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Protein

Neurogranin

Gene

Nrgn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the affinity of calmodulin for calcium. Involved in synaptic plasticity and spatial learning.1 Publication

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogranin
Short name:
Ng
Alternative name(s):
RC3
Cleaved into the following chain:
Gene namesi
Name:Nrgn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1927184. Nrgn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Synapse

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381R → A: Abolishes calmodulin binding, unable to potentiate synaptic transmission. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7878NeurograninPRO_0000159592Add
BLAST
Peptidei55 – 7824NEUG(55-78)By similarityPRO_0000377702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Disulfide bondi3 ↔ 51Or C-51 with C-4 or C-9
Modified residuei36 – 361Phosphoserine; by PHK and PKC1 Publication
Modified residuei68 – 681Citrulline; partialBy similarity

Post-translational modificationi

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).By similarity
Phosphorylated at Ser-36 by PHK and PKC, phosphorylation prevents interaction with Calmodulin and interrupts several learning- and memory-associated functions.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP60761.
PaxDbiP60761.
PRIDEiP60761.

PTM databases

iPTMnetiP60761.
PhosphoSiteiP60761.

Expressioni

Gene expression databases

BgeeiP60761.
CleanExiMM_NRGN.
GenevisibleiP60761. MM.

Interactioni

Subunit structurei

Interacts with apo-calmodulin; this interaction decreases the affinity of calmodulin for calcium ions.1 Publication

GO - Molecular functioni

  • calmodulin binding Source: MGI

Protein-protein interaction databases

BioGridi211017. 1 interaction.
IntActiP60761. 2 interactions.
STRINGi10090.ENSMUSP00000070113.

Structurei

Secondary structure

1
78
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 4518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E50X-ray2.70A25-50[»]
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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG410JNUP. Eukaryota.
ENOG41118RJ. LUCA.
GeneTreeiENSGT00440000039324.
HOGENOMiHOG000113769.
HOVERGENiHBG000470.
InParanoidiP60761.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiP60761.
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.

P60761-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE
60 70
CGRKGPGPGG PGGAGGARGG AGGGPSGD
Length:78
Mass (Da):7,496
Last modified:April 13, 2004 - v1
Checksum:i8E47CDB38E095794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230869 Genomic DNA. Translation: AAG27519.1.
AK002933 mRNA. Translation: BAB22466.1.
AK158630 mRNA. Translation: BAE34589.1.
BC061102 mRNA. Translation: AAH61102.1.
BC138511 mRNA. Translation: AAI38512.1.
BC138513 mRNA. Translation: AAI38514.1.
CCDSiCCDS40585.1.
RefSeqiNP_071312.1. NM_022029.2.
UniGeneiMm.335065.

Genome annotation databases

EnsembliENSMUST00000065668; ENSMUSP00000070113; ENSMUSG00000053310.
GeneIDi64011.
KEGGimmu:64011.
UCSCiuc009ovc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230869 Genomic DNA. Translation: AAG27519.1.
AK002933 mRNA. Translation: BAB22466.1.
AK158630 mRNA. Translation: BAE34589.1.
BC061102 mRNA. Translation: AAH61102.1.
BC138511 mRNA. Translation: AAI38512.1.
BC138513 mRNA. Translation: AAI38514.1.
CCDSiCCDS40585.1.
RefSeqiNP_071312.1. NM_022029.2.
UniGeneiMm.335065.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4E50X-ray2.70A25-50[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211017. 1 interaction.
IntActiP60761. 2 interactions.
STRINGi10090.ENSMUSP00000070113.

PTM databases

iPTMnetiP60761.
PhosphoSiteiP60761.

Proteomic databases

MaxQBiP60761.
PaxDbiP60761.
PRIDEiP60761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065668; ENSMUSP00000070113; ENSMUSG00000053310.
GeneIDi64011.
KEGGimmu:64011.
UCSCiuc009ovc.1. mouse.

Organism-specific databases

CTDi4900.
MGIiMGI:1927184. Nrgn.

Phylogenomic databases

eggNOGiENOG410JNUP. Eukaryota.
ENOG41118RJ. LUCA.
GeneTreeiENSGT00440000039324.
HOGENOMiHOG000113769.
HOVERGENiHBG000470.
InParanoidiP60761.
OMAiPQESACS.
OrthoDBiEOG7BCNFV.
PhylomeDBiP60761.
TreeFamiTF342962.

Miscellaneous databases

ChiTaRSiNrgn. mouse.
NextBioi319863.
PROiP60761.
SOURCEiSearch...

Gene expression databases

BgeeiP60761.
CleanExiMM_NRGN.
GenevisibleiP60761. MM.

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. "Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice."
    Pak J.H., Huang F.L., Li J., Balschun D., Reymann K.G., Chiang C., Westphal H., Huang K.P.
    Proc. Natl. Acad. Sci. U.S.A. 97:11232-11237(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: 129/SvJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Visual cortex.
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with Calmodulin."
    Kumar V., Chichili V.P., Zhong L., Tang X., Velazquez-Campoy A., Sheu F.S., Seetharaman J., Gerges N.Z., Sivaraman J.
    Sci. Rep. 3:1392-1392(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 27-50 IN COMPLEX WITH CALMODULIN, SUBUNIT, IQ DOMAIN, PHOSPHORYLATION AT SER-36, MUTAGENESIS OF ARG-38.

Entry informationi

Entry nameiNEUG_MOUSE
AccessioniPrimary (citable) accession number: P60761
Secondary accession number(s): B2RRN7, Q3TYH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: January 20, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.