Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8WWY3: Variant p.Ala194Glu

U4/U6 small nuclear ribonucleoprotein Prp31
Gene: PRPF31
Feedback?
Variant information Variant position: help 194 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 Alanine (A) to Glutamate (E) at position 194 (A194E, p.Ala194Glu). 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 small size and hydrophobic (A) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 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 RP11; mislocation of the protein in the cytoplasm and reduced interaction with PRPF6; the result may be a deficiency in splicing function in the retina. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 194 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 499 The length of the canonical sequence.
Location on the sequence: help TQGQQLSEEELERLEEACDM A LELNASKHRIYEYVESRMSF 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                         T--QGQQLSEEELERLEEACDMALELNASKHRIYEYVESRMSF

Mouse                         T--QGQQLSDEELERLEEACDMALELNASKHRIYEYVESRM

Xenopus laevis                T--QGQQLTDEELERIEEACDMALELNQSKHRIYEYVESRM

Xenopus tropicalis            T--QGQQLTDEELERIEEACDMALELNQSKHRIYEYVESRM

Zebrafish                     T--QGTMLGDDELQRLEEACDMALELNQSKHRIYEYVESRM

Baker's yeast                 SFKNKEPLDIKTRTQILEANSILENLWKLQEDIGQYIASKI

Fission yeast                 T--VGKPLPDEMIKNVKNCCEAIQQLGEEKQKIIEYVQSRI
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 1 – 499 U4/U6 small nuclear ribonucleoprotein Prp31
Coiled coil 181 – 215
Helix 181 – 215



Literature citations
Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Liu S.; Li P.; Dybkov O.; Nottrott S.; Hartmuth K.; Luehrmann R.; Carlomagno T.; Wahl M.C.;
Science 316:115-120(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-333 IN COMPLEX WITH SNU13 AND STEM-LOOP RNA OF U4 SNRNA; COILED-COIL DOMAIN; INTERACTION WITH PRPF6; CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216; MUTAGENESIS OF HIS-270; A human homolog of yeast pre-mRNA splicing gene, PRP31, underlies autosomal dominant retinitis pigmentosa on chromosome 19q13.4 (RP11).
Vithana E.N.; Abu-Safieh L.; Allen M.J.; Carey A.; Papaioannou M.; Chakarova C.; Al-Maghtheh M.; Ebenezer N.D.; Willis C.; Moore A.T.; Bird A.C.; Hunt D.M.; Bhattacharya S.S.;
Mol. Cell 8:375-381(2001)
Cited for: VARIANTS RP11 GLU-194 AND PRO-216; TISSUE SPECIFICITY; Disease mechanism for retinitis pigmentosa (RP11) caused by mutations in the splicing factor gene PRPF31.
Deery E.C.; Vithana E.N.; Newbold R.J.; Gallon V.A.; Bhattacharya S.S.; Warren M.J.; Hunt D.M.; Wilkie S.E.;
Hum. Mol. Genet. 11:3209-3219(2002)
Cited for: CHARACTERIZATION OF VARIANTS RP11 GLU-194 AND PRO-216; SUBCELLULAR LOCATION; NUCLEAR LOCALIZATION SIGNAL; MUTAGENESIS OF 351-ARG--GLU-364;
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.