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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P30153: Variant p.Pro179Leu

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Gene: PPP2R1A
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Variant information Variant position: help 179 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 Proline (P) to Leucine (L) at position 179 (P179L, p.Pro179Leu). 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 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: 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; does not affect 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 179 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 SSAVKAELRQYFRNLCSDDT P MVRRAAASKLGEFAKVLELD 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                         SSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV------LELD

Mouse                         SSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV----

Pig                           SSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV----

Bovine                        SSAVKAELRQYFRNLCSDDTPMVRRAAASKLGEFAKV----

Caenorhabditis elegans        SPAIKSELKSMFRTLCRDDTPMVRRAAAAKLGEFAKV----

Drosophila                    TQPVKAELRANFRKLCQDETPMVRRAAANKLGEFAKV----

Slime mold                    NAEMKKSLRKTFGGLCHDDTPMVKRAAATNLGSFAKQ----

Baker's yeast                 DDSLRKNILALYLQLAQDDTPMVKRAVGKNLPILIDLLTQN

Fission yeast                 NPAVKVSLRQSFSHLCHDEAPMVRRPAATNCAKFVFL----
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.