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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P21912: Variant p.Asp48Val

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Gene: SDHB
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Variant information Variant position: help 48 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Aspartate (D) to Valine (V) at position 48 (D48V, p.Asp48Val). 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: help Change from medium size and acidic (D) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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: help In MC2DN4; decreased succinate dehydrogenase (ubiquinone) activity in homozygous patient cells; decreased protein levels in homozygous patient cells. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 48 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 280 The length of the canonical sequence.
Location on the sequence: help GAQTAAATAPRIKKFAIYRW D PDKAGDKPHMQTYEVDLNKC 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         GAQTAAATAP------RIKK---------FAIYRWDPDKAGDKPHMQTYEVDLNKC

Mouse                         GAQTAAAAAP------RIKK---------FAIYRWDPDKTG

Rat                           EAQTAAAAAP------RIKT---------FAIYRWDPDKAG

Pig                           GAQTAAATAP------RIKK---------FAIYRWDPDKTG

Bovine                        GAQTAAAAAP------RIKK---------FAIYRWDPDKTG

Chicken                       GAQTAAAATS------RIKK---------FSIYRWDPDKPG

Xenopus laevis                GAQTAAAPASQAAA--RIKK---------FAIYRWDPDKPG

Xenopus tropicalis            GAQTAAAAAPASQAEARIKK---------FAIYRWDPDKPG

Zebrafish                     FAQTAAAPAAQP----RIKK---------FQIYRWDPDTVG

Caenorhabditis elegans        PSTDDVAAKTKKTGN-RIKT---------FEIYRFNPEAPG

Drosophila                    QAQPKEAQEP------QIKK---------FEIYRWNPDNAG

Slime mold                    TAKTEASSSP----QMKIKTAEKKDHFVNFQVYRYN-EETT

Baker's yeast                 ATTAAATHTP------RLKT---------FKVYRWNPDEPS

Fission yeast                 ANISATSANPQSQGE-NLKT---------FEIYRWNPEKPE
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 29 – 280 Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
Domain 40 – 133 2Fe-2S ferredoxin-type
Modified residue 51 – 51 N6-acetyllysine
Modified residue 55 – 55 N6-acetyllysine



Literature citations
Recessive germline SDHA and SDHB mutations causing leukodystrophy and isolated mitochondrial complex II deficiency.
Alston C.L.; Davison J.E.; Meloni F.; van der Westhuizen F.H.; He L.; Hornig-Do H.T.; Peet A.C.; Gissen P.; Goffrini P.; Ferrero I.; Wassmer E.; McFarland R.; Taylor R.W.;
J. Med. Genet. 49:569-577(2012)
Cited for: VARIANT MC2DN4 VAL-48; INVOLVEMENT IN MC2DN4; Mitochondrial leukoencephalopathy and complex II deficiency associated with a recessive SDHB mutation with reduced penetrance.
Ardissone A.; Invernizzi F.; Nasca A.; Moroni I.; Farina L.; Ghezzi D.;
Mol. Genet. Metab. Rep. 5:51-54(2015)
Cited for: VARIANT MC2DN4 VAL-48; CHARACTERIZATION OF VARIANT MC2DN4 VAL-48; INVOLVEMENT IN MC2DN4; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; Magnetic resonance imaging spectrum of succinate dehydrogenase-related infantile leukoencephalopathy.
Helman G.; Caldovic L.; Whitehead M.T.; Simons C.; Brockmann K.; Edvardson S.; Bai R.; Moroni I.; Taylor J.M.; Van Haren K.; Taft R.J.; Vanderver A.; van der Knaap M.S.;
Ann. Neurol. 79:379-386(2016)
Cited for: VARIANTS MC2DN4 VAL-48 AND THR-103; INVOLVEMENT IN MC2DN4; Leukoencephalopathy due to Complex II Deficiency and Bi-Allelic SDHB Mutations: Further Cases and Implications for Genetic Counselling.
Groenborg S.; Darin N.; Miranda M.J.; Damgaard B.; Cayuela J.A.; Oldfors A.; Kollberg G.; Hansen T.V.O.; Ravn K.; Wibrand F.; Oestergaard E.;
JIMD Rep. 33:69-77(2017)
Cited for: VARIANTS MC2DN4 VAL-48; HIS-230 AND VAL-257; CHARACTERIZATION OF VARIANT MC2DN4 VAL-257; FUNCTION; CATALYTIC ACTIVITY; ALTERNATIVE SPLICING;
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.