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Search results 201 to 221 out of 221 for Btbd1

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0.017s
Type Details Score
Publication
First Author: Sampathkumar P
Year: 2010
Journal: J Mol Biol
Title: Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1.
Volume: 397
Issue: 4
Pages: 883-92
Protein
Organism: Mus musculus/domesticus
Length: 74  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
Protein Domain
Type: Homologous_superfamily
Description: This domain is called PHR as it was originally found in the E3 ubiquitin-protein ligase proteins PAM (), highwire () and RPM-1 () [].PHR proteins are conserved, large multi-domain E3 ubiquitin ligases with modular architecture. PHR proteins presynaptically control synaptic growth and axon guidance and postsynaptically regulate endocytosis of glutamate receptors. Dysfunction of neuronal ubiquitin-mediated proteasomal degradation is implicated in various neurodegenerative diseases. PHR proteins are characterised by the presence of two PHR domains near the N terminus, which are essential for proper localisation and function. The domain has a β-sandwich fold composed of 11 anti-parallel β-strands [].The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils [].
Protein Domain
Type: Domain
Description: This domain is called PHR as it was originally found in the E3 ubiquitin-protein ligase proteins PAM (), highwire () and RPM-1 () [].PHR proteins are conserved, large multi-domain E3 ubiquitin ligases with modular architecture. PHR proteins presynaptically control synaptic growth and axon guidance and postsynaptically regulate endocytosis of glutamate receptors. Dysfunction of neuronal ubiquitin-mediated proteasomal degradation is implicated in various neurodegenerative diseases. PHR proteins are characterised by the presence of two PHR domains near the N terminus, which are essential for proper localisation and function. The domain has a β-sandwich fold composed of 11 anti-parallel β-strands [].The C-terminal region of the protein BTBD1 includes the PHR domain and is known to interact with Topoisomerase I, an enzyme which relaxes DNA supercoils [].
Protein
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 361  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 488  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 392  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 547  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 539  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 461  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4749  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 4636  
Fragment?: true