Variant position: 389 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 2677 The length of the canonical sequence.
Location on the sequence:
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 GWRTAICPDYCPNMYEEMET LASVLQSDIGQDMRVHNSTFL
Mouse GWRSAICPDYCPNMYEEMET LANVLQSDIGQDMRVHNSTFL
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
1 – 2677 Probable helicase senataxin
A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage.
Richard P.; Feng S.; Manley J.L.;
Genes Dev. 27:2227-2232(2013)
Cited for: FUNCTION; INTERACTION WITH EXOSC9 AND UBE2I; SUMOYLATION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SCAN2 CYS-305 AND LEU-413; CHARACTERIZATION OF VARIANTS ALS4 ILE-3 AND SER-389; MUTAGENESIS OF GLU-65;
DNA/RNA helicase gene mutations in a form of juvenile amyotrophic lateral sclerosis (ALS4).
Chen Y.-Z.; Bennett C.L.; Huynh H.M.; Blair I.P.; Puls I.; Irobi J.; Dierick I.; Abel A.; Kennerson M.L.; Rabin B.A.; Nicholson G.A.; Auer-Grumbach M.; Wagner K.; De Jonghe P.; Griffin J.W.; Fischbeck K.H.; Timmerman V.; Cornblath D.R.; Chance P.F.;
Am. J. Hum. Genet. 74:1128-1135(2004)
Cited for: VARIANTS ALS4 SER-389 AND HIS-2136; TISSUE SPECIFICITY;
Protein interaction analysis of senataxin and the ALS4 L389S mutant yields insights into senataxin post-translational modification and uncovers mutant-specific binding with a brain cytoplasmic RNA-encoded peptide.
Bennett C.L.; Chen Y.; Vignali M.; Lo R.S.; Mason A.G.; Unal A.; Huq Saifee N.P.; Fields S.; La Spada A.R.;
PLoS ONE 8:E78837-E78837(2013)
Cited for: VARIANT SER-389; CHARACTERIZATION OF VARIANT ALS4 SER-389; SUBUNIT; LACK OF INTERACTION WITH C14ORF178; UBIQUITINATION; SUMOYLATION;
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.