Literature summary for 2.3.2.33 extracted from

Sampathkumar, P.; Ozyurt, S.A.; Miller, S.A.; Bain, K.T.; Rutter, M.E.; Gheyi, T.; Abrams, B.; Wang, Y.; Atwell, S.; Luz, J.G.; Thompson, D.A.; Wasserman, S.R.; Emtage, J.S.; Park, E.C.; Rongo, C.; Jin, Y.; Klemke, R.L.; Sauder, J.M.; Burley, S.K.
Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092-->Glu) of the C. elegans ortholog RPM-1 (2010), J. Mol. Biol., 397, 883-892 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of both the first and second PHR domains, displaying a beta sandwich fold composed of 11 anti-parallel beta-strands	Mus musculus

Protein Variants

Protein Variants	Comment	Organism
G1092E	loss of function mutant. The residue is expected to disturb the topography of the conserved apical surface of RPM-1	Caenorhabditis elegans

Organism

Organism	UniProt	Comment	Textmining
Caenorhabditis elegans	Q17551	-	-
Mus musculus	Q7TPH6	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
neuron	localizes to synaptic regions and the tip of the head motor neurons	Caenorhabditis elegans	-

Synonyms

Synonyms	Comment	Organism
E3 ubiquitin-protein ligase	-	Mus musculus
MYCBP2	-	Mus musculus
PHR1	-	Mus musculus
RPM-1	-	Caenorhabditis elegans

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Release 2023.1 (January 2023)