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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P01112: Variant p.Gln61Lys

GTPase HRas
Gene: HRAS
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Variant information Variant position: help 61 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 Glutamine (Q) to Lysine (K) at position 61 (Q61K, p.Gln61Lys). 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 (Q) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 NMTC2; somatic mutation; increases transformation of cultured cell lines. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 61 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 189 The length of the canonical sequence.
Location on the sequence: help RKQVVIDGETCLLDILDTAG Q EEYSAMRDQYMRTGEGFLCV 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                         RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCV

Mouse                         RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCV

Rat                           RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCV

Chicken                       RKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCV

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 – 186 GTPase HRas
Chain 2 – 186 GTPase HRas, N-terminally processed
Mutagenesis 59 – 59 A -> T. Loss of GTPase activity and creation of an autophosphorylation site.
Mutagenesis 61 – 61 Q -> I. Moderately increased transformation of cultured cell lines.
Mutagenesis 61 – 61 Q -> R. Promotes interaction with SHOC2 and PP1C.
Mutagenesis 61 – 61 Q -> V. Strongly increased transformation of cultured cell lines.
Beta strand 60 – 63



Literature citations
Transformation efficiency of RasQ61 mutants linked to structural features of the switch regions in the presence of Raf.
Buhrman G.; Wink G.; Mattos C.;
Structure 15:1618-1629(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-166 IN COMPLEXES WITH GTP ANALOG; CHARACTERIZATION OF VARIANTS LEU-61 AND LYS-61; MUTAGENESIS OF GLN-61; RAS point mutations and PAX8-PPAR gamma rearrangement in thyroid tumors: evidence for distinct molecular pathways in thyroid follicular carcinoma.
Nikiforova M.N.; Lynch R.A.; Biddinger P.W.; Alexander E.K.; Dorn G.W. II; Tallini G.; Kroll T.G.; Nikiforov Y.E.;
J. Clin. Endocrinol. Metab. 88:2318-2326(2003)
Cited for: INVOLVEMENT IN NMTC2; VARIANT NMTC2 LYS-61;
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.