Variant position: 172 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 452 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 IICKNIPRLVPGWTKPITIG RHAHGDQYKATDFVADRAGTF
Mouse IICKNIPRLVPGWTKPITIG RHAHGDQYKATDFVVDRAGTF
Rat IICKNIPRLVPGWTKPITIG RHAHGDQYKATDFVVDRAGMF
Bovine IICKNIPRLVPGWTKPITIG RHAHGDQYKATDFVVDRAGTF
Slime mold IICKNLPLLVPGWKKPIIIG RHAHGDQYKATDFVVNGPGKL
Baker's yeast IVIPRIPRLVPRWEKPIIIG RHAHGDQYKATDTLIPGPGSL
Fission yeast ILIKNIPKYIPGWTNPICIG RHAFGDQYKSTDLVASGPGKL
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
40 – 452 Isocitrate dehydrogenase [NADP], mitochondrial
172 – 172 Substrate
179 – 179 Critical for catalysis
155 – 155 N6-acetyllysine
166 – 166 N6-acetyllysine; alternate
166 – 166 N6-succinyllysine; alternate
180 – 180 N6-acetyllysine; alternate
180 – 180 N6-succinyllysine; alternate
169 – 173
IDH1 and IDH2 mutations in gliomas.
Yan H.; Parsons D.W.; Jin G.; McLendon R.; Rasheed B.A.; Yuan W.; Kos I.; Batinic-Haberle I.; Jones S.; Riggins G.J.; Friedman H.; Friedman A.; Reardon D.; Herndon J.; Kinzler K.W.; Velculescu V.E.; Vogelstein B.; Bigner D.D.;
N. Engl. J. Med. 360:765-773(2009)
Cited for: VARIANTS GLM GLY-172; LYS-172 AND MET-172; CHARACTERIZATION OF VARIANTS GLM GLY-172; LYS-172 AND MET-172;
IDH2 mutation in gliomas including novel mutation.
Koh J.; Cho H.; Kim H.; Kim S.I.; Yun S.; Park C.K.; Lee S.H.; Choi S.H.; Park S.H.;
Cited for: VARIANTS GLM LEU-158; SER-162 AND LYS-172;
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.