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| Gene Symbol | PTEN | ||||||||||
| Synonyms | 10q23del | BZS | CWS1 | DEC | GLM2 | MHAM | MMAC1 | PTEN1 | PTENbeta | TEP1 | ||||||||||
| Gene Description | PTEN, phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN, is a tumor suppressor (PMID: 30562755) with roles in the cell cycle, growth, DNA repair, cell survival and regulation of the Akt-mTOR pathway (PMID: 24656806, PMID: 30145641). PTEN germline mutations are common in Cowden syndrome (PMID: 30562755) and PTEN somatic alterations resulting in loss of function have been found in many types of cancer including, but not limited to endometrial (PMID: 30142194), melanoma (PMID: 30148988), and prostate (PMID: 18767981, PMID: 30153654). | ||||||||||
| ACMG Incidental List v3.0: |
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| Variant | Impact | Protein Effect | Variant Description | Associated with drug Resistance |
|---|---|---|---|---|
| A120T | missense | unknown | PTEN A120T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A120T has been identified in sequencing studies (PMID: 23633456, PMID: 25424851), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| A121E | missense | loss of function | PTEN A121E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A121E demonstrates loss of phosphatase activity in yeast (PMID: 21828076), reduced Pten protein stability, failure to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| A121P | missense | loss of function | PTEN A121P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A121P demonstrates loss of phosphatase activity in an in-vitro assay (PMID: 10866302) and reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| A121T | missense | unknown | PTEN A121T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A121T has been identified in the scientific literature (PMID: 24336570), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| A121V | missense | no effect - predicted | PTEN A121V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A121V demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| A126D | missense | loss of function | PTEN A126D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126D demonstrates Pten protein stability similar to wild-type protein (PMID: 32366478, PMID: 32350270), however, results in a loss of phosphatase activity in yeast (PMID: 21828076), loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270), and is associated with homologous recombination deficiency in a patient sample (PMID: 29246904). | |
| A126fs | frameshift | loss of function - predicted | PTEN A126fs results in a change in the amino acid sequence of the Pten protein beginning at 126 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). A126fs has not been characterized, however, due to the effects of other truncation mutations downstream of A126 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| A126G | missense | loss of function | PTEN A126G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126G confers a loss of function to the Pten protein as demonstrated by a shift in substrate specificity of Pten from 3- to 5-phosphatase (PMID: 29987362), an inability to regulate Pi3k/Akt signaling, and increased cell proliferation and transformation in culture (PMID: 26504226). | |
| A126P | missense | loss of function | PTEN A126P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126P demonstrates loss of phosphatase activity (PMID: 26504226) and reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| A126S | missense | loss of function | PTEN A126S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126S results in a loss of Pten phosphatase activity in culture and reduced inhibition of Pi3k activity in yeast (PMID: 26504226, PMID: 21828076). | |
| A126T | missense | unknown | PTEN A126T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126T is predicted to lead to a collapsed P loop formation incapable of interacting with the WPD loop resulting in dehydration of the catalytic site (Cancer Res (2023) 83 (7_Supplement): 3845), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| A126V | missense | loss of function | PTEN A126V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A126V results in a loss of Pten phosphatase activity in cell culture and loss of Pi3k inhibition in yeast (PMID: 21828076, PMID: 26504226). | |
| A151P | missense | loss of function | PTEN A151P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A151P demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| A309S | missense | unknown | PTEN A309S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). A309S demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, however, leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| A328fs | frameshift | loss of function - predicted | PTEN A328fs results in a change in the amino acid sequence of the Pten protein beginning at aa 328 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). A328fs has not been characterized, however, due to the effects of other truncation mutations downstream of A328 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| A34D | missense | loss of function | PTEN A34D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A34D results in a loss of phosphatase activity in yeast and loss of nuclear localization in cell culture (PMID: 21828076, PMID: 25875300), and demonstrates reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| A34P | missense | loss of function | PTEN A34P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A34P demonstrates reduced Pten protein stability, fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| A39P | missense | loss of function - predicted | PTEN A39P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A39P fails to inhibit Akt phosphorylation in cell culture (PMID: 25527629), and therefore, is predicted to lead to a loss of Pten protein function. | |
| A72fs | frameshift | loss of function - predicted | PTEN A72fs results in a change in the amino acid sequence of the Pten protein beginning at aa 72 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). A72fs results in lack of protein expression in culture (PMID: 21358673), and due to the effects of other truncation mutations downstream of A72 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| A79T | missense | unknown | PTEN A79T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). A79T demonstrates Pten protein stability (PMID: 32366478, PMID: 32350270), suppression of Akt phosphorylation (PMID: 32350270), and cell proliferation and viability levels similar to wild-type Pten in culture (PMID: 29533785), however, fails to rescue spheroid formation (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| C105F | missense | loss of function | PTEN C105F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105F results in a loss of Pten phosphatase activity and is unable to suppress cell proliferation in culture (PMID: 9823298). | |
| C105G | missense | loss of function - predicted | PTEN C105G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C105R | missense | unknown | PTEN C105R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105R has been identified in the scientific literature (PMID: 17219201), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| C105S | missense | unknown | PTEN C105S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105S has been identified in the scientific literature (PMID: 11916965), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| C105W | missense | loss of function - predicted | PTEN C105W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105W results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C105Y | missense | loss of function | PTEN C105Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C105Y results in a loss of Lkb1 binding in the context of an N-terminal truncated Pten protein in a yeast two-hybrid assay (PMID: 15987703), and reduced lipid and protein phosphatase activities of Pten in an in vitro assays (PMID: 34561453). | |
| C124F | missense | loss of function - predicted | PTEN C124F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124F results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C124fs | frameshift | loss of function - predicted | PTEN C124fs results in a change in the amino acid sequence of the Pten protein beginning at 124 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). C124fs has not been characterized, however, due to the effects of other truncation mutations downstream of C124 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| C124G | missense | loss of function | PTEN C124G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124G results in a loss of Pten phosphatase activity and is unable to suppress cell proliferation in culture (PMID: 9823298). | |
| C124L | missense | loss of function - predicted | PTEN C124L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C124N | missense | loss of function - predicted | PTEN C124N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124N results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C124R | missense | loss of function | PTEN C124R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124R demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation in cell culture (PMID: 32366478), and results in a loss of Pten phosphatase activity, and contributes to tumorigenesis in transgenic animal models (PMID: 10866302, PMID: 20194734). | |
| C124S | missense | loss of function | PTEN C124S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124S demonstrates Pten protein stability similar to wild-type protein, however, does not rescue spheroid formation (PMID: 32366478), demonstrates loss of phosphatase activity (PMID: 9256433, PMID: 22413754, PMID: 25263454), and fails to suppress cell proliferation and migration in culture (PMID: 17213812, PMID: 25263454, PMID: 34943931). | |
| C124W | missense | unknown | PTEN C124W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124W has been identified in the scientific literature (PMID: 29706350), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| C124Y | missense | unknown | PTEN C124Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C124Y has been identified in sequencing studies (PMID: 12695913, PMID: 37686092), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| C136F | missense | loss of function | PTEN C136F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C136F confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and increased transformation ability in two different cell lines (PMID: 29533785). | |
| C136fs | frameshift | loss of function - predicted | PTEN C136fs results in a change in the amino acid sequence of the Pten protein beginning at aa 136 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). C136fs has not been characterized, however, due to the effects of other truncation mutations downstream of C136 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| C136R | missense | loss of function | PTEN C136R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C136R confers a loss of function on the Pten protein as demonstrated by increased proteasome-mediated degradation of Pten protein, activation of Akt and Erk signaling in cell culture (PMID: 23475934), and by increased transformation ability in two different cell lines, as compared to wild-type Pten (PMID: 29533785). | |
| C136W | missense | loss of function - predicted | PTEN C136W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C136W results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C136Y | missense | loss of function | PTEN C136Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C136Y confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350), and failure to suppress phosphorylation of Pdk1, Akt, and Gsk3beta in cultured cells (PMID: 32704382). | |
| C211* | nonsense | loss of function - predicted | PTEN C211* results in a premature truncation of the Pten protein at amino acid 211 of 403 (UniProt.org). C211* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C211W | missense | loss of function - predicted | PTEN C211W lies within the C2 tensin-type domain of the Pten protein (UniProt.org). C211W leads to developmental growth similar to wild-type Pten in flies, however, demonstrates reduced Pten protein stability and impaired suppression of Akt phosphorylation in cell culture (PMID: 32350270), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C211Y | missense | unknown | PTEN C211Y lies within the C2 tensin-type domain of the Pten protein (UniProt.org). C211Y has been identified in the scientific literature (PMID: 28027320), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| C218* | nonsense | loss of function - predicted | PTEN C218* results in a premature truncation of the Pten protein at amino acid 218 of 403 (UniProt.org). C218* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C250fs | frameshift | loss of function - predicted | PTEN C250fs results in a change in the amino acid sequence of the Pten protein beginning at 250 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). C250fs has not been characterized, however, due to the effects of other truncation mutations downstream of C250 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| C71F | missense | unknown | PTEN C71F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C71F has been identified in sequencing studies (PMID: 30181556), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| C71W | missense | loss of function - predicted | PTEN C71W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C71W results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C71Y | missense | loss of function - predicted | PTEN C71Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). C71Y results in loss of phosphatase activity in an in vitro assay (PMID: 11051241), and therefore, is predicted to lead to a loss of Pten protein function. | |
| C83* | nonsense | loss of function - predicted | PTEN C83* results in a premature truncation of the Pten protein at amino acid 83 of 403 (UniProt.org). C83* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D107G | missense | loss of function | PTEN D107G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D107G demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| D107H | missense | unknown | PTEN D107H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D107H has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| D107N | missense | unknown | PTEN D107N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D107N has been identified in the scientific literature (PMID: 27221918, PMID: 26462025, PMID: 26800850), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| D107V | missense | loss of function | PTEN D107V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D107V demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| D107Y | missense | loss of function | PTEN D107Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D107Y confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay and a yeast assay (PMID: 29706350, PMID: 10866302). | |
| D109* | nonsense | loss of function - predicted | PTEN D109* results in a premature truncation of the Pten protein at amino acid 109 of 403 (UniProt.org). D109* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D109fs | frameshift | loss of function - predicted | PTEN D109fs results in a change in the amino acid sequence of the Pten protein beginning at aa 109 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). D109fs has not been characterized, however, due to the effects of other truncation mutations downstream of D109 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| D109N | missense | unknown | PTEN D109N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D109N retains Akt phosphorylation and results in mRNA expression similar to wild-type Pten but demonstrates reduced protein expression in a patient sample in the context of a G36R mutation (PMID: 36591942), but has not been individually characterized, and therefore, its effect on protein function is unknown. | |
| D115Y | missense | unknown | PTEN D115Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D115Y has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| D116fs | frameshift | loss of function - predicted | PTEN D116fs results in a change in the amino acid sequence of the Pten protein beginning at 116 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). D116fs has not been characterized, however, due to the effects of other truncation mutations downstream of D116 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| D162del | deletion | loss of function - predicted | PTEN D162del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 162 (UniProt.org). D162del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D162G | missense | no effect - predicted | PTEN D162G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D162G demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| D162H | missense | no effect | PTEN D162H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D162H demonstrates protein stability and inhibition of Akt signaling, similar to levels of wild-type Pten protein in cell culture (PMID: 23840064). | |
| D162Y | missense | loss of function - predicted | PTEN D162Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D162Y results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D22E | missense | loss of function | PTEN D22E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D22E demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| D24del | deletion | loss of function - predicted | PTEN D24del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 24 (UniProt.org). D24del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D24E | missense | unknown | PTEN D24E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24E has been identified in sequencing studies (PMID: 32187361), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| D24G | missense | loss of function | PTEN D24G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24G confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and increased transformation ability in two different cell lines (PMID: 29533785). | |
| D24H | missense | loss of function - predicted | PTEN D24H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24H results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and results in abnormal cellular localization and loss of PI3K/AKT/MTOR pathway inhibition, as indicated by increased expression of S6rp in patient samples (PMID: 30626916), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D24N | missense | loss of function | PTEN D24N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24N retains phosphatase activity, but has aberrant nuclear localization and fails to inhibit Akt phosphorylation, cell proliferation, and transformation in cell culture (PMID: 17213812) and therefore, confers a loss of function to the Pten protein. | |
| D24V | missense | loss of function | PTEN D24V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24V confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and increased phosphorylation of Akt and S6rp in culture (PMID: 24498881). | |
| D24Y | missense | loss of function | PTEN D24Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D24Y confers a loss of function to the Pten protein, as demonstrated by loss of phosphatase activity and reduced nuclear localization in cell culture (PMID: 25875300, PMID: 17213812). | |
| D252G | missense | loss of function | PTEN D252G lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D252G demonstrates reduced lipid phosphatase activity in a yeast assay and in cell culture (PMID: 21828076, PMID: 25527629, PMID: 29373119), decreased Pten protein stability (PMID: 25527629, PMID: 29706633, PMID: 32350270), and results in impaired nuclear localization, and failure to regulate neuronal growth (PMID: 29373119), and loss of ability to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| D252V | missense | loss of function - predicted | PTEN D252V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D252V results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D252Y | missense | loss of function | PTEN D252Y lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D252Y results in reduced phosphatase activity in a yeast assay (PMID: 29706350) and reduced stability of the Pten protein resulting in decreased expression in culture (PMID: 17942903). | |
| D268E | missense | no effect | PTEN D268E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D268E demonstrates Pten protein stability (PMID: 32350270, PMID: 32366478), ability to rescue spheroid formation (PMID: 32366478), and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, and leads to normal developmental growth in flies (PMID: 32350270). | |
| D268Gfs*30 | frameshift | loss of function - predicted | PTEN D268Gfs*30 indicates a shift in the reading frame starting at amino acid 268 and terminating 30 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). D268Gfs*30 has not been characterized, however, due to the effects of other truncation mutations downstream of D268 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| D301N | missense | no effect - predicted | PTEN D301N lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D301N demonstrates inhibition of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 19329485), and therefore, is predicted to have no effect on Pten protein function. | |
| D324del | deletion | loss of function - predicted | PTEN D324del results in the deletion of an amino acid in the C2 tensin-type domain of the Pten protein at amino acid 324 (UniProt.org). D324del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D326* | nonsense | loss of function - predicted | PTEN D326* results in a premature truncation of the Pten protein at amino acid 326 of 403 (UniProt.org). D326* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D326H | missense | loss of function - predicted | PTEN D326H lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D326H results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D326N | missense | loss of function | PTEN D326N lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D326N demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478), and reduced protein stability in other studies (PMID: 32350270, PMID: 25527629), and fails to rescue spheroid formation in cell culture (PMID: 32366478), and results in moderately decreased phosphatase activity in yeast (PMID: 21828076). | |
| D326Y | missense | loss of function - predicted | PTEN D326Y lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D326Y results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D331fs | frameshift | loss of function - predicted | PTEN D331fs results in a change in the amino acid sequence of the Pten protein beginning at 331 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). D331fs has not been characterized, however, due to the effects of other truncation mutations downstream of D331 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| D331G | missense | unknown | PTEN D331G lies within the C2 tensin-type domain of the Pten protein (UniProt.org). D331G results in reduced protein stability and decreased phosphatase activity (PMID: 10866302), but demonstrates growth inhibition similar to wild-type Pten in cell culture (PMID: 11156408), and maintains suppression of E2f1-mediated transcripts (PMID: 29108454), and therefore, its effect on Pten protein function is unknown. | |
| D331Tfs*13 | frameshift | loss of function - predicted | PTEN D331Tfs*13 indicates a shift in the reading frame starting at amino acid 331 and terminating 13 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). D331Tfs*13 has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D52del | deletion | loss of function - predicted | PTEN D52del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 52 (UniProt.org). D52del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D77* | nonsense | loss of function - predicted | PTEN D77* results in a premature truncation of the Pten protein at amino acid 77 of 403 (UniProt.org). D77* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| D92A | missense | loss of function | PTEN D92A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92A results in a loss of Pten phosphatase activity in yeast (PMID: 21828076) and demonstrates impaired dephosphorylation of FAK in cell culture (PMID: 10400703). | |
| D92E | missense | loss of function | PTEN D92E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92E confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| D92G | missense | loss of function | PTEN D92G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92G confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| D92H | missense | loss of function | PTEN D92H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92H confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| D92N | missense | unknown | PTEN D92N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92N demonstrates Pten protein stability in cell culture (PMID: 32366478) and phosphatase activity in a yeast assay (PMID: 21828076) similar to wild-type Pten, however, in a Drosophila wing overgrowth assay demonstrates loss of Pten activity (PMID: 34492006), and results in a partial loss of ability to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| D92V | missense | loss of function | PTEN D92V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92V confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| D92Y | missense | loss of function - predicted | PTEN D92Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). D92Y results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| dec exp | none | no effect | PTEN dec exp indicates decreased expression of the Pten protein and/or mRNA. However, the mechanism causing the decreased expression is unspecified. | |
| del | deletion | loss of function | PTEN del indicates a deletion of the PTEN gene. | |
| E106* | nonsense | loss of function - predicted | PTEN E106* results in a premature truncation of the Pten protein at amino acid 106 of 403 (UniProt.org). E106* has not been characterized, however, due to the effects of other truncation mutations downstream of E106 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E114* | nonsense | loss of function - predicted | PTEN E114* results in a premature truncation of the Pten protein at amino acid 114 of 403 (UniProt.org). E114* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E150* | nonsense | loss of function - predicted | PTEN E150* results in a premature truncation of the Pten protein at amino acid 150 of 403 (UniProt.org). E150* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E150K | missense | unknown | PTEN E150K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). E150K is predicted to affect the function of Pten by structural modeling (PMID: 31074114), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| E157* | nonsense | loss of function - predicted | PTEN E157* results in a premature truncation of the Pten protein at amino acid 157 of 403 (UniProt.org). E157* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E157G | missense | loss of function | PTEN E157G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). E157G demonstrates moderate decrease in phosphatase activity in yeast (PMID: 21828076), and leads to reduced Pten protein stability, fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| E18* | nonsense | loss of function - predicted | PTEN E18* results in a premature truncation of the Pten protein at amino acid 18 of 403 (UniProt.org). E18* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E18G | missense | unknown | PTEN E18G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). E18G results in mRNA and protein expression similar to wild-type Pten in culture but leads to a loss of phosphatase activity as indicated by loss of Akt phosphorylation and reduced expression in a patient sample in the context of a C105F mutation (PMID: 36591942), but has not been individually characterized, and therefore, its effect on protein function is unknown. | |
| E201* | nonsense | loss of function - predicted | PTEN E201* results in a premature truncation of the Pten protein at amino acid 201 of 403 (UniProt.org). E201* has not been characterized, however, due to the effects of other truncation mutations downstream of E201 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E235* | nonsense | loss of function - predicted | PTEN E235* results in a premature truncation of the Pten protein at amino acid 235 of 403 (UniProt.org). E235* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E242* | nonsense | loss of function - predicted | PTEN E242* results in a premature truncation of the Pten protein at amino acid 242 of 403 (UniProt.org). E242* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E242fs | frameshift | loss of function - predicted | PTEN E242fs results in a change in the amino acid sequence of the Pten protein beginning at 242 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). E242fs has not been characterized, however, due to the effects of other truncation mutations downstream of E242 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E242K | missense | unknown | PTEN E242K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E242K has been identified in sequencing studies (PMID: 15069681), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E256* | nonsense | loss of function - predicted | PTEN E256* results in a premature truncation of the Pten protein at amino acid 256 of 403 (UniProt.org). E256* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E256K | missense | unknown | PTEN E256K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E256K results in suppression of Akt phosphorylation similar to wild-type Pten, however, demonstrates reduced Pten protein stability in cell culture, and leads to delayed developmental growth in flies (PMID: 32350270), but results in gain of Pten protein function in a Drosophila wing overgrowth assay (PMID: 34492006), and therefore, its effect on Pten protein function is unknown. | |
| E256Q | missense | unknown | PTEN E256Q lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E256Q has been identified in sequencing studies (PMID: 23633456), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E284* | nonsense | loss of function - predicted | PTEN E284* results in a premature truncation of the Pten protein at amino acid 284 of 403 (UniProt.org). E284* has not been characterized, however, due to the effects of other truncation mutations downstream of E284 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E284fs | frameshift | loss of function - predicted | PTEN E284fs results in a change in the amino acid sequence of the Pten protein beginning at aa 284 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). E284fs has not been characterized, however, due to the effects of other truncation mutations downstream of E284 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E285* | nonsense | loss of function - predicted | PTEN E285* results in a premature truncation of the Pten protein at amino acid 285 of 403 (UniProt.org). E285* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E285K | missense | unknown | PTEN E285K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E285K has been identified in sequencing studies (PMID: 25148578), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E288* | nonsense | loss of function - predicted | PTEN E288* results in a premature truncation of the Pten protein at amino acid 288 of 403 (UniProt.org). E288* has not been characterized, however, due to the effects of other truncation mutations downstream of E288 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E288fs | frameshift | loss of function - predicted | PTEN E288fs results in a change in the amino acid sequence of the Pten protein beginning at aa 288 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). E288fs has not been characterized, however, due to the effects of other truncation mutations downstream of E288 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E288K | missense | unknown | PTEN E288K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E288K has been identified in sequencing studies (PMID: 10955808), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E291* | nonsense | loss of function - predicted | PTEN E291* results in a premature truncation of the Pten protein at amino acid 291 of 403 (UniProt.org). E291* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E291Gfs*7 | frameshift | loss of function - predicted | PTEN E291Gfs*7 indicates a shift in the reading frame starting at amino acid 291 and terminating 7 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). E291Gfs*7 results in loss of Pten expression in cell culture (PMID: 35012940), and based on the effects of other truncation mutations downstream of E291 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E291K | missense | unknown | PTEN E291K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E291K has been identified in sequencing studies (PMID: 15923161, PMID: 17924977), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E299* | nonsense | loss of function - predicted | PTEN E299* results in a premature truncation of the Pten protein at amino acid 299 of 403 (UniProt.org). E299* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E307* | nonsense | loss of function - predicted | PTEN E307* results in a premature truncation of the Pten protein at amino acid 307 of 403 (UniProt.org). E307* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E307K | missense | unknown | PTEN E307K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E307K results in similar phosphatase activity as wild-type Pten, but leads to increased polyubiquitination and membrane localization, and decreased nuclear localization of Pten in cell culture (PMID: 22103913), and therefore, its effect on Pten protein function is unknown. | |
| E314* | nonsense | loss of function - predicted | PTEN E314* results in a premature truncation of the Pten protein at amino acid 314 of 403 (UniProt.org). E314* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E314V | missense | unknown | PTEN E314V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). E314V has been identified in the scientific literature (PMID: 29785012, PMID: 29706350), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| E43* | nonsense | loss of function - predicted | PTEN E43* results in a premature truncation of the Pten protein at amino acid 43 of 403 (UniProt.org). E43* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E43fs | frameshift | loss of function - predicted | PTEN E43fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 43 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). E43fs has not been characterized, however, due to the effects of other truncation mutations downstream of E43 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E7* | nonsense | loss of function - predicted | PTEN E7* results in a premature truncation of the Pten protein at amino acid 7 of 403 (UniProt.org). E7* has not been characterized, however, due to the effects of other truncation mutations downstream of E7 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| E73K | missense | loss of function | PTEN E73K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). E73K leads to normal developmental growth in flies, but demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270). | |
| E91* | nonsense | loss of function - predicted | PTEN E91* results in a premature truncation of the Pten protein at amino acid 91 of 403 (UniProt.org). E91* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| E99* | nonsense | loss of function - predicted | PTEN E99* results in a premature truncation of the Pten protein at amino acid 99 of 403 (UniProt.org). E99* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| F145* | nonsense | loss of function - predicted | PTEN F145* results in a premature truncation of the Pten protein at amino acid 145 of 403 (UniProt.org). F145* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| F154L | missense | loss of function | PTEN F154L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F154L confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and failure to inhibit Akt phosphorylation in cell culture (PMID: 19329485). | |
| F21A | missense | loss of function | PTEN F21A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F21A retains lipid phosphatase activity (PMID: 25875300, PMID: 17213812), but aberrantly localizes to the nucleus and fails to inhibit Akt phosphorylation and cell proliferation in culture (PMID: 17213812) and therefore, confers a loss of function on the Pten protein. | |
| F241fs | frameshift | loss of function - predicted | PTEN F241fs results in a change in the amino acid sequence of the Pten protein beginning at 241 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). F241fs has not been characterized, however, due to the effects of other truncation mutations downstream of F241 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| F241L | missense | unknown | PTEN F241L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F241L has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| F241S | missense | loss of function | PTEN F241S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F241S demonstrates loss of phosphatase activity (PMID: 21828076, PMID: 29373119), and decreased nuclear localization (PMID: 29373119), and reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| F257L | missense | unknown | PTEN F257L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F257L has been identified in the scientific literature (PMID: 29706350), but has not been biochemically characterized and therefore, its effect Pten protein function is unknown (PubMed, Oct 2023). | |
| F271S | missense | loss of function | PTEN F271S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F271S confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and failure to suppress E2f1-mediated transcription in cultured cells (PMID: 29108454). | |
| F278Lfs*12 | frameshift | loss of function - predicted | PTEN F278Lfs*12 indicates a shift in the reading frame starting at amino acid 278 and terminating 12 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). F278Lfs*12 has not been characterized, however, due to the effects of other truncation mutations downstream of F278 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| F279I | missense | unknown | PTEN F279I lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F279I demonstrates reduced Pten protein stability, however, results in suppression of Akt phosphorylation similar to wild-type Pten in cell culture, and leads to normal developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| F279L | missense | unknown | PTEN F279L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F279L results in suppression of Akt phosphorylation similar to wild-type Pten, however, demonstrates reduced Pten protein stability in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| F337fs | frameshift | loss of function - predicted | PTEN F337fs results in a change in the amino acid sequence of the Pten protein beginning at 337 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). F337fs has not been characterized, however, due to the effects of other truncation mutations downstream of F337 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| F341C | missense | unknown | PTEN F341C lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F341C has been identified in the scientific literature (PMID: 35252866), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| F341V | missense | loss of function | PTEN F341V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F341V results in a loss of Pten phosphatase activity in an in vitro assay (PMID: 11051241) and loss of binding to PICT-1 (PMID: 15355975). | |
| F347L | missense | loss of function - predicted | PTEN F347L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). F347L is predicted to confer a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302). | |
| F56C | missense | loss of function | PTEN F56C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F56C demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270). | |
| F56fs | frameshift | loss of function - predicted | PTEN F56fs results in a change in the amino acid sequence of the Pten protein beginning at aa 56 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). F56fs has not been characterized, however, due to the effects of other truncation mutations downstream of F56 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| F56S | missense | loss of function - predicted | PTEN F56S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F56S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| F56V | missense | unknown | PTEN F56V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F56V has been identified in sequencing studies (PMID: 18757403, PMID: 11395387), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| F90Lfs*90 | frameshift | loss of function - predicted | PTEN F90Lfs*90 indicates a shift in the reading frame starting at amino acid 90 and terminating 90 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). F90Lfs*90 has not been characterized, however, due to the effects of other truncation mutations downstream of F90 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| F90S | missense | loss of function | PTEN F90S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). F90S demonstrates phosphatase activity comparable to wild-type Pten however, F90S results in reduced membrane localization of the Pten protein due to impaired binding with membrane lipids (PMID: 25448479, PMID: 25263454) and subsequently, is unable to prevent Akt signaling, cell proliferation, and cell migration and therefore, confers a loss of function to the Pten protein (PMID: 25263454). | |
| fusion | fusion | unknown | PTEN fusion indicates a fusion of the PTEN gene, but the fusion partner is unknown. | |
| G127* | nonsense | loss of function - predicted | PTEN G127* results in a premature truncation of the Pten protein at amino acid 127 of 403 (UniProt.org). G127* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G127E | missense | loss of function | PTEN G127E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G127E retains Pten protein expression in a patient sample (PMID: 32610572), but demonstrates loss of phosphatase activity in a yeast assay (PMID: 21828076, PMID: 29706350). | |
| G127N | missense | loss of function | PTEN G127N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G127N confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| G127R | missense | loss of function | PTEN G127R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G127R demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), however, results in a loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and delays development in flies (PMID: 32350270), increased transformation ability in two different cell lines (PMID: 29533785), and results in a gene expression profile similar to G129E loss of function mutation (PMID: 27147599). | |
| G127V | missense | unknown | PTEN G127V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G127V demonstrates a gene expression profile that correlates with a PTEN loss-of-function variant (PMID: 27147599), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| G129* | nonsense | loss of function - predicted | PTEN G129* results in a premature truncation of the Pten protein at amino acid 129 of 403 (UniProt.org). G129* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G129A | missense | no effect - predicted | PTEN G129A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G129A demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| G129D | missense | loss of function | PTEN G129D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G129D confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| G129E | missense | loss of function | PTEN G129E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G129E demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), retains protein phosphatase activity (PMID: 9256433, PMID: 9811831), however, demonstrates loss of lipid phosphatase activity in in vitro assays (PMID: 9811831), loss of ability to rescue spheroid formation (PMID: 32366478), fails to suppress Akt phosphorylation in cell culture, and delays development in flies (PMID: 32350270), and is unable to inhibit cell survival and proliferation in culture (PMID: 9811831, PMID: 9823298). | |
| G129R | missense | loss of function | PTEN G129R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G129R confers a loss of function to the Pten protein, as demonstrated by loss of phosphatase activity (PMID: 9256433, PMID: 9823298), reduced protein stability and failure to rescue spheroid formation (PMID: 32366478), and is unable to suppress cell proliferation and inhibit cell growth in culture (PMID: 9823298). | |
| G129V | missense | loss of function | PTEN G129V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G129V confers a loss of function to the Pten protein, as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076) and induction of a gene expression signature distinct from wild-type Pten (PMID: 27147599). | |
| G132A | missense | unknown | PTEN G132A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G132A has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| G132C | missense | loss of function - predicted | PTEN G132C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G132C results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G132D | missense | loss of function | PTEN G132D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G132D demonstrates Pten protein stability similar to wild-type in one study (PMID: 32366478) and reduced protein stability in others (PMID: 32350270, PMID: 37907589), however, fails to suppress Akt phosphorylation (PMID: 32350270, PMID: 37907589), does not rescue spheroid formation in PTEN null cells in culture (PMID: 32366478), increases proliferation rate, and decreases apoptosis in culture (PMID: 37907589). | |
| G132del | deletion | loss of function - predicted | PTEN G132del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 132 (UniProt.org). G132del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G132S | missense | loss of function - predicted | PTEN G132S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G132S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G132V | missense | loss of function - predicted | PTEN G132V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G132V results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G143fs | frameshift | loss of function - predicted | PTEN G143fs results in a change in the amino acid sequence of the Pten protein beginning at 143 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). G143fs has not been characterized, however, due to the effects of other truncation mutations downstream of G143 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| G156R | missense | unknown | PTEN G156R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G156R has been identified in sequencing studies (PMID: 11123721, PMID: 27531351), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| G156V | missense | loss of function - predicted | PTEN G156V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G156V results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G156W | missense | loss of function - predicted | PTEN G156W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G156W results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G165* | nonsense | loss of function - predicted | PTEN G165* results in a premature truncation of the Pten protein at amino acid 165 of 403 (UniProt.org). G165* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G165E | missense | loss of function | PTEN G165E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G165E confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| G165R | missense | loss of function - predicted | PTEN G165R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G165R results in suppression of Akt signaling similar to wild-type Pten in cell culture (PMID: 32704382), but results in a loss of phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G165V | missense | loss of function | PTEN G165V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G165V confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| G20E | missense | loss of function | PTEN G20E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G20E retains some, if not all, phosphatase activity compared to wild-type Pten (PMID: 10866302, PMID: 25263454, PMID: 17213812), however, G20E results in reduced membrane localization of the Pten protein due to impaired binding with membrane lipids, and subsequently, is unable to prevent Akt signaling, cell proliferation (PMID: 17213812), and cell migration and therefore, confers a loss of function to the Pten protein (PMID: 25263454). | |
| G230* | nonsense | loss of function - predicted | PTEN G230* results in a premature truncation of the Pten protein at amino acid 230 of 403 (UniProt.org). G230* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G251A | missense | unknown | PTEN G251A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G251A has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| G251C | missense | loss of function | PTEN G251C lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G251C results in a loss of Pten phosphatase activity and is unable to suppress Akt activation and cell proliferation in culture (PMID: 11156408, PMID: 10866302). | |
| G251D | missense | unknown | PTEN G251D lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G251D is associated with decreased Pten protein level and increased phosphorylation of Akt and S6 in a patient tumor sample (PMID: 25003235), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| G251del | deletion | unknown | PTEN G251del results in the deletion of an amino acid in the C2 tensin-type domain of the Pten protein at amino acid 251 (UniProt.org). G251del has been identified in the scientific literature (PMID: 35171658), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| G251S | missense | unknown | PTEN G251S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G251S has been identified in sequencing studies (PMID: 26010451), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| G251V | missense | loss of function - predicted | PTEN G251V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G251V has not been biochemically characterized, but results in increased transformation ability (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G251_D252del | deletion | unknown | PTEN G251_D252del results in the deletion of two amino acids in the C2 tensin-type domain of the Pten protein from amino acids 251 to 252 (UniProt.org). G251_D252del has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| G282* | nonsense | loss of function - predicted | PTEN G282* results in a premature truncation of the Pten protein at amino acid 282 of 403 (UniProt.org). G282* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G293* | nonsense | loss of function - predicted | PTEN G293* results in a premature truncation of the Pten protein at amino acid 293 of 403 (UniProt.org). G293* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G293fs | frameshift | loss of function - predicted | PTEN G293fs results in a change in the amino acid sequence of the Pten protein beginning at 293 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). G293fs has not been characterized, however, due to the effects of other truncation mutations downstream of G293 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| G293V | missense | unknown | PTEN G293V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). G293V has been identified in the scientific literature (PMID: 27194209, PMID: 30181556), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| G36* | nonsense | loss of function - predicted | PTEN G36* results in a premature truncation of the Pten protein at amino acid 36 of 403 (UniProt.org). G36* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| G36E | missense | loss of function | PTEN G36E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G36E demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| G36R | missense | loss of function | PTEN G36R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G36R results in impaired Pten nuclear localization (PMID: 25875300), loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| G44D | missense | loss of function | PTEN G44D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). G44D demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation in cell culture (PMID: 32366478), and demonstrates loss of phosphatase activity in a yeast assay (PMID: 21828076). | |
| H118fs | frameshift | loss of function - predicted | PTEN H118fs results in a change in the amino acid sequence of the Pten protein beginning at 118 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). H118fs has not been characterized, however, due to the effects of other truncation mutations downstream of H118 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| H118P | missense | loss of function | PTEN H118P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H118P demonstrates moderate loss of phosphatase activity in yeast and in an in-vitro assay (PMID: 21828076, PMID: 25527629), and reduced Pten protein stability (PMID: 25527629, PMID: 32350270), and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| H123D | missense | loss of function - predicted | PTEN H123D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H123D results in a loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H123L | missense | loss of function - predicted | PTEN H123L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H123L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H123P | missense | loss of function - predicted | PTEN H123P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H123P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H123Q | missense | loss of function | PTEN H123Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H123Q demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation in cell culture (PMID: 32366478), and demonstrates loss of phosphatase activity in a yeast assay (PMID: 21828076). | |
| H123R | missense | loss of function - predicted | PTEN H123R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H123R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H123Y | missense | unknown | PTEN H123Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). The functional effect of H123Y is conflicting as it results in increased Akt activation and cell survival in culture in one study (PMID: 11448956), but suppresses Akt signaling similar to wild-type Pten in another study (PMID: 32704382), and demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation (PMID: 32366478), and results in a loss of phosphatase activity (PMID: 9256433, PMID: 11448956, PMID: 29706350), and therefore, its effect on Pten protein function is unknown. | |
| H141P | missense | loss of function - predicted | PTEN H141P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H141P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H272P | missense | loss of function - predicted | PTEN H272P lies within the C2 tensin-type domain of the Pten protein (UniProt.org). H272P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H61D | missense | loss of function | PTEN H61D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61D results in a loss of Pten phosphatase activity in yeast (PMID: 21828076, PMID: 17942903) and has high protein instability (PMID: 17942903). | |
| H61K | missense | loss of function - predicted | PTEN H61K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H61L | missense | loss of function - predicted | PTEN H61L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H61N | missense | unknown | PTEN H61N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61N has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| H61P | missense | loss of function - predicted | PTEN H61P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H61R | missense | loss of function | PTEN H61R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61R confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350). | |
| H61Y | missense | unknown | PTEN H61Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H61Y has been identified in the scientific literature (PMID: 21470976, PMID: 18215105), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| H93D | missense | loss of function | PTEN H93D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93D confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| H93L | missense | loss of function - predicted | PTEN H93L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H93P | missense | loss of function - predicted | PTEN H93P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| H93Q | missense | loss of function | PTEN H93Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93Q demonstrates Pten protein stability similar to wild-type protein (PMID: 32350270, PMID: 32366478), however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), fails to suppress Akt phosphorylation in cell culture, and delays normal developmental growth in flies (PMID: 32350270), and demonstrates loss of phosphatase activity in yeast (PMID: 21828076). | |
| H93R | missense | unknown | PTEN H93R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93R results in phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), however, results in reduced catalytic activity (PMID: 25647146, PMID: 20718038), decreased suppression of TH (PMID: 26579216), enhanced membrane association and increased binding affinity to phosphatidylserine (PMID: 22505997, PMID: 20718038), and demonstrates reduced ability to dephosphorylate PIP3 in culture and is not able to rescue neuronal hypertrophy and pS6 signaling in PTEN-null animal models (PMID: 29373119), and therefore, its effect on Pten protein function is unknown. | |
| H93Y | missense | loss of function | PTEN H93Y lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). H93Y demonstrates loss of phosphatase activity (PMID: 10866302, PMID: 21828076), and increased Pten protein stability, but fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| I101F | missense | loss of function | PTEN I101F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I101F demonstrates protein stability similar to wild-type Pten, however, results in reduced ability to rescue spheroid formation in cell culture (PMID: 32366478) and reduced phosphatase activity in a yeast assay (PMID: 29706350). | |
| I101N | missense | loss of function - predicted | PTEN I101N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I101N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I101S | missense | loss of function - predicted | PTEN I101S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I101S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I101T | missense | loss of function | PTEN I101T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I101T confers a loss of function to the Pten protein as demonstrated by decreased lipid phosphatase activity (PMID: 32350270, PMID: 29608813), reduced protein stability (PMID: 32366478, PMID: 32350270, PMID: 29608813), enhanced polyubiquitination, decreased Pten phosphorylation at Threonine (T)-366, and reduced nuclear localization (PMID: 29608813), and fails to rescue spheroid formation in cell culture (PMID: 32366478). | |
| I122F | missense | loss of function - predicted | PTEN I122F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I122F results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I122fs | frameshift | loss of function - predicted | PTEN I122fs results in a change in the amino acid sequence of the Pten protein beginning at 122 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). I122fs has not been characterized, however, due to the effects of other truncation mutations downstream of I122 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| I122L | missense | loss of function - predicted | PTEN I122L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I122L results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I122N | missense | loss of function - predicted | PTEN I122N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I122N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I122S | missense | loss of function | PTEN I122S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I122S confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| I122V | missense | no effect - predicted | PTEN I122V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I122V demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| I135K | missense | loss of function | PTEN I135K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I135K confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 29706350) and failure to suppress phosphorylation of Pdk1, Akt, and Gsk3beta in cultured cells (PMID: 32704382). | |
| I135R | missense | loss of function | PTEN I135R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I135R results in reduced phosphatase activity in a yeast assay (PMID: 29706350) and cell culture (PMID: 32150788), decreased Pten protein expression and stability, reduced ability to suppress Akt phosphorylation, and results in reduced nuclear localization and increased ubiquitination and sumoylation in culture (PMID: 32150788). | |
| I135T | missense | no effect | PTEN I135T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I135T results in minimal colony formation in yeast (PMID: 32471850), and leads to Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, and normal developmental growth in flies (PMID: 32350270). | |
| I135V | missense | unknown | PTEN I135V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I135V demonstrates Pten protein stability (PMID: 32350270, PMID: 32366478), and Akt phosphorylation (PMID: 32350270) similar to wild-type Pten, however, results in an intermediate ability to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| I168F | missense | no effect - predicted | PTEN I168F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I168F demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| I203V | missense | no effect - predicted | PTEN I203V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). I203V demonstrates decreased Pten protein stability, but results in suppression of Akt phosphorylation similar to wild-type Pten in culture, and leads to normal developmental growth in flies (PMID: 32350270), and therefore, is predicted to have no effect on Pten protein function. | |
| I253* | nonsense | loss of function - predicted | PTEN I253* results in a premature truncation of the Pten protein at amino acid 253 of 403 (UniProt.org). I253* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I253N | missense | loss of function - predicted | PTEN I253N lies within the C2 tensin-type domain of the Pten protein (UniProt.org). I253N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I253T | missense | unknown | PTEN I253T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). I253T has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| I28N | missense | loss of function - predicted | PTEN I28N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I28N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I33del | deletion | loss of function - predicted | PTEN I33del results in the deletion of an amino acid in the phosphatase tensin-type domain of the Pten protein at amino acid 33 (UniProt.org). I33del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I33N | missense | loss of function - predicted | PTEN I33N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I33N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I33S | missense | loss of function | PTEN I33S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I33S results in reduced Pten protein expression and phosphatase activity in a yeast assay (PMID: 29706350, PMID: 17942903), and reduced protein stability (PMID: 17942903) and decreased nuclear localization in cell culture (PMID: 25875300). | |
| I400V | missense | unknown | PTEN I400V does not lie within any known functional domains of the Pten protein (UniProt.org). I400V demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, but leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| I67K | missense | loss of function - predicted | PTEN I67K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I67K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| I67T | missense | unknown | PTEN I67T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I67T has been identified in sequencing studies (PMID: 30205045), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| I67V | missense | unknown | PTEN I67V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). I67V has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| I8Dfs*3 | frameshift | loss of function - predicted | PTEN I8Dfs*3 indicates a shift in the reading frame starting at amino acid 8 and terminating 3 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). I8Dfs*3 has not been characterized, however, due to the effects of other truncation mutations downstream of I8 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| I8N | missense | unknown | PTEN I8N lies within the lipid binding domain of the Pten protein (PMID: 25263454). I8N has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Jan 2024). | |
| inact mut | unknown | loss of function | PTEN inact mut indicates that this variant results in a loss of function of the Pten protein. However, the specific amino acid change has not been identified. | |
| K102fs | frameshift | loss of function - predicted | PTEN K102fs results in a change in the amino acid sequence of the Pten protein beginning at aa 102 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K102fs has not been characterized, however, due to the effects of other truncation mutations downstream of K102 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K125* | nonsense | loss of function - predicted | PTEN K125* results in a premature truncation of the Pten protein at amino acid 125 of 403 (UniProt.org). K125* has not been characterized, however, due to the effects of other truncation mutations downstream of K125 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K125E | missense | loss of function | PTEN K125E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K125E results in a loss of Pten phosphatase activity, decreased p53 transcriptional activity, and increased cell proliferation in culture (PMID: 21828076, PMID: 19457929, PMID: 20926450). | |
| K125L | missense | loss of function | PTEN K125L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K125L confers a loss of function to the Pten protein as demonstrated by decreased phosphatase activity in yeast (PMID: 21828076) and loss of phosphatase activity in cell culture (PMID: 25873899). | |
| K125M | missense | loss of function - predicted | PTEN K125M lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K125M results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K125N | missense | loss of function - predicted | PTEN K125N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K125N results in a loss of phosphatase activity in culture (PMID: 25873899), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K128E | missense | loss of function - predicted | PTEN K128E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K128E results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K128N | missense | unknown | PTEN K128N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K128N demonstrates intermediate phosphatase activity against Pip3 in a yeast assay (PMID: 21828076), but has not been fully biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| K128Q | missense | loss of function - predicted | PTEN K128Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K128Q results in increased Akt phosphorylation in cell culture (PMID: 16829519), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K128R | missense | no effect | PTEN K128R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K128R demonstrates inhibition of Akt phosphorylation at similar levels of wild-type Pten in cell culture (PMID: 16829519, PMID: 29739874) and therefore, has no effect on Pten protein function. | |
| K128T | missense | loss of function - predicted | PTEN K128T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K128T results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K128_R130del | deletion | loss of function | PTEN K128_R130del results in the deletion of 3 amino acids in the phosphatase tensin-type domain of the Pten protein from amino acids 128 to 130 (UniProt.org). K128_R130del confers a loss of function on the Pten protein as indicated by failure to regulate glucose uptake and to dephosphorylate AKT in cell culture (PMID: 27829222). | |
| K13* | nonsense | loss of function - predicted | PTEN K13* results in a premature truncation of the Pten protein at amino acid 13 of 403 (UniProt.org). K13* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K13E | missense | loss of function | PTEN K13E lies within the lipid binding domain of the Pten protein (PMID: 25263454). K13E has phosphatase activity similar to wild-type Pten, but fails to translocate into the nucleus, and is unable to inhibit Akt activation and cell proliferation in culture (PMID: 14711368, PMID: 17213812) and therefore, confers a loss of function to the Pten protein. | |
| K13Q | missense | loss of function - predicted | PTEN K13Q lies within the lipid binding domain of the Pten protein (PMID: 25263454). K13Q results in loss of phosphatase activity in cultured cells (PMID: 16088943), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K144* | nonsense | loss of function - predicted | PTEN K144* results in a premature truncation of the Pten protein at amino acid 144 of 403 (UniProt.org). K144* has not been characterized, however, due to the effects of other truncation mutations downstream of K144 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K144I | missense | no effect - predicted | PTEN K144I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K144I demonstrates phosphatase activity similar to wild-type Pten in an in vitro assay (PMID: 10340391), and therefore, is predicted to have no effect on Pten protein function. | |
| K147* | nonsense | loss of function - predicted | PTEN K147* results in a premature truncation of the Pten protein at amino acid 147 of 403 (UniProt.org). K147* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K163* | nonsense | loss of function - predicted | PTEN K163* results in a premature truncation of the Pten protein at amino acid 163 of 403 (UniProt.org). K163* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K163fs | frameshift | loss of function - predicted | PTEN K163fs results in a change in the amino acid sequence of the Pten protein beginning at aa 163 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K163fs has not been characterized, however, due to the effects of other truncation mutations downstream of K163 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K183Ifs*15 | frameshift | loss of function - predicted | PTEN K183Ifs*15 indicates a shift in the reading frame starting at amino acid 183 and terminating 15 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). K183Ifs*15 has not been characterized, however, due to the effects of other truncation mutations downstream of K183 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K197* | nonsense | loss of function - predicted | PTEN K197* results in a premature truncation of the Pten protein at amino acid 197 of 403 (UniProt.org). K197* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K221* | nonsense | loss of function - predicted | PTEN K221* results in a premature truncation of the Pten protein at amino acid 221 of 403 (UniProt.org). K221* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K237fs | frameshift | loss of function - predicted | PTEN K237fs results in a change in the amino acid sequence of the Pten protein beginning at 237 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K237fs has not been characterized, however, due to the effects of other truncation mutations downstream of K237 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K254* | nonsense | loss of function | PTEN K254* results in a premature truncation of the Pten protein at amino acid 254 of 403 (UniProt.org). K254* confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay (PMID: 10468583) and reduced phosphatase activity in a yeast assay (PMID: 29706350). | |
| K254fs | frameshift | loss of function - predicted | PTEN K254fs results in a change in the amino acid sequence of the Pten protein beginning at 254 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K254fs has not been characterized, however, due to the effects of other truncation mutations downstream of K254 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K254Rfs*42 | frameshift | loss of function - predicted | PTEN K254Rfs*42 indicates a shift in the reading frame starting at amino acid 254 and terminating 42 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). K254Rfs*42 has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K260* | nonsense | loss of function | PTEN K260* results in a premature truncation of the Pten protein at amino acid 260 of 403 (UniProt.org). K260* confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and failure to suppress transcription of E2f1-regulated genes in culture (PMID: 29108454). | |
| K260fs | frameshift | loss of function - predicted | PTEN K260fs results in a change in the amino acid sequence of the Pten protein beginning at 260 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K260fs has not been characterized, however, due to the effects of other truncation mutations downstream of K260 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K263* | nonsense | loss of function - predicted | PTEN K263* results in a premature truncation of the Pten protein at amino acid 263 of 403 (UniProt.org). K263* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K266* | nonsense | loss of function - predicted | PTEN K266* results in a premature truncation of the Pten protein at amino acid 266 of 403 (UniProt.org). K266* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K267* | nonsense | loss of function - predicted | PTEN K267* results in a premature truncation of the Pten protein at amino acid 267 of 403 (UniProt.org). K267* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K267fs | frameshift | loss of function - predicted | PTEN K267fs results in a change in the amino acid sequence of the Pten protein beginning at aa 267 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K267fs has not been characterized, however, due to the effects of other truncation mutations downstream of K267 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K269* | nonsense | loss of function - predicted | PTEN K269* results in a premature truncation of the Pten protein at amino acid 269 of 403 (UniProt.org). K269* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K289E | missense | unknown | PTEN K289E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). K289E results in reduced apoptosis in combination with K13E in culture (PMID: 18716620), impaired Pten nuclear import in culture (PMID: 17218261), and reduced phosphatase activity in culture (PMID: 37437018) and in an in vitro assay (PMID: 10866302), however, retains wild-type Pten phosphatase activity in another study (PMID: 33828082), demonstrates growth suppression (PMID: 11156408), demonstrates lysosomal regulation similar to wild-type (PMID: 36436593), and retains binding to large multilamellar vesicles similar to wild-type Pten in cell culture (PMID: 10866302), and therefore, its effect on Pten protein function is unknown. | |
| K289Nfs*8 | frameshift | loss of function - predicted | PTEN K289Nfs*8 indicates a shift in the reading frame starting at amino acid 289 and terminating 8 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). K289Nfs*8 has not been characterized, however, due to the effects of other truncation mutations downstream of K289 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K322E | missense | loss of function | PTEN K322E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). K322E demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| K330* | nonsense | loss of function - predicted | PTEN K330* results in a premature truncation of the Pten protein at amino acid 330 of 403 (UniProt.org). K330* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K330E | missense | unknown | PTEN K330E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). K330E results in suppression of Akt phosphorylation similar to wild-type Pten, however, demonstrates reduced Pten protein stability in cell culture, leads to impaired developmental growth in flies (PMID: 32350270), and results in gain of Pten protein function in a Drosophila wing overgrowth assay (PMID: 34492006), and therefore, its effect on Pten protein function is unknown. | |
| K342* | nonsense | loss of function | PTEN K342* results in a premature truncation of the Pten protein at amino acid 342 of 403 (UniProt.org). K342* results in decreased Pten protein stability, loss of phosphatase activity, and failure to inhibit Akt phosphorylation and transformation in culture (PMID: 10468583). | |
| K342N | missense | unknown | PTEN K342N lies within the C2 tensin-type domain of the Pten protein (UniProt.org). K342N demonstrates phosphatase activity similar to wild-type Pten in an in vitro assay (PMID: 10866302) and in a Drosophila wing overgrowth assay (PMID: 34492006), and Pten protein stability similar to wild-type Pten, however, fails to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| K402N | missense | no effect | PTEN K402N lies within the PDZ domain-binding region of the Pten protein (UniProt.org). K402N demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270). | |
| K6* | nonsense | loss of function - predicted | PTEN K6* results in a premature truncation of the Pten protein at amino acid 6 of 403 (UniProt.org). K6* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K60fs | frameshift | loss of function - predicted | PTEN K60fs results in a change in the amino acid sequence of the Pten protein beginning at aa 60 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K60fs has not been characterized, however, due to the effects of other truncation mutations downstream of K60 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K60N | missense | unknown | PTEN K60N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K60N has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| K60T | missense | unknown | PTEN K60T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K60T has been identified in the scientific literature (PMID: 24647592), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| K62R | missense | loss of function | PTEN K62R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K62R confers a loss of function to the Pten protein, as demonstrated by reduced ATP-binding, increased cell proliferation, and cell transformation in culture (PMID: 19457929). | |
| K66E | missense | unknown | PTEN K66E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K66E has been identified in sequencing studies (PMID: 21103049, PMID: 29575851), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| K66fs | frameshift | loss of function - predicted | PTEN K66fs results in a change in the amino acid sequence of the Pten protein beginning at aa 66 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K66fs has not been characterized, however, due to the effects of other truncation mutations downstream of K66 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K66N | missense | unknown | PTEN K66N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K66N has been identified in sequencing studies (PMID: 23525077, PMID: 21266528), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| K66Q | missense | unknown | PTEN K66Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). K66Q has been identified in sequencing studies (PMID: 10851265), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| K6del | deletion | loss of function - predicted | PTEN K6del results in the deletion of an amino acid within the Pten protein at amino acid 6 (UniProt.org). K6del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| K6E | missense | loss of function | PTEN K6E lies within the lipid binding domain of the Pten protein (PMID: 25263454). K6E demonstrates protein stability similar to wild-type Pten (PMID: 32350270), however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), fails to suppress Akt phosphorylation in cell culture, and delays development in flies (PMID: 32350270). | |
| K6fs | frameshift | loss of function - predicted | PTEN K6fs results in a change in the amino acid sequence of the Pten protein beginning at aa 6 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). K6fs has not been characterized, however, due to the effects of other truncation mutations downstream of K6 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| K6I | missense | loss of function | PTEN K6I lies within the lipid binding domain of the Pten protein (PMID: 25263454). K6I demonstrates similar Pten protein stability to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), however, results in an intermediate ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and leads to developmental delay in flies (PMID: 32350270). | |
| K6N | missense | unknown | PTEN K6N lies within the lipid binding domain of the Pten protein (PMID: 25263454). K6N demonstrates a gene expression signature correlated with wild-type Pten in culture (PMID: 27147599), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| L108F | missense | unknown | PTEN L108F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L108F has been identified in sequencing studies (PMID: 30715630), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Apr 2024). | |
| L108H | missense | loss of function - predicted | PTEN L108H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L108H results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L108P | missense | loss of function | PTEN L108P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L108P results in a loss of Pten phosphatase activity, is unable to suppress Akt activation in cell culture (PMID: 25527629), and has reduced protein stability (PMID: 27405757). | |
| L108R | missense | loss of function | PTEN L108R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L108R results in decreased Pten expression and increased Akt phosphorylation in cultured cells (PMID: 10582703) and reduced phosphatase activity in a yeast assay (PMID: 29706350). | |
| L108_D109del | deletion | unknown | PTEN L108_D109del results in the deletion of two amino acids in the phosphatase tensin-type domain of the Pten protein from amino acids 108 to 109 (UniProt.org). L108_D109del has been identified in sequencing studies (PMID: 18757403), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| L112I | missense | unknown | PTEN L112I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L112I has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| L112P | missense | loss of function | PTEN L112P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L112P results in a loss of Pten phosphatase activity and is unable to suppress Akt activation in cell culture (PMID: 10866302, PMID: 25527629). | |
| L112R | missense | loss of function | PTEN L112R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L112R results in loss of Pten phosphatase activity in an in vitro assay and a yeast assay (PMID: 29706350, PMID: 10866302). | |
| L112V | missense | unknown | PTEN L112V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L112V has not been biochemically characterized, however, the genomic change leads to activation of a cryptic splice site and aberrant splicing of PTEN (PMID: 18669439). | |
| L139* | nonsense | loss of function - predicted | PTEN L139* results in a premature truncation of the Pten protein at amino acid 139 of 403 (UniProt.org). L139* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L140* | nonsense | loss of function - predicted | PTEN L140* results in a premature truncation of the Pten protein at amino acid 140 of 403 (UniProt.org). L140* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L140F | missense | loss of function - predicted | PTEN L140F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L140F results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L146* | nonsense | loss of function - predicted | PTEN L146* results in a premature truncation of the Pten protein at amino acid 146 of 403 (UniProt.org). L146* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L152P | missense | loss of function | PTEN L152P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L152P is associated with decreased Pten expression and increased Akt phosphorylation in cultured cells (PMID: 30289966), and results in reduced phosphatase activity in a yeast assay (PMID: 29706350). | |
| L152R | missense | loss of function - predicted | PTEN L152R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L152R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L181P | missense | loss of function | PTEN L181P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L181P onfers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| L182fs | frameshift | loss of function - predicted | PTEN L182fs results in a change in the amino acid sequence of the Pten protein beginning at aa 182 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L182fs has not been characterized, however, due to the effects of other truncation mutations downstream of L182 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L182P | missense | loss of function - predicted | PTEN L182P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L182P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L193fs | frameshift | loss of function - predicted | PTEN L193fs results in a change in the amino acid sequence of the Pten protein beginning at aa 193 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L193fs has not been characterized, however, due to the effects of other truncation mutations downstream of L193 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L193P | missense | loss of function - predicted | PTEN L193P lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L193P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L194fs | frameshift | loss of function - predicted | PTEN L194fs results in a change in the amino acid sequence of the Pten protein beginning at aa 194 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L194fs has not been characterized, however, due to the effects of other truncation mutations downstream of L194 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L23F | missense | loss of function | PTEN L23F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L23F retains phosphatase activity, but results in nuclear accumulation of Pten and failure to inhibit Akt phosphorylation and cell proliferation in culture (PMID: 17213812) and therefore, confers a loss of function to the Pten protein. | |
| L23S | missense | loss of function - predicted | PTEN L23S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L23S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L23V | missense | loss of function - predicted | PTEN L23V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L23V results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L247* | nonsense | loss of function - predicted | PTEN L247* results in a premature truncation of the Pten protein at amino acid 247 of 403 (UniProt.org). L247* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L247F | missense | unknown | PTEN L247F lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L247F has been identified in sequencing studies (PMID: 23274167), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| L247Sfs*6 | frameshift | loss of function - predicted | PTEN L247Sfs*6 indicates a shift in the reading frame starting at amino acid 247 and terminating 6 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). L247Sfs*6 has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L247_P248del | deletion | loss of function - predicted | PTEN L247_P248del results in the deletion of two amino acids in the C2 tensin-type domain of the Pten protein from amino acids 247 to 248 (UniProt.org). L247_P248del has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L265fs | frameshift | loss of function - predicted | PTEN L265fs results in a change in the amino acid sequence of the Pten protein beginning at aa 265 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L265fs has not been characterized, however, due to the effects of other truncation mutations downstream of L265 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L295V | missense | unknown | PTEN L295V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L295V demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, however, leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| L318fs | frameshift | loss of function - predicted | PTEN L318fs results in a change in the amino acid sequence of the Pten protein beginning at aa 318 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L318fs has not been characterized, however, due to the effects of other truncation mutations downstream of L318 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L320* | nonsense | loss of function - predicted | PTEN L320* results in a premature truncation of the Pten protein at amino acid 320 of 403 (UniProt.org). L320* has not been characterized, however, due to the effects of other truncation mutations downstream of L320 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L320S | missense | loss of function | PTEN L320S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L320S results in similar phosphatase activity to wild-type Pten in an in vitro assay (PMID: 28263967), but results in reduced phosphatase activity in a yeast assay (PMID: 29706350), increased cell proliferation and migration, failure to suppress Akt signaling, reduced protein stability, decreased suppression of Pip3, and defective membrane and nuclear localization in cell culture (PMID: 28263967). | |
| L320V | missense | unknown | PTEN L320V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L320V has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| L325F | missense | loss of function - predicted | PTEN L325F lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L325F results in a loss of phosphatase activity through failure to inhibit Akt phosphorylation in cell culture (PMID: 19329485), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L325R | missense | loss of function | PTEN L325R lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L325R results in reduced Pten phosphatase activity in a yeast assay (PMID: 29706350) and in increased transformation ability in two different cell lines (PMID: 29533785). | |
| L345Q | missense | loss of function | PTEN L345Q lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L345Q confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302) and reduced ability to suppress transformation of cells in culture (PMID: 10468583). | |
| L345R | missense | unknown | PTEN L345R lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L345R has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Feb 2024). | |
| L345V | missense | no effect - predicted | PTEN L345V lies within the C2 tensin-type domain of the Pten protein (UniProt.org). L345V demonstrates reduced Pten protein stability and leads to impaired developmental growth in flies, but demonstrates suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270), and shows phosphatase activity and growth similar to wild-type Pten in yeast (PMID: 25448481, PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| L42P | missense | loss of function - predicted | PTEN L42P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L42P results in reduced phosphatase activity in yeast assays (PMID: 29706350, PMID: 25875300), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L42R | missense | loss of function | PTEN L42R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L42R demonstrates phosphatase activity comparable to wild-type Pten however, L42R results in reduced membrane localization of the Pten protein due to impaired binding with membrane lipids (PMID: 25448479, PMID: 25263454) and subsequently, is unable to prevent Akt signaling, cell proliferation, and cell migration and therefore, confers a loss of function to the Pten protein (PMID: 25263454). | |
| L57* | nonsense | loss of function - predicted | PTEN L57* results in a premature truncation of the Pten protein at amino acid 57 of 403 (UniProt.org). L57* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L57fs | frameshift | loss of function - predicted | PTEN L57fs results in a change in the amino acid sequence of the Pten protein beginning at aa 57 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L57fs has not been characterized, however, due to the effects of other truncation mutations downstream of L57 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L57S | missense | loss of function - predicted | PTEN L57S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L57S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L57W | missense | loss of function | PTEN L57W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L57W confers a loss of function to the Pten protein, as demonstrated by loss of phosphatase activity (PMID: 9256433, PMID: 9356475) and is unable to inhibit cell proliferation in culture (PMID: 9356475). | |
| L70fs | frameshift | loss of function - predicted | PTEN L70fs results in a change in the amino acid sequence of the Pten protein beginning at aa 70 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). L70fs has not been characterized, however, due to the effects of other truncation mutations downstream of L70 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| L70H | missense | unknown | PTEN L70H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L70H has been identified in sequencing studies (PMID: 26831717), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| L70P | missense | loss of function - predicted | PTEN L70P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L70P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L70R | missense | loss of function - predicted | PTEN L70R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L70R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| L70V | missense | loss of function | PTEN L70V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). L70V leads to impaired developmental growth in flies, and reduced Pten protein stability and impaired suppression of Akt phosphorylation in cell culture (PMID: 32350270). | |
| LOH | deletion | unknown | PTEN LOH indicates the loss of one parental copy of the PTEN gene, resulting in loss of heterozygosity. | |
| loss | unknown | loss of function | PTEN loss indicates a loss of the PTEN gene, mRNA, and protein, which leads to suppression of Ar-dependent gene expression (PMID: 21620777), epithelial-mesenchymal transition in cell culture (PMID: 20032390), and promotes KRAS-dependent tumor formation (PMID: 20807812), and decreased apoptosis and increased cell survival in a mouse model (PMID: 12782594). PTEN loss has been identified in a number of cancers (PMID: 30738865), including prostate cancer (PMID: 29460925) and glioblastoma (PMID: 9331071). | |
| M134del | deletion | loss of function - predicted | PTEN M134del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 134 (UniProt.org). M134del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M134I | missense | loss of function | PTEN M134I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M134I demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), however, results in a loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and leads to delayed developmental growth in flies (PMID: 32350270). | |
| M134L | missense | loss of function - predicted | PTEN M134L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M134L results in a loss of phosphatase activity (PMID: 10866302), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M134R | missense | loss of function - predicted | PTEN M134R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M134R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), decreased protein stability, and loss of Pten expression in culture (PMID: 37907589), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M134T | missense | loss of function | PTEN M134T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M134T rescues growth of yeast cells similar to wild-type Pten in culture, but demonstrates reduced lipid phosphatase activity in a yeast assay (PMID: 21828076) and cell culture (PMID: 32150788), and decreased Pten protein expression and stability in cell culture (PMID: 32150788, PMID: 32350270), and results in reduced nuclear localization and increased sumoylation (PMID: 32150788), failure to suppress Akt phosphorylation in cell culture, and impaired developmental growth in flies (PMID: 32350270). | |
| M198I | missense | no effect | PTEN M198I lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M198I results in Akt phosphorylation (PMID: 32350270), and demonstrates Pten protein stability and the ability to rescue spheroid formation similar to wild-type Pten in cell culture (PMID: 32366478, PMID: 32350270). | |
| M198K | missense | loss of function - predicted | PTEN M198K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M198K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M198R | missense | loss of function | PTEN M198R lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M198R confers a loss of function to the Pten protein as it results in reduced phosphatase activity in a yeast assay (PMID: 29706350, PMID: 17942903) and fails to suppress Akt phosphorylation in culture (PMID: 17942903). | |
| M199del | deletion | loss of function | PTEN M199del results in the deletion of an amino acid in the C2 tensin-type domain of the Pten protein at amino acid 199 (UniProt.org). M199del confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay and in a yeast assay (PMID: 29706350, PMID: 11051241). | |
| M205I | missense | loss of function - predicted | PTEN M205I lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M205I results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M264R | missense | loss of function - predicted | PTEN M264R lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M264R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M264T | missense | loss of function - predicted | PTEN M264T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). M264T results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M270fs | frameshift | loss of function - predicted | PTEN M270fs results in a change in the amino acid sequence of the Pten protein beginning at aa 270 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). M270fs has not been characterized, however, due to the effects of other truncation mutations downstream of M270 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| M35I | missense | unknown | PTEN M35I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M35I has been identified in the scientific literature (PMID: 29416795), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| M35K | missense | loss of function - predicted | PTEN M35K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M35K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| M35L | missense | unknown | PTEN M35L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M35L has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| M35R | missense | loss of function | PTEN M35R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M35R confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 17942903). | |
| M35V | missense | loss of function - predicted | PTEN M35V lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). M35V demonstrates protein stability similar to wild-type Pten (PMID: 32350270, PMID: 32366478), however, results in an intermediate ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270), and therefore, is predicted to lead to a loss of Pten protein function. | |
| mutant | unknown | unknown | PTEN mutant indicates an unspecified mutation in the PTEN gene. | |
| N117fs | frameshift | loss of function - predicted | PTEN N117fs results in a change in the amino acid sequence of the Pten protein beginning at 117 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N117fs has not been characterized, however, due to the effects of other truncation mutations downstream of N117 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N117S | missense | loss of function - predicted | PTEN N117S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N117S demonstrates Pten protein stability (PMID: 32366478, PMID: 32350270) and Akt phosphorylation similar to wild-type Pten in culture, and results in normal developmental growth in flies (PMID: 32350270), but results in an intermediate ability to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N12T | missense | loss of function | PTEN N12T lies within the lipid binding domain of the Pten protein (PMID: 25263454). N12T demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270), and results in increased transformation ability in two different cell lines, as compared to wild-type Pten (PMID: 29533785). | |
| N184Efs*16 | frameshift | loss of function - predicted | PTEN N184Efs*16 indicates a shift in the reading frame starting at amino acid 184 and terminating 16 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). N184Efs*16 has not been characterized, however, due to the effects of other truncation mutations downstream of N184 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N212Kfs*10 | frameshift | loss of function - predicted | PTEN N212Kfs*10 indicates a shift in the reading frame starting at amino acid 212 and terminating 10 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). N212Kfs*10 has not been characterized, however, due to the effects of other truncation mutations downstream of N212 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N228S | missense | unknown | PTEN N228S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N228S demonstrates the ability to rescue spheroid formation (PMID: 32366478), Pten protein stability (PMID: 32350270, PMID: 32366478), and Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270) and phosphatase activity similar to wild-type Pten in a Drosophila wing overgrowth assay (PMID: 34492006), but results in delayed developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| N262S | missense | no effect | PTEN N262S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N262S demonstrates ability to rescue spheroid formation (PMID: 32366478), Pten protein stability (PMID: 32350270, PMID: 32366478), and Akt phosphorylation similar to wild-type Pten in cell culture, and results in normal developmental growth in flies (PMID: 32350270). | |
| N276A | missense | loss of function - predicted | PTEN N276A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N276A results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N276K | missense | loss of function - predicted | PTEN N276K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N276K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N276S | missense | loss of function | PTEN N276S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N276S demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), but reduced Akt phosphorylation in culture and reduced expression in culture and in patient samples (PMID: 36591942), is unable to localize to the nucleus (PMID: 29373119), and leads to reduced Pten protein stability (PMID: 25527629, PMID: 32350270), and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| N276T | missense | loss of function - predicted | PTEN N276T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N276T results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N292fs | frameshift | loss of function - predicted | PTEN N292fs results in a change in the amino acid sequence of the Pten protein beginning at aa 292 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N292fs has not been characterized, however, due to the effects of other truncation mutations downstream of N292 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N323fs | frameshift | loss of function - predicted | PTEN N323fs results in a change in the amino acid sequence of the Pten protein beginning at aa 323 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N323fs has not been characterized, however, due to the effects of other truncation mutations downstream of N323 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N323K | missense | unknown | PTEN N323K lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N323K has been identified in the scientific literature (PMID: 14724591), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| N323Kfs*2 | frameshift | loss of function - predicted | PTEN N323Kfs*2 indicates a shift in the reading frame starting at amino acid 323 and terminating 2 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). N323Kfs*2 has not been characterized, however, due to the effects of other truncation mutations downstream of N323 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N323T | missense | unknown | PTEN N323T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). N323T has been identified in sequencing studies (PMID: 33720082), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| N329fs | frameshift | loss of function - predicted | PTEN N329fs results in a change in the amino acid sequence of the Pten protein beginning at aa 329 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N329fs has not been characterized, however, due to the effects of other truncation mutations downstream of N329 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N340fs | frameshift | loss of function - predicted | PTEN N340fs results in a change in the amino acid sequence of the Pten protein beginning at aa 340 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N340fs has not been characterized, however, due to the effects of other truncation mutations downstream of N340 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N340H | missense | no effect | PTEN N340H lies within the C2 tensin-type domain and NOP53-interacting region of the Pten protein (UniProt.org). N340H demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270). | |
| N356D | missense | no effect | PTEN N356D does not lie within any known functional domains of the Pten protein (UniProt.org). N356D demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270). | |
| N356H | missense | no effect | PTEN N356H does not lie within any known functional domains of the Pten protein (UniProt.org). N356H demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270). | |
| N48I | missense | loss of function - predicted | PTEN N48I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N48I results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N48K | missense | loss of function | PTEN N48K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N48K results in a loss of Pten phosphatase activity as indicated by increased Akt phosphorylation in cell culture (PMID: 14675182, PMID: 25527629). | |
| N48S | missense | loss of function - predicted | PTEN N48S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N48S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| N63fs | frameshift | loss of function - predicted | PTEN N63fs results in a change in the amino acid sequence of the Pten protein beginning at aa 63 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). N63fs has not been characterized, however, due to the effects of other truncation mutations downstream of N63 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| N69D | missense | unknown | PTEN N69D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N69D has been identified in the scientific literature (PMID: 26561558), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| N94I | missense | loss of function - predicted | PTEN N94I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). N94I results in loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| negative | unknown | loss of function | PTEN negative indicates a lack of the PTEN gene, mRNA, and/or protein. | |
| over exp | none | no effect | PTEN over exp indicates an over expression of the Pten protein. However, the mechanism causing the over expression is unspecified. | |
| P169H | missense | no effect - predicted | PTEN P169H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P169H demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| P204A | missense | unknown | PTEN P204A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P204A has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| P213S | missense | unknown | PTEN P213S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P213S has been identified in the scientific literature (PMID: 18953432, PMID: 27756406), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| P246fs | frameshift | loss of function - predicted | PTEN P246fs results in a change in the amino acid sequence of the Pten protein beginning at aa 246 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). P246fs has not been characterized, however, due to the effects of other truncation mutations downstream of P246 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| P246L | missense | unknown | PTEN P246L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P246L demonstrates inhibition of Pi3k signaling similar to wild-type Pten in yeast (PMID: 17942903), and retains the ability to suppress transcription of E2f1-regulated genes in culture (PMID: 29108454) and suppresses Akt signaling in culture (PMID: 32704382), however, demonstrates reduced Pten protein stability, and fails to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| P246S | missense | unknown | PTEN P246S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P246S has been identified in the scientific literature (PMID: 15195137), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Apr 2024). | |
| P248fs | frameshift | loss of function - predicted | PTEN P248fs results in a change in the amino acid sequence of the Pten protein beginning at aa 248 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). P248fs has not been characterized, however, due to the effects of other truncation mutations downstream of P248 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| P248H | missense | unknown | PTEN P248H lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P248H has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| P248L | missense | unknown | PTEN P248L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P248L has been identified in the scientific literature (PMID: 25495427), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| P283L | missense | unknown | PTEN P283L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P283L has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| P339L | missense | loss of function - predicted | PTEN P339L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P339L fails to suppress E2f1-mediated transcription in cultured cells (PMID: 29108454), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P339S | missense | unknown | PTEN P339S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). P339S has been identified in the scientific literature (PMID: 26645239, PMID: 27998968), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| P354Q | missense | no effect | PTEN P354Q does not lie within any known functional domains of the Pten protein (UniProt.org). P354Q demonstrates ability to rescue spheroid formation (PMID: 32366478), Pten protein stability (PMID: 32350270, PMID: 32366478), and Akt phosphorylation similar to wild-type Pten in cell culture, and results in normal developmental growth in flies (PMID: 32350270). | |
| P38F | missense | loss of function - predicted | PTEN P38F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38F results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P38H | missense | loss of function | PTEN P38H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38H demonstrates Pten protein stability similar to wild-type protein (PMID: 32366478, PMID: 32350270), however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and delays normal developmental growth in flies (PMID: 32350270). | |
| P38L | missense | loss of function - predicted | PTEN P38L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P38R | missense | loss of function - predicted | PTEN P38R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P38S | missense | unknown | PTEN P38S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38S has been identified in the scientific literature (PMID: 15195137, PMID: 9288767, PMID: 32913971), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| P38T | missense | loss of function - predicted | PTEN P38T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P38T results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P89fs | frameshift | loss of function - predicted | PTEN P89fs results in a change in the amino acid sequence of the Pten protein beginning at aa 89 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). P89fs has not been characterized, however, due to the effects of other truncation mutations downstream of P89 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| P95L | missense | loss of function | PTEN P95L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P95L confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| P95Q | missense | loss of function - predicted | PTEN P95Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P95Q results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P95R | missense | loss of function - predicted | PTEN P95R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P95R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P95S | missense | loss of function - predicted | PTEN P95S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P95S results in a loss of phosphatase activity as indicated by failure to inhibit Akt phosphorylation in cell culture (PMID: 19329485), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P96del | deletion | loss of function - predicted | PTEN P96del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 96 (UniProt.org). P96del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P96L | missense | unknown | PTEN P96L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P96L has been identified in sequencing studies (PMID: 18772396, PMID: 33294271), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| P96Q | missense | loss of function | PTEN P96Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P96Q confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity and instability in yeast (PMID: 21828076, PMID: 17942903). | |
| P96R | missense | loss of function - predicted | PTEN P96R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P96R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| P96S | missense | unknown | PTEN P96S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P96S has been identified in the scientific literature (PMID: 22653804, PMID: 29681454, PMID: 24468202), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| P96T | missense | unknown | PTEN P96T lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). P96T has been identified in sequencing studies (PMID: 24132290), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| positive | unknown | unknown | PTEN positive indicates the presence of the PTEN gene, mRNA, and/or protein. | |
| Q110* | nonsense | loss of function - predicted | PTEN Q110* results in a premature truncation of the Pten protein at amino acid 110 of 403 (UniProt.org). Q110* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q110K | missense | unknown | PTEN Q110K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q110K has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| Q110R | missense | no effect - predicted | PTEN Q110R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q110R demonstrates inhibition of Akt phosphorylation similar to wild-type Pten in culture (PMID: 19329485), and therefore, is predicted to have no effect on Pten protein function. | |
| Q149* | nonsense | loss of function - predicted | PTEN Q149* results in a premature truncation of the Pten protein at amino acid 149 of 403 (UniProt.org). Q149* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q17* | nonsense | loss of function - predicted | PTEN Q17* results in a premature truncation of the Pten protein at amino acid 17 of 403 (UniProt.org). Q17* has not been characterized, however, due to the effects of other truncation mutations downstream of Q17 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Q171* | nonsense | loss of function - predicted | PTEN Q171* results in a premature truncation of the Pten protein at amino acid 171 of 403 (UniProt.org). Q171* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q171E | missense | loss of function | PTEN Q171E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q171E demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and leads to developmental delay in flies (PMID: 32350270). | |
| Q171K | missense | loss of function - predicted | PTEN Q171K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q171K results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q171P | missense | loss of function - predicted | PTEN Q171P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q171P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q171R | missense | loss of function | PTEN Q171R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Q171R confers a loss of function on Pten as demonstrated by altered cell morphology and cytoskeletal organization, decreased ability to suppress proliferation and migration, increased phosphorylation of Akt, and decreased apoptotic activity upon induction in cultured cells (PMID: 34943931). | |
| Q17del | deletion | loss of function - predicted | PTEN Q17del results in the deletion of an amino acid in the phosphatase tensin-type domain of the Pten protein at amino acid 17 (UniProt.org). Q17del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q17Kfs*7 | frameshift | loss of function - predicted | PTEN Q17Kfs*7 indicates a shift in the reading frame starting at amino acid 17 and terminating 7 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). Q17Kfs*7 has not been characterized, however, due to the effects of other truncation mutations downstream of Q17 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Q214* | nonsense | loss of function | PTEN Q214* results in a premature truncation of the Pten protein at amino acid 214 of 403 UniProt.org). Q214* confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and failure to suppress transcription of E2f1-regulated genes in culture (PMID: 29108454). | |
| Q214_F215del | deletion | unknown | PTEN Q214_F215del results in the deletion of two amino acids in the C2 tensin-type domain of the Pten protein from amino acids 214 to 215 (UniProt.org). Q214_F215del has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Apr 2024). | |
| Q219* | nonsense | loss of function - predicted | PTEN Q219* results in a premature truncation of the Pten protein at amino acid 219 of 403 (UniProt.org). Q219* has not been characterized, however, due to the effects of other truncation mutations downstream of Q219 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Q245* | nonsense | loss of function - predicted | PTEN Q245* results in a premature truncation of the Pten protein at amino acid 245 of 403 (UniProt.org). Q245* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q245P | missense | loss of function - predicted | PTEN Q245P lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Q245P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q261* | nonsense | loss of function | PTEN Q261* results in a premature truncation of the Pten protein at amino acid 261 of 403 (UniProt.org). Q261* confers a loss of Pten protein function as demonstrated by reduced phosphatase activity in a yeast assay (PMID: 29706350) and decreased protein levels and increased phosphorylation of Akt and S6 in a patient tumor sample (PMID: 25003235). | |
| Q298* | nonsense | loss of function - predicted | PTEN Q298* results in a premature truncation of the Pten protein at amino acid 298 of 403 (UniProt.org). Q298* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Q298E | missense | no effect - predicted | PTEN Q298E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Q298E leads to slowed developmental growth rate in flies, but demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270), and therefore, is predicted to have no effect on Pten protein function. | |
| Q298fs | frameshift | loss of function - predicted | PTEN Q298fs results in a change in the amino acid sequence of the Pten protein beginning at aa 298 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Q298fs has not been characterized, however, due to the effects of other truncation mutations downstream of Q298 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Q396R | missense | no effect - predicted | PTEN Q396R does not lie within any known functional domains of the Pten protein (UniProt.org). Q396R demonstrates increased suppression of Akt phosphorylation, but leads to Pten protein stability similar to wild-type Pten in cell culture (PMID: 32350270), and therefore, is predicted to have no effect on Pten protein function. | |
| Q399* | nonsense | unknown | PTEN Q399* results in a premature truncation of the Pten protein at amino acid 399 of 403 (UniProt.org). Q399* results in reduced ability to inhibit PDGF-induced membrane ruffling and proliferation in PTEN-null cells (PMID: 10698713), fails to rescue epithelial morphogenesis in culture (PMID: 23085752), abrogates fibroblast conditioned medium-induced PI3K activation in culture (PMID: 35719951), but maintains similar levels of phosphatase activity to wild-type Pten in cell culture (PMID: 10698713), and therefore, its effect on Pten protein function is unknown. | |
| Q87* | nonsense | loss of function - predicted | PTEN Q87* results in a premature truncation of the Pten protein at amino acid 87 of 403 (UniProt.org). Q87* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R130* | nonsense | loss of function | PTEN R130* results in a premature truncation of the Pten protein at amino acid 130 of 403 within the phosphatase tensin-type domain (UniProt.org). R130* confers a loss of function to the Pten protein as demonstrated by loss of Pten expression in a patient sample (PMID: 32610572), demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270), and results in decreased p53 signaling and increased DNA damage in xenografts (PMID: 24721394), and increased transformation ability compared to wild-type Pten in two different cell lines in culture (PMID: 29533785). | |
| R130A | missense | loss of function | PTEN R130A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130A confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| R130fs | frameshift | loss of function - predicted | PTEN R130fs results in a change in the amino acid sequence of the Pten protein beginning at aa 130 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R130fs has not been characterized, however, due to the effects of other truncation mutations downstream of R130 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R130G | missense | loss of function | PTEN R130G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130G confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 11051241, PMID: 10866302) and increased transformation ability in two different cell lines, as compared to wild-type Pten (PMID: 29533785). | |
| R130K | missense | loss of function | PTEN R130K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130K confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| R130L | missense | loss of function | PTEN R130L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130L demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation (PMID: 32366478), demonstrates loss of phosphatase activity in cell culture (PMID: 10866302, PMID: 25527629), and fails to inhibit Akt signaling in culture (PMID: 32704382). | |
| R130P | missense | loss of function | PTEN R130P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130P demonstrates Pten protein stability similar to wild-type protein (PMID: 32350270, PMID: 32366478), however, fails to decrease Akt phosphorylation (PMID: 32350270, PMID: 32704382), and demonstrates loss of ability to rescue spheroid formation in cell culture (PMID: 32366478). | |
| R130Q | missense | loss of function | PTEN R130Q lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130Q demonstrates Pten protein stability similar to wild-type protein, however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), loss of phosphatase activity (PMID: 10866302), and increased transformation ability in two different cell lines in culture (PMID: 29533785). | |
| R130S | missense | loss of function - predicted | PTEN R130S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R130S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R142fs | frameshift | loss of function - predicted | PTEN R142fs results in a change in the amino acid sequence of the Pten protein beginning at aa 142 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R142fs has not been characterized, however, due to the effects of other truncation mutations downstream of R142 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R142P | missense | loss of function - predicted | PTEN R142P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R142P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R142W | missense | loss of function - predicted | PTEN R142W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R142W demonstrates protein stability similar to wild-type Pten and suppresses Akt signaling similar to wild-type Pten (PMID: 32704382), but results in reduced ability to rescue spheroid formation in culture (PMID: 32366478), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R14fs | frameshift | loss of function - predicted | PTEN R14fs results in a change in the amino acid sequence of the Pten protein beginning at aa 14 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R14fs has not been characterized, however, due to the effects of other truncation mutations downstream of R14 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R14G | missense | loss of function | PTEN R14G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R14G demonstrates Pten protein stability similar to wild-type protein (PMID: 32350270), however, results in a loss of Pip3 phosphatase activity in yeast (PMID: 29706633), and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| R14K | missense | unknown | PTEN R14K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R14K has been predicted to have no effect on protein stability by structural modeling (PMID: 32859654) and results in phosphatase activity similar to wild-type Pten in a yeast assay (PMID: 25875300), but results in impaired nuclear localization in cultured cells (PMID: 25875300), and therefore, its effect on Pten protein function is unknown. | |
| R159F | missense | loss of function - predicted | PTEN R159F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R159F results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R159I | missense | loss of function - predicted | PTEN R159I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R159I results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R159L | missense | loss of function - predicted | PTEN R159L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R159L results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R159S | missense | loss of function - predicted | PTEN R159S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R159S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R15I | missense | loss of function | PTEN R15I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R15I confers a loss of Pten protein function as demonstrated by loss of phosphatase activity and impaired nuclear localization in yeast (PMID: 25875300, PMID: 29706350). | |
| R15K | missense | loss of function - predicted | PTEN R15K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R15K results in nuclear localization similar to wild-type Pten, but results in a loss of phosphatase activity in culture (PMID: 25875300), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R15S | missense | loss of function | PTEN R15S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R15S demonstrates Pten protein stability similar to wild-type protein, however, results in a partial loss of ability to rescue spheroid formation (PMID: 32366478), loss of Pten phosphatase activity, is unable to suppress cell proliferation in culture (PMID: 9823298), and has impaired nuclear localization (PMID: 17213812). | |
| R161G | missense | loss of function - predicted | PTEN R161G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R161G results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R172fs | frameshift | loss of function - predicted | PTEN R172fs results in a change in the amino acid sequence of the Pten protein beginning at aa 172 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R172fs has not been characterized, however, due to the effects of other truncation mutations downstream of R172 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R173C | missense | loss of function | PTEN R173C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R173C results in suppressed phosphorylation of Pdk1, Akt, and Gsk3beta similar to wild-type Pten in culture (PMID: 32704382), but confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302) and increased transformation ability in two different cell lines, as compared to wild-type Pten (PMID: 29533785). | |
| R173fs | frameshift | loss of function - predicted | PTEN R173fs results in a change in the amino acid sequence of the Pten protein beginning at aa 173 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R173fs has not been characterized, however, due to the effects of other truncation mutations downstream of R173 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R173H | missense | loss of function - predicted | PTEN R173H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R173H correlates with wild-type Pten phenotype in a gene expression profile analysis (PMID: 27147599) and leads to normal developmental growth in flies, but fails to suppress Akt phosphorylation in cell culture (PMID: 32350270), demonstrates reduced Pten protein stability (PMID: 32366478, PMID: 32350270), results in a loss of Pten phosphatase activity in an in vitro assay (PMID: 10866302), partial loss of ability to rescue spheroid formation (PMID: 32366478), and is associated with increased copy number variation in patient samples (PMID: 24721394), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R173P | missense | loss of function | PTEN R173P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R173P demonstrates loss of phosphatase activity in an in-vitro assay (PMID: 10866302), and reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| R173S | missense | unknown | PTEN R173S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R173S has been identified in the scientific literature (PMID: 23434733), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| R189* | nonsense | loss of function - predicted | PTEN R189* results in a premature truncation of the Pten protein at amino acid 189 of 403 (UniProt.org). R189* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R233* | nonsense | loss of function | PTEN R233* results in a premature truncation of the Pten protein at amino acid 233 of 403 (UniProt.org). R233* confers a loss of function to the Pten protein, as indicated by failure to suppress transcription of E2f1-regulated genes in culture (PMID: 29108454), and increased transformation of two different cell lines (PMID: 29533785). | |
| R233Q | missense | no effect - predicted | PTEN R233Q lies within the C2 tensin-type domain of the Pten protein (UniProt.org). R233Q has not been biochemically characterized, however, induces a similar gene expression signature as wild-type Pten in cell culture (PMID: 27147599), and therefore, is predicted to have no effect on Pten protein function. | |
| R234* | nonsense | loss of function - predicted | PTEN R234* results in a premature truncation of the Pten protein at amino acid 234 of 403 (UniProt.org). R234* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R308C | missense | unknown | PTEN R308C lies within the C2 tensin-type domain of the Pten protein (UniProt.org). R308C has been identified in the scientific literature (PMID: 32754865), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| R335* | nonsense | loss of function | PTEN R335* results in a premature truncation of the Pten protein at amino acid 335 of 403 within the C2 tensin-type domain (UniProt.org). R335* results in increased transformation ability in two different cell lines (PMID: 29533785), demonstrates reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270), and fails to suppress transcription of E2f1-regulated genes in culture (PMID: 29108454). | |
| R335G | missense | unknown | PTEN R335G lies within the C2 tensin-type domain of the Pten protein (UniProt.org). R335G has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| R335L | missense | loss of function - predicted | PTEN R335L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). R335L results in decreased phosphatase activity in yeast (PMID: 21828076), and is predicted to have reduced interaction with lipids (PMID: 23442912), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R335P | missense | unknown | PTEN R335P lies within the C2 tensin-type domain of the Pten protein (UniProt.org). R335P has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| R41* | nonsense | loss of function - predicted | PTEN R41* results in a premature truncation of the Pten protein at amino acid 41 of 403 (UniProt.org). R41* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| R47K | missense | unknown | PTEN R47K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R47K results in increased lipid phosphatase activity in an in vitro assay (PMID: 25429968) and demonstrates Pten protein stability similar to wild-type protein, but fails to suppress Akt phosphorylation in cell culture and leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| R47M | missense | unknown | PTEN R47M lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R47M has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| R47W | missense | unknown | PTEN R47W lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). R47W demonstrates increased Pten protein stability, but fails to suppress Akt phosphorylation in cell culture, and leads to impaired growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| R55fs | frameshift | loss of function - predicted | PTEN R55fs results in a change in the amino acid sequence of the Pten protein beginning at aa 55 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). R55fs has not been characterized, however, due to the effects of other truncation mutations downstream of R55 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| R74Dfs*25 | frameshift | loss of function - predicted | PTEN R74Dfs*25 indicates a shift in the reading frame starting at amino acid 74 and terminating 25 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). R74Dfs*25 has not been characterized, however, due to the effects of other truncation mutations downstream of R74 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| S10del | deletion | loss of function - predicted | PTEN S10del results in the deletion of an amino acid within the Pten protein at amino acid ten (UniProt.org). S10del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| S10I | missense | loss of function - predicted | PTEN S10I lies within the lipid binding domain of the Pten protein (PMID: 25263454). S10I results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| S10N | missense | loss of function | PTEN S10N lies within the lipid binding domain of the Pten protein (PMID: 25263454). S10N demonstrates phosphatase activity comparable to wild-type Pten (PMID: 10468583, PMID: 25263454), however, S10N results in reduced membrane localization of the Pten protein due to impaired binding with membrane lipids, and subsequently, is unable to prevent Akt signaling, cell proliferation, and cell migration and therefore, confers a loss of function to the Pten protein (PMID: 25263454, PMID: 17213812). | |
| S170G | missense | unknown | PTEN S170G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S170G has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| S170I | missense | loss of function - predicted | PTEN S170I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S170I results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| S170N | missense | loss of function | PTEN S170N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S170N confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302) and increased transformation ability in two different cell lines, as compared to wild-type Pten (PMID: 29533785). | |
| S170R | missense | loss of function | PTEN S170R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S170R results in loss of Pten phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350). | |
| S227F | missense | loss of function - predicted | PTEN S227F lies within the C2 tensin-type domain of the Pten protein (UniProt.org). S227F is predicted to confer a loss of function to the Pten protein, as demonstrated by loss of phosphatase activity in an in vitro assay (PMID: 10866302). | |
| S229* | nonsense | loss of function - predicted | PTEN S229* results in a premature truncation of the Pten protein at amino acid 229 of 403 (UniProt.org). S229* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| S229T | missense | no effect | PTEN S229T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). S229T demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270). | |
| S287* | nonsense | loss of function - predicted | PTEN S287* results in a premature truncation of the Pten protein at aa 287 of 403 within the C2 tensin-type domain (UniProt.org). S287* has not been characterized, however, due to the effects of other truncation mutations downstream of S287 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| S294fs | frameshift | loss of function - predicted | PTEN S294fs results in a change in the amino acid sequence of the Pten protein beginning at aa 294 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). S294fs has not been characterized, however, due to the effects of other truncation mutations downstream of S294 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| S294R | missense | no effect - predicted | PTEN S294R lies within the C2 tensin-type domain of the Pten protein (UniProt.org). S294R results in similar cell proliferation and viability levels as wild-type Pten (PMID: 29533785), and therefore, is predicted to have no effect on Pten protein function. | |
| S302Afs*5 | frameshift | loss of function - predicted | PTEN S302Afs*5 indicates a shift in the reading frame starting at amino acid 302 and terminating 5 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). S302Afs*5 has not been characterized, however, due to the effects of other truncation mutations downstream of S302 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| S338fs | frameshift | loss of function - predicted | PTEN S338fs results in a change in the amino acid sequence of the Pten protein beginning at 338 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). S338fs has not been characterized, however, due to the effects of other truncation mutations downstream of S338 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| S338T | missense | unknown | PTEN S338T lies within the C2 tensin-type domain of the Pten protein (UniProt.org). S338T has been identified in sequencing studies (PMID: 11555573), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| S362L | missense | no effect - predicted | PTEN S362L does not lie within any known functional domains of the Pten protein (UniProt.org). S362L demonstrates inhibition of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 19329485), and therefore, is predicted to have no effect on Pten protein function. | |
| S380A | missense | unknown | PTEN S380A does not lie within any known functional domains of the Pten protein (UniProt.org). S380A retains the ability to respond to PIP2, but demonstrates reduced lipid phosphatase activity (PMID: 17565999), decreased Pten protein stability and reduced Pten phosphorylation (PMID: 10866658, PMID: 11035045), loss of ability to undergo phosphorylation by Topk in an in vitro assay, and results in reduced mitotic entry and increased cell cycle arrest (PMID: 24012691, PMID: 10866658), increased nuclear and membrane localization (PMID: 16807353, PMID: 17565999), and increased transcriptional activation of FKHR in culture (PMID: 10866658), and therefore, its effect on Pten protein function is unknown. | |
| S385* | nonsense | loss of function | PTEN S385* results in a premature truncation of the Pten protein at amino acid 398 of 403 (UniProt.org). S385* results in decreased Pten protein stability and reduced ability to inhibit Akt phosphorylation and transformation in culture (PMID: 10468583). | |
| S385A | missense | unknown | PTEN S385A does not lie within any known functional domains of the Pten protein (UniProt.org). The functional effect of S385A is conflicting as it demonstrates Pten protein stability, cell cycle arrest, and transcriptional activation of FKHR similar to wild-type Pten in culture (PMID: 10866658), however, demonstrates reduced phosphorylation and Pten protein stability (PMID: 11035045) and decreased ability to undergo phosphorylation by Ck2 in cell culture (PMID: 16107342), and demonstrates increased lipid phosphatase activity, but not enhanced catalytic activity via PIP2, and leads to increased nuclear and membrane localization in cell culture (PMID: 17565999, PMID: 16807353), and therefore, its effect on Pten protein function is unknown. | |
| S59* | nonsense | loss of function - predicted | PTEN S59* results in a premature truncation of the Pten protein at amino acid 59 of 403 (UniProt.org). S59* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| S59L | missense | unknown | PTEN S59L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S59L has been identified in sequencing studies (PMID: 19962665), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| S59P | missense | loss of function - predicted | PTEN S59P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). S59P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T131A | missense | loss of function - predicted | PTEN T131A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131A is predicted to confer a loss of function to the Pten protein, as demonstrated by decreased Pten phosphatase activity (PMID: 21828076). | |
| T131fs | frameshift | loss of function - predicted | PTEN T131fs results in a change in the amino acid sequence of the Pten protein beginning at aa 131 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). T131fs has not been characterized, however, due to the effects of other truncation mutations downstream of T131 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| T131I | missense | loss of function - predicted | PTEN T131I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131I demonstrates Pten protein stability similar to wild-type protein, however, results in a partial loss of ability to rescue spheroid formation in cell culture (PMID: 32366478), and demonstrates loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T131L | missense | loss of function | PTEN T131L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131L confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| T131N | missense | loss of function - predicted | PTEN T131N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T131P | missense | loss of function - predicted | PTEN T131P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131P results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T131S | missense | no effect - predicted | PTEN T131S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T131S demonstrates phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| T160del | deletion | loss of function - predicted | PTEN T160del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 160 (UniProt.org). T160del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function | |
| T160I | missense | loss of function - predicted | PTEN T160I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T160I results in a loss of phosphatase activity in yeast (PMID: 21828076), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T167A | missense | loss of function | PTEN T167A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T176A results in decreased phosphatase activity and partial inhibition of Pi3k activity in an yeast assay (PMID: 21828076). | |
| T167N | missense | loss of function | PTEN T167N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T167N demonstrates protein stability similar to wild-type Pten (PMID: 32366478, PMID: 32350270), however, results in a loss of ability to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and delays development in flies (PMID: 32350270). | |
| T167P | missense | loss of function | PTEN T167P lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T167P confers a loss of function on the Pten protein as demonstrated by a loss of phosphatase activity in yeast and in cell culture (PMID: 29706350, PMID: 9256433). | |
| T202I | missense | unknown | PTEN T202I lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T202I leads to reduced developmental growth rate in flies (PMID: 32350270) and reduced Pten protein expression and increased sumoylation, however, retains the ability to suppress PI3K signaling, and demonstrates nuclear localization and lipid phosphatase activity similar to wild-type Pten in culture (PMID: 32150788, PMID: 21828076), and therefore, its effect on Pten protein function is unknown. | |
| T232A | missense | loss of function - predicted | PTEN T232A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T232A demonstrates binding to Dlc1 and p85 (PMID: 26166433) and protein stability similar to wild-type Pten, but, results in an intermediate ability to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T277A | missense | loss of function | PTEN T277A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T277A results in similar phosphatase activity to wild-type Pten in an in vitro assay (PMID: 28263967), and in cultured cells and a yeast assay (PMID: 36543932) but results in reduced protein stability (PMID: 28263967, PMID: 36543932), altered subcellular localization (PMID: 36543932), decreased suppression of Akt phosphorylation and Pip3 levels, increased cell proliferation and migration, and inhibition of Pten membrane and nuclear localization in cell culture (PMID: 28263967). | |
| T277del | deletion | loss of function - predicted | PTEN T277del results in the deletion of an amino acid in the C2 tensin-type domain of the Pten protein at amino acid 277 (UniProt.org). T277del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T277I | missense | unknown | PTEN T277I lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T277I has been identified in sequencing studies (PMID: 23917401, PMID: 32351019, PMID: 35052351), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| T277N | missense | loss of function - predicted | PTEN T277N lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T277N results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T319* | nonsense | loss of function | PTEN T319* results in a premature truncation of the Pten protein at amino acid 254 of 403 (UniProt.org). T319* results in decreased Pten protein stability, failure to inhibit Akt phosphorylation and cell transformation in culture (PMID: 10468583). | |
| T319del | deletion | loss of function | PTEN T319del results in the deletion of an amino acid within the C2 tensin-type domain of the Pten protein at amino acid 319 (UniProt.org). T319del confers a loss of function to the Pten protein as demonstrated by increased Pten degradation in cultured cells and decreased phosphatase activity in an in vitro assay (PMID: 10468583). | |
| T319fs | frameshift | loss of function - predicted | PTEN T319fs results in a change in the amino acid sequence of the Pten protein beginning at aa 319 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). T319fs has not been characterized, however, due to the effects of other truncation mutations downstream of T319 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| T321* | nonsense | loss of function - predicted | PTEN T321* results in a premature truncation of the Pten protein at amino acid 321 of 403 (UniProt.org). T321* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| T321fs | frameshift | loss of function - predicted | PTEN T321fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 321 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). T321fs has not been characterized, however, due to the effects of other truncation mutations downstream of T321 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| T348I | missense | loss of function | PTEN T348I lies within the C2 tensin-type domain and NOP53-interacting region of the Pten protein (UniProt.org). T348I results in decreased phosphatase activity in an in vitro assay, and increased Pten degradation, increased Akt phosphorylation, and partial reduction in the inhibition of transformation relative to wild-type Pten in cultured cells (PMID: 10468583). | |
| T348S | missense | no effect - predicted | PTEN T348S lies within the C2 tensin-type domain of the Pten protein (UniProt.org). T348S demonstrates reduced Pten protein stability, but suppression of Akt phosphorylation similar to wild-type Pten in cell culture (PMID: 32350270), and therefore, is predicted to have no effect on Pten protein function. | |
| T363* | nonsense | unknown | PTEN T363* results in a premature truncation of the Pten protein at amino acid 363 of 403 (UniProt.org). T363* results in decreased Pten protein expression in culture (PMID: 10468583), but has not been fully biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| T363N | missense | unknown | PTEN T363N does not lie within any known functional domains of the Pten protein (UniProt.org). T363N demonstrates Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, however, leads to impaired developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| T382A | missense | unknown | PTEN T382A does not lie within any known functional domains of the Pten protein (UniProt.org). T382A results in nuclear and membrane localization similar to wild-type Pten (PMID: 25823029, PMID: 17565999), but results in increased ubiquitination (PMID: 11431330), increased cell cycle arrest and transcriptional activation of FKHR, and retains the ability to undergo phosphorylation by Topk in an in vitro assay (PMID: 24012691) and the ability to respond to PIP2, but demonstrates reduced lipid phosphatase activity (PMID: 17565999), decreased Pten protein stability (PMID: 10866658, PMID: 11035045), and impaired nuclear localization in cell culture (PMID: 16807353), and therefore, its effect on Pten protein function is unknown. | |
| T382S | missense | loss of function | PTEN T382S does not lie within any known functional domains of the Pten protein (UniProt.org). T382S demonstrates reduced Pten protein stability and fails to rescue spheroid formation in cell culture (PMID: 32366478). | |
| T383A | missense | unknown | PTEN T383A does not lie within any known functional domains of the Pten protein (UniProt.org). The functional effect of T383A is conflicting, as it results in nuclear localization similar to wild-type Pten (PMID: 25823029), however, leads to increased nuclear localization (PMID: 16807353), and retains the ability to undergo phosphorylation by Topk (PMID: 24012691) and the ability to respond to PIP2, but demonstrates reduced lipid phosphatase activity, impaired membrane localization (PMID: 17565999), reduced protein stability, increased cell cycle arrest and FKHR transcriptional activation (PMID: 10866658, PMID: 11035045), and increased ubiquitination in culture (PMID: 11431330), and therefore, its effect on Pten protein function is unknown. | |
| T398* | nonsense | unknown | PTEN T398* results in a premature truncation of the Pten protein at amino acid 398 of 403 (UniProt.org). T398* demonstrates protein stability similar to wild-type Pten in cultured cells (PMID: 10468583), but has not been fully biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| T401* | nonsense | no effect - predicted | PTEN T401* results in a premature truncation of the Pten protein at amino acid 401 of 403 (UniProt.org). T401* demonstrates protein stability and the ability to inhibit Akt phosphorylation and cell transformation to similar levels as wild-type Pten in culture (PMID: 10468583), and therefore, is predicted to have no effect on Pten protein function. | |
| T401I | missense | unknown | PTEN T401I lies within the PDZ domain-binding region of the Pten protein (UniProt.org). T401I demonstrates phosphatase activity (PMID: 10866302, PMID: 30993208) and subcellular localization (PMID: 30993208) similar to wild-type Pten in culture, but has impaired regulation of Glut1 plasma membrane expression and glucose uptake (PMID: 29117568), and therefore, its effect on Pten protein function is unknown. | |
| T78A | missense | no effect | PTEN T78A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). T78A results in minimal colony formation in yeast (PMID: 32471850), and Pten protein stability and suppression of Akt phosphorylation similar to wild-type Pten in cell culture, and leads to normal developmental growth in flies (PMID: 32350270). | |
| V119del | deletion | loss of function - predicted | PTEN V119del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 119 (UniProt.org). V119del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V119fs | frameshift | loss of function - predicted | PTEN V119fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 119 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V119fs has not been characterized, however, due to the effects of other truncation mutations downstream of V119 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V119G | missense | loss of function - predicted | PTEN V119G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V119G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V119K | missense | unknown | PTEN V119K lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V119K has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| V133I | missense | loss of function | PTEN V133I lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V133I demonstrates Pten protein stability similar to wild-type protein, however, fails to rescue spheroid formation in cell culture (PMID: 32366478), and demonstrates loss of phosphatase activity in an in-vitro assay (PMID: 10866302). | |
| V158fs | frameshift | loss of function - predicted | PTEN V158fs results in a change in the amino acid sequence of the Pten protein beginning at aa 158 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V158fs has not been characterized, however, due to the effects of other truncation mutations downstream of V158 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V166E | missense | loss of function - predicted | PTEN V166E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V166E results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V166G | missense | loss of function - predicted | PTEN V166G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V166G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V166Sfs*14 | frameshift | loss of function - predicted | PTEN V166Sfs*14 indicates a shift in the reading frame starting at amino acid 166 and terminating 14 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). V166Sfs*14 has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V175A | missense | unknown | PTEN V175A lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V175A has been identified in the scientific literature (PMID: 27494611), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| V175E | missense | loss of function - predicted | PTEN V175E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V175E results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V217D | missense | loss of function | PTEN V217D lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V217D confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| V217fs | frameshift | loss of function - predicted | PTEN V217fs results in a change in the amino acid sequence of the Pten protein beginning at aa 217 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V217fs has not been characterized, however, due to the effects of other truncation mutations downstream of V217 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V217G | missense | loss of function - predicted | PTEN V217G lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V217G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V249E | missense | loss of function - predicted | PTEN V249E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V249E results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V255A | missense | loss of function | PTEN V255A lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V255A demonstrates reduced phosphatase activity in an in vitro assay (PMID: 10340391), decreased Pten protein stability and fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| V255del | deletion | loss of function - predicted | PTEN V255del results in the deletion of an amino acid in the C2 tensin-type domain of the Pten protein at amino acid 255 (UniProt.org). V255del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V275* | nonsense | loss of function - predicted | PTEN V275* results in a premature truncation of the Pten protein at amino acid 275 of 403 (UniProt.org). V275* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V275G | missense | loss of function - predicted | PTEN V275G lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V275G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V290* | nonsense | loss of function - predicted | PTEN V290* results in a premature truncation of the Pten protein at amino acid 290 of 403 (UniProt.org). V290* has not been characterized, however, due to the effects of other truncation mutations downstream of V290 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V290fs | frameshift | loss of function - predicted | PTEN V290fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 290 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V290fs has not been characterized, however, due to the effects of other truncation mutations downstream of V290 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V290Sfs*8 | frameshift | loss of function - predicted | PTEN V290Sfs*8 indicates a shift in the reading frame starting at amino acid 290 and terminating 8 residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). V290Sfs*8 has not been characterized, however, due to the effects of other truncation mutations downstream of V290 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V317fs | frameshift | loss of function - predicted | PTEN V317fs results in a change in the amino acid sequence of the Pten protein beginning at aa 317 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V317fs has not been characterized, however, due to the effects of other truncation mutations downstream of V317 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| V343E | missense | loss of function | PTEN V343E lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V343E confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302) and the inability to bind the Pten interacting protein, PICT-1 (PMID: 15355975). | |
| V343L | missense | unknown | PTEN V343L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). V343L has not been identified in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| V351* | nonsense | unknown | PTEN V351* results in a premature truncation of the Pten protein at amino acid 351 of 403 (UniProt.org). V351* demonstrates phosphatase activity and inhibition of Akt phosphorylation similar to wild-type, but results in decreased Pten protein stability and reduced ability to inhibit transformation in culture (PMID: 10468583), and therefore, its effect on Pten protein function is unknown. | |
| V369G | missense | no effect - predicted | PTEN V369G does not lie within any known functional domains of the Pten protein (UniProt.org). V369G demonstrates phosphatase activity similar to wild-type Pten in an in vitro assay (PMID: 10866302), and therefore, is predicted to have no effect on Pten protein function. | |
| V45del | deletion | loss of function - predicted | PTEN V45del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 45 (UniProt.org). V45del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V53E | missense | loss of function - predicted | PTEN V53E lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). V53E results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V54del | deletion | loss of function - predicted | PTEN V54del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 54 (UniProt.org). V54del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| V54fs | frameshift | loss of function - predicted | PTEN V54fs results in a change in the amino acid sequence of the Pten protein beginning at aa 54 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). V54fs has not been characterized, however, due to the effects of other truncation mutations downstream of V54 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| W111* | nonsense | loss of function - predicted | PTEN W111* results in a premature truncation of the Pten protein at amino acid 111 of 403 (UniProt.org). W111* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| W111fs | frameshift | loss of function - predicted | PTEN W111fs results in a change in the amino acid sequence of the Pten protein beginning at 111 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). W111fs has not been characterized, however, due to the effects of other truncation mutations downstream of W111 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| W111G | missense | loss of function - predicted | PTEN W111G lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). W111G results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| W111R | missense | loss of function - predicted | PTEN W111R lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). W111R results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| W111S | missense | loss of function - predicted | PTEN W111S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). W111S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| W274* | nonsense | loss of function - predicted | PTEN W274* results in a premature truncation of the Pten protein at amino acid 274 of 403 (UniProt.org). W274* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| W274fs | frameshift | loss of function - predicted | PTEN W274fs results in a change in the amino acid sequence of the Pten protein beginning at aa 274 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). W274fs has not been characterized, however, due to the effects of other truncation mutations downstream of W274 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| W274L | missense | unknown | PTEN W274L lies within the C2 tensin-type domain of the Pten protein (UniProt.org). W274L fails to suppress Akt phosphorylation, and demonstrates reduced Pten protein stability (PMID: 32350270), reduced lipid phosphatase activity (PMID: 32150788), decreased nuclear localization (PMID: 32150788, PMID: 29373119), and reduced ability to dephosphorylate Pip3, but results in increased neuronal cell size (PMID: 29373119), increased sumoylation (PMID: 32150788), rescues growth of yeast cells similar to wild-type Pten in culture (PMID: 21828076), and leads to normal developmental growth in flies (PMID: 32350270), and therefore, its effect on Pten protein function is unknown. | |
| wild-type | none | no effect | Wild-type PTEN indicates that no mutation has been detected within the PTEN gene. | |
| Y138* | nonsense | loss of function - predicted | PTEN Y138* results in a premature truncation of the Pten protein at amino acid 138 of 403 (UniProt.org). Y138* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y138L | missense | loss of function | PTEN Y138L lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y138L demonstrates Pten protein stability similar to wild-type protein in one study (PMID: 32366478) and reduced protein stability in another study (PMID: 32350270), and retains lipid phosphatase activity, however, demonstrates loss of protein phosphatase activity (PMID: 22413754), fails to rescue spheroid formation (PMID: 32366478), and fails to suppress Akt phosphorylation in cell culture, and delays development in flies (PMID: 32350270). | |
| Y155C | missense | loss of function | PTEN Y155C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y155C confers a loss of function to the Pten protein as demonstrated by loss of phosphatase activity (PMID: 10866302, PMID: 27829222), and reduced Pten protein stability and failure to rescue spheroid formation in cell culture (PMID: 32366478). | |
| Y155fs | frameshift | loss of function - predicted | PTEN Y155fs results in a change in the amino acid sequence of the Pten protein beginning at aa 155 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Y155fs has not been characterized, however, due to the effects of other truncation mutations downstream of Y155 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y155H | missense | loss of function | PTEN Y155H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y155H demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270). | |
| Y155N | missense | loss of function | PTEN Y155N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y155N demonstrates reduced Pten protein stability and fails to suppress Akt phosphorylation in cell culture (PMID: 32350270). | |
| Y16C | missense | unknown | PTEN Y16C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y16C demonstrates phosphatase activity similar to wild-type Pten (PMID: 17213812, PMID: 25875300), but does not suppress downstream Akt signaling in culture (PMID: 21536651, PMID: 17942903), and therefore, its effect on Pten protein function is unknown. | |
| Y16D | missense | loss of function - predicted | PTEN Y16D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y16D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y16fs | frameshift | loss of function - predicted | PTEN Y16fs results in a change in the amino acid sequence of the Pten protein beginning at aa 16 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Y16fs has not been characterized, however, due to the effects of other truncation mutations downstream of Y16 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y174* | nonsense | loss of function - predicted | PTEN Y174* results in a premature truncation of the Pten protein at amino acid 174 of 403 (UniProt.org). Y174* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y174D | missense | loss of function - predicted | PTEN Y174D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y174D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y174H | missense | unknown | PTEN Y174H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y174H has been identified in the scientific literature (PMID: 32376656), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y174N | missense | loss of function | PTEN Y174N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y174N results in a loss of Pten phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350). | |
| Y176* | nonsense | loss of function - predicted | PTEN Y176* results in a premature truncation of the Pten protein at amino acid 176 of 403 (UniProt.org). Y176* has not been characterized, however, due to the effects of other truncation mutations downstream of Y176 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y176C | missense | unknown | PTEN Y176C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y176C demonstrates phosphatase activity in yeast and in a Drosophila wing overgrowth assay (PMID: 21828076, PMID: 34492006), protein stability (PMID: 32366478, PMID: 32350270), suppression of Akt phosphorylation, and developmental growth in flies similar to wild-type Pten (PMID: 32350270), however, results in decreased catalytic activity (PMID: 25647146), and loss of the ability to rescue spheroid formation in cell culture (PMID: 32366478), and therefore, its effect on Pten protein function is unknown. | |
| Y176del | deletion | loss of function - predicted | PTEN Y176del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 176 (UniProt.org). Y176del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y177* | nonsense | loss of function - predicted | PTEN Y177* results in a premature truncation of the Pten protein at amino acid 177 of 403 (UniProt.org). Y177* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y177C | missense | loss of function - predicted | PTEN Y177C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y177C results in nuclear localization in cultured cells (PMID: 33828082) and reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y177D | missense | loss of function - predicted | PTEN Y177D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y177D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y177F | missense | unknown | PTEN Y177F lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y177F has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y177S | missense | loss of function - predicted | PTEN Y177S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y177S results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y178* | nonsense | loss of function - predicted | PTEN Y178* results in a premature truncation of the Pten protein at amino acid 178 of 403 (UniProt.org). Y178* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y178C | missense | unknown | PTEN Y178C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y178C has been identified in the scientific literature (PMID: 34775732), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y178del | deletion | loss of function - predicted | PTEN Y178del results in the deletion of an amino acid within the phosphatase tensin-type domain of the Pten protein at amino acid 178 (UniProt.org). Y178del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y178H | missense | unknown | PTEN Y178H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y178H has been identified in the scientific literature (PMID: 17942903), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y180H | missense | no effect | PTEN Y180H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y180H demonstrates ability to rescue spheroid formation (PMID: 32366478), Pten protein stability (PMID: 32350270, PMID: 32366478), and Akt phosphorylation similar to wild-type Pten in cell culture, and results in normal developmental growth in flies (PMID: 32350270). | |
| Y188* | nonsense | loss of function - predicted | PTEN Y188* results in a premature truncation of the Pten protein at amino acid 188 of 403 (UniProt.org). Y188* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y188del | deletion | loss of function - predicted | PTEN Y188del results in the deletion of an amino acid of the Pten protein at amino acid 188 (UniProt.org). Y188del results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y225* | nonsense | loss of function - predicted | PTEN Y225* results in a premature truncation of the Pten protein at amino acid 225 of 403 (UniProt.org). Y225* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y240* | nonsense | loss of function - predicted | PTEN Y240* results in a premature truncation of the Pten protein at amino acid 240 of 403 (UniProt.org). Y240* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y240Ffs*2 | frameshift | loss of function - predicted | PTEN Y240Ffs*2 indicates a shift in the reading frame starting at amino acid 240 and terminating two residues downstream causing a premature truncation of the 403 amino acid Pten protein (UniProt.org). Y240Ffs*2 has not been characterized, however, due to the effects of other truncation mutations downstream of Y240 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y27C | missense | loss of function | PTEN Y27C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y27C demonstrates reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270), and has been associated with resistance to Egfr inhibitors as a secondary resistance mutation in cell culture (PMID: 26181354, PMID: 29325035). | Y |
| Y27D | missense | loss of function - predicted | PTEN Y27D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y27D has not been biochemically characterized, but results in increased transformation ability in two different cell lines (PMID: 29533785), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y27fs | frameshift | loss of function - predicted | PTEN Y27fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 27 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Y27fs has not been characterized, however, due to the effects of other truncation mutations downstream of Y27 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y27H | missense | unknown | PTEN Y27H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y27H has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y27N | missense | loss of function | PTEN Y27N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y27N results in reduced Pten phosphatase activity in a yeast assay (PMID: 29706350) and failure to suppress Akt signaling in cultured cells (PMID: 32704382). | |
| Y27S | missense | loss of function - predicted | PTEN Y27S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y27S results in loss of phosphatase activity in an in vitro assay (PMID: 10866302), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y315* | nonsense | loss of function - predicted | PTEN Y315* results in a premature truncation of the Pten protein at amino acid 315 of 403 (UniProt.org). Y315* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y336* | nonsense | loss of function | PTEN Y336* results in a premature truncation within the C2 tensin-type domain of the Pten protein at amino acid 336 of 403 (UniProt.org). Y336* inhibits Akt phosphorylation and associates with heterochromatin to similar levels of wild-type Pten, but fails to stabilize Hp1alpha protein and enhances Hp1alpha polyubiquitination, leading to satellite DNA overexpression, failure to suppress cell growth, arrest cycle cycle progression, or inhibit transformation in cultured cells (PMID: 25946202). | |
| Y346* | nonsense | unknown | PTEN Y346* results in a premature truncation of the Pten protein at amino acid 346 of 403 (UniProt.org). Y346* has been identified in sequencing studies (PMID: 33876771), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y346C | missense | unknown | PTEN Y346C lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Y346C has not been characterized in the scientific literature and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y346D | missense | unknown | PTEN Y346D lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Y346D has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y346F | missense | no effect - predicted | PTEN Y346F lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Y346F demonstrates increased Pten protein stability, but suppression of Akt phosphorylation similar to wild-type Pten in cell culture, and leads to normal developmental growth in flies (PMID: 32350270), and therefore, is predicted to have no effect on Pten protein function. | |
| Y346H | missense | unknown | PTEN Y346H lies within the C2 tensin-type domain of the Pten protein (UniProt.org). Y346H has not been characterized and therefore, its effect on Pten protein function is unknown (PubMed, Dec 2023). | |
| Y379* | nonsense | unknown | PTEN Y379* results in a premature truncation of the Pten protein at amino acid 379 of 403 (UniProt.org). Y379* results in decreased Pten protein expression in cultured cells (PMID: 10468583), but has not been fully biochemically characterized and therefore, its effect on Pten protein function is unknown. | |
| Y46* | nonsense | loss of function - predicted | PTEN Y46* results in a premature truncation of the Pten protein at amino acid 46 of 403 (UniProt.org). Y46* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y46C | missense | unknown | PTEN Y46C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y46C has been identified in sequencing studies (PMID: 20530683, PMID: 28683746), but has not been biochemically characterized and therefore, its effect on Pten protein function is unknown (PubMed, Oct 2023). | |
| Y46D | missense | loss of function - predicted | PTEN Y46D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y46D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y46H | missense | loss of function - predicted | PTEN Y46H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y46H results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y65* | nonsense | loss of function - predicted | PTEN Y65* results in a premature truncation of the Pten protein at amino acid 65 of 403 (UniProt.org). Y65* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y65C | missense | loss of function | PTEN Y65C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y65C confers a loss of function to the Pten protein as demonstrated by reduced ATP-binding, nuclear accumulation (PMID: 20926450), increased cell proliferation, decreased apoptosis, and is transforming in culture (PMID: 19457929), and leads to reduced Pten protein stability, fails to suppress Akt phosphorylation in cell culture, and leads to impaired developmental growth in flies (PMID: 32350270). | |
| Y65D | missense | loss of function - predicted | PTEN Y65D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y65D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y65S | missense | loss of function | PTEN Y65S lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y65S confers a loss of function on Pten as demonstrated by altered cell morphology and cytoskeletal organization, decreased ability to suppress proliferation and migration, and increased phosphorylation of Akt in cultured cells, and resistance to apoptotic induction in one of two assays (PMID: 34943931). | |
| Y68* | nonsense | loss of function - predicted | PTEN Y68* results in a premature truncation of the Pten protein at amino acid 68 of 403 (UniProt.org). Y68* has not been characterized, however, due to the effects of other truncation mutations downstream of Y68 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y68C | missense | loss of function | PTEN Y68C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y68C confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in an in vitro assay and a yeast assay (PMID: 10866302, PMID: 29706350). | |
| Y68D | missense | loss of function | PTEN Y68D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y68D confers a loss of Pten protein function as demonstrated by loss of phosphatase activity in yeast (PMID: 21828076, PMID: 29706350). | |
| Y68fs | frameshift | loss of function - predicted | PTEN Y68fs results in a change in the amino acid sequence of the PTEN protein beginning at aa 68 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Y68fs has not been characterized, however, due to the effects of other truncation mutations downstream of Y68 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y68H | missense | loss of function | PTEN Y68H lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y68H demonstrates loss of phosphatase activity (PMID: 10866302) and reduced Pten protein stability (PMID: 20926450, PMID: 32350270), and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| Y68N | missense | loss of function | PTEN Y68N lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y68N demonstrates reduced Pten protein stability, and fails to suppress Akt phosphorylation in cell culture, and delays developmental growth in flies (PMID: 32350270). | |
| Y76* | nonsense | loss of function - predicted | PTEN Y76* results in a premature truncation of the Pten protein at amino acid 76 of 403 (UniProt.org). Y76* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y76fs | frameshift | loss of function - predicted | PTEN Y76fs results in a change in the amino acid sequence of the Pten protein beginning at aa 76 of 403, likely resulting in premature truncation of the functional protein (UniProt.org). Y76fs has not been characterized, however, due to the effects of other truncation mutations downstream of Y76 (PMID: 10468583), is predicted to lead to a loss of Pten protein function. | |
| Y88* | nonsense | loss of function - predicted | PTEN Y88* results in a premature truncation of the Pten protein at amino acid 88 of 403 (UniProt.org). Y88* results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. | |
| Y88C | missense | no effect - predicted | PTEN Y88C lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y88C results in lipid phosphatase activity similar to wild-type Pten in yeast (PMID: 21828076), and therefore, is predicted to have no effect on Pten protein function. | |
| Y88D | missense | loss of function - predicted | PTEN Y88D lies within the phosphatase tensin-type domain of the Pten protein (UniProt.org). Y88D results in reduced phosphatase activity in a yeast assay (PMID: 29706350), and therefore, is predicted to lead to a loss of Pten protein function. |
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