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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P18074: Variant p.Arg112His

General transcription and DNA repair factor IIH helicase subunit XPD
Gene: ERCC2
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Variant information Variant position: help 112 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 112 (R112H, p.Arg112His). 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 TTD1 and XP-D. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 112 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 760 The length of the canonical sequence.
Location on the sequence: help NFYEKQEGEKLPFLGLALSS R KNLCIHPEVTPLRFGKDVDG 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                         NFYEKQEGEKLP-FLGLALSSRKNLCIHPEVTPLRFGKDVDG

Mouse                         SFYEQQEGEKLP-FLGLALSSRKNLCIHPEVTPLRFGKDVD

Bovine                        SFYEKQEGEKLP-FLGLALSSRKNLCIHPEVTPLRFGKDVD

Slime mold                    QYRNSEMGEESPKTLCMSMSSRRNLCIQPRVSEERDGKVVD
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 – 760 General transcription and DNA repair factor IIH helicase subunit XPD
Domain 7 – 283 Helicase ATP-binding
Binding site 116 – 116
Turn 112 – 114



Literature citations
Mutations in the xeroderma pigmentosum group D DNA repair/transcription gene in patients with trichothiodystrophy.
Broughton B.C.; Steingrimsdottir H.; Weber C.A.; Lehmann A.R.;
Nat. Genet. 7:189-194(1994)
Cited for: VARIANTS TTD1 HIS-112; PRO-616; TRP-722 AND 488-VAL--MET-493 DEL; Analysis of mutations in the XPD gene in Italian patients with trichothiodystrophy: site of mutation correlates with repair deficiency, but gene dosage appears to determine clinical severity.
Botta E.; Nardo T.; Broughton B.C.; Marinoni S.; Lehmann A.R.; Stefanini M.;
Am. J. Hum. Genet. 63:1036-1048(1998)
Cited for: VARIANTS TTD1 HIS-112; TYR-259; VAL-461; THR-482 DEL; GLY-673 AND TRP-722; Two individuals with features of both xeroderma pigmentosum and trichothiodystrophy highlight the complexity of the clinical outcomes of mutations in the XPD gene.
Broughton B.C.; Berneburg M.; Fawcett H.; Taylor E.M.; Arlett C.F.; Nardo T.; Stefanini M.; Menefee E.; Price V.H.; Queille S.; Sarasin A.; Bohnert E.; Krutmann J.; Davidson R.; Kraemer K.H.; Lehmann A.R.;
Hum. Mol. Genet. 10:2539-2547(2001)
Cited for: VARIANTS XP-D HIS-112; PRO-485 AND 582-GLU-LYS-583 DELINS VAL-SER-GLU; VARIANTS ASN-312 AND GLN-751;
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.