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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P60484: Variant p.Asp331Gly

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information Variant position: help 331 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 Aspartate (D) to Glycine (G) at position 331 (D331G, p.Asp331Gly). 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 acidic (D) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CWS1; reduced phosphatase activity towards Ins(1,3,4,5)P4; retains ability to bind phospholipid membranes. Any additional useful information about the variant.


Sequence information Variant position: help 331 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 NDKEYLVLTLTKNDLDKANK D KANRYFSPNFKVKLYFTKTV 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                         NDKEY----------------LVLTLTKNDLDKANKDKANRY------------------FSPN--------------------------------------------------------------FKVKLY------------------------------FTKTV

                              NDKEY----------------LVLTLTKNDLDKANKDKANR

Mouse                         NDKEY----------------LVLTLTKNDLDKANKDKANR

Rat                           NDKEY----------------LVLTLTKNDLDKANKDKANR

Xenopus laevis                NDKEY----------------LTLALTKNDLDKANKDKANR

Caenorhabditis elegans        SDKVKPATEDELPPARLPDNVRRFPVVGVDFENPEEESCEH

Slime mold                    NNQHYPQSSNNVATSSSHHDNITVVASDAPQNNNNNNNLNS

Fission yeast                 KD-------------------LLLRV----------ERKGQ
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
Modified residue 319 – 319 Phosphothreonine
Modified residue 321 – 321 Phosphothreonine
Modified residue 336 – 336 Phosphotyrosine; by FRK
Alternative sequence 191 – 403 Missing. In isoform 3.
Mutagenesis 319 – 319 T -> A. Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain; when associated with A-321.
Mutagenesis 319 – 319 T -> E. Constitutive interaction with DLC1.
Mutagenesis 319 – 319 T -> Y. Constitutive interaction with DLC1 and interaction with p85 following EGF stimulation.
Mutagenesis 321 – 321 T -> A. Reduces phosphorylation of the C2 tensin-like domain and abolishes interaction with DLC1 following EGF stimulation. Abolishes phosphorylation of the C2 tensin-like domain; when associated with A-319.
Mutagenesis 321 – 321 T -> E. Constitutive interaction with DLC1.
Mutagenesis 327 – 335 KANKDKANR -> AAGADAANA. Reduces growth suppression activity and promotes anchorage-independent growth. Reduces binding to phospholipid membranes in vitro; phosphatase activity towards PtdIns(3,4,5)P3 is not affected.
Mutagenesis 336 – 336 Y -> F. Significantly lower phosphatase activity, reduced protein stability and decreased growth-inhibitory effect.



Literature citations
Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay.
Han S.-Y.; Kato H.; Kato S.; Suzuki T.; Shibata H.; Ishii S.; Shiiba K.; Matsuno S.; Kanamaru R.; Ishioka C.;
Cancer Res. 60:3147-3151(2000)
Cited for: CHARACTERIZATION OF VARIANTS ASN-10; CYS-16; GLU-20; SER-27; ARG-61; HIS-68; ARG-112; PRO-121; ARG-129; GLY-130; ILE-133; LEU-134; ARG-165; ASN-170; CYS-173; HIS-173; PRO-173; ASN-174; PHE-227; CYS-251; GLN-345; GLY-369 AND ILE-401; CHARACTERIZATION OF VARIANTS CWS1 TYR-71; TYR-93; PHE-105; TYR-107; PRO-112; ARG-124; GLU-129; LEU-130; GLN-130; TYR-136; CYS-155; ARG-170; GLU-289; GLY-331; VAL-341; ASN-342; GLU-343 AND LEU-347;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.