NEUG_HUMAN
ID NEUG_HUMAN Reviewed; 78 AA.
AC Q92686;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Neurogranin;
DE Short=Ng;
DE AltName: Full=RC3;
DE Contains:
DE RecName: Full=NEUG(55-78);
GN Name=NRGN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8929222;
RA Mertsalov I.B., Gundelfinger E.D., Tsetlin V.I.;
RT "Cloning cDNA for human neurogranin.";
RL Bioorg. Khim. 22:366-369(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9499372;
RA Mertsalov I.B., Stumm M., Wieacker P., tom Dieck S., Gundelfinger E.D.,
RA Tsetlin V.I.;
RT "Structure and chromosomal localization of human neurogranin gene.";
RL Bioorg. Khim. 23:961-968(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9143500; DOI=10.1006/geno.1997.4622;
RA Martinez de Arrieta C., Perez Jurado L., Bernal J., Coloma A.;
RT "Structure, organization, and chromosomal mapping of the human neurogranin
RT gene (NRGN).";
RL Genomics 41:243-249(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=9329454; DOI=10.1097/00005072-199710000-00004;
RA Chang J.W., Schumacher E., Coulter P.M. II, Vinters H.V., Watson J.B.;
RT "Dendritic translocation of RC3/neurogranin mRNA in normal aging, Alzheimer
RT disease and fronto-temporal dementia.";
RL J. Neuropathol. Exp. Neurol. 56:1105-1118(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mertsalov I.B., Tsetlin V.I.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP CITRULLINATION AT ARG-68.
RX PubMed=23828821; DOI=10.1002/pmic.201300064;
RA Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.;
RT "Identification and Characterization of citrulline-modified brain proteins
RT by combining HCD and CID fragmentation.";
RL Proteomics 13:2682-2691(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-68, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Acts as a 'third messenger' substrate of protein kinase C-
CC mediated molecular cascades during synaptic development and remodeling.
CC Binds to calmodulin in the absence of calcium (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In the cerebral cortex, found in the cell bodies of
CC neurons in layers II-VI, and in apical and basal dendrites of pyramidal
CC neurons. Is not found in the dendrites in patients with Alzheimer
CC disease. {ECO:0000269|PubMed:9329454}.
CC -!- DOMAIN: Neurogranin is intrinsically unstructured; however, upon
CC binding with CaM, The IQ domain adopts a helical conformation.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents
CC interaction with Calmodulin and interrupts several learning- and
CC memory-associated functions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the neurogranin family. {ECO:0000305}.
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DR EMBL; Y09689; CAA70867.1; -; mRNA.
DR EMBL; Y15058; CAA75343.1; -; Genomic_DNA.
DR EMBL; Y15059; CAA75343.1; JOINED; Genomic_DNA.
DR EMBL; X99076; CAA67533.1; -; Genomic_DNA.
DR EMBL; X99075; CAA67533.1; JOINED; Genomic_DNA.
DR EMBL; U89165; AAB49458.1; -; mRNA.
DR EMBL; AJ317956; CAC37631.1; -; Genomic_DNA.
DR EMBL; BT007325; AAP35989.1; -; mRNA.
DR EMBL; BC002835; AAH02835.1; -; mRNA.
DR CCDS; CCDS8451.1; -.
DR RefSeq; NP_001119653.1; NM_001126181.1.
DR RefSeq; NP_006167.1; NM_006176.2.
DR AlphaFoldDB; Q92686; -.
DR BMRB; Q92686; -.
DR SMR; Q92686; -.
DR BioGRID; 110956; 14.
DR IntAct; Q92686; 9.
DR STRING; 9606.ENSP00000284292; -.
DR iPTMnet; Q92686; -.
DR PhosphoSitePlus; Q92686; -.
DR BioMuta; NRGN; -.
DR DMDM; 2498625; -.
DR jPOST; Q92686; -.
DR MassIVE; Q92686; -.
DR MaxQB; Q92686; -.
DR PaxDb; Q92686; -.
DR PeptideAtlas; Q92686; -.
DR PRIDE; Q92686; -.
DR ProteomicsDB; 75408; -.
DR TopDownProteomics; Q92686; -.
DR Antibodypedia; 45991; 190 antibodies from 36 providers.
DR DNASU; 4900; -.
DR Ensembl; ENST00000284292.11; ENSP00000284292.5; ENSG00000154146.13.
DR Ensembl; ENST00000412681.2; ENSP00000399591.1; ENSG00000154146.13.
DR GeneID; 4900; -.
DR KEGG; hsa:4900; -.
DR MANE-Select; ENST00000284292.11; ENSP00000284292.5; NM_006176.3; NP_006167.1.
DR UCSC; uc001qaq.3; human.
DR CTD; 4900; -.
DR DisGeNET; 4900; -.
DR GeneCards; NRGN; -.
DR HGNC; HGNC:8000; NRGN.
DR HPA; ENSG00000154146; Tissue enriched (brain).
DR MIM; 602350; gene.
DR neXtProt; NX_Q92686; -.
DR OpenTargets; ENSG00000154146; -.
DR PharmGKB; PA31779; -.
DR VEuPathDB; HostDB:ENSG00000154146; -.
DR eggNOG; ENOG502S6YP; Eukaryota.
DR GeneTree; ENSGT00440000039324; -.
DR HOGENOM; CLU_129609_1_0_1; -.
DR InParanoid; Q92686; -.
DR OMA; KSKDPEC; -.
DR PhylomeDB; Q92686; -.
DR TreeFam; TF342962; -.
DR PathwayCommons; Q92686; -.
DR Reactome; R-HSA-9620244; Long-term potentiation.
DR SignaLink; Q92686; -.
DR SIGNOR; Q92686; -.
DR BioGRID-ORCS; 4900; 16 hits in 1078 CRISPR screens.
DR ChiTaRS; NRGN; human.
DR GenomeRNAi; 4900; -.
DR Pharos; Q92686; Tbio.
DR PRO; PR:Q92686; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92686; protein.
DR Bgee; ENSG00000154146; Expressed in Brodmann (1909) area 10 and 124 other tissues.
DR ExpressionAtlas; Q92686; baseline and differential.
DR Genevisible; Q92686; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0012510; C:trans-Golgi network transport vesicle membrane; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR GO; GO:0070300; F:phosphatidic acid binding; IEA:Ensembl.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl.
DR GO; GO:0008306; P:associative learning; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Calmodulin-binding; Citrullination; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..78
FT /note="Neurogranin"
FT /id="PRO_0000159591"
FT PEPTIDE 55..78
FT /note="NEUG(55-78)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000377703"
FT DOMAIN 26..47
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 48..78
FT /note="Collagen-like"
FT REGION 39..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 38
FT /note="Crucial for interaction with calmodulin"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 36
FT /note="Phosphoserine; by PHK and PKC"
FT /evidence="ECO:0000250|UniProtKB:P35722"
FT MOD_RES 68
FT /note="Citrulline; partial"
FT /evidence="ECO:0000269|PubMed:23828821"
FT MOD_RES 68
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 78 AA; 7618 MW; 0D6ED790A31D5785 CRC64;
MDCCTENACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE RGRKGPGPGG
PGGAGVARGG AGGGPSGD
