Variant position: 230 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 510 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 GLQKLHDALDAKSKEFAQII KIGRTHTQDAVPLTLGQEFSG
Mouse GLQKLHDALSAKSKEFAQVI KIGRTHTQDAVPLTLGQEFSG
Rat GLQKLHDALSAKSKEFAQVI KIGRTHTQDAVPLTLGQEFSG
Pig GLQKLHDALDAKSREFAQII KIGRTHTQDAVPLTLGQEFSG
Zebrafish GLQTLHDALAAKAEQFKDII KIGRTHTQDAVPLSLGQEFGG
Caenorhabditis elegans ALKKLRTALHNKAEEFKDII KIGRTHTQDAVPLTLGQEFSA
Slime mold ALEMLLAAMRTKQNEFNHII KIGRTHLQDATPLTLGQEFSG
Baker's yeast ELTNLKNALEAKSKEFDHIV KIGRTHLQDATPLTLGQEFSG
Fission yeast AMKHLHRALKGKEEEFKNII KIGRTHMQDATPLSLGQEFSG
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
45 – 510 Fumarate hydratase, mitochondrial
235 – 235 Proton donor/acceptor
234 – 234 Substrate
213 – 213 N6-acetyllysine
223 – 223 N6-acetyllysine; alternate
223 – 223 N6-succinyllysine; alternate
236 – 236 Phosphothreonine; by PRKDC
236 – 236 T -> A. Abolished interaction with H2AZ1 and localization to chromatin in response to DNA damage.
236 – 236 T -> D. Phosphomimetic mutant; promotes interaction with H2AZ1, leading to increased localization to chromatin in response to DNA damage.
229 – 234
Molecular analysis and prenatal diagnosis of human fumarase deficiency.
Coughlin E.M.; Christensen E.; Kunz P.L.; Krishnamoorthy K.S.; Walker V.; Dennis N.R.; Chalmers R.A.; Elpeleg O.N.; Whelan D.; Pollitt R.J.; Ramesh V.; Mandell R.; Shih V.E.;
Mol. Genet. Metab. 63:254-262(1998)
Cited for: VARIANTS FMRD ARG-230; THR-308; CYS-312 AND VAL-425;
Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer.
Tomlinson I.P.M.; Alam N.A.; Rowan A.J.; Barclay E.; Jaeger E.E.M.; Kelsell D.; Leigh I.; Gorman P.; Lamlum H.; Rahman S.; Roylance R.R.; Olpin S.; Bevan S.; Barker K.; Hearle N.; Houlston R.S.; Kiuru M.; Lehtonen R.; Karhu A.; Vilkki S.; Laiho P.; Eklund C.; Vierimaa O.; Aittomaeki K.; Hietala M.; Sistonen P.; Paetau A.; Salovaara R.; Herva R.; Launonen V.; Aaltonen L.A.;
Nat. Genet. 30:406-410(2002)
Cited for: VARIANTS HLRCC THR-107; PRO-117; ARG-180; ARG-185; ARG-230; HIS-233; VAL-282 AND ARG-328;
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.