Search results for DCUN1D3

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Protein (2 results from a total of 2)

Identifier: R-HSA-8951782
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: DCUN1D3: Q8IWE4
Identifier: R-HSA-8956204
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: Q8IWE4

RNA Sequence (1 results from a total of 1)

Identifier: R-HSA-8956228
Species: Homo sapiens
Compartment: cytosol
Primary external reference: ENSEMBL: DCUN1D3: ENST00000324344

Reaction (5 results from a total of 5)

Identifier: R-HSA-8956234
Species: Homo sapiens
Compartment: nucleoplasm
PUM2 is a sequence-specific RNA binding protein that binds DCUN1D3 mRNA and decreases levels of mature DCUN1D3 protein, likely by promoting mRNA degradation (Galgano et al, 2008; Huang et al, 2014).
Identifier: R-HSA-8956200
Species: Homo sapiens
Compartment: plasma membrane
DCUN1D3 binds to CRL1 ligase complexes to antagonize their neddylation and activation. DCUN1D3 is unique among the DCUN1D family members in that is N-terminally myristolyated, resulting in plasma membrane localization. Binding of DCUN1D3 to CUL1-containing E3 ligase complexes sequesters the cullin complexes at the plasma membrane, inhibiting their DCUN1D1-mediated neddylation (Huang et al, 2014). Although in this reaction DCUN1D3 is shown binding to cullin E3 ligases in complex with COMMD proteins and CCDC22, DCUN1D3 has also been shown to interact with CAND1 and the precise timing of this sequestration binding event remains to be clarified.
Identifier: R-HSA-8952620
Species: Homo sapiens
Compartment: cytosol
UBE2M is the E2 for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). Interaction between UBE2M and the CUL1 E3 complex is facilitated by a DCUN1D (also known as DCNL) scaffold protein, of which there are 5 in human cells (Kim et al, 2008; Kurz et al, 2008; Meyer-Schaller et al, 2009; Monda et al, 2013; Keuss et al, 2016). DCUN1D proteins interact with higher affinity to the N-terminally acetylated forms of UBE2F and UBE2M (Scott et al, 2011; Monda et al, 2013). Although each of the 5 DCUN1D proteins appears to interact with most cullin subtypes, specificity may arise through differences in expression and localization, and DCUN1D3 may play a specialized role in sequestering CRL E3 ligase complexes at the cell membrane (Monda et al, 2013; Keuss et al, 2016; Meyer-Schaller et al, 2009; Huang et al, 2014; reviewed in Enchev et al, 2103). Although in this pathway, COMMD proteins and DCUN1D are shown acting sequentially in the activation of the CRL E3 ligase complex, the relationship between these protein families is not totally clear, as DCUN1D proteins have been identified in complexes that also contain the inhibitor CAND1 (Kim et al, 2008; Huang et al, 2014). Target specificity of the CRL1 complex is directed by the nature of the F box substrate recognition protein, of which there are more than 60 in humans. Identified targets of CRL1-containing complexes include signaling molecules, transcriptional regulators and regulators of cell cycle progression, among others (reviewed in Gutierrez and Ronai, 2006; Lipkowitz and Weissman, 2011). CRL1 complexes are also hijacked by a number of viruses, redirecting the ubiquitin ligase complex to target host proteins and in this way promoting viral propagation (reveiwed in Mahon et al, 2014).
Identifier: R-HSA-8952039
Species: Homo sapiens
Compartment: cytosol
UBE2F is specific for the CUL5:RBX2-containing E3 ligase complex (Huang et al, 2009; Monda et al, 2013). Interaction between UBE2F and the CUL5 E3 complex is facilitated by a DCUN1D (also known as DCNL) scaffold protein, of which there are 5 in human cells (Kim et al, 2008; Kurz et al, 2008; Meyer-Schaller et al, 2009; Monda et al, 2013; Keuss et al, 2016). DCUN1D proteins interact with higher affinity to the N-terminally acetylated forms of UBE2F and UBE2M (Scott et al, 2011; Monda et al, 2013). Although each of the 5 DCUN1D proteins appears to interact with most cullin subtypes, specificity may arise through differences in expression and localization, and DCUN1D3 may play a specialized role in sequestering CRL E3 ligase complexes at the cell membrane (Monda et al, 2013; Keuss et al, 2016; Meyer-Schaller et al, 2009; Huang et al, 2014; reviewed in Enchev et al, 2103). Although in this pathway, COMMD proteins and DCUN1D are shown acting sequentially in the activation of the CRL E3 ligase complex, the relationship between these protein families is not totally clear, as DCUN1D proteins have been identified in complexes that also contain the inhibitor CAND1 (Kim et al, 2008; Huang et al, 2014).
CUL5 RING complexes target a variety of cellular proteins for ubiquitination and degradation, including receptor and non-receptor tyrosine kinases, signaling molecules transcriptional regulators (reviewed in Okumura et al, 2016). CRL5 complexes are also hijacked by viruses such as HIV and HPV, among others. Interaction with viral proteins redirects the ubiquitin ligase complex, targeting host proteins such as immune factors and in this way promoting viral propagation (reveiwed in Mahon et al, 2014).
Identifier: R-HSA-8952639
Species: Homo sapiens
Compartment: nucleoplasm
UBE2M is the E2 for CRL complexes containing cullin 1, 2, 3 and 4 (Huang et al, 2009; Monda et al, 2013). Interaction between UBE2M and the CUL4A and 4B E3 complex is facilitated by a DCUN1D (also known as DCNL) scaffold protein, of which there are 5 in human cells (Kim et al, 2008; Kurz et al, 2008; Meyer-Schaller et al, 2009; Monda et al, 2013; Keuss et al, 2016). DCUN1D proteins interact with higher affinity to the N-terminally acetylated forms of UBE2F and UBE2M (Scott et al, 2011; Monda et al, 2013). Although each of the 5 DCUN1D proteins appears to interact with most cullin subtypes, specificity may arise through differences in expression and localization, and DCUN1D3 may play a specialized role in sequestering CRL E3 ligase complexes at the cell membrane (Monda et al, 2013; Keuss et al, 2016; Meyer-Schaller et al, 2009; Huang et al, 2014; reviewed in Enchev et al, 2103). Although in this pathway, COMMD proteins and DCUN1D are shown acting sequentially in the activation of the CRL E3 ligase complex, the relationship between these protein families is not totally clear, as DCUN1D proteins have been identified in complexes that also contain the inhibitor CAND1 (Kim et al, 2008; Huang et al, 2014).
CRL4 complexes ubiquitinate target proteins involved in processes such as cell cycle progression, DNA repair and replication, cell growth and metabolism (reviewed in Hannah and Zhou, 2015; Sang et al, 2015). CRL4 complexes are also hijacked by a number of viruses, redirecting the ubiquitin ligase complex to target host proteins and in this way promoting viral propagation (reviewed in Mahon et al, 2014). Note that because many of the key CRL4 ubiquitin targets are nuclear, these complexes are depicted in the nucleus. Cytoplasmic targets have also been identified, however (reviewed in Hannah and Zhou, 2015).

Complex (2 results from a total of 2)

Identifier: R-HSA-8956232
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-8956203
Species: Homo sapiens
Compartment: plasma membrane
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