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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9GZZ9: Variant p.Gly168Glu

Ubiquitin-like modifier-activating enzyme 5
Gene: UBA5
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Variant information Variant position: help 168 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 Glycine (G) to Glutamate (E) at position 168 (G168E, p.Gly168Glu). 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 glycine (G) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In DEE44; abolishes UFM1 activating enzyme activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 168 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 404 The length of the canonical sequence.
Location on the sequence: help NYNITTVENFQHFMDRISNG G LEEGKPVDLVLSCVDNFEAR 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                         NYNITTVENFQHFMDRISNGGLEEGKPVDLVLSCVDNFEAR

Mouse                         NYNITTVEHFEHFMNRISNGGLEEGQPVDLVLSCVDNFEAR

Rat                           NYNITTVEHFEHFMNRISNGGLEEGQPVDLVLSCVDNFEAR

Bovine                        NYNITTVENFEHFMNRISNGGLEEGKPVDLVLSCVDNFEAR

Chicken                       NYNITTLDNFEHFMDRISNGALEEGKPVDLVLSCVDNFEAR

Xenopus laevis                NYNITTLDNFQHFMDRISKGGLKEGSPVDLVLSCVDNFEAR

Xenopus tropicalis            NYNITTLDNFQHFMDRISKGGLKEGTPVDLVLSCVDNFEAR

Zebrafish                     NYNITTMDNFTHFMDRVSHGGLEEGKPVDLILSCVDNFEAR

Caenorhabditis elegans        NFNITTMDNFDTFVNRIRKGSLTDGK-IDLVLSCVDNFEAR

Drosophila                    NYNITTVENFDRFLDTISQGGRIAGQPVDLVLSCVDNFEAR

Slime mold                    NYNITTIDNFEHFKGRIEKGGLVEGEPVDLVLGCVDNFEAR
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 – 404 Ubiquitin-like modifier-activating enzyme 5
Binding site 150 – 150
Binding site 184 – 184
Mutagenesis 188 – 188 R -> A. Abolished ability to activate UFM1.
Beta strand 167 – 170



Literature citations
Biallelic variants in UBA5 reveal that disruption of the UFM1 cascade can result in early-onset encephalopathy.
Colin E.; Daniel J.; Ziegler A.; Wakim J.; Scrivo A.; Haack T.B.; Khiati S.; Denomme A.S.; Amati-Bonneau P.; Charif M.; Procaccio V.; Reynier P.; Aleck K.A.; Botto L.D.; Herper C.L.; Kaiser C.S.; Nabbout R.; N'Guyen S.; Mora-Lorca J.A.; Assmann B.; Christ S.; Meitinger T.; Strom T.M.; Prokisch H.; Miranda-Vizuete A.; Hoffmann G.F.; Lenaers G.; Bomont P.; Liebau E.; Bonneau D.;
Am. J. Hum. Genet. 99:695-703(2016)
Cited for: VARIANTS DEE44 VAL-57; GLU-168; MET-260; THR-371 AND TYR-389; CHARACTERIZATION OF VARIANTS DEE44 VAL-57; GLU-168; MET-260; THR-371 AND TYR-389; FUNCTION; INVOLVEMENT IN DEE44;
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.