14-3-3 protein eta

<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

• actin binding Source: Ensembl
• enzyme binding Source: BHF-UCL <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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Protein kinase A phosphorylation of human phosphodiesterase 3B promotes 14-3-3 protein binding and inhibits phosphatase-catalyzed inactivation."
    Palmer D., Jimmo S.L., Raymond D.R., Wilson L.S., Carter R.L., Maurice D.H.
    J. Biol. Chem. 282:9411-9419(2007) [PubMed] [Europe PMC] [Abstract]
• glucocorticoid receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein."
    Wakui H., Wright A.P., Gustafsson J., Zilliacus J.
    J. Biol. Chem. 272:8153-8156(1997) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.24

    "Structural basis for protein-protein interactions in the 14-3-3 protein family."
    Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
  • "A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes."
    Gloeckner C.J., Boldt K., Schumacher A., Roepman R., Ueffing M.
    Proteomics 7:4228-4234(2007) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor receptor binding Source: UniProtKB
• ion channel binding Source: BHF-UCLInferred from physical interactionⁱ
  • "14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity."
    Kagan A., Melman Y.F., Krumerman A., McDonald T.V.
    EMBO J. 21:1889-1898(2002) [PubMed] [Europe PMC] [Abstract]
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: UniProtKB
• protein heterodimerization activity Source: BHF-UCLInferred from physical interactionⁱ
  • "14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity."
    Kagan A., Melman Y.F., Krumerman A., McDonald T.V.
    EMBO J. 21:1889-1898(2002) [PubMed] [Europe PMC] [Abstract]
• sodium channel regulator activity Source: BHF-UCL <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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• glucocorticoid catabolic process Source: UniProtKBInferred from direct assayⁱ
  • "Role of 14-3-3 eta as a positive regulator of the glucocorticoid receptor transcriptional activation."
    Kim Y.S., Jang S.W., Sung H.J., Lee H.J., Kim I.S., Na D.S., Ko J.
    Endocrinology 146:3133-3140(2005) [PubMed] [Europe PMC] [Abstract]
• glucocorticoid receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • "Role of 14-3-3 eta as a positive regulator of the glucocorticoid receptor transcriptional activation."
    Kim Y.S., Jang S.W., Sung H.J., Lee H.J., Kim I.S., Na D.S., Ko J.
    Endocrinology 146:3133-3140(2005) [PubMed] [Europe PMC] [Abstract]
• intracellular protein transport Source: UniProtKB
• membrane depolarization during action potential Source: BHF-UCLInferred from direct assayⁱ
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]
• membrane organization Source: Reactome
• negative regulation of dendrite morphogenesis Source: UniProtKB
• positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
• positive regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • "Role of 14-3-3 eta as a positive regulator of the glucocorticoid receptor transcriptional activation."
    Kim Y.S., Jang S.W., Sung H.J., Lee H.J., Kim I.S., Na D.S., Ko J.
    Endocrinology 146:3133-3140(2005) [PubMed] [Europe PMC] [Abstract]
• regulation of neuron differentiation Source: UniProtKB
• regulation of sodium ion transmembrane transporter activity Source: BHF-UCLInferred from direct assayⁱ
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of sodium ion transport Source: BHF-UCLInferred from direct assayⁱ
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of synaptic plasticity Source: UniProtKB
• substantia nigra development Source: UniProtKBInferred from high throughput expression patternⁱ
  • "Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis."
    Chen S., Lu F.F., Seeman P., Liu F.
    Neurochem. Res. 37:2805-2813(2012) [PubMed] [Europe PMC] [Abstract]

Enzyme and pathway databases

<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 disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<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>Keywords - PTMⁱ

Proteomic databases

PTM databases

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific 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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Sites

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• actin binding Source: Ensembl
• enzyme binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Protein kinase A phosphorylation of human phosphodiesterase 3B promotes 14-3-3 protein binding and inhibits phosphatase-catalyzed inactivation."
    Palmer D., Jimmo S.L., Raymond D.R., Wilson L.S., Carter R.L., Maurice D.H.
    J. Biol. Chem. 282:9411-9419(2007) [PubMed] [Europe PMC] [Abstract]
• glucocorticoid receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Interaction of the ligand-activated glucocorticoid receptor with the 14-3-3 eta protein."
    Wakui H., Wright A.P., Gustafsson J., Zilliacus J.
    J. Biol. Chem. 272:8153-8156(1997) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.24

    "Structural basis for protein-protein interactions in the 14-3-3 protein family."
    Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS), IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, SUBUNIT.
  • "A novel tandem affinity purification strategy for the efficient isolation and characterisation of native protein complexes."
    Gloeckner C.J., Boldt K., Schumacher A., Roepman R., Ueffing M.
    Proteomics 7:4228-4234(2007) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor receptor binding Source: UniProtKB
• ion channel binding Source: BHF-UCLInferred from physical interactionⁱ
  • "14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity."
    Kagan A., Melman Y.F., Krumerman A., McDonald T.V.
    EMBO J. 21:1889-1898(2002) [PubMed] [Europe PMC] [Abstract]
  • "14-3-3 is a regulator of the cardiac voltage-gated sodium channel Nav1.5."
    Allouis M., Le Bouffant F., Wilders R., Peroz D., Schott J.J., Noireaud J., Le Marec H., Merot J., Escande D., Baro I.
    Circ. Res. 98:1538-1546(2006) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: UniProtKB
• protein heterodimerization activity Source: BHF-UCLInferred from physical interactionⁱ
  • "14-3-3 amplifies and prolongs adrenergic stimulation of HERG K+ channel activity."
    Kagan A., Melman Y.F., Krumerman A., McDonald T.V.
    EMBO J. 21:1889-1898(2002) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous 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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

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_length">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>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK 
        60         70         80         90        100
NVVGARRSSW RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV 
       110        120        130        140        150
LSLLDKFLIK NCNDFQYESK VFYLKMKGDY YRYLAEVASG EKKNSVVEAS 
       160        170        180        190        200
EAAYKEAFEI SKEQMQPTHP IRLGLALNFS VFYYEIQNAP EQACLLAKQA 
       210        220        230        240 
FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE EAGEGN     

Experimental Info

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

• 100% Identity
• 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

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous 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

Documents

1. Human chromosome 22
   Human chromosome 22: entries, gene names and cross-references to MIM
2. SIMILARITY comments
   Index of protein domains and families
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references