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UniProtKB/Swiss-Prot Q9H9Q4: Variant p.Gln256Leu

Non-homologous end-joining factor 1
Gene: NHEJ1
Variant information

Variant position:  256
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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:  From Glutamine (Q) to Leucine (L) at position 256 (Q256L, p.Gln256Leu).
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:  Change from medium size and polar (Q) to medium size and hydrophobic (L)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  256
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  299
The length of the canonical sequence.

Location on the sequence:   GDPHTSNSASLQGIDSQCVN  Q PEQLVSSAPTLSAPEKESTG
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         GDP-----------HTSNSASLQGIDSQCVNQPEQLVSSAPTLSAPEKESTG

Mouse                         GET-----------QASSSTSPRGTD----NQPEEPVSLSS

Rat                           GEP-----------QTSSSTSPQGTDSQLQNQPEQQISPTP

Zebrafish                     SSPAAQENHITDHQHISESTDVGPSLASQEHNNAKESGRSQ

Sequence annotation in neighborhood:  
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 255 – 299 Disordered
Compositional bias 255 – 284 Polar residues
Modified residue 245 – 245 Phosphoserine; by PRKDC
Modified residue 251 – 251 Phosphoserine; by PRKDC
Modified residue 263 – 263 Phosphoserine
Modified residue 266 – 266 Phosphothreonine
Mutagenesis 245 – 245 S -> A. In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-251, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-132, A-203 and A-251.
Mutagenesis 245 – 245 S -> D. In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-132, D-203 and D-251.
Mutagenesis 251 – 251 S -> A. In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-263 and A-266. In XLF-Ala mutant; abolished phosphorylation by PRKDC; does not affect ability to bridge DNA when associated with XRCC4 phosphorylation-defective mutant; when associated with A-132, A-203 and A-245.
Mutagenesis 251 – 251 S -> D. In XLF-Asp mutant; phospho-mimetic mutant; abolished ability to bridge DNA when associated with XRCC4 phospho-mimetic mutant; when associated with D-132, D-203 and D-245.
Mutagenesis 263 – 263 S -> A. In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-251 and A-266.
Mutagenesis 266 – 266 T -> A. In 6A mutant; abolished phosphorylation; does not affect ability to repair double-strand breaks (DSBs), possibly because of redundancy with XRCC4 phosphorylation sites; when associated with A-132, A-203, A-245, A-251 and A-263.


Literature citations

No reference for the current variant in UniProtKB/Swiss-Prot.

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.