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  • 11.0 [archived version]
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TRIM11 TRIM11 RNF182 RNF182 BTRC BTRC RNF19B RNF19B TRIM32 TRIM32 TRIM69 TRIM69 FBXW11 FBXW11 TRIM21 TRIM21 TRIM4 TRIM4 TRIM50 TRIM50 TRIM9 TRIM9
"TRIM9" - E3 ubiquitin-protein ligase TRIM9 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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TRIM9E3 ubiquitin-protein ligase TRIM9; E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation; Belongs to the TRIM/RBCC family (710 aa)    
Predicted Functional Partners:
TRIM11
E3 ubiquitin-protein ligase TRIM11; E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation [...] (468 aa)
         
  0.940
TRIM50
E3 ubiquitin-protein ligase TRIM50; E3 ubiquitin-protein ligase; Ring finger proteins (487 aa)
         
  0.939
TRIM32
E3 ubiquitin-protein ligase TRIM32; Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo; Belongs to the TRIM/RBCC family (653 aa)
     
 
  0.939
RNF182
E3 ubiquitin-protein ligase RNF182; E3 ubiquitin-protein ligase that mediates the ubiquitination of ATP6V0C and targets it to degradation via the ubiquitin-proteasome pathway; Ring finger proteins (247 aa)
     
 
  0.937
TRIM4
E3 ubiquitin-protein ligase TRIM4; E3 ubiquitin-protein ligase. Mediates ’Lys-63’-linked polyubiquitination of the innate immune receptor DDX58, this linkage doesn’t lead to proteasomal degradation but seems to enhance IFN induction; Belongs to the TRIM/RBCC family (500 aa)
         
  0.932
FBXW11
F-box/WD repeat-containing protein 11; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) media [...] (542 aa)
       
  0.931
RNF19B
E3 ubiquitin-protein ligase RNF19B; 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 UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects against staurosporin-induced cell death (732 aa)
     
 
  0.930
TRIM69
E3 ubiquitin-protein ligase TRIM69; May have E3 ubiquitin-protein ligase activity. May play a role in apoptosis; Ring finger proteins (500 aa)
         
  0.930
BTRC
F-box/WD repeat-containing protein 1A; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Recognizes and binds to phosphorylated target proteins. SCF(BTRC) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(BTRC) mediates the ubiquitination of NFKBIA, NFKBIB and NFKBIE; the degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. Ubiquitination of NFKBIA occurs at ’Lys- 21 [...] (605 aa)
     
  0.930
TRIM21
E3 ubiquitin-protein ligase TRIM21; E3 ubiquitin-protein ligase whose activity is dependent on E2 enzymes, UBE2D1, UBE2D2, UBE2E1 and UBE2E2. Forms a ubiquitin ligase complex in cooperation with the E2 UBE2D2 that is used not only for the ubiquitination of USP4 and IKBKB but also for its self-ubiquitination. Component of cullin-RING-based SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes such as SCF(SKP2)-like complexes. A TRIM21-containing SCF(SKP2)- like complex is shown to mediate ubiquitination of CDKN1B (’Thr- 187’ phosphorylated-form), thereby promoting its degr [...] (475 aa)
         
  0.929
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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