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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14003: Variant p.Phe448Leu

Potassium voltage-gated channel subfamily C member 3
Gene: KCNC3
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Variant information Variant position: help 448 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 Phenylalanine (F) to Leucine (L) at position 448 (F448L, p.Phe448Leu). 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 aromatic (F) to medium size and hydrophobic (L) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 SCA13; alters gating; slows channel closing; decreases protein abundance; no effect on localization to the plasma membrane; no effect on N-glycosylation; no effect on tetramerization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 448 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 757 The length of the canonical sequence.
Location on the sequence: help TRHFVGLRVLGHTLRASTNE F LLLIIFLALGVLIFATMIYY 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                         TRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYY

Mouse                         TRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYY

Rat                           TRHFVGLRVLGHTLRASTNEFLLLIIFLALGVLIFATMIYY
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 – 757 Potassium voltage-gated channel subfamily C member 3
Transmembrane 448 – 469 Helical; Name=Segment S5



Literature citations
Altered Kv3.3 channel gating in early-onset spinocerebellar ataxia type 13.
Minassian N.A.; Lin M.C.; Papazian D.M.;
J. Physiol. (Lond.) 590:1599-1614(2012)
Cited for: CHARACTERIZATION OF VARIANTS SCA13 HIS-420; HIS-423 AND LEU-448; FUNCTION; SUBCELLULAR LOCATION; Spinocerebellar ataxia-13 Kv3.3 potassium channels: arginine-to-histidine mutations affect both functional and protein expression on the cell surface.
Zhao J.; Zhu J.; Thornhill W.B.;
Biochem. J. 454:259-265(2013)
Cited for: CHARACTERIZATION OF VARIANTS SCA13 HIS-366; HIS-420; HIS-423 AND LEU-448; FUNCTION; SUBCELLULAR LOCATION; SUBUNIT; INTERACTION WITH KCNC1; MUTAGENESIS OF ARG-366; ARG-420 AND ARG-423; KCNC3(R420H), a K(+) channel mutation causative in spinocerebellar ataxia 13 displays aberrant intracellular trafficking.
Gallego-Iradi C.; Bickford J.S.; Khare S.; Hall A.; Nick J.A.; Salmasinia D.; Wawrowsky K.; Bannykh S.; Huynh D.P.; Rincon-Limas D.E.; Pulst S.M.; Nick H.S.; Fernandez-Funez P.; Waters M.F.;
Neurobiol. Dis. 71:270-279(2014)
Cited for: CHARACTERIZATION OF VARIANTS SCA13 HIS-420 AND LEU-448; SUBCELLULAR LOCATION; GLYCOSYLATION; Mutations in voltage-gated potassium channel KCNC3 cause degenerative and developmental nervous system phenotypes.
Waters M.F.; Minassian N.A.; Stevanin G.; Figueroa K.P.; Bannister J.P.A.; Nolte D.; Mock A.F.; Evidente V.G.H.; Fee D.B.; Mueller U.; Duerr A.; Brice A.; Papazian D.M.; Pulst S.M.;
Nat. Genet. 38:447-451(2006)
Cited for: VARIANTS SCA13 HIS-420 AND LEU-448; CHARACTERIZATION OF VARIANTS SCA13 HIS-420 AND LEU-448; FUNCTION; SUBCELLULAR LOCATION;
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.