Anterior gradient protein 2 homolog

<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

• dystroglycan binding Source: UniProtKB <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
  • Ref.9

    "hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan."
    Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.
    Br. J. Cancer 88:579-585(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH LYPD3 AND DAG1.
• epidermal growth factor receptor 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
  • "Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface."
    Dong A., Wodziak D., Lowe A.W.
    J Biol Chem 290:8016-8027(2015) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from physical interactionⁱ
  • "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78."
    Ryu J., Park S.G., Lee P.Y., Cho S., Lee D.H., Kim G.H., Kim J.H., Park B.C.
    Biochem Biophys Res Commun 430:610-615(2013) [PubMed] [Europe PMC] [Abstract]
  • Ref.13

    "Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion."
    Patel P., Clarke C., Barraclough D.L., Jowitt T.A., Rudland P.S., Barraclough R., Lian L.Y.
    J. Mol. Biol. 425:929-943(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 41-175, FUNCTION, SUBUNIT, HOMODIMERIZATION, MUTAGENESIS OF GLU-60; TYR-63 AND LYS-64, CELL ADHESION REGION.

GO - Biological processⁱ

• digestive tract morphogenesis Source: UniProtKB
• lung goblet cell differentiation Source: Ensembl
• mucus secretion Source: UniProtKB
• negative regulation of cell death 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
  • "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78."
    Ryu J., Park S.G., Lee P.Y., Cho S., Lee D.H., Kim G.H., Kim J.H., Park B.C.
    Biochem Biophys Res Commun 430:610-615(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell-substrate adhesion Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.13

    "Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion."
    Patel P., Clarke C., Barraclough D.L., Jowitt T.A., Rudland P.S., Barraclough R., Lian L.Y.
    J. Mol. Biol. 425:929-943(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 41-175, FUNCTION, SUBUNIT, HOMODIMERIZATION, MUTAGENESIS OF GLU-60; TYR-63 AND LYS-64, CELL ADHESION REGION.
• positive regulation of developmental growth Source: UniProtKB
• positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface."
    Dong A., Wodziak D., Lowe A.W.
    J Biol Chem 290:8016-8027(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: UniProtKBInferred from mutant phenotypeⁱ
  • "AGR2 gene function requires a unique endoplasmic reticulum localization motif."
    Gupta A., Dong A., Lowe A.W.
    J Biol Chem 287:4773-4782(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of IRE1-mediated unfolded protein response Source: UniProtKBInferred from direct assayⁱ
  • "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78."
    Ryu J., Park S.G., Lee P.Y., Cho S., Lee D.H., Kim G.H., Kim J.H., Park B.C.
    Biochem Biophys Res Commun 430:610-615(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of PERK-mediated unfolded protein response Source: UniProtKBInferred from direct assayⁱ
  • "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78."
    Ryu J., Park S.G., Lee P.Y., Cho S., Lee D.H., Kim G.H., Kim J.H., Park B.C.
    Biochem Biophys Res Commun 430:610-615(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein localization to plasma membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface."
    Dong A., Wodziak D., Lowe A.W.
    J Biol Chem 290:8016-8027(2015) [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

• UniProt annotation
• GO - Cellular component

<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 - Cellular componentⁱ

<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

Mutagenesis

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation 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

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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• dystroglycan binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan."
    Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.
    Br. J. Cancer 88:579-585(2003) [PubMed] [Europe PMC] [Abstract]

    Cited for: INTERACTION WITH LYPD3 AND DAG1.
• epidermal growth factor receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • "Epidermal growth factor receptor (EGFR) signaling requires a specific endoplasmic reticulum thioredoxin for the post-translational control of receptor presentation to the cell surface."
    Dong A., Wodziak D., Lowe A.W.
    J Biol Chem 290:8016-8027(2015) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from physical interactionⁱ
  • "Dimerization of pro-oncogenic protein Anterior Gradient 2 is required for the interaction with BiP/GRP78."
    Ryu J., Park S.G., Lee P.Y., Cho S., Lee D.H., Kim G.H., Kim J.H., Park B.C.
    Biochem Biophys Res Commun 430:610-615(2013) [PubMed] [Europe PMC] [Abstract]
  • Ref.13

    "Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion."
    Patel P., Clarke C., Barraclough D.L., Jowitt T.A., Rudland P.S., Barraclough R., Lian L.Y.
    J. Mol. Biol. 425:929-943(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: STRUCTURE BY NMR OF 41-175, FUNCTION, SUBUNIT, HOMODIMERIZATION, MUTAGENESIS OF GLU-60; TYR-63 AND LYS-64, CELL ADHESION REGION.

Protein-protein interaction databases

Miscellaneous 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

<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

Region

Motif

<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%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>Sequence (1+)ⁱ

<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.

<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 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
MEKIPVSAFL LLVALSYTLA RDTTVKPGAK KDTKDSRPKL PQTLSRGWGD 
        60         70         80         90        100
QLIWTQTYEE ALYKSKTSNK PLMIIHHLDE CPHSQALKKV FAENKEIQKL 
       110        120        130        140        150
AEQFVLLNLV YETTDKHLSP DGQYVPRIMF VDPSLTVRAD ITGRYSNRLY 
       160        170 
AYEPADTALL LDNMKKALKL LKTEL                            

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

PTM databases

Genetic variation 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 7
   Human chromosome 7: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families