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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P67775: Variant p.Tyr127Cys

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Gene: PPP2CA
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Variant information Variant position: help 127 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 Tyrosine (Y) to Cysteine (C) at position 127 (Y127C, p.Tyr127Cys). 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 aromatic (Y) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 HJS3; almost complete loss of phosphatase activity in an in vitro assay; strong decrease in C-terminal methylation; no effect on the interaction with PP2A subunit A PPP2R1A/PPP2R1B; decreased interaction with PP2A subunit B components PPP2R5A, PPP2R5B, PPP2R5C, PPP2R5D, PPP2R5E and PPP2R3A; no effect on interaction with PP2A subunit B component PPP2R2A. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 127 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 309 The length of the canonical sequence.
Location on the sequence: help YRERITILRGNHESRQITQV Y GFYDECLRKYGNANVWKYFT 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                         YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Mouse                         YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Rat                           YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Pig                           YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Bovine                        YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Rabbit                        YRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Chicken                       YPERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFT

Slime mold                    YKDRVTILRGNHESRQITQVYGFYDECLRKYGNPNVWKLFT
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 – 309 Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Active site 118 – 118 Proton donor
Binding site 117 – 117
Helix 121 – 127



Literature citations
De novo mutations affecting the catalytic C alpha subunit of PP2A, PPP2CA, cause syndromic intellectual disability resembling other PP2A-related neurodevelopmental disorders.
Reynhout S.; Jansen S.; Haesen D.; van Belle S.; de Munnik S.A.; Bongers E.M.H.F.; Schieving J.H.; Marcelis C.; Amiel J.; Rio M.; Mclaughlin H.; Ladda R.; Sell S.; Kriek M.; Peeters-Scholte C.M.P.C.D.; Terhal P.A.; van Gassen K.L.; Verbeek N.; Henry S.; Scott Schwoerer J.; Malik S.; Revencu N.; Ferreira C.R.; Macnamara E.; Braakman H.M.H.; Brimble E.; Ruzhnikov M.R.Z.; Wagner M.; Harrer P.; Wieczorek D.; Kuechler A.; Tziperman B.; Barel O.; de Vries B.B.A.; Gordon C.T.; Janssens V.; Vissers L.E.L.M.;
Am. J. Hum. Genet. 104:139-156(2019)
Cited for: INVOLVEMENT IN HJS3; VARIANTS HJS3 VAL-60; GLY-88; HIS-122; 125-GLN--LEU-309 DEL; CYS-127; HIS-131; ARG-191; 214-ARG--LEU-309 DEL; HIS-223; VAL-223; CYS-265; 295-ARG--LEU-309 DEL AND PHE-308 INS; CHARACTERIZATION OF VARIANTS HJS3 GLY-88; HIS-122; 125-GLN--LEU-309 DEL; CYS-127; HIS-131; ARG-191; 214-ARG--LEU-309 DEL; HIS-223; VAL-223; CYS-265; 295-ARG--LEU-309 DEL AND PHE-308 INS; CATALYTIC ACTIVITY; MUTAGENESIS OF ASP-85; CARBOXYMETHYLATION; INTERACTION WITH PP2A SUBUNIT A AND PP2A SUBUNITS B;
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.