P60761 · NEUG_MOUSE
- ProteinNeurogranin
- GeneNrgn
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 38 | Crucial for interaction with calmodulin | ||||
Sequence: R |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | dendrite | |
Cellular Component | dendritic spine head | |
Cellular Component | glutamatergic synapse | |
Cellular Component | mitochondrial membrane | |
Cellular Component | neuronal cell body | |
Cellular Component | postsynapse | |
Cellular Component | postsynaptic membrane | |
Cellular Component | trans-Golgi network transport vesicle membrane | |
Molecular Function | calmodulin binding | |
Molecular Function | phosphatidic acid binding | |
Molecular Function | phosphatidylinositol-3,4,5-trisphosphate binding | |
Biological Process | intracellular signal transduction | |
Biological Process | positive regulation of long-term synaptic potentiation | |
Biological Process | postsynaptic modulation of chemical synaptic transmission |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameNeurogranin
- Short namesNg
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP60761
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Restricted to dendritic spines of a subset of neurons.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 38 | Abolishes calmodulin binding, unable to potentiate synaptic transmission. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for modified residue, chain, disulfide bond, peptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000159592 | 1-78 | Neurogranin | |||
Sequence: MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD | ||||||
Disulfide bond | 3↔51 | Or C-51 with C-4 or C-9 | ||||
Sequence: CCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGEC | ||||||
Modified residue | 36 | Phosphoserine; by PHK and PKC | ||||
Sequence: S | ||||||
Peptide | PRO_0000377702 | 55-78 | NEUG(55-78) | |||
Sequence: GPGPGGPGGAGGARGGAGGGPSGD | ||||||
Modified residue | 68 | Citrulline; partial | ||||
Sequence: R | ||||||
Modified residue | 68 | Omega-N-methylarginine | ||||
Sequence: R |
Post-translational modification
Disulfide bond formation is redox-sensitive. The cysteine residues are readily oxidized by several nitric acid (NO) donors and other oxidants to form intramolecular disulfide. Cys-51 can form a disulfide with any other of the cysteine residues with an order of reactivity Cys-9 > Cys-4 > Cys-3 (By similarity).
Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 26-47 | IQ | ||||
Sequence: ANAAAAKIQASFRGHMARKKIK | ||||||
Region | 39-78 | Disordered | ||||
Sequence: GHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD | ||||||
Domain | 48-78 | Collagen-like | ||||
Sequence: SGECGRKGPGPGGPGGAGGARGGAGGGPSGD |
Domain
Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.
Sequence similarities
Belongs to the neurogranin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length78
- Mass (Da)7,496
- Last updated2004-04-13 v1
- Checksum8E47CDB38E095794
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF230869 EMBL· GenBank· DDBJ | AAG27519.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK002933 EMBL· GenBank· DDBJ | BAB22466.1 EMBL· GenBank· DDBJ | mRNA | ||
AK158630 EMBL· GenBank· DDBJ | BAE34589.1 EMBL· GenBank· DDBJ | mRNA | ||
BC061102 EMBL· GenBank· DDBJ | AAH61102.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138511 EMBL· GenBank· DDBJ | AAI38512.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138513 EMBL· GenBank· DDBJ | AAI38514.1 EMBL· GenBank· DDBJ | mRNA |