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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9NPF4: Variant p.Cys110Arg

tRNA N6-adenosine threonylcarbamoyltransferase
Gene: OSGEP
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Variant information Variant position: help 110 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 Cysteine (C) to Arginine (R) at position 110 (C110R, p.Cys110Arg). 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 polar (C) to large size and basic (R) 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 GAMOS3; strongly reduced formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 110 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 335 The length of the canonical sequence.
Location on the sequence: help AVVARTVAQLWNKPLVGVNH C IGHIEMGRLITGATSPTVLY 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                         AVVARTVAQLWNKPLVGVNHCIGHIEMGRLITGATSPTVLY

Mouse                         AVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLY

Rat                           AVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGAVNPTVLY

Bovine                        AVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGATNPTVLY

Xenopus laevis                AIVARTVAQLWKKPLLGVNHCIGHIEMGRLITGAENPTVLY

Zebrafish                     AIVARTVAQLWGKPLLGVNHCIGHIEMGRLITNAQNPTVLY

Drosophila                    AIVARTLSLLWNIPLLGVNHCIGHIEMGRLITGAQNPTVLY

Slime mold                    AVTVRMLSQLWDRPIVAVNHCIAHIEMGRLITGAVDPTILY
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 – 335 tRNA N6-adenosine threonylcarbamoyltransferase
Binding site 109 – 109
Binding site 113 – 113
Binding site 130 – 130
Helix 109 – 121



Literature citations
Mutations in KEOPS-complex genes cause nephrotic syndrome with primary microcephaly.
Braun D.A.; Rao J.; Mollet G.; Schapiro D.; Daugeron M.C.; Tan W.; Gribouval O.; Boyer O.; Revy P.; Jobst-Schwan T.; Schmidt J.M.; Lawson J.A.; Schanze D.; Ashraf S.; Ullmann J.F.P.; Hoogstraten C.A.; Boddaert N.; Collinet B.; Martin G.; Liger D.; Lovric S.; Furlano M.; Guerrera I.C.; Sanchez-Ferras O.; Hu J.F.; Boschat A.C.; Sanquer S.; Menten B.; Vergult S.; De Rocker N.; Airik M.; Hermle T.; Shril S.; Widmeier E.; Gee H.Y.; Choi W.I.; Sadowski C.E.; Pabst W.L.; Warejko J.K.; Daga A.; Basta T.; Matejas V.; Scharmann K.; Kienast S.D.; Behnam B.; Beeson B.; Begtrup A.; Bruce M.; Ch'ng G.S.; Lin S.P.; Chang J.H.; Chen C.H.; Cho M.T.; Gaffney P.M.; Gipson P.E.; Hsu C.H.; Kari J.A.; Ke Y.Y.; Kiraly-Borri C.; Lai W.M.; Lemyre E.; Littlejohn R.O.; Masri A.; Moghtaderi M.; Nakamura K.; Ozaltin F.; Praet M.; Prasad C.; Prytula A.; Roeder E.R.; Rump P.; Schnur R.E.; Shiihara T.; Sinha M.D.; Soliman N.A.; Soulami K.; Sweetser D.A.; Tsai W.H.; Tsai J.D.; Topaloglu R.; Vester U.; Viskochil D.H.; Vatanavicharn N.; Waxler J.L.; Wierenga K.J.; Wolf M.T.F.; Wong S.N.; Leidel S.A.; Truglio G.; Dedon P.C.; Poduri A.; Mane S.; Lifton R.P.; Bouchard M.; Kannu P.; Chitayat D.; Magen D.; Callewaert B.; van Tilbeurgh H.; Zenker M.; Antignac C.; Hildebrandt F.;
Nat. Genet. 49:1529-1538(2017)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; IDENTIFICATION IN THE EKC/KEOPS COMPLEX; INVOLVEMENT IN GAMOS3; VARIANTS GAMOS3 PHE-14; GLU-78; MET-107; ARG-110; THR-111; THR-139; ALA-177; ARG-198; GLN-247; CYS-280; HIS-280; LEU-280; GLN-325 AND TRP-325; CHARACTERIZATION OF VARIANTS GAMOS3 PHE-14; ARG-110; THR-111; ARG-198; GLN-247; LEU-280 AND GLN-325;
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.