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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BT40: Variant p.Ile363Thr

Inositol polyphosphate 5-phosphatase K
Gene: INPP5K
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Variant information Variant position: help 363 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 Isoleucine (I) to Threonine (T) at position 363 (I363T, p.Ile363Thr). 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 (I) to medium size and polar (T) 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 MDCCAID; shows a diffuse perinuclear mislocalization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 363 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 448 The length of the canonical sequence.
Location on the sequence: help NDMMVSYSSTSDFPSSPWDW I GLYKVGLRDVNDYVSYAWVG 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                         NDMMVSYSSTSDFPSSPWDWIGLYKVGLRDVNDYVSYAWVG

Mouse                         NDMLISYTSTPEFLSSSWDWIGLYKVGMRHINDYVAYVWVG
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 1 – 448 Inositol polyphosphate 5-phosphatase K
Region 318 – 448 Required for interaction with GPR78 and PAK1
Region 321 – 448 Required for ruffle localization
Mutagenesis 349 – 349 Y -> AF. No effect on EGF-induced ruffle localization.
Mutagenesis 361 – 361 D -> A. Significant decrease in EGF-induced ruffle localization.
Mutagenesis 362 – 362 W -> A. Significant decrease in EGF-induced ruffle localization.
Mutagenesis 376 – 376 Y -> AF. No effect on EGF-induced ruffle localization.



Literature citations
Mutations in INPP5K, Encoding a Phosphoinositide 5-Phosphatase, Cause Congenital muscular dystrophy with cataracts and mild cognitive impairment.
Wiessner M.; Roos A.; Munn C.J.; Viswanathan R.; Whyte T.; Cox D.; Schoser B.; Sewry C.; Roper H.; Phadke R.; Marini Bettolo C.; Barresi R.; Charlton R.; Boennemann C.G.; Abath Neto O.; Reed U.C.; Zanoteli E.; Araujo Martins Moreno C.; Ertl-Wagner B.; Stucka R.; De Goede C.; Borges da Silva T.; Hathazi D.; Dell'Aica M.; Zahedi R.P.; Thiele S.; Mueller J.; Kingston H.; Mueller S.; Curtis E.; Walter M.C.; Strom T.M.; Straub V.; Bushby K.; Muntoni F.; Swan L.E.; Lochmueller H.; Senderek J.;
Am. J. Hum. Genet. 100:523-536(2017)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; INVOLVEMENT IN MDCCAID; VARIANTS MDCCAID THR-50; SER-294 DEL; CYS-300 AND THR-363; CHARACTERIZATION OF VARIANTS MDCCAID THR-50; SER-294 DEL; CYS-300 AND THR-363; MUTAGENESIS OF ASP-310;
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.