Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P60484: Variant p.Val343Glu

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
Feedback?
Variant information Variant position: help 343 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Valine (V) to Glutamate (E) at position 343 (V343E, p.Val343Glu). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from medium size and hydrophobic (V) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CWS1; loss of interaction with NOP53; decreased phosphorylation at S-380; decreased stability; loss of phosphatase activity towards Ins(1,3,4,5)P4. Any additional useful information about the variant.


Sequence information Variant position: help 343 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 403 The length of the canonical sequence.
Location on the sequence: help NDLDKANKDKANRYFSPNFK V KLYFTKTVEEPSNPEASSST The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         NDLDKANKDKANRY------------------FSPN--------------------------------------------------------------FKVKLY------------------------------FTKTVEEPS----NPEASSS-------T

                              NDLDKANKDKANRY------------------FSPN-----

Mouse                         NDLDKANKDKANRY------------------FSPN-----

Rat                           NDLDKANKDKANRY------------------FSPN-----

Xenopus laevis                NDLDKANKDKANRL------------------FSPN-----

Caenorhabditis elegans        VDFENPEEESCEHKTVESIAGFEPLEHLFHESYHPNTAGNM

Slime mold                    APQNNNNNNNLNSSNSNNA-------------TTTT-----

Fission yeast                 --------ERKGQF------------------YFPS-----
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 2 – 403 Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Domain 190 – 350 C2 tensin-type
Region 338 – 348 Required for interaction with NOP53
Modified residue 336 – 336 Phosphotyrosine; by FRK
Alternative sequence 191 – 403 Missing. In isoform 3.
Mutagenesis 336 – 336 Y -> F. Significantly lower phosphatase activity, reduced protein stability and decreased growth-inhibitory effect.
Beta strand 342 – 349



Literature citations
Regulation of PTEN phosphorylation and stability by a tumor suppressor candidate protein.
Okahara F.; Ikawa H.; Kanaho Y.; Maehama T.;
J. Biol. Chem. 279:45300-45303(2004)
Cited for: INTERACTION WITH NOP53; REGION; CHARACTERIZATION OF VARIANTS CWS1 VAL-341; GLU-343 AND GLN-345; Inherited mutations in PTEN that are associated with breast cancer, Cowden disease, and juvenile polyposis.
Lynch E.D.; Ostermeyer E.A.; Lee M.K.; Arena J.F.; Ji H.; Dann J.; Swisshelm K.; Suchard D.; MacLeod P.M.; Kvinnsland S.; Gjertsen B.T.; Heimdal K.; Lubs H.; Moeller P.; King M.-C.;
Am. J. Hum. Genet. 61:1254-1260(1997)
Cited for: VARIANTS CWS1 GLU-343 AND LEU-347; Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay.
Han S.-Y.; Kato H.; Kato S.; Suzuki T.; Shibata H.; Ishii S.; Shiiba K.; Matsuno S.; Kanamaru R.; Ishioka C.;
Cancer Res. 60:3147-3151(2000)
Cited for: CHARACTERIZATION OF VARIANTS ASN-10; CYS-16; GLU-20; SER-27; ARG-61; HIS-68; ARG-112; PRO-121; ARG-129; GLY-130; ILE-133; LEU-134; ARG-165; ASN-170; CYS-173; HIS-173; PRO-173; ASN-174; PHE-227; CYS-251; GLN-345; GLY-369 AND ILE-401; CHARACTERIZATION OF VARIANTS CWS1 TYR-71; TYR-93; PHE-105; TYR-107; PRO-112; ARG-124; GLU-129; LEU-130; GLN-130; TYR-136; CYS-155; ARG-170; GLU-289; GLY-331; VAL-341; ASN-342; GLU-343 AND LEU-347;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.