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UniProtKB/Swiss-Prot Q9UBX5: Variant p.Pro87Ser

Fibulin-5
Gene: FBLN5
Variant information

Variant position:  87
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Proline (P) to Serine (S) at position 87 (P87S, p.Pro87Ser).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from medium size and hydrophobic (P) to small size and polar (S)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Involvement in disease:  Macular degeneration, age-related, 3 (ARMD3) [MIM:608895]: A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane. {ECO:0000269|PubMed:15269314, ECO:0000269|PubMed:16652333, ECO:0000269|PubMed:20007835, ECO:0000269|PubMed:20599547}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In ARMD3; no effect on secretion; slightly increases homodimerization in absence of Ca(2+).
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  87
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  448
The length of the canonical sequence.

Location on the sequence:   LCIPRTNPVYRGPYSNPYST  P YSGPYPAAAPPLSAPNYPTI
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         LCIPRTNPVYRGPYSNPYSTPYSGPYPAAAPPLSAPNYPTI

Mouse                         LCIPRTNPVYRGPYSNPYSTSYSGPYPAAAPPVPASNYPTI

Rat                           LCIPRTNPVYRGPYSNPYSTSYSGPYPAAAPPVPASNYPTI

Bovine                        LCIPRTNPVYRGPYSNPYSNPYSASYPAAAPPLSAPNYPTI

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 24 – 448 Fibulin-5


Literature citations

Missense variations in the fibulin 5 gene and age-related macular degeneration.
Stone E.M.; Braun T.A.; Russell S.R.; Kuehn M.H.; Lotery A.J.; Moore P.A.; Eastman C.G.; Casavant T.L.; Sheffield V.C.;
N. Engl. J. Med. 351:346-353(2004)
Cited for: VARIANTS ARMD3 LEU-60; GLN-71; SER-87; THR-169; TRP-351; THR-363 AND GLU-412;

Reduced secretion of fibulin 5 in age-related macular degeneration and cutis laxa.
Lotery A.J.; Baas D.; Ridley C.; Jones R.P.; Klaver C.C.; Stone E.; Nakamura T.; Luff A.; Griffiths H.; Wang T.; Bergen A.A.; Trump D.;
Hum. Mutat. 27:568-574(2006)
Cited for: VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351; THR-363 AND GLU-412; CHARACTERIZATION OF VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351; THR-363 AND GLU-412; VARIANTS ARCL1A ARG-217 AND PRO-227; CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND PRO-227; VARIANTS MET-126 AND ARG-202; SUBCELLULAR LOCATION;

Structural effects of fibulin 5 missense mutations associated with age-related macular degeneration and cutis laxa.
Jones R.P.; Ridley C.; Jowitt T.A.; Wang M.C.; Howard M.; Bobola N.; Wang T.; Bishop P.N.; Kielty C.M.; Baldock C.; Lotery A.J.; Trump D.;
Invest. Ophthalmol. Vis. Sci. 51:2356-2362(2010)
Cited for: CHARACTERIZATION OF VARIANTS MET-126 AND ARG-202; CHARACTERIZATION OF VARIANTS ARMD3 LEU-60; GLN-71; SER-87; PRO-124; THR-169; SER-267; TRP-351 AND GLU-412; CHARACTERIZATION OF VARIANTS ARCL1A ARG-217 AND PRO-227; SUBUNIT;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.