UniProtKB/Swiss-Prot P60484: Variant p.Val119Leu

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information Variant position:

119 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 Valine (V) to Leucine (L) at position 119 (V119L, p.Val119Leu). 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:

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:

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:

In multiple cancers. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs139767111 [ dbSNP | Ensembl ]

Sequence information Variant position:

119 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:

ELIKPFCEDLDQWLSEDDNH V AAIHCKAGKGRTGVMICAYL 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                         ELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYL

                              ELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYL

Mouse                         ELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYL

Rat                           ELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYL

Xenopus laevis                ELIKPFCEDLDQLLSENEN-VAAIHCKAGKGRTGVMICAYL

Caenorhabditis elegans        ELMAPFCREAKEWLEADDKHVIAVHCKAGKGRTGVMICALL

Slime mold                    EMIDAFCRDVDAWMKEDSKNIAVIHCKAGKGRTGLMICCWL

Fission yeast                 LFLWAIVMNMDALFQTQPLLTLVVHCKAGKGRTGTVICSYL

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.
Beta strand	118 – 123

Literature citations
Novel germline mutations in the PTEN tumour suppressor gene found in women with multiple cancers.
De Vivo I.; Gertig D.M.; Nagase S.; Hankinson S.E.; O'Brien R.; Speizer F.E.; Parsons R.; Hunter D.J.;
J. Med. Genet. 37:336-341(2000)
Cited for: VARIANTS MULTIPLE CANCERS LEU-119 AND LEU-158;

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.