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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30153: Variant p.Arg182Trp

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Gene: PPP2R1A
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Variant information Variant position: help 182 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 Arginine (R) to Tryptophan (W) at position 182 (R182W, p.Arg182Trp). 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 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: help -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: help In HJS2; reduces PPP2CA binding; reduces PPP2R5A binding; reduces PPP2R5C binding; does not affect PPP2R5D binding; reduces PPP2R2A binding; reduces PPP2R2B binding; reduces PPP2R3A binding; decreases phosphatase activity of PPP2CA. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 182 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 589 The length of the canonical sequence.
Location on the sequence: help VKAELRQYFRNLCSDDTPMV R RAAASKLGEFAKVLELDNVK 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                         VKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV------LELDNVK

Mouse                         VKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV------L

Pig                           VKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV------L

Bovine                        VKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV------L

Caenorhabditis elegans        IKSELKSMFRTLCRDDTPMVRRAAAAKLGEFAKV------F

Drosophila                    VKAELRANFRKLCQDETPMVRRAAANKLGEFAKV------V

Slime mold                    MKKSLRKTFGGLCHDDTPMVKRAAATNLGSFAKQ------I

Baker's yeast                 LRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQNLGL

Fission yeast                 VKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFL------V
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 2 – 589 Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Repeat 162 – 200 HEAT 5
Region 8 – 399 PP2A subunit B binding
Region 47 – 321 Polyoma small and medium T antigens Binding
Region 85 – 239 SV40 small T antigen binding
Helix 179 – 194



Literature citations
B56delta-related protein phosphatase 2A dysfunction identified in patients with intellectual disability.
Houge G.; Haesen D.; Vissers L.E.; Mehta S.; Parker M.J.; Wright M.; Vogt J.; McKee S.; Tolmie J.L.; Cordeiro N.; Kleefstra T.; Willemsen M.H.; Reijnders M.R.; Berland S.; Hayman E.; Lahat E.; Brilstra E.H.; van Gassen K.L.; Zonneveld-Huijssoon E.; de Bie C.I.; Hoischen A.; Eichler E.E.; Holdhus R.; Steen V.M.; Doeskeland S.O.; Hurles M.E.; FitzPatrick D.R.; Janssens V.;
J. Clin. Invest. 125:3051-3062(2015)
Cited for: VARIANTS HJS2 LEU-179; TRP-182 AND HIS-258; CHARACTERIZATION HJS2 OF VARIANTS LEU-179; TRP-182 AND HIS-258;
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.