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P10997

- IAPP_HUMAN

UniProt

P10997 - IAPP_HUMAN

Protein

Islet amyloid polypeptide

Gene

IAPP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. receptor binding Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cell-cell signaling Source: ProtInc
    3. eating behavior Source: Ensembl
    4. endocrine pancreas development Source: Reactome
    5. negative regulation of bone resorption Source: Ensembl
    6. negative regulation of cell differentiation Source: Ensembl
    7. sensory perception of pain Source: Ensembl
    8. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Hormone

    Enzyme and pathway databases

    ReactomeiREACT_13819. Regulation of gene expression in beta cells.
    REACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.
    REACT_75925. Amyloids.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Islet amyloid polypeptide
    Alternative name(s):
    Amylin
    Diabetes-associated peptide
    Short name:
    DAP
    Insulinoma amyloid peptide
    Gene namesi
    Name:IAPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5329. IAPP.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: Ensembl
    3. neuronal cell body Source: Ensembl

    Keywords - Cellular componenti

    Amyloid, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481F → A, D or S: Promotes formation of fibrillar aggregates. 1 Publication

    Organism-specific databases

    PharmGKBiPA29579.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 319PRO_0000004105
    Peptidei34 – 7037Islet amyloid polypeptidePRO_0000004106Add
    BLAST
    Propeptidei74 – 8916PRO_0000004107Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 403 Publications
    Modified residuei70 – 701Tyrosine amide2 Publications

    Post-translational modificationi

    Amyloid fibrils are degraded by IDE.

    Keywords - PTMi

    Amidation, Cleavage on pair of basic residues, Disulfide bond

    Proteomic databases

    PaxDbiP10997.
    PRIDEiP10997.

    PTM databases

    PhosphoSiteiP10997.

    Miscellaneous databases

    PMAP-CutDBP10997.

    Expressioni

    Gene expression databases

    ArrayExpressiP10997.
    BgeeiP10997.
    CleanExiHS_IAPP.
    GenevestigatoriP10997.

    Organism-specific databases

    HPAiCAB000352.
    HPA053194.

    Interactioni

    Subunit structurei

    Interacts with IDE and INS. Can form homodimers. Interaction with INS inhibits homodimerization and fibril formation.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself7EBI-8526679,EBI-8526679

    Protein-protein interaction databases

    DIPiDIP-29913N.
    MINTiMINT-8074874.
    STRINGi9606.ENSP00000240652.

    Structurei

    Secondary structure

    1
    89
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 383
    Helixi43 – 497
    Helixi53 – 608
    Turni63 – 697

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KUWNMR-A53-62[»]
    2G48X-ray2.60C/D34-70[»]
    2KB8NMR-A34-70[»]
    2L86NMR-A34-70[»]
    3DG1X-ray1.66A61-66[»]
    3FPOX-ray1.50A51-56[»]
    3FR1X-ray1.85A47-52[»]
    3FTHX-ray1.84A/B47-53[»]
    3FTKX-ray1.50A64-70[»]
    3FTLX-ray1.60A/B64-70[»]
    3FTRX-ray1.61A61-66[»]
    3G7VX-ray1.86A/B/C/D34-69[»]
    3G7WX-ray1.75A34-55[»]
    3HGZX-ray2.91D/E34-70[»]
    ProteinModelPortaliP10997.
    SMRiP10997. Positions 34-70.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10997.

    Family & Domainsi

    Domaini

    The mature protein is largely unstructured in the absence of a cognate ligand, and has a strong tendency to form fibrillar aggregates. Homodimerization may be the first step of amyloid formation.3 Publications

    Sequence similaritiesi

    Belongs to the calcitonin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG38926.
    HOGENOMiHOG000038203.
    HOVERGENiHBG096065.
    InParanoidiP10997.
    KOiK08039.
    OMAiSHQMEKR.
    OrthoDBiEOG7TMZVK.
    PhylomeDBiP10997.
    TreeFamiTF330783.

    Family and domain databases

    InterProiIPR018360. Calcitonin_CS.
    IPR001693. Calcitonin_peptide-like.
    IPR000443. Pro-islet_amyloid_polypep.
    IPR021117. Procalcitonin-like.
    IPR021116. Procalcitonin/adrenomedullin.
    [Graphical view]
    PANTHERiPTHR10505. PTHR10505. 1 hit.
    PfamiPF00214. Calc_CGRP_IAPP. 1 hit.
    [Graphical view]
    PRINTSiPR00818. ISLETAMYLOID.
    SMARTiSM00113. CALCITONIN. 1 hit.
    [Graphical view]
    PROSITEiPS00258. CALCITONIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10997-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV   50
    HSSNNFGAIL SSTNVGSNTY GKRNAVEVLK REPLNYLPL 89
    Length:89
    Mass (Da):9,806
    Last modified:July 1, 1989 - v1
    Checksum:iAA8B1F7FD9FCB4BD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531S → C in CAA39504. (PubMed:2365085)Curated

    Mass spectrometryi

    Molecular mass is 3936 Da from positions 34 - 70. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti53 – 531S → G.2 Publications
    Corresponds to variant rs1800203 [ dbSNP | Ensembl ].
    VAR_012080

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27503 Genomic DNA. Translation: AAA35524.1.
    X14904 mRNA. Translation: CAA33032.1.
    X14905 mRNA. Translation: CAA33033.1.
    X14902 Genomic DNA. Translation: CAA33031.1.
    X14903 Genomic DNA. Translation: CAB57804.1.
    X13859 Genomic DNA. Translation: CAB57803.1.
    J04422 mRNA. Translation: AAA52281.1.
    M21785 Genomic DNA. Translation: AAA51728.1.
    M26650 Genomic DNA. Translation: AAA35983.1.
    X52818, X52819 Genomic DNA. Translation: CAA37002.1.
    X56030, X55634 Genomic DNA. Translation: CAA39504.1.
    X68830 Genomic DNA. Translation: CAA48724.1.
    DQ516082 mRNA. Translation: ABG27010.1.
    CH471094 Genomic DNA. Translation: EAW96426.1.
    CCDSiCCDS8688.1.
    PIRiS04016. TCHUIA.
    RefSeqiNP_000406.1. NM_000415.2.
    UniGeneiHs.46835.

    Genome annotation databases

    EnsembliENST00000240652; ENSP00000240652; ENSG00000121351.
    ENST00000539393; ENSP00000437357; ENSG00000121351.
    GeneIDi3375.
    KEGGihsa:3375.
    UCSCiuc001rev.3. human.

    Polymorphism databases

    DMDMi124006.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Amylin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M27503 Genomic DNA. Translation: AAA35524.1 .
    X14904 mRNA. Translation: CAA33032.1 .
    X14905 mRNA. Translation: CAA33033.1 .
    X14902 Genomic DNA. Translation: CAA33031.1 .
    X14903 Genomic DNA. Translation: CAB57804.1 .
    X13859 Genomic DNA. Translation: CAB57803.1 .
    J04422 mRNA. Translation: AAA52281.1 .
    M21785 Genomic DNA. Translation: AAA51728.1 .
    M26650 Genomic DNA. Translation: AAA35983.1 .
    X52818 , X52819 Genomic DNA. Translation: CAA37002.1 .
    X56030 , X55634 Genomic DNA. Translation: CAA39504.1 .
    X68830 Genomic DNA. Translation: CAA48724.1 .
    DQ516082 mRNA. Translation: ABG27010.1 .
    CH471094 Genomic DNA. Translation: EAW96426.1 .
    CCDSi CCDS8688.1.
    PIRi S04016. TCHUIA.
    RefSeqi NP_000406.1. NM_000415.2.
    UniGenei Hs.46835.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KUW NMR - A 53-62 [» ]
    2G48 X-ray 2.60 C/D 34-70 [» ]
    2KB8 NMR - A 34-70 [» ]
    2L86 NMR - A 34-70 [» ]
    3DG1 X-ray 1.66 A 61-66 [» ]
    3FPO X-ray 1.50 A 51-56 [» ]
    3FR1 X-ray 1.85 A 47-52 [» ]
    3FTH X-ray 1.84 A/B 47-53 [» ]
    3FTK X-ray 1.50 A 64-70 [» ]
    3FTL X-ray 1.60 A/B 64-70 [» ]
    3FTR X-ray 1.61 A 61-66 [» ]
    3G7V X-ray 1.86 A/B/C/D 34-69 [» ]
    3G7W X-ray 1.75 A 34-55 [» ]
    3HGZ X-ray 2.91 D/E 34-70 [» ]
    ProteinModelPortali P10997.
    SMRi P10997. Positions 34-70.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29913N.
    MINTi MINT-8074874.
    STRINGi 9606.ENSP00000240652.

    Chemistry

    ChEMBLi CHEMBL1914266.
    DrugBanki DB00790. Perindopril.

    PTM databases

    PhosphoSitei P10997.

    Polymorphism databases

    DMDMi 124006.

    Proteomic databases

    PaxDbi P10997.
    PRIDEi P10997.

    Protocols and materials databases

    DNASUi 3375.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240652 ; ENSP00000240652 ; ENSG00000121351 .
    ENST00000539393 ; ENSP00000437357 ; ENSG00000121351 .
    GeneIDi 3375.
    KEGGi hsa:3375.
    UCSCi uc001rev.3. human.

    Organism-specific databases

    CTDi 3375.
    GeneCardsi GC12P021507.
    HGNCi HGNC:5329. IAPP.
    HPAi CAB000352.
    HPA053194.
    MIMi 147940. gene.
    neXtProti NX_P10997.
    PharmGKBi PA29579.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG38926.
    HOGENOMi HOG000038203.
    HOVERGENi HBG096065.
    InParanoidi P10997.
    KOi K08039.
    OMAi SHQMEKR.
    OrthoDBi EOG7TMZVK.
    PhylomeDBi P10997.
    TreeFami TF330783.

    Enzyme and pathway databases

    Reactomei REACT_13819. Regulation of gene expression in beta cells.
    REACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.
    REACT_75925. Amyloids.

    Miscellaneous databases

    EvolutionaryTracei P10997.
    GeneWikii Amylin.
    GenomeRNAii 3375.
    NextBioi 13352.
    PMAP-CutDB P10997.
    PROi P10997.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10997.
    Bgeei P10997.
    CleanExi HS_IAPP.
    Genevestigatori P10997.

    Family and domain databases

    InterProi IPR018360. Calcitonin_CS.
    IPR001693. Calcitonin_peptide-like.
    IPR000443. Pro-islet_amyloid_polypep.
    IPR021117. Procalcitonin-like.
    IPR021116. Procalcitonin/adrenomedullin.
    [Graphical view ]
    PANTHERi PTHR10505. PTHR10505. 1 hit.
    Pfami PF00214. Calc_CGRP_IAPP. 1 hit.
    [Graphical view ]
    PRINTSi PR00818. ISLETAMYLOID.
    SMARTi SM00113. CALCITONIN. 1 hit.
    [Graphical view ]
    PROSITEi PS00258. CALCITONIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete islet amyloid polypeptide precursor is encoded by two exons."
      Mosselman S., Hoeppener J.W.M., Lips C.J.M., Jansz H.S.
      FEBS Lett. 247:154-158(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AMIDATION AT TYR-70.
    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].
    3. "An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing."
      Sanke T., Bell G.I., Sample C., Rubenstein A.H., Steiner D.F.
      J. Biol. Chem. 263:17243-17246(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    4. "The human islet amyloid polypeptide (IAPP) gene. Organization, chromosomal localization and functional identification of a promoter region."
      Christmanson L., Rorsman F., Stenman G., Westermark P., Betsholtz C.
      FEBS Lett. 267:160-166(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Islet amyloid polypeptide: structure and upstream sequences of the IAPP gene in rat and man."
      van Mansfeld A.D.M., Mosselman S., Hoeppener J.W.M., Zandberg J., van Teeffelen H.A.A.M., Baas P.D., Lips C.J.M., Jansz H.S.
      Biochim. Biophys. Acta 1087:235-240(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Characterization of the human islet amyloid polypeptide/amylin gene transcripts: identification of a new polyadenylation site."
      Hoeppener J.W.M., Oosterwijk C., Visser-Vernooy H.J., Lips C.J.M., Jansz H.S.
      Biochem. Biophys. Res. Commun. 189:1569-1577(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Cloning and expression of human islet amyloid polypeptide in cultured cells."
      Bhattacharya S., Naveena Lavanya Latha J., Kumresan R., Singh S.
      Biochem. Biophys. Res. Commun. 356:622-628(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DOMAIN, MASS SPECTROMETRY.
      Tissue: Fetal pancreas.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "Islet amyloid polypeptide: identification and chromosomal localization of the human gene."
      Mosselman S., Hoeppener J.W.M., Zandberg J., van Mansfeld A.D.M., Geurts van Kessel A.H.M., Lips C.J.M., Jansz H.S.
      FEBS Lett. 239:227-232(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-89.
    10. "Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients."
      Cooper G.J., Willis A.C., Clark A., Turner R.C., Sim R.B., Reid K.B.
      Proc. Natl. Acad. Sci. U.S.A. 84:8628-8632(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-70, DISULFIDE BOND.
    11. "Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species."
      Betsholtz C., Christmansson L., Engstroem U., Rorsman F., Svensson V., Johnson K.H., Westermark P.
      FEBS Lett. 251:261-264(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-70, SYNTHESIS OF 53-62.
    12. "Isolation and identification of islet amyloid polypeptide in normal human pancreas."
      Nakazato M., Asai J., Miyazato M., Matsukura S., Kangawa K., Matsuo H.
      Regul. Pept. 31:179-186(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-70.
    13. "A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas."
      Westermark P., Wernstedt C., Wilander E., Sletten K.
      Biochem. Biophys. Res. Commun. 140:827-831(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-52.
    14. "Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells."
      Westermark P., Wernstedt C., Wilander E., Hayden D.W., O'Brien T.D., Johnson K.H.
      Proc. Natl. Acad. Sci. U.S.A. 84:3881-3885(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-70.
    15. "Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus."
      Roberts A.N., Leighton B., Todd J.A., Cockburn D., Schofield P.N., Sutton R., Holt S., Boyd Y., Day A.J., Foot E.A., Willis A.C., Reid K.B.M., Cooper G.J.S.
      Proc. Natl. Acad. Sci. U.S.A. 86:9662-9666(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 30-89.
    16. "Solution structures of calcitonin-gene-related-peptide analogues of calcitonin-gene-related peptide and amylin."
      Hubbard J.A.M., Martin S.R., Chaplin L.C., Bose C., Kelly S.M., Price N.C.
      Biochem. J. 275:785-788(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF IAPP.
    17. "Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study."
      Mascioni A., Porcelli F., Ilangovan U., Ramamoorthy A., Veglia G.
      Biopolymers 69:29-41(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 53-62 IN DETERGENT MICELLES.
    18. "Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism."
      Shen Y., Joachimiak A., Rosner M.R., Tang W.-J.
      Nature 443:870-874(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 34-70 IN COMPLEX WITH IDE, INTERACTION WITH IDE.
    19. "Dynamic alpha-helix structure of micelle-bound human amylin."
      Patil S.M., Xu S., Sheftic S.R., Alexandrescu A.T.
      J. Biol. Chem. 284:11982-11991(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 34-70 IN DETERGENT MICELLES, DOMAIN, DISULFIDE BOND.
    20. "Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process."
      Wiltzius J.J., Sievers S.A., Sawaya M.R., Eisenberg D.
      Protein Sci. 18:1521-1530(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) IN COMPLEX WITH INS, DISULFIDE BOND, MUTAGENESIS OF PHE-48, DOMAIN.
    21. "Missense mutation of amylin gene (S20G) in Japanese NIDDM patients."
      Sakagashira S., Sanke T., Hanabusa T., Shimomura H., Ohagi S., Kumagaye K.Y., Nakajima K., Nanjo K.
      Diabetes 45:1279-1281(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLY-53.
    22. "Role of S20G mutation of amylin gene in insulin secretion, insulin sensitivity, and type II diabetes mellitus in Taiwanese patients."
      Chuang L.M., Lee K.C., Huang C.N., Wu H.P., Tai T.Y., Lin B.J.
      Diabetologia 41:1250-1251(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLY-53.

    Entry informationi

    Entry nameiIAPP_HUMAN
    AccessioniPrimary (citable) accession number: P10997
    Secondary accession number(s): Q0ZD87, Q14598
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    IAPP is the peptide subunit of amyloid found in pancreatic islets of type 2 diabetic patients and in insulinomas.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3