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Search results 101 to 113 out of 113 for Tax1bp1

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0.017s
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.
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