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P10997

- IAPP_HUMAN

UniProt

P10997 - IAPP_HUMAN

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Protein

Islet amyloid polypeptide

Gene

IAPP

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP10997.
CleanExiHS_IAPP.
ExpressionAtlasiP10997. baseline and differential.
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.
GeneTreeiENSGT00510000048671.
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

        10         20         30         40         50
MGILKLQVFL IVLSVALNHL KATPIESHQV EKRKCNTATC ATQRLANFLV
60 70 80
HSSNNFGAIL SSTNVGSNTY GKRNAVEVLK REPLNYLPL
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.

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.
GeneTreei ENSGT00510000048671.
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

Bgeei P10997.
CleanExi HS_IAPP.
ExpressionAtlasi P10997. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 150 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