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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95352: Variant p.Pro234Thr

Ubiquitin-like modifier-activating enzyme ATG7
Gene: ATG7
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Variant information Variant position: help 234 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 Proline (P) to Threonine (T) at position 234 (P234T, p.Pro234Thr). 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 medium size and hydrophobic (P) to medium size and polar (T) 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 SCAR31; results in decreased LC3-I lipidation to form LC3-II. Any additional useful information about the variant.


Sequence information Variant position: help 234 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 703 The length of the canonical sequence.
Location on the sequence: help KHYSDFFQGQRTKITIGVYD P CNLAQYPGWPLRNFLVLAAH 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                         KHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAH

Mouse                         KHYSDFFQGQRTKITVGVYDPCNLAQYPGWPLRNFLVLAAH

Rat                           KHYSDFFQGQRTKLTVGVYDPCNLTQHPGWPLRNFLVLAAH

Chicken                       KKWDGFFQDQGGKVTVGVYDPCNLSHYPGWPLRNFLILASH

Slime mold                    QYLNECLENDLIPL-VGFCDPCSLPLNPGWPLRNFLIYLSI

Baker's yeast                 -NYDKCII-RKTKV-LAIRDTSTMENVPSALTKNFLSVLQY

Fission yeast                 KELSHCVD-KSLQFYLVAEDSVQLAEYPSWPVRNILAFAFI
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 2 – 703 Ubiquitin-like modifier-activating enzyme ATG7
Mutagenesis 243 – 243 W -> A. Moderately impairs ATG3 binding. Moderately reduces GABARAP-ATG3 thioester bond formation. Moderately reduces GABARAP lipidation.
Mutagenesis 246 – 246 R -> D. Almost completely impairs ATG3 binding. Severely reduces GABARAP-ATG3 thioester bond formation. Severely reduces GABARAP lipidation.



Literature citations
Developmental Consequences of Defective ATG7-Mediated Autophagy in Humans.
Collier J.J.; Guissart C.; Olahova M.; Sasorith S.; Piron-Prunier F.; Suomi F.; Zhang D.; Martinez-Lopez N.; Leboucq N.; Bahr A.; Azzarello-Burri S.; Reich S.; Schoels L.; Polvikoski T.M.; Meyer P.; Larrieu L.; Schaefer A.M.; Alsaif H.S.; Alyamani S.; Zuchner S.; Barbosa I.A.; Deshpande C.; Pyle A.; Rauch A.; Synofzik M.; Alkuraya F.S.; Rivier F.; Ryten M.; McFarland R.; Delahodde A.; McWilliams T.G.; Koenig M.; Taylor R.W.;
N. Engl. J. Med. 384:2406-2417(2021)
Cited for: VARIANTS SCAR31 THR-234; ARG-261; ASP-511; PRO-512; HIS-576; MET-588; TYR-624 AND 659-ARG--ILE-703 DEL; INVOLVEMENT IN SCAR31; CHARACTERIZATION OF VARIANTS SCAR31 THR-234; ASP-511; HIS-576; MET-588 AND TYR-624; MUTAGENESIS OF CYS-572; FUNCTION;
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.