Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95967: Variant p.Cys267Tyr

EGF-containing fibulin-like extracellular matrix protein 2
Gene: EFEMP2
Feedback?
Variant information Variant position: help 267 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Cysteine (C) to Tyrosine (Y) at position 267 (C267Y, p.Cys267Tyr). 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: help Change from medium size and polar (C) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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: help In ARCL1B; loss of protein expression in patient dermal fibroblasts; increased transforming growth factor beta receptor signaling pathway in patient fibroblasts; loss of protein expression; strongly decreased secretion. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 267 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 443 The length of the canonical sequence.
Location on the sequence: help CSYSSYLCQYRCINEPGRFS C HCPQGYQLLATRLCQDIDEC 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         CSYSSYLCQYRCINEPGRFSCHCPQGYQLLATRLCQDIDEC

Mouse                         CGYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDEC
Sequence annotation in neighborhood: help 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 – 443 EGF-containing fibulin-like extracellular matrix protein 2
Domain 243 – 282 EGF-like 5; calcium-binding
Disulfide bond 254 – 267



Literature citations
Functional consequence of fibulin-4 missense mutations associated with vascular and skeletal abnormalities and cutis laxa.
Sasaki T.; Hanisch F.G.; Deutzmann R.; Sakai L.Y.; Sakuma T.; Miyamoto T.; Yamamoto T.; Hannappel E.; Chu M.L.; Lanig H.; von der Mark K.;
Matrix Biol. 56:132-149(2016)
Cited for: PROTEIN SEQUENCE OF 88-94 AND 91-98; CHARACTERIZATION OF VARIANTS ARCL1B LYS-57; LYS-126; TYR-267; CYS-279 AND THR-397; GLYCOSYLATION; SUBCELLULAR LOCATION; FUNCTION; INTERACTION WITH LOX; LOXL1; LOXL2; LTBP1; LTBP3; LTBP4 AND TGFB1; CLEAVAGE BY ELANE; MMP2 AND MMP9; Lethal cutis laxa with contractural arachnodactyly, overgrowth and soft tissue bleeding due to a novel homozygous fibulin-4 gene mutation.
Hoyer J.; Kraus C.; Hammersen G.; Geppert J.P.; Rauch A.;
Clin. Genet. 76:276-281(2009)
Cited for: VARIANT ARCL1B TYR-267; Altered TGFbeta signaling and cardiovascular manifestations in patients with autosomal recessive cutis laxa type I caused by fibulin-4 deficiency.
Renard M.; Holm T.; Veith R.; Callewaert B.L.; Ades L.C.; Baspinar O.; Pickart A.; Dasouki M.; Hoyer J.; Rauch A.; Trapane P.; Earing M.G.; Coucke P.J.; Sakai L.Y.; Dietz H.C.; De Paepe A.M.; Loeys B.L.;
Eur. J. Hum. Genet. 18:895-901(2010)
Cited for: VARIANTS ARCL1B LYS-126; VAL-126 AND THR-397; CHARACTERIZATION OF VARIANTS ARCL1B LYS-126 AND TYR-267; SUBCELLULAR LOCATION;
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.