Literature summary 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 .

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
2.3.2.33	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

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.3.2.33	Caenorhabditis elegans	Q17551	-	-
2.3.2.33	Mus musculus	Q7TPH6	-	-

Source Tissue

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

Synonyms

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

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Release 2023.1 (January 2023)