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The protein encoded by UBR4 is an E3 ubiquitin-protein ligase that interacts with the retinoblastoma-associated protein in the nucleus and with calcium-bound calmodulin in the cytoplasm. Additionally we are shipping UBR4 Antibodies (34) and and many more products for this protein.
Showing 7 out of 14 products:
Ubiquitin ligase Ubr4 is a key component of the podocin interactome purified from podocytes. Ubiquitylation of one podocin site, K301, do not only target podocin for proteasomal degradation, but may also affect stability and disassembly of the multimeric complex.
Results showed KCMF1 (show KCMF1 ELISA Kits) C-terminus binds directly to RAD6, whereas N-terminal domains interact with UBR4 and point mutations found in X-linked intellectual disability (XLID) patients specifically lose the interaction with KCMF1 (show KCMF1 ELISA Kits) and UBR4.
This review summarizes the central nervous system functions of p600 (show IL13 ELISA Kits) and proposes new perspectives on its biological complexity in neuronal physiology and neurological diseases.
Although UBR4 is not an ion channel gene, the potential for disrupted Ca(2 (show CA2 ELISA Kits)+) control within neuronal cells highlights its potential for a role in this form of episodic ataxia (show USP14 ELISA Kits).
Dengue virus co-opts UBR4 to degrade STAT2 (show STAT2 ELISA Kits) and antagonize type I interferon (show IFNA ELISA Kits) signaling.
Human papillomavirus E7 oncoprotein associates with p600 (show IL13 ELISA Kits); interaction strongly contributes to cellular transformation independent of ability of E7 to bind pRB (show RB1 ELISA Kits).
Results identify and characterize p600, a unique 600-kDa retinoblastoma protein- and calmodulin-binding protein.
Ubiquitin ligase Ubr4 is a key component of the podocin interactome purified from cultured podocytes and native glomeruli. Ubiquitylomic analysis of mouse glomeruli revealed that podocin is ubiquitylated at two lysine residues. Ubiquitylation of one podocin site, K301, do not only target podocin for proteasomal degradation, but may also affect stability and disassembly of the multimeric complex.
This study is the first to identify a novel E3 ubiquitin ligase component, UBR4, in the murine SCN (show SRI ELISA Kits) and to implicate the N-end rule degradation pathway as a potential player in regulating core clock mechanisms and photic entrainment.
UBR4-deficient mice die during embryogenesis and exhibit pleiotropic abnormalities, including impaired vascular development in the yolk sac (show ADCY10 ELISA Kits).
Found murine p600 (formally called RBAF600) copurified with the E7 oncoprotein in C127 cells. This interaction was found to correlate with the ability of E7 to increase transformation.
This study identified protein 600 (p600) as a novel microtubule-associated protein (show SPAG5 ELISA Kits) (MAP) developmentally regulated in neurons. p600 exhibits the unique feature to interact with the endoplasmic reticulum (ER).
Member of UBR box protein family, termed Ubr4. Binds to destabilizing N-terminal residues of N-end rule substrates. Participates in degradation of N-end rule substrates.
The protein encoded by this gene is an E3 ubiquitin-protein ligase that interacts with the retinoblastoma-associated protein in the nucleus and with calcium-bound calmodulin in the cytoplasm. The encoded protein appears to be a cytoskeletal component in the cytoplasm and part of the chromatin scaffold in the nucleus. In addition, this protein is a target of the human papillomavirus type 16 E7 oncoprotein.
retinoblastoma-associated factor 600
, zinc finger, UBR1 type 1
, E3 ubiquitin-protein ligase UBR4
, retinoblastoma-associated factor 600-like protein
, retinoblastoma-associated factor of 600 kDa
, zinc finger UBR1-type protein 1