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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UNE7: Variant p.Glu28Lys

E3 ubiquitin-protein ligase CHIP
Gene: STUB1
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Variant information Variant position: help 28 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 Glutamate (E) to Lysine (K) at position 28 (E28K, p.Glu28Lys). 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 acidic (E) to large size and basic (K) 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 SCAR16; reduces protein level; does not reduce ubiquitin ligase activity and autoubiquitination. Any additional useful information about the variant.


Sequence information Variant position: help 28 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 303 The length of the canonical sequence.
Location on the sequence: help EGGARLGAGGGSPEKSPSAQ E LKEQGNRLFVGRKYPEAAAC 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                         E---GGARLGA-------GGGSPEKSPSAQELKEQGNRLFVGRKYPEAAAC

Mouse                         E---GGARLGTG------GGGSPDKSPSAQELKEQGNRLFV

Rat                           E---GGARLGTG------GGGSPDKSPSAQELKEQGNRLFV

Chicken                       EREGGGGAVGPGAAGPGAGGGSPEKSHSAQEHKEQGNRLFG
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 – 303 E3 ubiquitin-protein ligase CHIP
Repeat 26 – 59 TPR 1
Region 1 – 30 Disordered
Modified residue 19 – 19 Phosphoserine
Modified residue 23 – 23 Phosphoserine
Modified residue 25 – 25 Phosphoserine
Cross 22 – 22 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 1 – 72 Missing. In isoform 2.
Mutagenesis 30 – 30 K -> A. Loss of interaction with FOXP3 and its ability to ubiquitinate FOXP3. Loss of interaction with SMAD3, HSPA8, HSP90AA1 and HSP90AB1. Reduces interaction, ubiquitination and proteasomal degradation of NFATC3. No effect on localization to the mitochondria following oxygen and glucose deprivation-induced cellular stress.
Helix 26 – 38



Literature citations
STUB1 mutations in autosomal recessive ataxias - evidence for mutation-specific clinical heterogeneity.
Heimdal K.; Sanchez-Guixe M.; Aukrust I.; Bollerslev J.; Bruland O.; Jablonski G.E.; Erichsen A.K.; Gude E.; Koht J.A.; Erdal S.; Fiskerstrand T.; Haukanes B.I.; Boman H.; Bjoerkhaug L.; Tallaksen C.M.; Knappskog P.M.; Johansson S.;
Orphanet J. Rare Dis. 9:146-146(2014)
Cited for: VARIANTS SCAR16 LYS-28; SER-65 AND MET-246; CHARACTERIZATION OF VARIANTS SCAR16 LYS-28; SER-65 AND MET-246;
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.