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 DPYSL4
-
DPYSL4 lacks the metal-cofactor-binding residues required for dihydropyrimidinase activity.
"Lacks most of the conserved residues that are essential for"
-
DPYSL4 belongs to the metallo-dependent hydrolase superfamily.
"Belongs to the metallo-dependent hydrolases superfamily."
A directed protein interaction network for investigating intracellular signal transduction.
Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to mediate Sema3A signalling.
A proteome-scale map of the human interactome network.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Multimodal cell maps as a foundation for structural and functional genomics.
The Ulip family phosphoproteins--common and specific properties.
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.
-
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.
-
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 DPYSL4
Collapsin response mediator protein 3 deacetylates histone H4 to mediate nuclear condensation and neuronal death.
-
Mouse CRMP3 full-length and fragment preparations exhibit deacetylation in two expression systems, with specificity controls. Exclusive intrinsic enzyme attribution and the identity of a listed commercial reagent remain unresolved.
"Here we found that mouse CRMP3 has robust histone H4 deacetylase activity."
-
The full-length protein, not only the cleaved form, was tested and had the strongest reported activity.
"purified full-length CRMP3 had the strongest HDAC activity, followed by that from the D domain and p54."
OpenScientist assessment of CRMP3 deacetylase and broad hydrolase activity