Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9GZZ9: Variant p.Ala371Thr

Ubiquitin-like modifier-activating enzyme 5
Gene: UBA5
Feedback?
Variant information Variant position: help 371 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 Alanine (A) to Threonine (T) at position 371 (A371T, p.Ala371Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; reduces UFM1 activating enzyme activity; reduces UFM1 activating enzyme activity; reduces UFM1-DDRGK1 formation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 371 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 EEELKNFSGPVPDLPEGITV A YTIPKKQEDSVTELTVEDSG 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                         EEELKNFSGPVPDLPEGITVAYT-IPKKQEDSVTELTVEDSG----

Mouse                         EEELKNSSGPVPTLPEGITVAYT-VPKKTEDSASEVTVEDS

Rat                           EEELKNSSGPVPTLPEGITVAYT-VPKKREDSVSEVTVEDS

Bovine                        EEELKKSSGPIPDLPEGIIVAYT-VPQKQEDSVPEVTVEDS

Chicken                       EDELKAASGPVPDLPVGITVAYT-IPNKEENLTAEETVAES

Xenopus laevis                EEELKAASGPVPDLPEGIKVAYT-IPIT--KPTSGFTVEDS

Xenopus tropicalis            EEELKAASGPVPELPEGIKVAYT-VPIT--EPTSGFIVEDS

Zebrafish                     EAELQDASGPIPDLPEGITVAYT-IPEK--DGGSGETVEET

Caenorhabditis elegans        PSAEQSSS---LNAGTGLKFAYE--PIKRDAQTELSPAQAA

Drosophila                    PES-NTTPAETPVMGEGLRLAYE-APEKSSETSEETVSAAT

Slime mold                    DFNNNNNNNNKPS-NNSFEFSYDKKPTVELNEQSTVKVNSS
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
Modified residue 358 – 358 Phosphoserine



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; Biallelic variants in UBA5 link dysfunctional UFM1 ubiquitin-like modifier pathway to severe infantile-onset encephalopathy.
Muona M.; Ishimura R.; Laari A.; Ichimura Y.; Linnankivi T.; Keski-Filppula R.; Herva R.; Rantala H.; Paetau A.; Poeyhoenen M.; Obata M.; Uemura T.; Karhu T.; Bizen N.; Takebayashi H.; McKee S.; Parker M.J.; Akawi N.; McRae J.; Hurles M.E.; Kuismin O.; Kurki M.I.; Anttonen A.K.; Tanaka K.; Palotie A.; Waguri S.; Lehesjoki A.E.; Komatsu M.;
Am. J. Hum. Genet. 99:683-694(2016)
Cited for: VARIANTS DEE44 HIS-55 AND THR-371; CHARACTERIZATION OF VARIANTS DEE44 HIS-55 AND THR-371; MUTAGENESIS OF CYS-250; 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.