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-----------HTSNSASLQGIDSQCVNQ PEQLVSSAPTLSAPEKESTG
Mouse GET-----------QASSSTSPRGTD----NQ PEEPVSLSS
Rat GEP-----------QTSSSTSPQGTDSQLQNQ PEQQISPTP
Zebrafish SSPAAQENHITDHQHISESTDVGPSLASQEHN NAKESGRSQ
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.
Type Positions Description
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.