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UniProtKB/Swiss-Prot P35555: Variant p.Arg62Cys

Gene: FBN1
Variant information

Variant position:  62
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Cysteine (C) at position 62 (R62C, p.Arg62Cys).
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 large size and basic (R) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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

Variant description:  In MFS; also in a patient with ectopia lentis and retinal detachment.
Any additional useful information about the variant.

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

Sequence information

Variant position:  62
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  2871
The length of the canonical sequence.

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.





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.

Chain 45 – 2731 Fibrillin-1
Region 45 – 450 N-terminal domain
Region 45 – 81 Fibrillin unique N-terminal (FUN) domain
Disulfide bond 59 – 68

Literature citations

Two novel mutations and a neutral polymorphism in EGF-like domains of the fibrillin gene (FBN1): SSCP screening of exons 15-21 in Marfan syndrome patients.
Hayward C.; Rae A.L.; Porteous M.E.M.; Logie L.J.; Brock L.J.;
Hum. Mol. Genet. 3:373-375(1994)
Cited for: VARIANT MFS CYS-627;

Mutation screening of all 65 exons of the fibrillin-1 gene in 60 patients with Marfan syndrome: report of 12 novel mutations.
Hayward C.; Porteous M.E.M.; Brock D.J.H.;
Hum. Mutat. 10:280-289(1997)
Cited for: VARIANTS MFS ARG-111; CYS-545; CYS-627; GLY-750; ARG-1074; HIS-1170; TRP-1171; LYS-1173; TYR-1404; GLY-1610; LYS-1893; TRP-2099; TYR-2111; ARG-2258; TRP-2282 AND ARG-2489;

TGGE screening of the entire FBN1 coding sequence in 126 individuals with Marfan syndrome and related fibrillinopathies.
Katzke S.; Booms P.; Tiecke F.; Palz M.; Pletschacher A.; Turkmen S.; Neumann L.M.; Pregla R.; Leitner C.; Schramm C.; Lorenz P.; Hagemeier C.; Fuchs J.; Skovby F.; Rosenberg T.; Robinson P.N.;
Hum. Mutat. 20:197-208(2002)
Cited for: VARIANTS MFS CYS-62; TYR-587; TYR-596; ASN-654; TYR-681; ARG-683; TRP-685; VAL-723; PHE-734; TYR-748; GLY-776; ARG-781; ARG-908; GLY-921; PRO-1790; SER-1806; VAL-1931 DEL; TYR-1998; GLY-2221; THR-2269 AND TRP-2335; VARIANTS ECTOL1 CYS-115; TYR-661 AND TYR-2339; VARIANT MET-2101;

Twelve novel FBN1 mutations in Marfan syndrome and Marfan related phenotypes test the feasibility of FBN1 mutation testing in clinical practice.
Halliday D.J.; Hutchinson S.; Lonie L.; Hurst J.A.; Firth H.; Handford P.A.; Wordsworth P.;
J. Med. Genet. 39:589-593(2002)
Cited for: VARIANTS MFS CYS-627; ASN-654; TYR-748; 1541-ARG--HIS-2871 DEL; TYR-1835; ARG-1977; TYR-2258; 2394-ARG--HIS-2871 DEL; 2466-TYR--HIS-2871 DEL AND 2467-GLN--HIS-2871 DEL; VARIANT PRO-2780;

Consequences of cysteine mutations in calcium-binding epidermal growth factor modules of fibrillin-1.
Vollbrandt T.; Tiedemann K.; El-Hallous E.; Lin G.; Brinckmann J.; John H.; Baetge B.; Notbohm H.; Reinhardt D.P.;
J. Biol. Chem. 279:32924-32931(2004)

Identification of 29 novel and nine recurrent fibrillin-1 (FBN1) mutations and genotype-phenotype correlations in 76 patients with Marfan syndrome.
Rommel K.; Karck M.; Haverich A.; von Kodolitsch Y.; Rybczynski M.; Muller G.; Singh K.K.; Schmidtke J.; Arslan-Kirchner M.;
Hum. Mutat. 26:529-539(2005)
Cited for: VARIANTS MFS ASN-507 DEL; TYR-541; CYS-627; TYR-781; ARG-985; ARG-1013; VAL-1113; GLY-1284; SER-1475; GLU-1475; THR-1576; ARG-1791; GLY-1928; TYR-1928; TYR-2038; ARG-2085; SER-2144; ARG-2536 AND TYR-2605;

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.