Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96Q11: Variant p.Arg190Ile

CCA tRNA nucleotidyltransferase 1, mitochondrial
Gene: TRNT1
Feedback?
Variant information Variant position: help 190 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 Arginine (R) to Isoleucine (I) at position 190 (R190I, p.Arg190Ile). 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 large size and basic (R) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 SIFD; loss of CCA tRNA nucleotidyltransferase activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 190 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 434 The length of the canonical sequence.
Location on the sequence: help FNGYEDLKNKKVRFVGHAKQ R IQEDYLRILRYFRFYGRIVD 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                         FNGYEDLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVD

Mouse                         FNGYADLKNKKVRFVGHAKQRIQEDYLRILRYFRFYGRIVD

Zebrafish                     FQGYEDLKNRKVRFVGSASLRIQEDYLRILRYFRFYGRVAA
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 42 – 434 CCA tRNA nucleotidyltransferase 1, mitochondrial
Binding site 194 – 194
Binding site 194 – 194
Binding site 197 – 197
Binding site 197 – 197
Binding site 200 – 200
Binding site 200 – 200
Binding site 203 – 203
Binding site 203 – 203
Site 193 – 193 Involved in nucleotide selection
Alternative sequence 58 – 434 Missing. In isoform 3.
Helix 187 – 193



Literature citations
Mutations in TRNT1 cause congenital sideroblastic anemia with immunodeficiency, fevers, and developmental delay (SIFD).
Chakraborty P.K.; Schmitz-Abe K.; Kennedy E.K.; Mamady H.; Naas T.; Durie D.; Campagna D.R.; Lau A.; Sendamarai A.K.; Wiseman D.H.; May A.; Jolles S.; Connor P.; Powell C.; Heeney M.M.; Giardina P.J.; Klaassen R.J.; Kannengiesser C.; Thuret I.; Thompson A.A.; Marques L.; Hughes S.; Bonney D.K.; Bottomley S.S.; Wynn R.F.; Laxer R.M.; Minniti C.P.; Moppett J.; Bordon V.; Geraghty M.; Joyce P.B.; Markianos K.; Rudner A.D.; Holcik M.; Fleming M.D.;
Blood 124:2867-2871(2014)
Cited for: INVOLVEMENT IN SIFD; VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190; THR-223; THR-326 AND GLU-416; CHARACTERIZATION OF VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190; THR-223 AND THR-326; FUNCTION; CATALYTIC ACTIVITY; Impaired activity of CCA-adding enzyme TRNT1 impacts OXPHOS complexes and cellular respiration in SIFD patient-derived fibroblasts.
Liwak-Muir U.; Mamady H.; Naas T.; Wylie Q.; McBride S.; Lines M.; Michaud J.; Baird S.D.; Chakraborty P.K.; Holcik M.;
Orphanet J. Rare Dis. 11:79-79(2016)
Cited for: VARIANTS SIFD ILE-154; SER-166 AND ILE-190; SUBCELLULAR LOCATION; TRNT1 deficiency: clinical, biochemical and molecular genetic features.
Wedatilake Y.; Niazi R.; Fassone E.; Powell C.A.; Pearce S.; Plagnol V.; Saldanha J.W.; Kleta R.; Chong W.K.; Footitt E.; Mills P.B.; Taanman J.W.; Minczuk M.; Clayton P.T.; Rahman S.;
Orphanet J. Rare Dis. 11:90-90(2016)
Cited for: VARIANTS SIFD ILE-190 AND THR-223; In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.
Leibovitch M.; Hanic-Joyce P.J.; Joyce P.B.M.;
Biochim. Biophys. Acta 1866:527-540(2018)
Cited for: VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190 AND THR-223; CHARACTERIZATION OF VARIANTS SIFD ILE-154; VAL-158; SER-166; ILE-190 AND THR-223; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
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.