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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13051: Variant p.Arg88Cys

Uracil-DNA glycosylase
Gene: UNG
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Variant information Variant position: help 88 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 Cysteine (C) at position 88 (R88C, p.Arg88Cys). 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 (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 HIGM5; loss of interaction with RPA2 resulting in impaired colocalization of UNG2 and RPA2 at nuclear foci; no effect on interaction with PCNA; no effect on protein expression and stability; confers resistance to activity reduction by RPA trimer. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 88 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 313 The length of the canonical sequence.
Location on the sequence: help AEQLDRIQRNKAAALLRLAA R NVPVGFGESWKKHLSGEFGK 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                         AEQLDRIQRNKAAALLR-----------LAARNVPVGFGESWKKHLSGEFGK

Mouse                         AEQLVRIQRNKAAALLR-----------LAARNVPAGFGES

Caenorhabditis elegans        -VKKMKLQAPEPTEIL------------LKSLLT----GES

Slime mold                    NNNNKKLKNEEKSEEINSTITDNNYYDDIENYFT----DKQ

Baker's yeast                 KDVYSKNLSSNLRTLLS-----------LELETI----DDS

Fission yeast                 KEKWAENLTPAQRKLLQ-----------LEIDTL----ESS
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 – 313 Uracil-DNA glycosylase
Region 73 – 88 Interaction with RPA2
Site 77 – 77 Essential for recruitment to stalled replication forks
Site 84 – 84 Essential for recruitment to stalled replication forks
Site 88 – 88 Essential for UNG2 recruitment to nuclear foci
Mutagenesis 73 – 73 R -> D. Impairs the interaction with RPA2.
Mutagenesis 76 – 76 R -> D. Impairs the interaction with RPA2.
Mutagenesis 77 – 77 N -> D. Impairs the interaction with RPA2. Loss of interaction with PCNA and RPA2; when associated with A-10, A-11 and D-84.
Mutagenesis 78 – 78 K -> D. Impairs the interaction with RPA2.
Mutagenesis 84 – 84 R -> D. Impairs the interaction with RPA2. Loss of interaction with PCNA and RPA2; when associated with A-10, A-11 and D-77.
Mutagenesis 88 – 88 R -> D. Impairs the interaction with RPA2.



Literature citations
The UNG2 Arg88Cys variant abrogates RPA-mediated recruitment of UNG2 to single-stranded DNA.
Torseth K.; Doseth B.; Hagen L.; Olaisen C.; Liabakk N.B.; Graesmann H.; Durandy A.; Otterlei M.; Krokan H.E.; Kavli B.; Slupphaug G.;
DNA Repair 11:559-569(2012)
Cited for: CHARACTERIZATION OF VARIANT HIGM5 CYS-88; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES (ISOFORM 2); INTERACTION WITH RPA2 AND PCNA (ISOFORM 2); REGION; MUTAGENESIS OF PHE-10; PHE-11; ARG-73; ARG-76; ASN-77; LYS-78; ARG-84 AND ARG-88;
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.