Sequence information
Variant position: 118 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:
GSVFFRNCRDCKCTLACQQF
R VRDCRKLEVFLCCATQPIIE
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 GSVFFRNCRDCKCTLACQQFR VRDCRKLEVFLCCATQPIIE
Mouse GSVFFRNCRDCKCTLACQQFR VRDCRKLEVFLCCATQPIIE
Chicken GSVFFRNCKDCKCIVACQQFR TRDCRRLEVFLCCATQPIIE
Xenopus laevis GSVFFRDCKDCKCVVACQQFR TRDCRRMDVFLCCSTQPIIE
Zebrafish GSVFFRDCKDIKCVVACQQFR TRDCKKMDVFLCCATQPIIE
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
Domain
24 – 179
C-CAP/cofactor C-like
Binding site
115 – 118
Mutagenesis
101 – 101
F -> A. Reduces affinity for mouse ARL3.
Mutagenesis
115 – 115
Q -> A. Reduces affinity for mouse ARL3.
Mutagenesis
116 – 116
Q -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
Mutagenesis
118 – 118
R -> A. Reduces affinity and GTP-hydrolysis rate for mouse ARL3.
Mutagenesis
120 – 120
R -> H. Reduces affinity for mouse ARL3; when associated with S-121.
Mutagenesis
121 – 121
D -> S. Reduces affinity for mouse ARL3; when associated with H-120.
Beta strand
106 – 121
Literature citations
Positional cloning of the gene for X-linked retinitis pigmentosa 2.
Schwahn U.; Lenzner S.; Dong J.; Feil S.; Hinzmann B.; van Duijnhoven G.; Kirschner R.; Hemberger M.; Bergen A.A.B.; Rosenberg T.; Pinckers A.J.L.G.; Fundele R.; Rosenthal A.; Cremers F.P.M.; Ropers H.-H.; Berger W.;
Nat. Genet. 19:327-332(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS RP2 SER-6 DEL AND HIS-118;
Mutations in the N-terminus of the X-linked retinitis pigmentosa protein RP2 interfere with the normal targeting of the protein to the plasma membrane.
Chapple J.P.; Hardcastle A.J.; Grayson C.; Spackman L.A.; Willison K.R.; Cheetham M.E.;
Hum. Mol. Genet. 9:1919-1926(2000)
Cited for: CHARACTERIZATION OF VARIANTS RP2 SER-6 DEL AND HIS-118; MYRISTOYLATION AT GLY-2; PALMITOYLATION AT CYS-3; MUTAGENESIS OF GLY-2 AND CYS-3; TISSUE SPECIFICITY; SUBCELLULAR LOCATION;
Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C.
Bartolini F.; Bhamidipati A.; Thomas S.; Schwahn U.; Lewis S.A.; Cowan N.J.;
J. Biol. Chem. 277:14629-14634(2002)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS RP2 SER-6 DEL AND HIS-118; INTERACTION WITH ARL3;
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;
Mutations in the RP2 gene cause disease in 10% of families with familial X-Linked retinitis pigmentosa assessed in this study.
Hardcastle A.J.; Thiselton D.L.; Van Maldergem L.; Saha B.K.; Jay M.; Plant C.; Taylor R.; Bird A.C.; Bhattacharya S.;
Am. J. Hum. Genet. 64:1210-1215(1999)
Cited for: VARIANT RP2 HIS-118;
Genotype-phenotype correlation in X-linked retinitis pigmentosa 2 (RP2).
Rosenberg T.; Schwahn U.; Feil S.; Berger W.;
Ophthalmic Genet. 20:161-172(1999)
Cited for: VARIANTS RP2 SER-6 DEL AND HIS-118;
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;
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;
X-linked retinitis pigmentosa: RPGR mutations in most families with definite X linkage and clustering of mutations in a short sequence stretch of exon ORF15.
Bader I.; Brandau O.; Achatz H.; Apfelstedt-Sylla E.; Hergersberg M.; Lorenz B.; Wissinger B.; Wittwer B.; Rudolph G.; Meindl A.; Meitinger T.;
Invest. Ophthalmol. Vis. Sci. 44:1458-1463(2003)
Cited for: VARIANTS RP2 HIS-118 AND CYS-118;
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