Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P57081: Variant p.Arg170Leu

tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4
Gene: WDR4
Feedback?
Variant information Variant position: help 170 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 Leucine (L) at position 170 (R170L, p.Arg170Leu). 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 (L) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 MIGSB; abolished formation of N(7)-methylguanine in tRNAs. Any additional useful information about the variant.


Sequence information Variant position: help 170 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 412 The length of the canonical sequence.
Location on the sequence: help DVAVSPDDRFILTADRDEKI R VSWAAAPHSIESFCLGHTEF 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                         DVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEF

Mouse                         DVAVSPDDQFVLTADRDEKIRVSWAAAPHSIESFCLGHTEF

Bovine                        DVAVSPDDRFVLTADRDEKIRVSWAAAPHSIESFCLGHTEF

Xenopus laevis                DVTVSLDGKHIITCDRDEKIRVSCWGAPHVIMSFCLGHTEF

Xenopus tropicalis            DVAVSPDGNHIITCDRDEKIRVSRWDSPHVIMSFCLGHTEF

Zebrafish                     DVALSPDDKYIITADRDEKIRVSFRRSPYNIQAFCLGHTEF

Caenorhabditis elegans        DVAFSPDGKRLLMADRDEKVRALRYPATSVIDSFFLGHTEY

Slime mold                    DIKFSPCFNYLLSADRDEKIRVSHYPNCFDIESFCLGHTKY

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 – 412 tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4
Repeat 137 – 174 WD 4
Mutagenesis 165 – 165 R -> A. Abolished formation of N(7)-methylguanine in tRNAs.
Mutagenesis 166 – 166 D -> A. Abolished formation of N(7)-methylguanine in tRNAs.
Mutagenesis 167 – 167 E -> A. Abolished formation of N(7)-methylguanine in tRNAs.
Mutagenesis 170 – 170 R -> A. Reduced formation of N(7)-methylguanine in tRNAs.
Beta strand 169 – 173



Literature citations
Structural insight into how WDR4 promotes the tRNA N7-methylguanosine methyltransferase activity of METTL1.
Jin X.; Guan Z.; Hu N.; He C.; Yin P.; Gong Z.; Zhang D.;
Cell Discov. 9:65-65(2023)
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 30-265 IN COMPLEX WITH METTL1; FUNCTION; PATHWAY; INTERACTION WITH METTL1; CHARACTERIZATION OF VARIANT GAMOS6 GLN-170; CHARACTERIZATION OF VARIANT MIGSB LEU-170; Mutation in WDR4 impairs tRNA m(7)G46 methylation and causes a distinct form of microcephalic primordial dwarfism.
Shaheen R.; Abdel-Salam G.M.; Guy M.P.; Alomar R.; Abdel-Hamid M.S.; Afifi H.H.; Ismail S.I.; Emam B.A.; Phizicky E.M.; Alkuraya F.S.;
Genome Biol. 16:RESEARCH210.1-RESEARCH210.11(2015)
Cited for: VARIANT MIGSB LEU-170;
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.