Nrgn
entrez
64356
canonical
uniprot
Q04940
canonical
ensembl
ENSRNOG00000010688
resolver
ensembl
ENSRNOG00055009766
resolver
ensembl
ENSRNOG00060011886
resolver
ensembl
ENSRNOG00065016951
resolver
ensp
ENSRNOP00000014404
resolver
ensp
ENSRNOP00055013334
resolver
ensp
ENSRNOP00060015782
resolver
ensp
ENSRNOP00065022344
resolver
enst
ENSRNOT00000014404
resolver
enst
ENSRNOT00055016539
resolver
enst
ENSRNOT00060020109
resolver
enst
ENSRNOT00065028270
resolver
genesymbol
Nrgn
resolver
uniprot_entry
NEUG_RAT
resolver
amino_acid_sequence
MDCCTESACSKPDDDILDIPLDDPGANAAAAKIQASFRGHMARKKIKSGECGRKGPGPGGPGGAGGARGGAGGGPSGD
uniprot
proteins
function
FUNCTION: Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning (By similarity). {ECO:0000250, ECO:0000269|PubMed:15262982}.
uniprot
proteins
mass_dalton
7496
uniprot
proteins
mutagenesis
MUTAGEN 3; /note="C->S: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with G-4 or S-9."; /evidence="ECO:0000269|PubMed:8910523"; MUTAGEN 4; /note="C->G: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with S-3 or S-9."; /evidence="ECO:0000269|PubMed:8910523"; MUTAGEN 9; /note="C->S: No effect on oxidant-mediated disulfide bond formation nor on in vitro PKC-mediated phosphorylation. No effect on oxidant-mediated disulfide bond formation; when associated with S-3 or G-4."; /evidence="ECO:0000269|PubMed:8910523"; MUTAGEN 51; /note="C->G: No oxidant-mediated disulfide bond formation. No effect on in vitro PKC-mediated phosphorylation. No oxidant-mediated disulfide bond formation; when associated with S-3; G-4 and S-9."; /evidence="ECO:0000269|PubMed:8910523
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-36 by PHK and PKC. Phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions (By similarity). {ECO:0000250}.; PTM: Phosphorylation is activated by calcium, phospholipids, and diacylglycerol. Phosphorylation inhibits binding to calmodulin both in the presence and absence of calcium. {ECO:0000269|PubMed:8080473, ECO:0000269|PubMed:8454596}.; PTM: 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.
uniprot
proteins
protein_family
Neurogranin family
uniprot
proteins
pubmed
15262982
uniprot
proteins
pubmed
1528865
uniprot
proteins
pubmed
19164277
uniprot
proteins
pubmed
2231781
uniprot
proteins
pubmed
7730337
uniprot
proteins
pubmed
8080473
uniprot
proteins
pubmed
8454596
uniprot
proteins
pubmed
8910523
uniprot
proteins
sequence_length
78
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1528865}. Synapse {ECO:0000269|PubMed:1528865}. Cell projection, dendritic spine {ECO:0000269|PubMed:1528865}. Note=Restricted to dendritic spines of a subset of neurons.
uniprot
proteins