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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O43293: Variant p.Asp161Asn

Death-associated protein kinase 3
Gene: DAPK3
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Variant information Variant position: help 161 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 Aspartate (D) to Asparagine (N) at position 161 (D161N, p.Asp161Asn). 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 acidic (D) to medium size and polar (N) 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 an ovarian mucinous carcinoma sample; somatic mutation; greatly reduces kinase activity, increases cell proliferation and cell survival. Any additional useful information about the variant.


Sequence information Variant position: help 161 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 454 The length of the canonical sequence.
Location on the sequence: help KPENIMLLDKNVPNPRIKLI D FGIAHKIEAGNEFKNIFGTP 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                         KPENIMLLDKNVPNPRIKLIDFGIAHKIEAGNEFKNIFGTP

Mouse                         KPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTP

Rat                           KPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTP

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 – 454 Death-associated protein kinase 3
Domain 13 – 275 Protein kinase
Region 161 – 204 Activation segment
Modified residue 180 – 180 Phosphothreonine
Mutagenesis 161 – 161 D -> A. Loss of kinase activity.
Mutagenesis 180 – 180 T -> A. Greatly reduced kinase activity.



Literature citations
Cancer-associated loss-of-function mutations implicate DAPK3 as a tumor-suppressing kinase.
Brognard J.; Zhang Y.W.; Puto L.A.; Hunter T.;
Cancer Res. 71:3152-3161(2011)
Cited for: FUNCTION AS TUMOR SUPPRESSOR; CHARACTERIZATION OF VARIANTS MET-112; ASN-161 AND SER-216; MUTAGENESIS OF THR-180; SELF-ASSOCIATION; 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] MET-112; ASN-161 AND SER-216;
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.