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UniProtKB/Swiss-Prot Q13315: Variant p.Asn3003Asp

Serine-protein kinase ATM
Gene: ATM
Variant information

Variant position:  3003
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Asparagine (N) to Aspartate (D) at position 3003 (N3003D, p.Asn3003Asp).
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:  Change from medium size and polar (N) to medium size and acidic (D)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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:  In AT; decreased protein abundance.
Any additional useful information about the variant.

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

Sequence information

Variant position:  3003
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  3056
The length of the canonical sequence.

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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.




Caenorhabditis elegans        -----------------PSY--ISEMAIGRLREKLRGTDDG

Drosophila                    -----------------ESVNLVAQRALLLVQNKLDGREAG

Baker's yeast                 FDNVSKFISNNDRNENQESY-----RALKGVEEKLMGNG--

Fission yeast                 DASRDPKIQRNNVSGESE-----AERAILKVRQKLSST---

Sequence annotation in neighborhood:  
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.

Chain 2 – 3056 Serine-protein kinase ATM
Modified residue 2996 – 2996 Phosphoserine
Modified residue 3016 – 3016 N6-acetyllysine
Mutagenesis 3016 – 3016 K -> Q. Mimics acetylation, preventing dephosphorylation and subsequent ATM deactivation during the late stage of DNA damage response.
Mutagenesis 3016 – 3016 K -> R. Loss of DNA damage-inducible acetylation. Retains constitutive kinase activity, but blocks DNA damage-induced kinase activation. Disrupts dimer and abolishes S-1981 autophosphorylation.
Mutagenesis 3018 – 3018 K -> R. Retains DNA damage-inducible acetylation and S-1981 autophosphorylation.
Helix 3001 – 3018

Literature citations

The complete sequence of the coding region of the ATM gene reveals similarity to cell cycle regulators in different species.
Savitsky K.; Sfez S.; Tagle D.A.; Ziv Y.; Sartiel A.; Collins F.S.; Shiloh Y.; Rotman G.;
Hum. Mol. Genet. 4:2025-2032(1995)

The ATM gene and susceptibility to breast cancer: analysis of 38 breast tumors reveals no evidence for mutation.
Vorechovsky I.; Rasio D.; Luo L.; Monaco C.; Hammarstroem L.; Webster A.D.B.; Zaloudik J.; Barbanti-Brodano G.; James M.R.; Russo G.; Croce C.M.; Negrini M.;
Cancer Res. 56:2726-2732(1996)

A single ataxia telangiectasia gene with a product similar to PI-3 kinase.
Savitsky K.; Bar-Shira A.; Gilad S.; Rotman G.; Ziv Y.; Vanagaite L.; Tagle D.A.; Smith S.; Uziel T.; Sfez S.; Ashkenazi M.; Pecker I.; Frydman M.; Harnik R.; Patanjali S.R.; Simmons A.; Clines G.A.; Sartiel A.; Gatti R.A.; Chessa L.; Sanal O.; Lavin M.F.; Jaspers N.G.J.; Taylor A.M.R.; Arlett C.F.; Miki T.; Weissman S.M.; Lovett M.; Collins F.S.; Shiloh Y.;
Science 268:1749-1753(1995)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1332-3056; VARIANTS 2427-LEU-ARG-2428 DEL; 2546-SER--ILE-2548 DEL; SER-2860 DEL AND ASP-3003;

Molecular and functional characterization of a cohort of Spanish patients with ataxia-telangiectasia.
Carranza D.; Vega A.K.; Torres-Rusillo S.; Montero E.; Martinez L.J.; Santamaria M.; Santos J.L.; Molina I.J.;
NeuroMolecular Med. 19:161-174(2017)
Cited for: VARIANTS AT VAL-323; PRO-1046; ARG-2023; SER-2068; ASP-2080; HIS-2627; LEU-2834 AND ASP-3003; CHARACTERIZATION OF VARIANTS AT VAL-323; PRO-1046; ARG-2023; SER-2068; ASP-2080; HIS-2627; LEU-2834 AND ASP-3003; PHOSPHORYLATION;

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.