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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q8IV48: Variant p.Asp134Gly

3'-5' exoribonuclease 1
Gene: ERI1
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Variant information Variant position: help 134 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 Aspartate (D) to Glycine (G) at position 134 (D134G, p.Asp134Gly). 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 acidic (D) to glycine (G) 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 SEMDGC; likely pathogenic; loss-of-function variant unable to rescue defective maturation of 5.8S rRNA in ERI1-deficient cells. Any additional useful information about the variant.


Sequence information Variant position: help 134 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 349 The length of the canonical sequence.
Location on the sequence: help KLMLKESNFADSYYDYICII D FEATCEEGNPPEFVHEIIEF 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                         KL----------MLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEF

Mouse                         KL----------MLKESSAGDSYYDYICIIDFEATCEEGNP

Rat                           KL----------MLKESNAVDSYYDYICIIDFEATCEEGNP

Caenorhabditis elegans        NALLNRK-----MEPNADKTARFFDYLIAIDFECTCVE-II

Baker's yeast                 GF-------------------------LVLGF---------

Fission yeast                 RLEEKRKQERYQKFSTSNENKTCLRYLLIVDVEATCEEGCG
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 – 349 3'-5' exoribonuclease 1
Domain 130 – 306 Exonuclease
Active site 136 – 136 Proton acceptor
Binding site 134 – 134
Binding site 134 – 134
Binding site 136 – 136
Binding site 136 – 136
Binding site 137 – 137



Literature citations
Null and missense mutations of ERI1 cause a recessive phenotypic dichotomy in humans.
Guo L.; Salian S.; Xue J.Y.; Rath N.; Rousseau J.; Kim H.; Ehresmann S.; Moosa S.; Nakagawa N.; Kuroda H.; Clayton-Smith J.; Wang J.; Wang Z.; Banka S.; Jackson A.; Zhang Y.M.; Wei Z.J.; Huening I.; Brunet T.; Ohashi H.; Thomas M.F.; Bupp C.; Miyake N.; Matsumoto N.; Mendoza-Londono R.; Costain G.; Hahn G.; Di Donato N.; Yigit G.; Yamada T.; Nishimura G.; Ansel K.M.; Wollnik B.; Hrabe de Angelis M.; Megarbane A.; Rosenfeld J.A.; Heissmeyer V.; Ikegawa S.; Campeau P.M.;
Am. J. Hum. Genet. 110:1068-1085(2023)
Cited for: VARIANTS SEMDGC 21-SER--LYS-349 DEL; GLY-134; ASP-150; LEU-155; GLY-298; ALA-298 AND PRO-299; CHARACTERIZATION OF VARIANTS SEMDGC GLY-134; ASP-150; LEU-155; GLY-298 AND PRO-299; VARIANTS HXAL 172-GLN--LYS-349 DEL AND 244-GLN--LYS-349 DEL; 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.