P60761 · NEUG_MOUSE

  • Protein
    Neurogranin
  • Gene
    Nrgn
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.

Features

Showing features for site.

17810203040506070
MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD
TypeIDPosition(s)Description
Site38Crucial for interaction with calmodulin

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentaxon
Cellular Componentdendrite
Cellular Componentdendritic spine head
Cellular Componentglutamatergic synapse
Cellular Componentmitochondrial membrane
Cellular Componentneuronal cell body
Cellular Componentpostsynapse
Cellular Componentpostsynaptic membrane
Cellular Componenttrans-Golgi network transport vesicle membrane
Molecular Functioncalmodulin binding
Molecular Functionphosphatidic acid binding
Molecular Functionphosphatidylinositol-3,4,5-trisphosphate binding
Biological Processintracellular signal transduction
Biological Processpositive regulation of long-term synaptic potentiation
Biological Processpostsynaptic modulation of chemical synaptic transmission

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Neurogranin
  • Short names
    Ng
  • Alternative names
    • RC3
  • Cleaved into 1 chains

Gene names

    • Name
      Nrgn

Organism names

  • Taxonomic identifier
  • Strains
    • 129/SvJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P60761
  • Secondary accessions
    • B2RRN7
    • Q3TYH4

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis38Abolishes calmodulin binding, unable to potentiate synaptic transmission.

PTM/Processing

Features

Showing features for modified residue, chain, disulfide bond, peptide.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00001595921-78Neurogranin
Disulfide bond3↔51Or C-51 with C-4 or C-9
Modified residue36Phosphoserine; by PHK and PKC
PeptidePRO_000037770255-78NEUG(55-78)
Modified residue68Citrulline; partial
Modified residue68Omega-N-methylarginine

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

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with apo-calmodulin; this interaction decreases the affinity of calmodulin for calcium ions.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain26-47IQ
Region39-78Disordered
Domain48-78Collagen-like

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 status
    Complete
  • Length
    78
  • Mass (Da)
    7,496
  • Last updated
    2004-04-13 v1
  • Checksum
    8E47CDB38E095794
MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp