UniProtKB/Swiss-Prot P35556: Variant p.Val965Ile

Fibrillin-2
Gene: FBN2
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Variant information Variant position:

965 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Valine (V) to Isoleucine (I) at position 965 (V965I, p.Val965Ile). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. 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
Other resources:

Links to websites of interest for the variant.

Variant rs154001 [ dbSNP | Ensembl ]

Sequence information Variant position:

965 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

2912 The length of the canonical sequence.
Location on the sequence:

LARIKGVTCEDVNECEVFPG V CPNGRCVNSKGSFHCECPEG 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                         LARIKGVTCEDVNECEVFPGVCPNGRCVNSKGSFHCECPEG

Mouse                         FARIKGVTCEDVNECEVFPGVCPNGRCVNSKGSFHCECPEG

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.

Type	Positions	Description
Chain	78 – 2779	Fibrillin-2
Domain	955 – 996	EGF-like 14; calcium-binding
Glycosylation	977 – 977	O-linked (Glc) serine
Disulfide bond	959 – 971

Literature citations
Rare and common variants in extracellular matrix gene Fibrillin 2 (FBN2) are associated with macular degeneration.
Ratnapriya R.; Zhan X.; Fariss R.N.; Branham K.E.; Zipprer D.; Chakarova C.F.; Sergeev Y.V.; Campos M.M.; Othman M.; Friedman J.S.; Maminishkis A.; Waseem N.H.; Brooks M.; Rajasimha H.K.; Edwards A.O.; Lotery A.; Klein B.E.; Truitt B.J.; Li B.; Schaumberg D.A.; Morgan D.J.; Morrison M.A.; Souied E.; Tsironi E.E.; Grassmann F.; Fishman G.A.; Silvestri G.; Scholl H.P.; Kim I.K.; Ramke J.; Tuo J.; Merriam J.E.; Merriam J.C.; Park K.H.; Olson L.M.; Farrer L.A.; Johnson M.P.; Peachey N.S.; Lathrop M.; Baron R.V.; Igo R.P. Jr.; Klein R.; Hagstrom S.A.; Kamatani Y.; Martin T.M.; Jiang Y.; Conley Y.; Sahel J.A.; Zack D.J.; Chan C.C.; Pericak-Vance M.A.; Jacobson S.G.; Gorin M.B.; Klein M.L.; Allikmets R.; Iyengar S.K.; Weber B.H.; Haines J.L.; Leveillard T.; Deangelis M.M.; Stambolian D.; Weeks D.E.; Bhattacharya S.S.; Chew E.Y.; Heckenlively J.R.; Abecasis G.R.; Swaroop A.;
Hum. Mol. Genet. 23:5827-5837(2014)
Cited for: TISSUE SPECIFICITY; INVOLVEMENT IN EOMD; VARIANTS EOMD LYS-1144 AND THR-1247; VARIANTS ILE-965; ASN-1381; ALA-1416 AND LYS-1438; Fibrillin-2 (FBN2) mutations result in the Marfan-like disorder, congenital contractural arachnodactyly.
Putnam E.A.; Zhang H.; Ramirez F.; Milewicz D.M.;
Nat. Genet. 11:456-458(1995)
Cited for: VARIANTS CCA TYR-1253 AND SER-1434; VARIANT ILE-965; Clustering of FBN2 mutations in patients with congenital contractural arachnodactyly indicates an important role of the domains encoded by exons 24 through 34 during human development.
Park E.-S.; Putnam E.A.; Chitayat D.; Child A.; Milewicz D.M.;
Am. J. Med. Genet. 78:350-355(1998)
Cited for: VARIANTS CCA ASP-1057 AND THR-1093; VARIANTS SER-594; HIS-681; ILE-965; GLY-1772; LEU-2266; THR-2428 AND PRO-2771; Ten novel FBN2 mutations in congenital contractural arachnodactyly: delineation of the molecular pathogenesis and clinical phenotype.
Gupta P.A.; Putnam E.A.; Carmical S.G.; Kaitila I.; Steinmann B.; Child A.; Danesino C.; Metcalfe K.; Berry S.A.; Chen E.; Delorme C.V.; Thong M.-K.; Ades L.C.; Milewicz D.M.;
Hum. Mutat. 19:39-48(2002)
Cited for: VARIANTS CCA ASP-1057; THR-1093; PHE-1142; CYS-1179; TYR-1198; ARG-1240; TRP-1253; TYR-1253; TRP-1257; ARG-1268 AND SER-1434; VARIANT ILE-965;

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.