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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P60484: Variant p.Lys289Glu

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information Variant position: help 289 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 Lysine (K) to Glutamate (E) at position 289 (K289E, p.Lys289Glu). 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 large size and basic (K) to medium size and acidic (E) 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; predominantly nuclear. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 289 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 KMFHFWVNTFFIPGPEETSE K VENGSLCDQEIDSICSIERA 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                         KMFHFW--------------------VNTFFIP--------G---------------PEETSEKVE-------------NGSLC-DQEI--DSICSIERA

                              KMFHFW--------------------VNTFFIP--------

Mouse                         KMFHFW--------------------VNTFFIP--------

Rat                           KMFHFW--------------------VNTFFIP--------

Xenopus laevis                KMFHFW--------------------VNTFFIP--------

Caenorhabditis elegans        YCRYFYKQRSTSRSRYPRKFRYCPLIKKHFYIP--------

Slime mold                    RMFMFW--------------------VNTSFVQQLEIIPKS

Fission yeast                 ----LW--------------------KSSDISS--------
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 294 – 294 Phosphoserine
Cross 289 – 289 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 191 – 403 Missing. In isoform 3.
Mutagenesis 289 – 289 K -> E. Cytoplasmic; when associated with E-13. Shows less tumor suppressive ability; when associated with E-13.



Literature citations
The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network.
Song M.S.; Salmena L.; Carracedo A.; Egia A.; Lo-Coco F.; Teruya-Feldstein J.; Pandolfi P.P.;
Nature 455:813-817(2008)
Cited for: FUNCTION; INTERACTION WITH USP7; UBIQUITINATION AT LYS-13 AND LYS-289; DEUBIQUITINATION BY USP7; SUBCELLULAR LOCATION; MUTAGENESIS OF LYS-13 AND LYS-289; CHARACTERIZATION OF VARIANT CWS1 GLU-289; Mutational abrogation of the PTEN/MMAC1 gene in gastrointestinal polyps in patients with Cowden disease.
Chi S.-G.; Kim H.-J.; Park B.-J.; Min H.-J.; Park J.-H.; Kim Y.-W.; Dong S.-H.; Kim B.-H.; Lee J.-I.; Chang Y.-W.; Chang R.; Kim W.-K.; Yang M.-H.;
Gastroenterology 115:1084-1089(1998)
Cited for: VARIANT CWS1 GLU-289; 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.