GO annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified annotations to orthologs by curator judgment
Annotation inferences using phylogenetic trees
GO annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping
GO annotation based on curation of immunofluorescence data (HPA)
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
UniProt entry for DPYSL3
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DPYSL3 lacks the metal-cofactor-binding residues required for dihydropyrimidinase activity.
"Lacks most of the conserved residues that are essential for"
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DPYSL3 belongs to the metallo-dependent hydrolase superfamily.
"Belongs to the metallo-dependent hydrolases superfamily."
Genome-wide YFP fluorescence complementation screen identifies new regulators for telomere signaling in human cells.
Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling.
A proteome-scale map of the human interactome network.
Architecture of the human interactome defines protein communities and disease networks.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Reactome pathway (CRMP/semaphorin signalling)
Reactome pathway (CRMP/semaphorin signalling)
Reactome pathway (CRMP/semaphorin signalling)
Collapsin response mediator protein 2: high-resolution crystal structure sheds light on small-molecule binding, post-translational modifications, and conformational flexibility.
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A human CRMP2 structure establishes loss of the ancestral dihydropyrimidinase active site; this is target evidence for DPYSL2 and comparative evidence for other CRMPs.
"Although CRMP-2, and other CRMPs, belong to the
dihydropyrimidinase family, they have lost the enzymatic active site."
Insights into the oligomerization of CRMPs: crystal structure of human collapsin response mediator protein 5.
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CRMP5 was directly tested for amidohydrolase activity and showed none; this is comparative, not a direct assay of the present target. CRMP1/2 oligomerization was also compared.
"CRMP-5 does not have any detectable amidohydrolase
activity."
openscientist.md evidence for DPYSL3