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Protein

Neurogranin

Gene

NRGN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a "third messenger" substrate of protein kinase C-mediated molecular cascades during synaptic development and remodeling. Binds to calmodulin in the absence of calcium (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei38 – 381Crucial for interaction with calmodulinBy similarity

GO - Molecular functioni

  1. calmodulin binding Source: ProtInc

GO - Biological processi

  1. intracellular signal transduction Source: GO_Central
  2. nervous system development Source: ProtInc
  3. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

SignaLinkiQ92686.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogranin
Short name:
Ng
Alternative name(s):
RC3
Cleaved into the following chain:
Gene namesi
Name:NRGN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:8000. NRGN.

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti3140. Schizophrenia.
PharmGKBiPA31779.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878NeurograninPRO_0000159591Add
BLAST
Peptidei55 – 7824NEUG(55-78)By similarityPRO_0000377703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei36 – 361Phosphoserine; by PHK and PKCBy similarity
Modified residuei68 – 681Citrulline; partial1 Publication

Post-translational modificationi

Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiQ92686.
PaxDbiQ92686.
PeptideAtlasiQ92686.
PRIDEiQ92686.

PTM databases

PhosphoSiteiQ92686.

Expressioni

Tissue specificityi

In the cerebral cortex, found in the cell bodies of neurons in layers II-VI, and in apical and basal dendrites of pyramidal neurons. Is not found in the dendrites in patients with Alzheimer disease.1 Publication

Gene expression databases

BgeeiQ92686.
CleanExiHS_NRGN.
ExpressionAtlasiQ92686. baseline and differential.
GenevestigatoriQ92686.

Organism-specific databases

HPAiCAB006908.
HPA038171.

Interactioni

Protein-protein interaction databases

BioGridi110956. 9 interactions.
IntActiQ92686. 1 interaction.
STRINGi9606.ENSP00000284292.

Structurei

3D structure databases

ProteinModelPortaliQ92686.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 4722IQPROSITE-ProRule annotationAdd
BLAST
Domaini48 – 7831Collagen-likeAdd
BLAST

Domaini

Neurogranin is intrinsically unstructured; however, upon binding with CaM, The IQ domain adopts a helical conformation.By similarity

Sequence similaritiesi

Belongs to the neurogranin family.Curated
Contains 1 collagen-like domain.Curated
Contains 1 IQ domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG41420.
GeneTreeiENSGT00780000122272.
HOVERGENiHBG000470.
InParanoidiQ92686.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiQ92686.
TreeFamiTF342962.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
[Graphical view]
SMARTiSM00015. IQ. 1 hit.
[Graphical view]
PROSITEiPS50096. IQ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92686-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDCCTENACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE
60 70
RGRKGPGPGG PGGAGVARGG AGGGPSGD
Length:78
Mass (Da):7,618
Last modified:February 1, 1997 - v1
Checksum:i0D6ED790A31D5785
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09689 mRNA. Translation: CAA70867.1.
Y15058, Y15059 Genomic DNA. Translation: CAA75343.1.
X99076, X99075 Genomic DNA. Translation: CAA67533.1.
U89165 mRNA. Translation: AAB49458.1.
AJ317956 Genomic DNA. Translation: CAC37631.1.
BT007325 mRNA. Translation: AAP35989.1.
BC002835 mRNA. Translation: AAH02835.1.
CCDSiCCDS8451.1.
RefSeqiNP_001119653.1. NM_001126181.1.
NP_006167.1. NM_006176.2.
UniGeneiHs.524116.

Genome annotation databases

EnsembliENST00000284292; ENSP00000284292; ENSG00000154146.
ENST00000412681; ENSP00000399591; ENSG00000154146.
GeneIDi4900.
KEGGihsa:4900.
UCSCiuc001qaq.2. human.

Polymorphism databases

DMDMi2498625.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09689 mRNA. Translation: CAA70867.1.
Y15058, Y15059 Genomic DNA. Translation: CAA75343.1.
X99076, X99075 Genomic DNA. Translation: CAA67533.1.
U89165 mRNA. Translation: AAB49458.1.
AJ317956 Genomic DNA. Translation: CAC37631.1.
BT007325 mRNA. Translation: AAP35989.1.
BC002835 mRNA. Translation: AAH02835.1.
CCDSiCCDS8451.1.
RefSeqiNP_001119653.1. NM_001126181.1.
NP_006167.1. NM_006176.2.
UniGeneiHs.524116.

3D structure databases

ProteinModelPortaliQ92686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110956. 9 interactions.
IntActiQ92686. 1 interaction.
STRINGi9606.ENSP00000284292.

PTM databases

PhosphoSiteiQ92686.

Polymorphism databases

DMDMi2498625.

Proteomic databases

MaxQBiQ92686.
PaxDbiQ92686.
PeptideAtlasiQ92686.
PRIDEiQ92686.

Protocols and materials databases

DNASUi4900.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000284292; ENSP00000284292; ENSG00000154146.
ENST00000412681; ENSP00000399591; ENSG00000154146.
GeneIDi4900.
KEGGihsa:4900.
UCSCiuc001qaq.2. human.

Organism-specific databases

CTDi4900.
GeneCardsiGC11P124609.
HGNCiHGNC:8000. NRGN.
HPAiCAB006908.
HPA038171.
MIMi602350. gene.
neXtProtiNX_Q92686.
Orphaneti3140. Schizophrenia.
PharmGKBiPA31779.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41420.
GeneTreeiENSGT00780000122272.
HOVERGENiHBG000470.
InParanoidiQ92686.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiQ92686.
TreeFamiTF342962.

Enzyme and pathway databases

SignaLinkiQ92686.

Miscellaneous databases

ChiTaRSiNRGN. human.
GenomeRNAii4900.
NextBioi18859.
PROiQ92686.
SOURCEiSearch...

Gene expression databases

BgeeiQ92686.
CleanExiHS_NRGN.
ExpressionAtlasiQ92686. baseline and differential.
GenevestigatoriQ92686.

Family and domain databases

InterProiIPR000048. IQ_motif_EF-hand-BS.
[Graphical view]
PfamiPF00612. IQ. 1 hit.
[Graphical view]
SMARTiSM00015. IQ. 1 hit.
[Graphical view]
PROSITEiPS50096. IQ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning cDNA for human neurogranin."
    Mertsalov I.B., Gundelfinger E.D., Tsetlin V.I.
    Bioorg. Khim. 22:366-369(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Structure and chromosomal localization of human neurogranin gene."
    Mertsalov I.B., Stumm M., Wieacker P., tom Dieck S., Gundelfinger E.D., Tsetlin V.I.
    Bioorg. Khim. 23:961-968(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Structure, organization, and chromosomal mapping of the human neurogranin gene (NRGN)."
    Martinez de Arrieta C., Perez Jurado L., Bernal J., Coloma A.
    Genomics 41:243-249(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Dendritic translocation of RC3/neurogranin mRNA in normal aging, Alzheimer disease and fronto-temporal dementia."
    Chang J.W., Schumacher E., Coulter P.M. II, Vinters H.V., Watson J.B.
    J. Neuropathol. Exp. Neurol. 56:1105-1118(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain cortex.
  5. Mertsalov I.B., Tsetlin V.I.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Identification and Characterization of citrulline-modified brain proteins by combining HCD and CID fragmentation."
    Jin Z., Fu Z., Yang J., Troncosco J., Everett A.D., Van Eyk J.E.
    Proteomics 13:2682-2691(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: CITRULLINATION AT ARG-68.

Entry informationi

Entry nameiNEUG_HUMAN
AccessioniPrimary (citable) accession number: Q92686
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 4, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.