UniProtKB/Swiss-Prot O75695: Variant p.Arg282Trp

Protein XRP2
Gene: RP2
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Variant information Variant position:

282 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 Arginine (R) to Tryptophan (W) at position 282 (R282W, p.Arg282Trp). 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 large size and aromatic (W) 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:

Reduces affinity for ARL3 3-fold. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1805147 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

FFLVQTKEVSMKAEDAQRVF R EKAPDFLPLLNKGPVIALEF 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                         FFLVQTKEVSMKAEDAQRVFREKAPDFLPLLNKGPVIALEF

Mouse                         FSLVQTKEMSMKTEDAQRVFQEKASDFLLLLNKGPVIALEF

Chicken                       FQLVQTKEVSMKAEDAQRVFQQCASEFIPLLERGPVVALEF

Xenopus laevis                LSLIQTKEVAMKIEDAKRVFQDNITDLICLLEKGPVVALEF

Zebrafish                     FVLIQTKEVSMRPEDVSRVFQNNAESLTEWITKGPVVALEL

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	2 – 350	Protein XRP2
Helix	282 – 287

Literature citations
Crystal structure of the human retinitis pigmentosa 2 protein and its interaction with Arl3.
Kuehnel K.; Veltel S.; Schlichting I.; Wittinghofer A.;
Structure 14:367-378(2006)
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS); INTERACTION WITH ARL3; CHARACTERIZATION OF VARIANTS RP2 HIS-118 AND GLY-138; CHARACTERIZATION OF VARIANT TRP-282; Novel frameshift mutations in the RP2 gene and polymorphic variants.
Thiselton D.L.; Zito I.; Plant C.; Jay M.; Hodgson S.V.; Bird A.C.; Bhattacharya S.S.; Hardcastle A.J.;
Hum. Mutat. 15:580-580(2000)
Cited for: VARIANTS TRP-282 AND TYR-338; X-linked retinitis pigmentosa: mutation spectrum of the RPGR and RP2 genes and correlation with visual function.
Sharon D.; Bruns G.A.P.; McGee T.L.; Sandberg M.A.; Berson E.L.; Dryja T.P.;
Invest. Ophthalmol. Vis. Sci. 41:2712-2721(2000)
Cited for: VARIANTS RP2 TYR-86; LEU-95; HIS-118 AND ILE-137 DEL; VARIANT TRP-282; Identification of novel RP2 mutations in a subset of X-linked retinitis pigmentosa families and prediction of new domains.
Miano M.G.; Testa F.; Filippini F.; Trujillo M.; Conte I.; Lanzara C.; Millan J.M.; De Bernardo C.; Grammatico B.; Mangino M.; Torrente I.; Carrozzo R.; Simonelli F.; Rinaldi E.; Ventruto V.; D'Urso M.; Ayuso C.; Ciccodicola A.;
Hum. Mutat. 18:109-119(2001)
Cited for: VARIANTS RP2 LEU-118 AND GLY-138; VARIANT TRP-282; A comprehensive mutation analysis of RP2 and RPGR in a North American cohort of families with X-linked retinitis pigmentosa.
Breuer D.K.; Yashar B.M.; Filippova E.; Hiriyanna S.; Lyons R.H.; Mears A.J.; Asaye B.; Acar C.; Vervoort R.; Wright A.F.; Musarella M.A.; Wheeler P.; MacDonald I.; Iannaccone A.; Birch D.; Hoffman D.R.; Fishman G.A.; Heckenlively J.R.; Jacobson S.G.; Sieving P.A.; Swaroop A.;
Am. J. Hum. Genet. 70:1545-1554(2002)
Cited for: VARIANTS RP2 TYR-67; HIS-118; ILE-137 DEL AND PRO-188; VARIANT TRP-282; RP2 and RPGR mutations and clinical correlations in patients with X-linked retinitis pigmentosa.
Sharon D.; Sandberg M.A.; Rabe V.W.; Stillberger M.; Dryja T.P.; Berson E.L.;
Am. J. Hum. Genet. 73:1131-1146(2003)
Cited for: VARIANTS RP2 TYR-86; LEU-95; HIS-118 AND ILE-137 DEL; VARIANT TRP-282; Analysis of protein-coding genetic variation in 60,706 humans.
Lek M.; Karczewski K.J.; Minikel E.V.; Samocha K.E.; Banks E.; Fennell T.; O'Donnell-Luria A.H.; Ware J.S.; Hill A.J.; Cummings B.B.; Tukiainen T.; Birnbaum D.P.; Kosmicki J.A.; Duncan L.E.; Estrada K.; Zhao F.; Zou J.; Pierce-Hoffman E.; Berghout J.; Cooper D.N.; Deflaux N.; DePristo M.; Do R.; Flannick J.; Fromer M.; Gauthier L.; Goldstein J.; Gupta N.; Howrigan D.; Kiezun A.; Kurki M.I.; Moonshine A.L.; Natarajan P.; Orozco L.; Peloso G.M.; Poplin R.; Rivas M.A.; Ruano-Rubio V.; Rose S.A.; Ruderfer D.M.; Shakir K.; Stenson P.D.; Stevens C.; Thomas B.P.; Tiao G.; Tusie-Luna M.T.; Weisburd B.; Won H.H.; Yu D.; Altshuler D.M.; Ardissino D.; Boehnke M.; Danesh J.; Donnelly S.; Elosua R.; Florez J.C.; Gabriel S.B.; Getz G.; Glatt S.J.; Hultman C.M.; Kathiresan S.; Laakso M.; McCarroll S.; McCarthy M.I.; McGovern D.; McPherson R.; Neale B.M.; Palotie A.; Purcell S.M.; Saleheen D.; Scharf J.M.; Sklar P.; Sullivan P.F.; Tuomilehto J.; Tsuang M.T.; Watkins H.C.; Wilson J.G.; Daly M.J.; MacArthur D.G.;
Nature 536:285-291(2016)
Cited for: VARIANT TRP-282;

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.