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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q2YD98: Variant p.Cys32Arg

UV-stimulated scaffold protein A
Gene: UVSSA
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Variant information Variant position: help 32 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 Cysteine (C) to Arginine (R) at position 32 (C32R, p.Cys32Arg). 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 polar (C) to large size and basic (R) 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 UVSS3; mild phenotype; impairs transcription-coupled nucleotide excision repair ability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 32 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 709 The length of the canonical sequence.
Location on the sequence: help LTTSGEPRLNPEKMKELKKI C KSSEEQLSRAYRLLIAQLTQ 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                         LTTSGEPRLNPEKMKELKK-ICKSSEEQLSRAYRLLIAQLTQ

Mouse                         LTTSGESQLNAQKMKELKK-ICKSSEEQLSHAYRLLITQLT

Rat                           LTTSGESQLNAQKMKELKK-ICKSSEEQLSHAYRLLMTQLT

Bovine                        LTTSGEPQLNPEKMKQLKK-ICKSSEEQLGHAYHLLMAQLS

Chicken                       LTTAGEPQLEPGRMKELKK-ICRSSEEHLSHAYHLLLTRLH

Xenopus tropicalis            LTTSGEPQLNPEKLKELKK-ICRSSDEHINHVYHLLMTQLN

Zebrafish                     LTTSGEPQLNQDKMKEVKK-ICRVSDSYIDHFYHLIMTQLN

Caenorhabditis elegans        LTDDGKLDFESIPYQNLQKEVANQDEEGCENVIEVLLDTTS
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 – 709 UV-stimulated scaffold protein A
Region 2 – 145 VHS-like
Alternative sequence 1 – 449 Missing. In isoform 2.
Helix 22 – 34



Literature citations
Mutations in UVSSA cause UV-sensitive syndrome and impair RNA polymerase IIo processing in transcription-coupled nucleotide-excision repair.
Nakazawa Y.; Sasaki K.; Mitsutake N.; Matsuse M.; Shimada M.; Nardo T.; Takahashi Y.; Ohyama K.; Ito K.; Mishima H.; Nomura M.; Kinoshita A.; Ono S.; Takenaka K.; Masuyama R.; Kudo T.; Slor H.; Utani A.; Tateishi S.; Yamashita S.; Stefanini M.; Lehmann A.R.; Yoshiura K.I.; Ogi T.;
Nat. Genet. 44:586-592(2012)
Cited for: FUNCTION; INVOLVEMENT IN UVSS3; MUTAGENESIS OF TRP-120 AND 157-ARG--ARG-159; VARIANT UVSS3 ARG-32; CHARACTERIZATION OF VARIANT UVSS3 ARG-32;
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.