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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H9Q4: Variant p.Arg57Gly

Non-homologous end-joining factor 1
Gene: NHEJ1
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Variant information Variant position: help 57 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 Glycine (G) at position 57 (R57G, p.Arg57Gly). 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 glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 NHEJ1-SCID; fails to translocate to the nucleus. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 57 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 299 The length of the canonical sequence.
Location on the sequence: help LVSDLQQVWHEQVDTSVVSQ R AKELNKRLTAPPAAFLCHLD 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                         LVSDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAAFLCHLD

Mouse                         LISDLQQVWHEQVDTSVVSQRAKELNKRLTAPPAALLCHLD

Rat                           LISDLQQVWHEQVDTLEVSQRAKELNKRLTAPPAAFLHHLD

Zebrafish                     LLTDLSTVWEEEMSTDDIQSRAQDLNKRLRAPAQAFFSHLC

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 – 299 Non-homologous end-joining factor 1
Region 1 – 135 Globular head
Mutagenesis 37 – 37 L -> A. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 40 – 40 D -> AP. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 41 – 41 L -> A. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 43 – 43 Q -> A. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 57 – 57 R -> G. Decreased ability to repair double-strand breaks (DSBs). Impaired ability to participate in V(D)J recombination.
Mutagenesis 61 – 61 L -> E. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 64 – 64 R -> E. Abolished ability to repair double-strand breaks (DSBs). Abolished interaction with XRCC4. Abolished ability to participate in V(D)J recombination.
Mutagenesis 64 – 64 R -> G. Does not affect ability to participate in V(D)J recombination.
Mutagenesis 65 – 65 L -> D. Abolished ability to repair double-strand breaks (DSBs). Abolished ability to participate in V(D)J recombination. Decreased interaction with XRCC4.
Helix 51 – 61



Literature citations
Cernunnos, a novel nonhomologous end-joining factor, is mutated in human immunodeficiency with microcephaly.
Buck D.; Malivert L.; de Chasseval R.; Barraud A.; Fondaneche M.-C.; Sanal O.; Plebani A.; Stephan J.-L.; Hufnagel M.; le Deist F.; Fischer A.; Durandy A.; de Villartay J.-P.; Revy P.;
Cell 124:287-299(2006)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; VARIANTS NHEJ1-SCID GLY-57 AND ARG-123; Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity.
Lu H.; Pannicke U.; Schwarz K.; Lieber M.R.;
J. Biol. Chem. 282:11155-11162(2007)
Cited for: INTERACTION WITH XRCC4-LIG4 COMPLEX; DNA-BINDING; CHARACTERIZATION OF VARIANT NHEJ1-SCID GLY-57;
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.