RGD Reference Report - PIN: an associated protein inhibitor of neuronal nitric oxide synthase. - Rat Genome Database

Send us a Message
Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   
Search RGD Grant Resources Citing RGD About Us Contact Us
Genes Variants Community Projects QTLs Strains Markers Genome Information Ontologies Cell Lines References Download Submit Data
OntoMate (Literature Search) JBrowse (Genome Browser) Synteny Browser (VCMap) Variant Visualizer Multi-Ontology Enrichment (MOET) Gene-Ortholog Location Finder (GOLF) InterViewer (Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine GViewer (Genome Viewer)
Aging & Age-Related Disease Cancer & Neoplastic Disease Cardiovascular Disease Coronavirus Disease Developmental Disease Diabetes Hematologic Disease Immune & Inflammatory Disease Infectious Disease Liver Disease Neurological Disease Obesity & Metabolic Syndrome Renal Disease Respiratory Disease Sensory Organ Disease
Find Models Genetic Models Autism Models Rat PhenoMiner (Quantitative Phenotypes) Chinchilla PhenoMiner Expected Ranges (Quantitative Phenotype) PhenoMiner Term Comparison Hybrid Rat Diversity Panel Phenotypes Phenotypes in Other Animal Models Animal Husbandry Strain Medical Records Phylogenetics Strain Availability Calendar Rats 101 Submissions Photo Archive
Pathways
Rat Community Forum Directory of Rat Laboratories Video Tutorials News RGD Publications RGD Presentations Archive Nomenclature Guidelines Resource Links Laboratory Resources Employment Resources
Advanced Search (OLGA)

PIN: an associated protein inhibitor of neuronal nitric oxide synthase.

Authors: Jaffrey, SR  Snyder, SH 
Citation: Jaffrey SR and Snyder SH, Science 1996 Nov 1;274(5288):774-7.
RGD ID: 633683
Pubmed: PMID:8864115   (View Abstract at PubMed)

The neurotransmitter functions of nitric oxide are dependent on dynamic regulation of its biosynthetic enzyme, neuronal nitric oxide synthase (nNOS). By means of a yeast two-hybrid screen, a 10-kilodalton protein was identified that physically interacts with and inhibits the activity of nNOS. This inhibitor, designated PIN, appears to be one of the most conserved proteins in nature, showing 92 percent amino acid identity with the nematode and rat homologs. Binding of PIN destabilizes the nNOS dimer, a conformation necessary for activity. These results suggest that PIN may regulate numerous biological processes through its effects on nitric oxide synthase activity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Dynll1Ratnegative regulation of nitric oxide biosynthetic process acts_upstream_of_or_withinIDA PMID:8864115MGI 
Dynll1Ratnegative regulation of nitric oxide biosynthetic process involved_inIDA PMID:8864115UniProt 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Dynll1Ratenzyme inhibitor activity enablesIDA PMID:8864115MGI 
Dynll1Ratnitric-oxide synthase inhibitor activity enablesIDA PMID:8864115UniProt 
Dynll1Ratnitric-oxide synthase regulator activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Dynll1  (dynein light chain LC8-type 1)

Objects referenced in this article
Gene DYNLL1 dynein light chain LC8-type 1 Homo sapiens

Additional Information