UniProtKB/Swiss-Prot P60484 : Variant p.Leu57Trp
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information
Variant position:
57
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 Leucine (L) to Tryptophan (W) at position 57 (L57W, p.Leu57Trp).
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 medium size and hydrophobic (L) to large size and aromatic (W)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-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:
In glioma; loss of protein phosphatase activity.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
57
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:
FPAERLEGVYRNNIDDVVRF
L DSKHKNHYKIYNLCAERHYD
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 FPAERLEGVYRNNIDDVVRFL DSKH-KNHYKIYNLCAERH-YD
FPAERLEGVYRNNIDDVVRFL DSKH-KNHYKIYNLCAERH-
Mouse FPAERLEGVYRNNIDDVVRFL DSKH-KNHYKIYNLCAERH-
Rat FPAERLEGVYRNNIDDVVRFL DSKH-KNHYKIYNLCAERH-
Xenopus laevis FPAERLEGVYRNNIDDVVRFL DSKH-KNHYKIYNLCAERH-
Caenorhabditis elegans YPATGIEANFRNSKVQTQQFL TRRHGKGNVKVFNLRGGYY-
Slime mold FPSEKVEGVFRNPMKDVQRFL DQYH-KDHFKVYNLCSERV-
Fission yeast TPAAGIHKLYRNDELDVFKYL TTQL-KDNWILLNLCAEETV
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
Alternative sequence
55 – 70
RFLDSKHKNHYKIYNL -> S. In isoform 3.
Helix
50 – 60
Literature citations
Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers.
Steck P.A.; Pershouse M.A.; Jasser S.A.; Lin H.; Yung W.K.A.; Ligon A.H.; Langford L.A.; Baumgard M.L.; Hattier T.; Davis T.; Frye C.; Hu R.; Swedlund B.; Teng D.H.-F.; Tavtigian S.V.;
Nat. Genet. 15:356-363(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); TISSUE SPECIFICITY; VARIANTS GLIOMA SER-15; GLU-36; ARG-42; TRP-57 AND THR-319 DEL;
P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase.
Myers M.P.; Stolarov J.P.; Eng C.; Li J.; Wang S.I.; Wigler M.H.; Parsons R.; Tonks N.K.;
Proc. Natl. Acad. Sci. U.S.A. 94:9052-9057(1997)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS GLIOMA TRP-57; ENDOMETRIAL CANCER TYR-123; GLIOBLASTOMA ARG-129; CWS1 ARG-129; PROSTATE CANCER LEU-134; GLIOBLASTOMA ARG-165; BREAST CANCER PRO-167 AND BZ ARG-170;
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.