEMBL)
UBE2I-G97-SUMO1 ProteinP63165 (Uniprot-TrEMBL)
UBE2IProteinP63279 (Uniprot-TrEMBL)
VHLProteinP40337 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
3SUMO1:VHLArrowR-HSA-4551721 (Reactome)
MDM2R-HSA-3000434 (Reactome)
MDM2R-HSA-5228523 (Reactome)
Nuclear Pore Complex (NPC)mim-catalysisR-HSA-5228523 (Reactome)
PIAS4mim-catalysisR-HSA-4551721 (Reactome)
PML,TRIM27,PIAS1,2-1mim-catalysisR-HSA-3000434 (Reactome)
R-HSA-3000434 (Reactome) PML TRIM27, PIAS1, and PIAS2-1 can each SUMOylate MDM2 with SUMO1 at lysine-182 (Miyauchi et al. 2002, Chu and Yang 2011). An unSUMOylatable mutant of MDM2 accumulates in the cytosol so SUMOylation may be part of the process of nuclear import of MDM2 (Miyauchi et al. 2002).
R-HSA-4551721 (Reactome) PIAS4 SUMOylates VHL at lysine-159, lysine-171, and lysine-196 with SUMO1 (Cai et al. 2010, Cai and Robertson 2010, Chien et al. 2013). SUMOylation facilitates the oligomerization of VHL, abolishes the inhibitory function of VHL on HIF1A, and abolishes the tumor suppressor function of VHL by inactivating the ubiquitinylation activity of VHL.
R-HSA-5228523 (Reactome) RANBP2 of the nuclear pore complex SUMOylates MDM2 with SUMO1 at lysine-182 (Mayauchi et al. 2002). An unSUMOylatable mutant of MDM2 accumulates in the cytosol so SUMOylation may be part of the process of nuclear import of MDM2 (Miyauchi et al. 2002).
SUMO1:C93-UBE2IR-HSA-3000434 (Reactome)
SUMO1:C93-UBE2IR-HSA-4551721 (Reactome)
SUMO1:C93-UBE2IR-HSA-5228523 (Reactome)
SUMO1:MDM2ArrowR-HSA-3000434 (Reactome)
SUMO1:MDM2ArrowR-HSA-5228523 (Reactome)
UBE2IArrowR-HSA-3000434 (Reactome)
UBE2IArrowR-HSA-4551721 (Reactome)
UBE2IArrowR-HSA-5228523 (Reactome)
VHLR-HSA-4551721 (Reactome)
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