UniProtKB/Swiss-Prot P60484 : Variant p.Val369Gly
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information
Variant position:
369
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
US
The variants are classified into three categories: LP/P, LB/B and US.LP/P: likely pathogenic or pathogenic. LB/B: likely benign or benign. US: uncertain significance
Residue change:
From Valine (V) to Glycine (G) at position 369 (V369G, p.Val369Gly).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:
Change from medium size and hydrophobic (V) to glycine (G)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-3
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:
Retains Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 phosphatase activity; retains ability to bind phospholipid membranes.
Any additional useful information about the variant.
Sequence information
Variant position:
369
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
403
The length of the canonical sequence.
Location on the sequence:
KTVEEPSNPEASSSTSVTPD
V SDNEPDHYRYSDTTDSDPEN
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:
The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KTVEEPS----NPEASSS-------TSVTPDV SDN------EPDHYRYSDTTDSDPEN
KTVEEPS----NPEASSS-------TSVTPDV SDN------
Mouse KTVEEPS----NPEASSS-------TSVTPDV SDN------
Rat KTVEEPS----NPEASSS-------TSVTPDV SDN------
Xenopus laevis KTVEESS----NSEASSS-------TSVTPDV SDN------
Caenorhabditis elegans HVVEESNGSSKNPKALKTREQMVKETGKDTQK TRNHVLLHL
Slime mold SSQSNPV----QQESNPS---------TTTQV S--------
Fission yeast PMLVEYT------------------NGINFQQ GINSFLQGQ
Sequence annotation in neighborhood:
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
Chain
2 – 403
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Region
352 – 403
Disordered
Compositional bias
353 – 370
Polar residues
Modified residue
366 – 366
Phosphothreonine; by GSK3-beta and PLK3
Modified residue
370 – 370
Phosphoserine; by CK2 and PLK3
Modified residue
380 – 380
Phosphoserine; by ROCK1 and CK2
Modified residue
382 – 382
Phosphothreonine; by ROCK1 and CK2
Modified residue
383 – 383
Phosphothreonine; by ROCK1 and CK2
Modified residue
385 – 385
Phosphoserine; by CK2
Alternative sequence
191 – 403
Missing. In isoform 3.
Mutagenesis
366 – 366
T -> A. Decreased stability.
Mutagenesis
370 – 370
S -> A. Decreased stability.
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.