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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92466: Variant p.Lys244Glu

DNA damage-binding protein 2
Gene: DDB2
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Variant information Variant position: help 244 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 Lysine (K) to Glutamate (E) at position 244 (K244E, p.Lys244Glu). 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 (K) to medium size and acidic (E) 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 XP-E; impairs DNA-binding of the UV-DDB complex. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 244 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 427 The length of the canonical sequence.
Location on the sequence: help NVILLNMDGKELWNLRMHKK K VTHVALNPCCDWFLATASVD 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                         NVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLATASVD

Mouse                         HVILLSTDGKELWNLRMHKKKVAHVALNPCCDWLLATASID

Bovine                        HVILLNMDGRELWNLRMHKKKVTHVALNPCCDWLLATASVD

Chicken                       NVVLLSTSGEEIWKLKLHKKKVTHVEFNSRCEWLLATASVD

Xenopus tropicalis            NVVLLETCGKEIWKLRLHKKKVTHVEFNPRCDWLLASASVD

Zebrafish                     RLLLLGLDGHEIFKEKLHKAKVTHAEFNPRCDWLMATSSVD

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 – 427 DNA damage-binding protein 2
Repeat 244 – 287 WD 4
Alternative sequence 153 – 341 Missing. In isoform D1.
Alternative sequence 157 – 427 Missing. In isoform D2.
Alternative sequence 236 – 244 WNLRMHKKK -> VSVPMEPGS. In isoform D4.
Mutagenesis 258 – 258 L -> A. Impairs interaction with DDB1.
Mutagenesis 262 – 262 S -> A. Impairs interaction with DDB1.
Mutagenesis 264 – 264 D -> A. Impairs interaction with DDB1.



Literature citations
p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity.
Hwang B.J.; Toering S.; Francke U.; Chu G.;
Mol. Cell. Biol. 18:4391-4399(1998)
Cited for: INTERACTION WITH DDB1; DNA-BINDING; CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273; Human damage-specific DNA-binding protein p48. Characterization of XPE mutations and regulation following UV irradiation.
Nichols A.F.; Itoh T.; Graham J.A.; Liu W.; Yamaizumi M.; Linn S.;
J. Biol. Chem. 275:21422-21428(2000)
Cited for: DNA-BINDING; SUBCELLULAR LOCATION; INDUCTION; CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273; DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA.
Wittschieben B.O.; Iwai S.; Wood R.D.;
J. Biol. Chem. 280:39982-39989(2005)
Cited for: INTERACTION WITH DDB1; DNA-BINDING; CHARACTERIZATION OF VARIANTS GLU-244 AND HIS-273; Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype.
Nichols A.F.; Ong P.; Linn S.;
J. Biol. Chem. 271:24317-24320(1996)
Cited for: VARIANTS XP-E GLU-244 AND HIS-273;
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.