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UniProtKB/Swiss-Prot Q9H1Y0: Variant p.Glu122Asp

Autophagy protein 5
Gene: ATG5
Variant information

Variant position:  122
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glutamate (E) to Aspartate (D) at position 122 (E122D, p.Glu122Asp).
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:  Similar physico-chemical property. Both residues are medium size and acidic.
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

Variant description:  In SCAR25; reduced conjugation to ATG12; decrease in autophagy activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  122
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  275
The length of the canonical sequence.

Location on the sequence:   VHFKSFPEKDLLHCPSKDAI  E AHFMSCMKEADALKHKSQVI
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                         VHFK-SFPEKDLLHCPSKDAIEAHFMSCMKEADALKH-KSQVI

Mouse                         VHFK-SFPEKDLLHCPSKDAVEAHFMSCMKEADALKH-KSQ

Rat                           VHFK-SFPEKDLLHCPCKDAVEAHFMSCVKEADALKH-KSQ

Pig                           VHFK-SFPEKDLLHCPSKDVIEAHFMSCVKEADALKH-KSR

Bovine                        VHFK-SFPEKDLLHCPSKDVIEAHFMSCVKEADALKH-KSQ

Caenorhabditis elegans        VRTS-QPPPQ--FQMVDRDMMEAMFMQNIKEADYLKT-KAE

Drosophila                    IHFS-KFPEDMLVKLNSKELLESHYMSCLKEADVLKH-RGL

Slime mold                    VHFQ-SYPDRILLRCPNIESVRTYYKNVLKEANFIKQGDIT

Baker's yeast                 LVMGDSLPPTIIPIASSKTQAEKFWFHQWKQVCFILNGSSK

Fission yeast                 LRSG-LFPTTKILQMETMDTFRTYFFNCLKESDYVRNGSSS

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 – 275 Autophagy protein 5
Cross 130 – 130 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ATG12)
Mutagenesis 130 – 130 K -> R. Loss of conjugaction with ATG12. Does affect interaction with DHX58, nor with MAVS.
Helix 118 – 137


Literature citations

Mutation in ATG5 reduces autophagy and leads to ataxia with developmental delay.
Kim M.; Sandford E.; Gatica D.; Qiu Y.; Liu X.; Zheng Y.; Schulman B.A.; Xu J.; Semple I.; Ro S.H.; Kim B.; Mavioglu R.N.; Tolun A.; Jipa A.; Takats S.; Karpati M.; Li J.Z.; Yapici Z.; Juhasz G.; Lee J.H.; Klionsky D.J.; Burmeister M.;
Elife 5:0-0(2016)
Cited for: VARIANT SCAR25 ASP-122; CHARACTERIZATION OF VARIANT SCAR25 ASP-122; FUNCTION; CONJUGATION TO ATG12;

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.