UniProtKB/Swiss-Prot P60484 : Variant p.Thr401Ile
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene: PTEN
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Variant information
Variant position:
401
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 Threonine (T) to Isoleucine (I) at position 401 (T401I, p.Thr401Ile).
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 polar (T) to medium size and hydrophobic (I)
The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:
-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:
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:
401
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:
DTTDSDPENEPFDEDQHTQI
T KV
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 DTTDSDPENEP--------------FDEDQHTQIT KV
DTTDSDPENEP------------
Mouse DTTDSDPENEP------------
Rat DTTDSDPENEP------------
Xenopus laevis DTTDSDPENEP------------
Caenorhabditis elegans ERRETCPELHPEDKIPRIAHFSE
Slime mold EAEKIENSNAS------------
Fission yeast EMDNSRRSDPF------------
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
Motif
401 – 403
PDZ domain-binding
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
Modified residue
401 – 401
Phosphothreonine
Alternative sequence
191 – 403
Missing. In isoform 3.
Mutagenesis
401 – 401
T -> A. Loss of DLG1-binding. No effect on MAGI2- and MAST2-binding.
Mutagenesis
402 – 402
K -> A. No effect on MAGI2-, MAST2- and DLG1-binding.
Mutagenesis
402 – 402
K -> W. Loss of DLG1-, MAGI2-, MAGI3- and MAST2-binding. Decrease of protein stability.
Mutagenesis
403 – 403
V -> A. Loss of DLG1-, MAGI2-, MAGI3-, MAST1-, MAST2- and MAST3-binding.
Beta strand
395 – 403
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.