Variant position: 132 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 414 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 IICKNIPRLVSGWVKPIIIG RHAYGDQYRATDFVVPGPGKV
Mouse IICKNIPRLVTGWVKPIIIG RHAYGDQYRATDFVVPGPGKV
Rat IICKNIPRLVTGWVKPIIIG RHAYGDQYRATDFVVPGPGKV
Bovine IICKNIPRLVSGWVKPIIIG RHAYGDQYRATDFVVPGPGKV
Sheep IICKNIPRLVSGWVKPIIIG RHAYGDQYRATDFVVPGPGKV
Slime mold IVCKNVPRLVTCWNKSIVIG RHAFGDQYRATDFVVKGAGKL
Baker's yeast IIIPRIPRLVPQWEKPIIIG RHAFGDQYKATDVIVPEEGEL
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
2 – 414 Isocitrate dehydrogenase [NADP] cytoplasmic
132 – 132 Substrate
139 – 139 Critical for catalysis
126 – 126 N6-succinyllysine
126 – 134
IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors.
Bleeker F.E.; Lamba S.; Leenstra S.; Troost D.; Hulsebos T.; Vandertop W.P.; Frattini M.; Molinari F.; Knowles M.; Cerrato A.; Rodolfo M.; Scarpa A.; Felicioni L.; Buttitta F.; Malatesta S.; Marchetti A.; Bardelli A.;
Hum. Mutat. 30:7-11(2009)
Cited for: VARIANTS CYS-132; GLY-132 AND LEU-132; INVOLVEMENT IN GLM;
Mutant IDH1 Dysregulates the Differentiation of Mesenchymal Stem Cells in Association with Gene-Specific Histone Modifications to Cartilage- and Bone-Related Genes.
Jin Y.; Elalaf H.; Watanabe M.; Tamaki S.; Hineno S.; Matsunaga K.; Woltjen K.; Kobayashi Y.; Nagata S.; Ikeya M.; Kato T. Jr.; Okamoto T.; Matsuda S.; Toguchida J.;
PLoS ONE 10:E0131998-E0131998(2015)
Cited for: VARIANTS CYS-132; GLY-132 AND HIS-132; INVOLVEMENT IN DISEASE; CHARACTERIZATIONOF VARIANT CYS-132;
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.