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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q92466: Variant p.Arg273His

DNA damage-binding protein 2
Gene: DDB2
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Variant information Variant position: help 273 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 Histidine (H) at position 273 (R273H, p.Arg273His). 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 (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 interaction with DDB1 and CUL4A. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 273 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 CCDWFLATASVDQTVKIWDL R QVRGKASFLYSLPHRHPVNA 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                         CCDWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNA

Mouse                         CCDWLLATASIDQTVKIWDLRQIKGKDSFLYSLPHRHPVNA

Bovine                        CCDWLLATASVDQTVKIWDLRQVRGKSSFLHSLPHRHPVNA

Chicken                       RCEWLLATASVDQTVKIWDLRNIKDKANFLHVLPHDKPVNA

Xenopus tropicalis            RCDWLLASASVDQTVKLWDLRNIKDKSSYLYTLPHARGVNS

Zebrafish                     RCDWLMATSSVDATVKLWDLRNIKDKNSYIAEMPHEKPVNA
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
Motif 256 – 274 DWD box
Alternative sequence 153 – 341 Missing. In isoform D1.
Alternative sequence 157 – 427 Missing. In isoform D2.
Alternative sequence 245 – 427 Missing. 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.
Mutagenesis 269 – 269 I -> A. Impairs interaction with DDB1.
Mutagenesis 270 – 270 W -> A. Impairs interaction with DDB1.
Mutagenesis 272 – 272 L -> A. Impairs interaction with DDB1.
Mutagenesis 273 – 273 R -> A. Impairs interaction with DDB1.
Turn 272 – 274



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; UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation.
Chen X.; Zhang Y.; Douglas L.; Zhou P.;
J. Biol. Chem. 276:48175-48182(2001)
Cited for: INTERACTION WITH CUL4A; UBIQUITINATION; CHARACTERIZATION OF VARIANT 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; A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1.
Jin J.; Arias E.E.; Chen J.; Harper J.W.; Walter J.C.;
Mol. Cell 23:709-721(2006)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY; INTERACTION WITH DDB1; MUTAGENESIS OF LEU-350; CHARACTERIZATION OF VARIANT HIS-273; Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery.
Angers S.; Li T.; Yi X.; MacCoss M.J.; Moon R.T.; Zheng N.;
Nature 443:590-593(2006)
Cited for: INTERACTION WITH DDB1; CHARACTERIZATION OF VARIANT 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.