Annexin A7

<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

• calcium-dependent phospholipid binding Source: MGI
• calcium-dependent protein binding Source: MGI
• calcium ion binding Source: InterPro
• identical protein binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: MGI

GO - Biological processⁱ

• autophagy Source: MGI
• cell population proliferation Source: MGI <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
  • "The lack of annexin A7 affects functions of primary astrocytes."
    Clemen C.S., Herr C., Hovelmeyer N., Noegel A.A.
    Exp. Cell Res. 291:406-414(2003) [PubMed] [Europe PMC] [Abstract]
• cellular calcium ion homeostasis Source: MGIInferred from mutant phenotypeⁱ
  • "The lack of annexin A7 affects functions of primary astrocytes."
    Clemen C.S., Herr C., Hovelmeyer N., Noegel A.A.
    Exp. Cell Res. 291:406-414(2003) [PubMed] [Europe PMC] [Abstract]
• cellular water homeostasis Source: MGIInferred from mutant phenotypeⁱ
  • "Function, expression and localization of annexin A7 in platelets and red blood cells: insights derived from an annexin A7 mutant mouse."
    Herr C., Clemen C.S., Lehnert G., Kutschkow R., Picker S.M., Gathof B.S., Zamparelli C., Schleicher M., Noegel A.A.
    BMC Biochem. 4:8-8(2003) [PubMed] [Europe PMC] [Abstract]
• epithelial cell differentiation Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• hemostasis Source: MGIInferred from mutant phenotypeⁱ
  • "Function, expression and localization of annexin A7 in platelets and red blood cells: insights derived from an annexin A7 mutant mouse."
    Herr C., Clemen C.S., Lehnert G., Kutschkow R., Picker S.M., Gathof B.S., Zamparelli C., Schleicher M., Noegel A.A.
    BMC Biochem. 4:8-8(2003) [PubMed] [Europe PMC] [Abstract]
• membrane fusion Source: MGI
• negative regulation of gene expression Source: MGI
• regulation of cell shape Source: MGIInferred from mutant phenotypeⁱ
  • "Function, expression and localization of annexin A7 in platelets and red blood cells: insights derived from an annexin A7 mutant mouse."
    Herr C., Clemen C.S., Lehnert G., Kutschkow R., Picker S.M., Gathof B.S., Zamparelli C., Schleicher M., Noegel A.A.
    BMC Biochem. 4:8-8(2003) [PubMed] [Europe PMC] [Abstract]
• response to calcium ion Source: MGI
• response to organic cyclic compound Source: MGI
• response to salt stress Source: MGIInferred from mutant phenotypeⁱ
  • "Function, expression and localization of annexin A7 in platelets and red blood cells: insights derived from an annexin A7 mutant mouse."
    Herr C., Clemen C.S., Lehnert G., Kutschkow R., Picker S.M., Gathof B.S., Zamparelli C., Schleicher M., Noegel A.A.
    BMC Biochem. 4:8-8(2003) [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

<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

Keywords - PTMⁱ

Proteomic databases

2D gel 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

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

<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

• calcium-dependent protein binding Source: MGI
• identical protein binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: MGI

Protein-protein interaction 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

3D structure 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 3 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSYPGYPPTG YPPFPGYPPA GQESSFPTAG QYPYPSGFPP MGGGAYPPAP 
        60         70         80         90        100
SGGYPGAGGY PAPGGYPAPG GYPGALSPGG PPAYPGGQGF GAPPGGAGFS 
       110        120        130        140        150
GYPQPPAQSY GGGPAQVPVP GGFPGGQMPS QYPGGQAPYP SQPASMTQGT 
       160        170        180        190        200
QGTILPASNF DAMRDAEILR KAMKGFGTDE QAIVDVVSNR SNDQRQQIKA 
       210        220        230        240        250
AFKTMYGKDL IKDLKSELSG NMEELILALF MPSTYYDAWS LRKAMQGAGT 
       260        270        280        290        300
QERVLIEILC TRTNQEIRDI VRCYQLEFGR DLEKDIRSDT SGHFERLLVS 
       310        320        330        340        350
MCQGNRDERQ SVNHQMAQED AQRLYQAGEG RLGTDESCFN MILATRSFPQ 
       360        370        380        390        400
LKATMEAYSR MANRDLLSSV SREFSGYVES GLKTILQCAL NRPAFFAERL 
       410        420        430        440        450
YYSMKGAGTD DSTLVRIVVT RSEIDLVQIK QMFTQMYQKT LSTMIASDTS 
       460 
GDYRKLLLAI VGQ                                         

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

• 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

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic 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. SIMILARITY comments
   Index of protein domains and families
2. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot