UniProtKB/Swiss-Prot P60484 : Variant p.Gly132Val
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information
Variant position:
132
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
US
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:
From Glycine (G) to Valine (V) at position 132 (G132V, p.Gly132Val).
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:
Change from glycine (G) to medium size and hydrophobic (V)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-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:
In one patient with clinical findings suggesting hamartoma tumor syndrome.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
132
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
403
The length of the canonical sequence.
Location on the sequence:
LSEDDNHVAAIHCKAGKGRT
G VMICAYLLHRGKFLKAQEAL
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 LSEDDNHVAAIHCKAGKGRTG VMICAYLLHRGKFLKAQEAL
LSEDDNHVAAIHCKAGKGRTG VMICAYLLHRGKFLKAQEAL
Mouse LSEDDNHVAAIHCKAGKGRTG VMICAYLLHRGKFLKAQEAL
Rat LSEDDNHVAAIHCKAGKGRTG VMICAYLLHRGKFLKAQEAL
Xenopus laevis LSENEN-VAAIHCKAGKGRTG VMICAYLLHRGKFPRAQEAL
Caenorhabditis elegans LEADDKHVIAVHCKAGKGRTG VMICALLIYINFYPSPRQIL
Slime mold MKEDSKNIAVIHCKAGKGRTG LMICCWLMYCGMWKNTEDSL
Fission yeast FQTQPLLTLVVHCKAGKGRTG TVICSYLVAFGG-LTAKQSL
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 – 403
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Domain
14 – 185
Phosphatase tensin-type
Active site
124 – 124
Phosphocysteine intermediate
Mutagenesis
124 – 124
C -> A. Loss of protein phosphatase activity. Unable to inhibit focal adhesion formation.
Mutagenesis
124 – 124
C -> S. Loss of phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity.
Mutagenesis
125 – 125
K -> M. Reduced phosphatase activity towards PtdIns(3,4,5)P3, PtdIns(3,4)P2 and PtdIns(3)P.
Mutagenesis
126 – 126
A -> P. Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2.
Mutagenesis
126 – 126
A -> S. Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2.
Mutagenesis
126 – 126
A -> V. Does not reduce phosphatase activity towards PtdIns(3,4,5)P3 and PtdIns(3,4)P2.
Mutagenesis
128 – 128
K -> M. 85% reduction in phosphatase activity towards PtdIns(3,4,5)P3.
Mutagenesis
128 – 128
K -> R. Does not reduce phosphatase activity towards PtdIns(3,4,5)P3.
Mutagenesis
130 – 130
R -> M. Does not affect the ability to inhibit AKT/PKB activation.
Helix
129 – 141
Literature citations
A germline PTEN mutation with manifestations of prenatal onset and verrucous epidermal nevus.
Tekin M.; Hismi B.O.; Fitoz S.; Yalcinkaya F.; Ekim M.; Kansu A.; Ertem M.; Deda G.; Tutar E.; Arsan S.; Zhou X.-P.; Pilarski R.; Eng C.; Akar N.;
Am. J. Med. Genet. A 140:1472-1475(2006)
Cited for: VARIANT VAL-132;
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.