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TRIM50 TRIM50 UBE2E3 UBE2E3 FBXW4 FBXW4 RNF34 RNF34 UBE2E2 UBE2E2 RNF19A RNF19A SPSB4 SPSB4 UBE2E1 UBE2E1 CDC16 CDC16 UBE2D3 UBE2D3 RNF220 RNF220
"RNF220" - E3 ubiquitin-protein ligase RNF220 in Homo sapiens
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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RNF220E3 ubiquitin-protein ligase RNF220; E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling; Ring finger proteins (566 aa)    
Predicted Functional Partners:
UBE2E3
Ubiquitin-conjugating enzyme E2 E3; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-, as well as ’Lys-63’-linked polyubiquitination. Participates in the regulation of transepithelial sodium transport in renal cells. May be involved in cell growth arrest; Ubiquitin conjugating enzymes E2 (207 aa)
     
  0.942
UBE2D3
Ubiquitin conjugating enzyme E2 D3; Belongs to the ubiquitin-conjugating enzyme family (149 aa)
     
    0.937
FBXW4
F-box/WD repeat-containing protein 4; Probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. Likely to be involved in key signaling pathways crucial for normal limb development. May participate in Wnt signaling; F-box and WD repeat domain containing (412 aa)
     
 
  0.937
TRIM50
E3 ubiquitin-protein ligase TRIM50; E3 ubiquitin-protein ligase; Ring finger proteins (487 aa)
         
  0.936
SPSB4
SPRY domain-containing SOCS box protein 4; Probable substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins; Belongs to the SPSB family (273 aa)
     
 
  0.936
UBE2E2
Ubiquitin-conjugating enzyme E2 E2; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes ’Lys- 11’- and ’Lys-48’-, as well as ’Lys-63’-linked polyubiquitination. Catalyzes the ISGylation of influenza A virus NS1 protein; Ubiquitin conjugating enzymes E2 (201 aa)
     
  0.935
UBE2E1
Ubiquitin-conjugating enzyme E2 E1; Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes ’Lys-48’-linked polyubiquitination; Belongs to the ubiquitin-conjugating enzyme family (193 aa)
     
  0.929
CDC16
Cell division cycle protein 16 homolog; Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins- it mainly mediates the formation of ’Lys-11’-linked polyubiquitin chains and, to a lower extent, the formation of ’Lys-48’- and ’Lys-63’-linked polyubiquitin chains; Belongs to the APC6/CDC16 family (620 aa)
     
 
  0.922
RNF19A
E3 ubiquitin-protein ligase RNF19A; E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection; Belongs to the RBR family. RNF19 subfamily (838 aa)
         
  0.921
RNF34
E3 ubiquitin-protein ligase RNF34; E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. May mediate ’Lys-48’-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively reg [...] (373 aa)
     
 
  0.918
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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