Staufen double-stranded RNA-binding protein 1

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• double-stranded RNA binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.1

    "Two rat brain staufen isoforms differentially bind RNA."
    Monshausen M., Putz U., Rehbein M., Schweizer M., DesGroseillers L., Kuhl D., Richter D., Kindler S.
    J. Neurochem. 76:155-165(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE.
• protein phosphatase 1 binding Source: RGD <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "The RNA-binding protein Staufen from rat brain interacts with protein phosphatase-1."
    Monshausen M., Rehbein M., Richter D., Kindler S.
    J Neurochem 81:557-564(2002) [PubMed] [Europe PMC] [Abstract]
• RNA binding Source: RGD

GO - Biological processⁱ

• cellular response to oxidative stress Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes."
    Thomas M.G., Martinez Tosar L.J., Loschi M., Pasquini J.M., Correale J., Kindler S., Boccaccio G.L.
    Mol. Biol. Cell 16:405-420(2005) [PubMed] [Europe PMC] [Abstract]
• dendritic transport of messenger ribonucleoprotein complex Source: RGD
• intracellular mRNA localization Source: RGD
• modification of postsynaptic structure Source: SynGOInferred from direct assayⁱ
  • "mRNA binding protein staufen 1-dependent regulation of pyramidal cell spine morphology via NMDA receptor-mediated synaptic plasticity."
    Lebeau G., DesGroseillers L., Sossin W., Lacaille J.C.
    Mol Brain 4:22-22(2011) [PubMed] [Europe PMC] [Abstract]
• modulation of chemical synaptic transmission Source: SynGOInferred from direct assayⁱ
  • "mRNA binding protein staufen 1-dependent regulation of pyramidal cell spine morphology via NMDA receptor-mediated synaptic plasticity."
    Lebeau G., DesGroseillers L., Sossin W., Lacaille J.C.
    Mol Brain 4:22-22(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation by virus of viral protein levels in host cell Source: RGD
• positive regulation of long-term synaptic potentiation Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Staufen 2 regulates mGluR long-term depression and Map1b mRNA distribution in hippocampal neurons."
    Lebeau G., Miller L.C., Tartas M., McAdam R., Laplante I., Badeaux F., DesGroseillers L., Sossin W.S., Lacaille J.C.
    Learn Mem 18:314-326(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of viral genome replication Source: RGD

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

GO - Molecular functionⁱ

• protein phosphatase 1 binding Source: RGDInferred from physical interactionⁱ
  • "The RNA-binding protein Staufen from rat brain interacts with protein phosphatase-1."
    Monshausen M., Rehbein M., Richter D., Kindler S.
    J Neurochem 81:557-564(2002) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

Compositional bias

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MYKPVDPHSR MQSTYSYGMR GGAYPPRYFY PFPVPPLLYQ VELSVGGQQF 
        60         70         80         90        100
NGKGKMRPPV KHDATARALR TLQSEPLPER LEVNGRESEE ENLNKSEISQ 
       110        120        130        140        150
VFEIALKRNL PVNFESFPLT QVARESGPPH MKNFVTRVSV GEFVGEGEGK 
       160        170        180        190        200
SKKISKKNAA RAVLEQLRRL PPLPAVERVK PRIKKKSQPT CKLQTAPDYG 
       210        220        230        240        250
QGMNPISRLA QIQQAKKEKE PEYMLLTERG LPRRREFVMQ VKVGHHTAEG 
       260        270        280        290        300
AGTNKKVAKR NAAENMLEIL GFKVPQAQPA KPALKSEEKT PVKKPGDGRK 
       310        320        330        340        350
VTFFEPSPGD ENGTSNKEDE FRMPYLSHQQ LPAGILPMVP EVAQAVGVSQ 
       360        370        380        390        400
GHHTKDFARA APNPAKATVT AMIARELLYG GTSPTAETIL KSNISSGHVP 
       410        420        430        440        450
HGPRTRPSEQ LYYLSRAQGF QVEYKDFPKN NKNECVSLIN CSSQPPLVSH 
       460        470        480        490 
GIGKDVESCH DMAALNILKL LSELDQQSTE MPRTGNGPVS ACGRC      

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ