Variant position: 246 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 2492 The length of the canonical sequence.
Location on the 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.
Human GGNLICCDFCHNAFCKKCIL RNLGRKELSTIMDENNQWYCY
Chimpanzee GGNLICCDFCHNAFCKKCIL RNLGRKELSTIMDENNQWYCY
Mouse GGNLICCDFCHNAFCKKCIL RNLGRKELSTIMDENNQWYCY
Caenorhabditis elegans -------------------- ---------------------
Drosophila -------------------- ---------------------
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.
Type Positions Description
1 – 2492 Transcriptional regulator ATRX
159 – 296 ADD
217 – 272 PHD-type; atypical
252 – 252 E -> L. Impairs interaction with histone H3 peptides and reduces localization to pericentromeric heterochromatin foci.
241 – 247
The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9.
Dhayalan A.; Tamas R.; Bock I.; Tattermusch A.; Dimitrova E.; Kudithipudi S.; Ragozin S.; Jeltsch A.;
Hum. Mol. Genet. 20:2195-2203(2011)
Cited for: INTERACTION WITH TRIMETHYLATED HISTONE H3 'LYS-9'; CHARACTERIZATION OF VARIANTS ATRX CYS-246; LEU-246 AND ASP-249; MUTAGENESIS OF TYR-203; TYR-204; ILE-209; ASP-214 AND ASP-217;
ATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndrome.
Iwase S.; Xiang B.; Ghosh S.; Ren T.; Lewis P.W.; Cochrane J.C.; Allis C.D.; Picketts D.J.; Patel D.J.; Li H.; Shi Y.;
Nat. Struct. Mol. Biol. 18:769-776(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (0.93 ANGSTROMS) OF 167-289 IN COMPLEX WITH HISTONE H3K9ME3 PEPTIDE; SUBCELLULAR LOCATION; CHARACTERIZATION OF ATRX VARIANTS ALA-190; PRO-219 AND CYS-246; MUTAGENESIS OF HIS-189; TYR-203; TYR-204; ASP-217; GLU-252 AND LYS-1600;
Molecular genetic study of Japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X).
Wada T.; Kubota T.; Fukushima Y.; Saitoh S.;
Am. J. Med. Genet. 94:242-248(2000)
Cited for: VARIANTS ATRX SER-179; LEU-190; ILE-194; CYS-246; PHE-1552; SER-1645 AND CYS-1847;
ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger domain and a totally skewed X-inactivation pattern.
Badens C.; Martini N.; Courrier S.; DesPortes V.; Touraine R.; Levy N.; Edery P.;
Am. J. Med. Genet. A 140:2212-2215(2006)
Cited for: VARIANT ATRX CYS-246;
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