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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14757: Variant p.Arg379Gln

Serine/threonine-protein kinase Chk1
Gene: CHEK1
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Variant information Variant position: help 379 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 Glutamine (Q) at position 379 (R379Q, p.Arg379Gln). 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 polar (Q) 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 OZEMA21; likely pathogenic; results in failure of male and female pronuclei fusion when injected in mouse zygotes; increased kinase activity. Any additional useful information about the variant.


Sequence information Variant position: help 379 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 476 The length of the canonical sequence.
Location on the sequence: help LLGTPGSSQNPWQRLVKRMT R FFTKLDADKSYQCLKETCEK 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                         LLGTP------GSSQNPWQRLVKR------------MTRFFTKLDAD-------------------KSYQCLKETCEK

Mouse                         LLGTP------GSSQNPWQRLVKR------------MTRFF

Rat                           LLGTP------GSSQNPWQRLVKR------------MTRFF

Chicken                       LLGTP------GSSQSPWQRLVRR------------MTRFF

Xenopus laevis                LIGTP------GSSQNVWQRLVKR------------MTRFF

Caenorhabditis elegans        HIDMS------QTNSNLLQRMVCR------------MTRFC

Drosophila                    MNQTQ------NASQNYFQRLVRR------------MTRFF

Baker's yeast                 FISYDIAALQFHSDENDCNELVKRHLQF----NPNKLTKFY

Fission yeast                 ILEKDPSLSQFCENEGFIKRLAKKAKNFYEICPPERLTRFY
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 – 476 Serine/threonine-protein kinase Chk1
Mutagenesis 366 – 366 S -> A. No effect on phosphorylation induced by hydroxyurea.
Mutagenesis 372 – 372 R -> E. In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-376 and E-379.
Mutagenesis 376 – 376 R -> E. In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-379.
Mutagenesis 379 – 379 R -> E. In 3RE mutant. Disrupts the folding and/or conformation, allowing increased accessibility to FBXO6 component of SCF-type E3 ubiquitin ligase complex; when associated with E-372 and E-376.
Beta strand 379 – 384



Literature citations
Dominant mutations in CHK1 cause pronuclear fusion failure and zygote arrest that can be rescued by CHK1 inhibitor.
Zhang H.; Chen T.; Wu K.; Hou Z.; Zhao S.; Zhang C.; Gao Y.; Gao M.; Chen Z.J.; Zhao H.;
Cell Res. 31:814-817(2021)
Cited for: VARIANTS OZEMA21 GLN-379; LYS-420 AND GLN-442; CHARACTERIZATION OF VARIANTS OZEMA21 GLN-379; LYS-420 AND GLN-442; INVOLVEMENT IN OZEMA21;
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.