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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O15091: Variant p.Ala485Val

Mitochondrial ribonuclease P catalytic subunit
Gene: PRORP
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Variant information Variant position: help 485 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 Valine (V) at position 485 (A485V, p.Ala485Val). 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 hydrophobic (V) 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 COXPD54; decreased protein levels in homozygous patient cells; impaired mitochondrial RNA processing in homozygous patient cells. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 485 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 583 The length of the canonical sequence.
Location on the sequence: help KQASCFFADDISEDDPFLLY A TLHSGNHCRFITRDLMRDHK 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                         KQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHK

Mouse                         KQAHCFFADNISEDDPFLLYATLNSGNHCKFITKDLLRDHK

Rat                           KQAHCFFADNISEDDPFLLYATLNSGSHCKFITKDLLRDHK

Drosophila                    CNASLFLTSNLSHDDPFLLYATLRSGQETDFFSRDLMRSHA
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 46 – 583 Mitochondrial ribonuclease P catalytic subunit
Domain 342 – 578 PRORP
Binding site 478 – 478
Binding site 479 – 479
Binding site 499 – 499
Mutagenesis 478 – 478 D -> N. Abolishes ribonuclease activity.
Mutagenesis 479 – 479 D -> N. Abolishes ribonuclease activity.
Mutagenesis 480 – 480 P -> G. Does not affect ribonuclease activity.
Mutagenesis 498 – 498 R -> DN. Does not affect ribonuclease activity.
Mutagenesis 499 – 499 D -> N. Abolishes ribonuclease activity.
Helix 481 – 489



Literature citations
Bi-allelic variants in the mitochondrial RNase P subunit PRORP cause mitochondrial tRNA processing defects and pleiotropic multisystem presentations.
Hochberg I.; Demain L.A.M.; Richer J.; Thompson K.; Urquhart J.E.; Rea A.; Pagarkar W.; Rodriguez-Palmero A.; Schlueter A.; Verdura E.; Pujol A.; Quijada-Fraile P.; Amberger A.; Deutschmann A.J.; Demetz S.; Gillespie M.; Belyantseva I.A.; McMillan H.J.; Barzik M.; Beaman G.M.; Motha R.; Ng K.Y.; O'Sullivan J.; Williams S.G.; Bhaskar S.S.; Lawrence I.R.; Jenkinson E.M.; Zambonin J.L.; Blumenfeld Z.; Yalonetsky S.; Oerum S.; Rossmanith W.; Yue W.W.; Zschocke J.; Munro K.J.; Battersby B.J.; Friedman T.B.; Taylor R.W.; O'Keefe R.T.; Newman W.G.;
Am. J. Hum. Genet. 108:2195-2204(2021)
Cited for: VARIANTS COXPD54 SER-412; CYS-421; ASP-434; GLN-445 AND VAL-485; CHARACTERIZATION OF VARIANTS COXPD54 SER-412; GLN-445 AND VAL-485; INVOLVEMENT IN COXPD54;
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.