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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P57081: Variant p.His144Pro

tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4
Gene: WDR4
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Variant information Variant position: help 144 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US 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 Histidine (H) to Proline (P) at position 144 (H144P, p.His144Pro). 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 (H) to medium size and hydrophobic (P) 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 Found in a patient with lung cancer; abolished formation of N(7)-methylguanine in tRNAs. Any additional useful information about the variant.


Sequence information Variant position: help 144 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 GDVYSFSVLEPHGCGRLELG H LSMLLDVAVSPDDRFILTAD 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                         GDVYSFSVL------------------EPHGCGRLELGHLSMLLDVAVSPDDRFILTAD

Mouse                         GDVYSFSVL------------------EPDGCGRLELGHLS

Bovine                        GDVYSFSVL------------------EPHGGGRLELGHLS

Xenopus laevis                GDVFSFSVP------------------RALEQGRLELGHLS

Xenopus tropicalis            GDVFSFSVR------------------RSREAGRLELGHLS

Zebrafish                     GDVYSFSIL------------------EPHKAGELKLGHLS

Caenorhabditis elegans        GDVHRFSVL--------------------NGSAIEMAGAIS

Slime mold                    GDVFKYSLIDDSKNKIEVSGDKSAKHDEKESDKNLVFGHYS

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
Alternative sequence 1 – 146 Missing. In isoform 3.
Mutagenesis 147 – 147 M -> A. Reduced formation of N(7)-methylguanine in tRNAs.



Literature citations
Structural basis of regulated m7G tRNA modification by METTL1-WDR4.
Li J.; Wang L.; Hahn Q.; Nowak R.P.; Viennet T.; Orellana E.A.; Roy Burman S.S.; Yue H.; Hunkeler M.; Fontana P.; Wu H.; Arthanari H.; Fischer E.S.; Gregory R.I.;
Nature 613:391-397(2023)
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH METTL1 AND TRNA; STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) IN COMPLEX WITH METTL1 AND TRNA; FUNCTION; PATHWAY; INTERACTION WITH METTL1; MUTAGENESIS OF LYS-83; 103-ARG-ARG-104; ARG-103; ARG-104; LYS-122; ARG-165; ASP-166 AND GLU-167; VARIANT PRO-144; VARIANT GAMOS6 GLN-170; CHARACTERIZATION OF VARIANT PRO-144; CHARACTERIZATION OF VARIANT GAMOS6 GLN-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.