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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8WXF7: Variant p.Arg217Gln

Atlastin-1
Gene: ATL1
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Variant information Variant position: help 217 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 Glutamine (Q) at position 217 (R217Q, p.Arg217Gln). 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 (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 SPG3; abolishes homodimerization and GTPase activity and alters endoplasmic reticulum morphology. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 217 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 558 The length of the canonical sequence.
Location on the sequence: help GRLAMEETFLKPFQSLIFLV R DWSFPYEFSYGADGGAKFLE 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                         GRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLE

Mouse                         GRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLE

Rat                           GRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGADGGAKFLE

Bovine                        GRLAMEETFLKPFQSLIFLVRDWSFPYEFSYGSDGGSKFLE
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 – 558 Atlastin-1
Topological domain 1 – 449 Cytoplasmic
Domain 64 – 309 GB1/RHD3-type G
Binding site 217 – 218
Beta strand 208 – 217



Literature citations
Atlastin GTPases are required for Golgi apparatus and ER morphogenesis.
Rismanchi N.; Soderblom C.; Stadler J.; Zhu P.-P.; Blackstone C.;
Hum. Mol. Genet. 17:1591-1604(2008)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANT SPAG3 GLN-217; MUTAGENESIS OF LYS-80; TISSUE SPECIFICITY; Cooperation of the ER-shaping proteins atlastin, lunapark, and reticulons to generate a tubular membrane network.
Wang S.; Tukachinsky H.; Romano F.B.; Rapoport T.A.;
Elife 5:0-0(2016)
Cited for: FUNCTION; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT GLN-217; MUTAGENESIS OF LYS-80; Structural basis for the nucleotide-dependent dimerization of the large G protein atlastin-1/SPG3A.
Byrnes L.J.; Sondermann H.;
Proc. Natl. Acad. Sci. U.S.A. 108:2216-2221(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 1-447 IN COMPLEX WITH GDP; FUNCTION; CHARACTERIZATION OF VARIANT CYS-196; CHARACTERIZATION OF VARIANT SPAG3 GLN-217; MUTAGENESIS OF ARG-77; GLN-191 AND HIS-247; SUBUNIT; Further evidence that SPG3A gene mutations cause autosomal dominant hereditary spastic paraplegia.
Muglia M.; Magariello A.; Nicoletti G.; Patitucci A.; Gabriele A.L.; Conforti F.L.; Mazzei R.; Caracciolo M.; Ardito B.; Lastilla M.; Tedeschi G.; Quattrone A.;
Ann. Neurol. 51:794-795(2002)
Cited for: VARIANT SPG3 GLN-217;
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.