UniProtKB/Swiss-Prot P36957: Variant p.Asp304Asn

Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Gene: DLST
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Variant information Variant position:

304 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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:

From Aspartate (D) to Asparagine (N) at position 304 (D304N, p.Asp304Asn). 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:

Change from medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 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:

Not changed dihydrolipoyllysine-residue succinyltransferase activity. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs373295097 [ dbSNP | Ensembl ]

Sequence information Variant position:

304 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

453 The length of the canonical sequence.
Location on the sequence:

FVKASAFALQEQPVVNAVID D TTKEVVYRDYIDISVAVATP 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                         FVKASAFALQEQPVVNAVIDDT--TKEVVYRDYIDISVAVATP

Mouse                         FVKASAFALQEQPVVNAVIDDA--TKEVVYRDYIDISVAVA

Rat                           FVKASAFALQEQPVVNAVIDDA--TKEVVYRDYIDISVAVA

Pig                           FVKASAFALQEQPVVNAVIDDT--TKEVVYRDYIDISVAVA

Bovine                        FVKASAFALQEQPVVNAVIDDA--TKEVVYRDYIDISVAVA

Slime mold                    FVKASTIALKEQPIVNASVE----ENDIVYHNNVNINVAVS

Baker's yeast                 FSKACTLAAKDIPAVNGAIE----GDQIVYRDYTDISVAVA

Fission yeast                 FSKACTQAMKQIPAINGSIEGEGKGDTLVYRDFCDLSIAVA

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
Chain	68 – 453	Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
Modified residue	307 – 307	N6-acetyllysine
Turn	304 – 307

Literature citations
Recurrent germline DLST mutations in individuals with multiple pheochromocytomas and paragangliomas.
Remacha L.; Pirman D.; Mahoney C.E.; Coloma J.; Calsina B.; Curras-Freixes M.; Leton R.; Torres-Perez R.; Richter S.; Pita G.; Herraez B.; Cianchetta G.; Honrado E.; Maestre L.; Urioste M.; Aller J.; Garcia-Uriarte O.; Galvez M.A.; Luque R.M.; Lahera M.; Moreno-Rengel C.; Eisenhofer G.; Montero-Conde C.; Rodriguez-Antona C.; Llorca O.; Smolen G.A.; Robledo M.; Cascon A.;
Am. J. Hum. Genet. 104:651-664(2019)
Cited for: INVOLVEMENT IN PPGL7; VARIANTS PPGL7 GLN-231; GLU-374 AND CYS-422; VARIANT ASN-304; CHARACTERIZATION OF VARIANTS PPGL7 GLN-231; GLU-374 AND CYS-422; CHARACTERIZATION OF VARIANT ASN-304; FUNCTION; CATALYTIC ACTIVITY; PATHWAY; MUTAGENESIS OF HIS-424; ACTIVE SITE;

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.