Islet amyloid polypeptide

<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

Miscellaneous

<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

• amyloid-beta binding Source: ARUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• hormone activity Source: UniProtKB-KW
• identical protein 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: ProtIncTraceable author statementⁱ
  • "An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3."
    Muff R., Buhlmann N., Fischer J.A., Born W.
    Endocrinology 140:2924-2927(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.2

    "Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history."
    Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.
    Mol. Endocrinol. 3:1775-1781(1989) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

GO - Biological processⁱ

• adenylate cyclase-activating G protein-coupled receptor signaling pathway Source: ARUK-UCL <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• amylin receptor signaling pathway Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• amyloid fibril formation Source: UniProtKBInferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• apoptotic process Source: ProtIncTraceable author statementⁱ
  • "Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus."
    Lorenzo A., Razzaboni B., Weir G.C., Yankner B.A.
    Nature 368:756-760(1994) [PubMed] [Europe PMC] [Abstract]
• cell-cell signaling Source: ProtIncTraceable author statementⁱ
  • Ref.2

    "Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history."
    Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.
    Mol. Endocrinol. 3:1775-1781(1989) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
• cellular protein metabolic process Source: Reactome
• eating behavior Source: Ensembl
• G protein-coupled receptor signaling pathway Source: Reactome
• negative regulation of amyloid fibril formation Source: ARUK-UCLTraceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of bone resorption Source: Ensembl
• negative regulation of cell differentiation Source: Ensembl
• negative regulation of cell population proliferation Source: UniProtKBInferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of mitochondrion organization Source: ARUK-UCLTraceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein-containing complex assembly Source: ARUK-UCLTraceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of apoptotic process Source: ARUK-UCLTraceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of calcium ion import across plasma membrane Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cell death Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of cytosolic calcium ion concentration Source: ARUK-UCL <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%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ERK1 and ERK2 cascade Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of gene expression Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of MAPK cascade Source: ARUK-UCLNon-traceable author statementⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of peptidyl-serine phosphorylation Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein kinase A signaling Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein kinase B signaling Source: ARUK-UCLInferred from genetic interactionⁱ
  • "Amyloid beta (Abeta) peptide directly activates amylin-3 receptor subtype by triggering multiple intracellular signaling pathways."
    Fu W., Ruangkittisakul A., MacTavish D., Shi J.Y., Ballanyi K., Jhamandas J.H.
    J. Biol. Chem. 287:18820-18830(2012) [PubMed] [Europe PMC] [Abstract]
• protein destabilization Source: UniProtKBInferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• protein homooligomerization Source: UniProtKBInferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• sensory perception of pain Source: Ensembl
• signal transduction Source: ProtIncTraceable author statementⁱ
  • "An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3."
    Muff R., Buhlmann N., Fischer J.A., Born W.
    Endocrinology 140:2924-2927(1999) [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

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

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

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%5Fprocessing%5Fsection">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

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%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="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

• hormone activity Source: UniProtKB-KW
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • "Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides."
    Wang L., Liu Q., Chen J.C., Cui Y.X., Zhou B., Chen Y.X., Zhao Y.F., Li Y.M.
    Biol. Chem. 393:641-646(2012) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: ProtIncTraceable author statementⁱ
  • "An amylin receptor is revealed following co-transfection of a calcitonin receptor with receptor activity modifying proteins-1 or -3."
    Muff R., Buhlmann N., Fischer J.A., Born W.
    Endocrinology 140:2924-2927(1999) [PubMed] [Europe PMC] [Abstract]
  • Ref.2

    "Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history."
    Nishi M., Sanke T., Seino S., Eddy R.L., Fan Y.-S., Byers M.G., Shows T.B., Bell G.I., Steiner D.F.
    Mol. Endocrinol. 3:1775-1781(1989) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

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

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 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%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
MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV 
        60         70         80 
HSSNNFGAIL SSTNVGSNTY GKRNAVEVLK REPLNYLPL             

Experimental Info

<p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryⁱ

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. Human chromosome 12
   Human chromosome 12: entries, gene names and cross-references to MIM