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MGRN1 MGRN1 RNF182 RNF182 ASB7 ASB7 ARIH2 ARIH2 ASB13 ASB13 MIB2 MIB2 TRIM37 TRIM37 KLHL20 KLHL20 TRIM9 TRIM9 SH3RF1 SH3RF1 TRIM11 TRIM11
"TRIM11" - E3 ubiquitin-protein ligase TRIM11 in Homo sapiens
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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TRIM11E3 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)    
Predicted Functional Partners:
ASB7
Ankyrin repeat and SOCS box protein 7; Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins; Belongs to the ankyrin SOCS box (ASB) family (318 aa)
     
  0.944
TRIM9
E3 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)
         
  0.940
TRIM37
E3 ubiquitin-protein ligase TRIM37; E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication. Mediates monoubiquitination of ’Lys-119’ of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression- associates with some Polycomb group (PcG) multiprotein PRC2-like complex and mediates repression of target genes. Has anti-HIV activity; Belongs to the TRIM/RBCC family (964 aa)
         
  0.940
ASB13
Ankyrin repeat and SOCS box protein 13; May be a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins; Ankyrin repeat domain containing (278 aa)
     
  0.934
MGRN1
E3 ubiquitin-protein ligase MGRN1; E3 ubiquitin-protein ligase. Mediates monoubiquitination at multiple sites of TSG101 in the presence of UBE2D1, but not of UBE2G1, nor UBE2H. Plays a role in the regulation of endosome-to- lysosome trafficking. Impairs MC1R- and MC4R-signaling by competing with GNAS-binding to MCRs and inhibiting agonist-induced cAMP production. Does not inhibit ADRB2-signaling. Does not promote MC1R ubiquitination; Ring finger proteins (576 aa)
         
  0.931
ARIH2
E3 ubiquitin-protein ligase ARIH2; E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin- conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates- associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activate [...] (493 aa)
     
 
  0.927
KLHL20
Kelch-like protein 20; Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in interferon response and anterograde Golgi to endosome transport. The BCR(KLHL20) E3 ubiquitin ligase complex mediates the ubiquitination of DAPK1, leading to its degradation by the proteasome, thereby acting as a negative regulator of apoptosis. The BCR(KLHL20) E3 ubiquitin ligase complex also specifically mediates ’Lys-33’- linked ubiquitination. Involved in anterograde Golgi to endosome transport by mediating ’Lys-33’-linked ubiquitination of CORO7, promoting int [...] (609 aa)
         
  0.924
MIB2
E3 ubiquitin-protein ligase MIB2; E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors; Ankyrin repeat domain containing (1070 aa)
     
  0.924
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)
         
  0.923
SH3RF1
E3 ubiquitin-protein ligase SH3RF1; Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). May be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane; Belongs to the SH3RF family (888 aa)
         
  0.923
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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