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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14757: Variant p.Val312Met

Serine/threonine-protein kinase Chk1
Gene: CHEK1
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Variant information Variant position: help 312 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Valine (V) to Methionine (M) at position 312 (V312M, p.Val312Met). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. 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

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 312 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 KHIQSNLDFSPVNSASSEEN V KYSSSQPEPRTGLSLWDTSP 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                         KHIQSNLDFSPVNSAS------SEENVKYSSSQPEP----------RTGLSLWDTSP

Mouse                         KHIHSNLDFSPVNNGS------SEETVKFSSSQPEP-----

Rat                           KHIHSNLDFSPINSGS------SEENVKFSSSQPEP-----

Chicken                       KHIRSDTDFSPVKSAL------GEDKASYSTSQPEP-----

Xenopus laevis                KQIRSDIDISHFSH--------SEEKTALSSTQPEP-----

Caenorhabditis elegans        LKRARN----------------NDENI--TCTQQAE-----

Drosophila                    QRLQSS---AHLSNGL------DDSISRNYCSQPMPTMRSD

Baker's yeast                 KKLFSHLKVSLSNENYLKFTQDTNSNNRYISTQPIG-----

Fission yeast                 LKLRIDLDKPRLASSRA-----SQNDSGFSMTQPAF-----

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 270 – 327 Disordered
Compositional bias 281 – 327 Polar residues
Modified residue 296 – 296 Phosphoserine
Modified residue 301 – 301 Phosphoserine
Modified residue 317 – 317 Phosphoserine; by ATM and ATR
Modified residue 331 – 331 Phosphoserine
Mutagenesis 317 – 317 S -> A. Abrogates interaction with RAD51; when associated with A-345. Reduces phosphorylation and impairs activation by hydroxyurea and ionizing radiation. Abrogates nuclear retention upon checkpoint activation. Impairs interaction with FBXO6.
Mutagenesis 317 – 317 S -> E. Enhances interaction with RAD51; when associated with E-345.



Literature citations
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-223 AND MET-312;
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.