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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P09936: Variant p.Arg178Gln

Ubiquitin carboxyl-terminal hydrolase isozyme L1
Gene: UCHL1
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Variant information Variant position: help 178 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 Arginine (R) to Glutamine (Q) at position 178 (R178Q, p.Arg178Gln). 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 basic (R) to medium size and polar (Q) 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 SPG79B; increased hydrolase activity; decreased protein abundance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 178 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 223 The length of the canonical sequence.
Location on the sequence: help VNFHFILFNNVDGHLYELDG R MPFPVNHGASSEDTLLKDAA 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                         VNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDTLLKDAA

Mouse                         VNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAA

Rat                           VNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAA

Pig                           VNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAA

Bovine                        VNFHFILFNNVDGHLYELDGRMPFPVNHGTSSEDSLLQDAA

Horse                         VNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDLLLQDAA
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 – 220 Ubiquitin carboxyl-terminal hydrolase isozyme L1
Domain 5 – 205 UCH
Active site 161 – 161 Proton donor
Site 176 – 176 Important for enzyme activity
Site 179 – 179 Susceptible to oxidation
Mutagenesis 161 – 161 H -> D. 10000-fold decrease in enzymatic activity; no change in affinity for ubiquitin ethyl ester.
Mutagenesis 161 – 161 H -> KQNY. Abolishes enzymatic activity.
Mutagenesis 176 – 176 D -> N. 6-fold decrease in affinity for ubiquitin ethyl ester; 97.5% decrease in enzymatic activity.



Literature citations
Novel UCHL1 mutations reveal new insights into ubiquitin processing.
Rydning S.L.; Backe P.H.; Sousa M.M.; Iqbal Z.; Oeye A.M.; Sheng Y.; Yang M.; Lin X.; Slupphaug G.; Nordenmark T.H.; Vigeland M.D.; Bjoeraas M.; Tallaksen C.M.; Selmer K.K.;
Hum. Mol. Genet. 26:1031-1040(2017)
Cited for: VARIANTS SPG79B GLN-178 AND ASP-216; CHARACTERIZATION OF VARIANTS SPG79B GLN-178 AND ASP-216;
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.