UniProtKB/Swiss-Prot P60484: Variant p.Gly20Glu

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

20 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Glutamate (E) at position 20 (G20E, p.Gly20Glu). 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 acidic (E) 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:

Reduced phosphatase activity towards Ins(1,3,4,5)P4; retains phosphatase activity towards PtdIns(3,4,5)P3. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1064795967 [ dbSNP | Ensembl ]

Sequence information Variant position:

20 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:

MTAIIKEIVSRNKRRYQED G FDLDLTYIYPNIIAMGFPAE 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                         MTAIIKEIVSRNKRRYQEDGFD-----LDLTYIYPNIIAMGFPAE

                              MTAIIKEIVSRNKRRYQEDGFD-----LDLTYIYPNIIAM

Mouse                         MTAIIKEIVSRNKRRYQEDGFD-----LDLTYIYPNIIAM

Rat                           MTAIIKEIVSRNKRRYQEDGFD-----LDLTYIYPNIIAM

Xenopus laevis                MTAIIKEFVSRNKRRYQEDGFD-----LDLTYIYPNIIAM

Caenorhabditis elegans        IRHIFRTAVSSNRCRTEYQNID-----LDCAYITDRIIAI

Slime mold                    MSNLLRVAVSKQKRRYQKNGYD-----LDLAYITDNIVAM

Fission yeast                 -MNILRSVVSRGRKGLKQEKVNRSFAYLDMVYITSKVIAM

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
Initiator methionine	1 – 1	Removed
Chain	2 – 403	Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Domain	14 – 185	Phosphatase tensin-type
Modified residue	2 – 2	N-acetylthreonine
Cross	13 – 13	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence	1 – 1	M -> MERGGEAAAAAAAAAAAPGRGSESPVTISRAGNAGELVSPLLLPPTRRRRRRHIQGPGPVLNLPSAAAAPPVARAPEAAGGGSRSEDYSSSPHSAAAAARPLAAEEKQAQSLQPSSSRRSSHYPAAVQSQAAAERGASATAKSRAISILQKKPRHQQLLPSLSSFFFSHRLPDM. In isoform alpha.
Mutagenesis	1 – 1	M -> I. Prevents expression of isoform 1 and increased expression of isoform alpha.
Mutagenesis	13 – 13	K -> E. Nuclear. Cytoplasmic; when associated with E-289. Shows less tumor suppressive ability; when associated with E-289.
Turn	19 – 22

Literature citations
Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay.
Han S.-Y.; Kato H.; Kato S.; Suzuki T.; Shibata H.; Ishii S.; Shiiba K.; Matsuno S.; Kanamaru R.; Ishioka C.;
Cancer Res. 60:3147-3151(2000)
Cited for: CHARACTERIZATION OF VARIANTS ASN-10; CYS-16; GLU-20; SER-27; ARG-61; HIS-68; ARG-112; PRO-121; ARG-129; GLY-130; ILE-133; LEU-134; ARG-165; ASN-170; CYS-173; HIS-173; PRO-173; ASN-174; PHE-227; CYS-251; GLN-345; GLY-369 AND ILE-401; CHARACTERIZATION OF VARIANTS CWS1 TYR-71; TYR-93; PHE-105; TYR-107; PRO-112; ARG-124; GLU-129; LEU-130; GLN-130; TYR-136; CYS-155; ARG-170; GLU-289; GLY-331; VAL-341; ASN-342; GLU-343 AND LEU-347;

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.