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 DPYSL2
-
DPYSL2 lacks the metal-cofactor-binding residues required for dihydropyrimidinase activity.
"Lacks most of the conserved residues that are essential for"
-
DPYSL2 belongs to the metallo-dependent hydrolase superfamily.
"Belongs to the metallo-dependent hydrolases superfamily."
GOA annotation export for DPYSL2
-
GOA records the phylogenetic IBA source for the DPYSL2 GO:0016812 annotation.
"UniProtKB Q16555 DPYSL2 enables GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides molecular_function ECO:0000318 IBA GO_REF:0000033 AGI_LocusCode:AT5G12200|FB:FBgn0023023|MGI:MGI:1928679|PANTHER:PTN000182670|RGD:68376|UniProtKB:Q14117|UniProtKB:Q46806|WB:WBGene00000963|WB:WBGene00000964|dictyBase:DDB_G0269246 9606 Homo sapiens GO_Central Dihydropyrimidinase-related protein 2 20221007"
OpenScientist hypothesis report for DPYSL2 GO:0016812
-
OpenScientist refutes cyclic-amide hydrolase activity for DPYSL2.
"DPYSL2 is a **catalytically dead pseudoenzyme**"
-
The report supports loss of cyclic-amide catalysis from missing metal-center residues and CRMP2 structural evidence. The CRMP5 negative assay is paralog evidence. Neither loss of this reaction nor a noncatalytic alternative role proves exclusion from all broader metabolic processes.
CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation.
Protein product of CLN6 gene responsible for variant late-onset infantile neuronal ceroid lipofuscinosis interacts with CRMP-2.
MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
Collapsin response mediator protein-2 (Crmp2) regulates trafficking by linking endocytic regulatory proteins to dynein motors.
Next-generation sequencing to generate interactome datasets.
A directed protein interaction network for investigating intracellular signal transduction.
Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism.
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.
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.
Protein interaction studies in human induced neurons indicate convergent biology underlying autism spectrum disorders.
Multimodal cell maps as a foundation for structural and functional genomics.
A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution.
Reactome pathway (CRMP/semaphorin signalling)
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 CRMP1 hypothesis report, including legacy CRMP metabolic annotations
-
The report recommends removal of broad nucleobase-metabolism annotations and extension of corrections to CRMP2, but its provenance specifies only verification of the PMID:8973361 abstract. That scope cannot establish absence of metabolic evidence in the full paper.
"**PMID:8973361 abstract verification**: confirmed paper contains cloning and naming only, no enzymatic assay."