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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14757: Variant p.Arg442Gln

Serine/threonine-protein kinase Chk1
Gene: CHEK1
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Variant information Variant position: help 442 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 442 (R442Q, p.Arg442Gln). 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; 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 442 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 NKLIFKVNLLEMDDKILVDF R LSKGDGLEFKRHFLKIKGKL 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                         NKLIFKVNLLEMDDKI-LVDFRLSKGDGLEFKRHFLKIKGKL

Mouse                         NKLIFKINLVEMDEKI-LVDFRLSKGDGLEFKRHFLKIKGK

Rat                           NKLIFKINLVEMDEKI-LVDFRLSKGDGLEFKRHFLKIKGK

Chicken                       NKLIFKVNLLEMESRI-LVDFRLSKGDGLEFKRHFLKIKGK

Xenopus laevis                NKLIFKVNLVEMEDRI-LLDFRLSKGDGLEFKRHFLKIKKK

Caenorhabditis elegans        MVSLYTMGDIPDKPRV-MVDFRRSRGDGIQFKKMFMDVRNR

Drosophila                    LRLVFKAHIIEMDGKI-LVDCRLSKGCGLEFKRRFIKIKNA

Baker's yeast                 YQLCGSISIIKIEEELKSVGFERKTGDPLEWRRLFKKI---

Fission yeast                 CLLQGVIELTNLGHNLELINFIKRNGDPLEWRKFFKNVVSS
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
Region 391 – 476 Autoinhibitory region
Cross 436 – 436 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence 412 – 445 Missing. In isoform 3.
Mutagenesis 436 – 436 K -> R. Enhances stability of the protein, probably by preventing ubiquitination at this site.
Beta strand 434 – 446



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; Maternal heterozygous mutation in CHEK1 leads to mitotic arrest in human zygotes.
Chen B.; Guo J.; Wang T.; Lee Q.; Ming J.; Ding F.; Li H.; Zhang Z.; Li L.; Cao Y.; Na J.;
Protein Cell 13:148-154(2022)
Cited for: VARIANT OZEMA21 GLN-442; CHARACTERIZATION OF VARIANT OZEMA21 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.