Type |
Details |
Score |
Publication |
First Author: |
Suzuki N |
Year: |
2016 |
Journal: |
FEBS J |
Title: |
A novel mode of ubiquitin recognition by the ubiquitin-binding zinc finger domain of WRNIP1. |
Volume: |
283 |
Issue: |
11 |
Pages: |
2004-17 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pujari R |
Year: |
2015 |
Journal: |
PLoS Pathog |
Title: |
Human T-cell leukemia virus type 1 (HTLV-1) tax requires CADM1/TSLC1 for inactivation of the NF-κB inhibitor A20 and constitutive NF-κB signaling. |
Volume: |
11 |
Issue: |
3 |
Pages: |
e1004721 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li H |
Year: |
2004 |
Journal: |
Oncogene |
Title: |
An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. |
Volume: |
23 |
Issue: |
10 |
Pages: |
1801-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jacque E |
Year: |
2009 |
Journal: |
EMBO J |
Title: |
RNF11, a new piece in the A20 puzzle. |
Volume: |
28 |
Issue: |
5 |
Pages: |
455-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kostaras E |
Year: |
2013 |
Journal: |
Oncogene |
Title: |
SARA and RNF11 interact with each other and ESCRT-0 core proteins and regulate degradative EGFR trafficking. |
Volume: |
32 |
Issue: |
44 |
Pages: |
5220-32 |
|
•
•
•
•
•
|
Publication |
First Author: |
Santonico E |
Year: |
2015 |
Journal: |
Oncogene |
Title: |
RNF11 is a GGA protein cargo and acts as a molecular adaptor for GGA3 ubiquitination mediated by Itch. |
Volume: |
34 |
Issue: |
26 |
Pages: |
3377-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kitching R |
Year: |
2003 |
Journal: |
Biochim Biophys Acta |
Title: |
The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases. |
Volume: |
1639 |
Issue: |
2 |
Pages: |
104-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
Subramaniam V |
Year: |
2003 |
Journal: |
Br J Cancer |
Title: |
The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase. |
Volume: |
89 |
Issue: |
8 |
Pages: |
1538-44 |
|
•
•
•
•
•
|
Publication |
First Author: |
Azmi PB |
Year: |
2009 |
Journal: |
Anticancer Res |
Title: |
The RING finger protein11 binds to Smad4 and enhances Smad4-dependant TGF-beta signalling. |
Volume: |
29 |
Issue: |
6 |
Pages: |
2253-63 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
RING finger protein 11 (RNF11) is an E3 ubiquitin-protein ligase that acts both as an adaptor and a modulator of itch-mediated control of ubiquitination events underlying membrane traffic. It is the downstream of an enzymatic cascade for the ubiquitination of specific substrates. It is also a molecular adaptor of homologous to E6-associated protein C terminus (HECT)-type ligases []. RNF11 has been implicated in the regulation of several signaling pathways. It enhances the transforming growth factor receptor (TGFR) signaling by both abrogating Smurf2-mediated receptor ubiquitination and by promoting the Smurf2-mediated degradation of AMSH (associated molecule with the SH3 domain of STAM), a de-ubiquitinating enzyme that enhances transforming growth factor-beta (TGF-beta) signalling and epidermal growth factor receptor (EGFR) endosomal recycling [, ]. It also acts directly on Smad4 to enhance Smad4 function, and plays a role in prolonged TGF-beta signalling []. Moreover, RNF11 functions as a critical component of the A20 ubiquitin-editing protein complex that negatively regulates tumor necrosis factor (TNF)-mediated nuclear factor (NF)-kappaB activation []. It also interacts with Smad anchor for receptor activation (SARA) and the endosomal sorting complex required for transport (ESCRT)-0 complex, thus participating in the regulation of lysosomal degradation of EGFR []. Furthermore, RNF11 acts as a novel GGA cargo actively participating in regulating the ubiquitination of the GGA protein family []. In addition, RNF11 functions together with TAX1BP1 to target TANK-binding kinase 1 (TBK1)/IkappaB kinase IKKi, and further restricts antiviral signaling and type I interferon (IFN)-beta production []. RNF11 contains an N-terminal PPPY motif that binds WW domain-containing proteins such as AIP4/itch, Nedd4 and Smurf1/2 (SMAD-specific E3 ubiquitin-protein ligase 1/2), and a C-terminal C3H2C3-type RING-H2 finger that functions as a scaffold for the coordinated transfer of ubiquitin to substrate proteins together with the E2 enzymes UbcH527 and Ubc13. |
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•
•
•
•
•
|
Publication |
First Author: |
Xu Y |
Year: |
2019 |
Journal: |
Autophagy |
Title: |
The cargo receptor SQSTM1 ameliorates neurofibrillary tangle pathology and spreading through selective targeting of pathological MAPT (microtubule associated protein tau). |
Volume: |
15 |
Issue: |
4 |
Pages: |
583-598 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
154
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
144
 |
Fragment?: |
true |
|
•
•
•
•
•
|