Synaptophysin

<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

• SNARE binding Source: UniProtKB <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
  • Ref.8

    "Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin."
    Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I., Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.
    J. Neurochem. 108:867-880(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH VAMP2.
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • Ref.7

    "Regulation of synaptophysin degradation by mammalian homologues of Seven in Absentia."
    Wheeler T.C., Chin L.-S., Li Y., Roudabush F.L., Li L.
    J. Biol. Chem. 277:10273-10282(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH SIAH1 AND SIAH2, DEGRADATION.
• protein-containing complex binding Source: RGDInferred from physical interactionⁱ
  • "The V0 sector of the V-ATPase, synaptobrevin, and synaptophysin are associated on synaptic vesicles in a Triton X-100-resistant, freeze-thawing sensitive, complex."
    Galli T., McPherson P.S., De Camilli P.
    J. Biol. Chem. 271:2193-2198(1996) [PubMed] [Europe PMC] [Abstract]
• syntaxin-1 binding Source: MGI <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
  • "Complexins: cytosolic proteins that regulate SNAP receptor function."
    McMahon H.T., Missler M., Li C., Suedhof T.C.
    Cell 83:111-119(1995) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• endocytosis Source: UniProtKB <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Interaction of the mu-opioid receptor with synaptophysin influences receptor trafficking and signaling."
    Liang Y.J., Wu D.F., Yang L.Q., Hollt V., Koch T.
    Mol. Pharmacol. 71:123-131(2007) [PubMed] [Europe PMC] [Abstract]
• regulation of neuronal synaptic plasticity Source: RGD <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Increased synaptophysin expression through whisker stimulation in rat."
    Ishibashi H.
    Cell. Mol. Neurobiol. 22:191-195(2002) [PubMed] [Europe PMC] [Abstract]
• regulation of opioid receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • "Interaction of the mu-opioid receptor with synaptophysin influences receptor trafficking and signaling."
    Liang Y.J., Wu D.F., Yang L.Q., Hollt V., Koch T.
    Mol. Pharmacol. 71:123-131(2007) [PubMed] [Europe PMC] [Abstract]
• response to amyloid-beta 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-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "Changed clathrin regulatory proteins in the brains of Alzheimer's disease patients and animal models."
    Cao Y., Xiao Y., Ravid R., Guan Z.Z.
    J. Alzheimers Dis. 22:329-342(2010) [PubMed] [Europe PMC] [Abstract]

<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

Topology

Keywords - Cellular componentⁱ

<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

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

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stageⁱ

<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

<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

• SNARE binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.8

    "Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin."
    Ito H., Atsuzawa K., Morishita R., Usuda N., Sudo K., Iwamoto I., Mizutani K., Katoh-Semba R., Nozawa Y., Asano T., Nagata K.
    J. Neurochem. 108:867-880(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH VAMP2.
• protein domain specific binding Source: RGDInferred from physical interactionⁱ
  • Ref.7

    "Regulation of synaptophysin degradation by mammalian homologues of Seven in Absentia."
    Wheeler T.C., Chin L.-S., Li Y., Roudabush F.L., Li L.
    J. Biol. Chem. 277:10273-10282(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH SIAH1 AND SIAH2, DEGRADATION.
• syntaxin-1 binding Source: MGIInferred from direct assayⁱ
  • "Complexins: cytosolic proteins that regulate SNAP receptor function."
    McMahon H.T., Missler M., Li C., Suedhof T.C.
    Cell 83:111-119(1995) [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

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<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

Keywords - Domainⁱ

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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MDVVNQLVAG GQFRVVKEPL GFVKVLQWVF AIFAFATCGS YTGELRLSVE 
        60         70         80         90        100
CANKTESALN IEVEFEYPFR LHQVYFDAPS CVKGGTTKIF LVGDYSSSAE 
       110        120        130        140        150
FFVTVAVFAF LYSMGALATY IFLQNKYREN NKGPMMDFLA TAVFAFMWLV 
       160        170        180        190        200
SSSAWAKGLS DVKMATDPEN IIKEMPMCRQ TGNTCKELRD PVTSGLNTSV 
       210        220        230        240        250
VFGFLNLVLW VGNLWFVFKE TGWAAPFMRA PPGAPEKQPA PGDAYGDAGY 
       260        270        280        290        300
GQGPGGYGPQ DSYGPQGGYQ PDYGQPASGG GGYGPQGDYG QQGYGQQGAP 

TSFSNQM                                                

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

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous 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. SIMILARITY comments
   Index of protein domains and families