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UniProtKB/Swiss-Prot Q13286: Variant p.Glu295Lys

Battenin
Gene: CLN3
Variant information

Variant position:  295
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glutamate (E) to Lysine (K) at position 295 (E295K, p.Glu295Lys).
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 acidic (E) to large size and basic (K)
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:  In CLN3; the mutant is located to vesicles clustered in a perinuclear region. Does not affect protein synthesis and maturation. Does not affect lysosomal localization..
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  295
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  438
The length of the canonical sequence.

Location on the sequence:   WTVFKGLLWYIVPLVVVYFA  E YFINQGLFELLFFWNTSLSH
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                         WTVFKGLLWY-IVPLVVVYFAEYFINQGLFELLFFW---NTSLSH

                              WTVFKGLLWY-IVPLVLVYFAEYFINQGLFELLFFR---NT

Mouse                         WTVFKGLLWY-IIPLVLVYFAEYFINQGLFELLFFR---NT

Slime mold                    YIRCARLVWFNAVNLALVYFFEYVASVGGADLALKKDPNND

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.

TypePositionsDescription
Chain 1 – 435 Battenin
Transmembrane 278 – 298 Helical
Glycosylation 310 – 310 N-linked (GlcNAc...) asparagine
Alternative sequence 280 – 302 GLLWYIVPLVVVYFAEYFINQGL -> VRMMAG. In isoform 3.
Mutagenesis 310 – 310 N -> Q. Does not affect glycosylation.


Literature citations

Defective intracellular transport of CLN3 is the molecular basis of Batten disease (JNCL).
Jaervelae I.; Lehtovirta M.; Tikkanen R.; Kyttaelae A.; Jalanko A.;
Hum. Mol. Genet. 8:1091-1098(1999)
Cited for: CHARACTERIZATION OF VARIANT CLN3 LYS-295; SUBCELLULAR LOCATION;

Neuronal ceroid lipofuscinosis protein CLN3 interacts with motor proteins and modifies location of late endosomal compartments.
Uusi-Rauva K.; Kyttala A.; van der Kant R.; Vesa J.; Tanhuanpaa K.; Neefjes J.; Olkkonen V.M.; Jalanko A.;
Cell. Mol. Life Sci. 69:2075-2089(2012)
Cited for: FUNCTION IN ANTEROGRADE TRANSPORT OF LATE ENDOSOMES AND LYSOSOMES; SUBCELLULAR LOCATION; INTERACTION WITH DCTN1; KIF3A; RAB7A AND RILP; CHARACTERIZATION OF VARIANT CLN3 LYS-295;

Spectrum of mutations in the Batten disease gene, CLN3.
Munroe P.B.; Mitchison H.M.; O'Rawe A.M.; Anderson J.W.; Boustany R.-M.N.; Lerner T.J.; Taschner P.E.M.; de Vos N.; Breuning M.H.; Gardiner R.M.; Mole S.E.;
Am. J. Hum. Genet. 61:310-316(1997)
Cited for: VARIANTS CLN3 PRO-101; PRO-170; LYS-295; PHE-330; CYS-334 AND HIS-334;

Molecular screening of Batten disease: identification of a missense mutation (E295K) in the CLN3 gene.
Zhong N.; Wisniewski K.E.; Kaczmarski A.L.; Ju W.; Xu W.M.; Xu W.W.; McLendon L.; Liu B.; Kaczmarski W.; Brooks S.S.; Brown W.T.;
Hum. Genet. 102:57-62(1998)
Cited for: VARIANT CLN3 LYS-295;

Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses.
Kousi M.; Lehesjoki A.E.; Mole S.E.;
Hum. Mutat. 33:42-63(2012)
Cited for: VARIANTS CLN3 PRO-101; ARG-134; PRO-170; ALA-187; ARG-189; LYS-295 AND HIS-334;

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.