UniProtKB/SwissProt variant VAR

Variant information

Variant position:

235

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

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:

From Glutamine (Q) to Histidine (H) at position 235 (Q235H, p.Gln235His).

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:

Similar physico-chemical property. Both residues are medium size and polar.

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

0

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:

In SEMDHL; severe decrease of protein expression.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs377527583 [ dbSNP | Ensembl ]

Sequence information

Variant position:

235

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

613

The length of the canonical sequence.

Location on the sequence:

QDLPHIENGGVAVLTGKKVV Q LDVRDNMVKLNDGSQITYEK

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                         QDLPHIENGGVAVLTGKKVVQLDVRDNMVKLNDGSQITYEK

Mouse                         QDLPNIENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEK

Rat                           QDLPHIENGGVAVLTGKKVVHLDVRGNMVKLNDGSQITFEK

Drosophila                    EDLDDNANGGIAVAQGFSVKKVDAQKRIVTLNDGYEISYDE

Slime mold                    ------GNEILQFIRTKKVIDLHIDEKLVLLNDGKLIRYDK

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	102 – 613	Apoptosis-inducing factor 1, mitochondrial
Region	134 – 483	FAD-dependent oxidoreductase
Binding site	233 – 233	FAD; via amide nitrogen and carbonyl oxygen
Cross	255 – 255	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Alternative sequence	1 – 352	Missing. In isoform 5.
Alternative sequence	36 – 322	Missing. In isoform 2.
Alternative sequence	44 – 613	Missing. In isoform 6.
Beta strand	233 – 237

Literature citations

X-linked hypomyelination with spondylometaphyseal dysplasia (H-SMD) associated with mutations in AIFM1.
Miyake N.; Wolf N.I.; Cayami F.K.; Crawford J.; Bley A.; Bulas D.; Conant A.; Bent S.J.; Gripp K.W.; Hahn A.; Humphray S.; Kimura-Ohba S.; Kingsbury Z.; Lajoie B.R.; Lal D.; Micha D.; Pizzino A.; Sinke R.J.; Sival D.; Stolte-Dijkstra I.; Superti-Furga A.; Ulrick N.; Taft R.J.; Ogata T.; Ozono K.; Matsumoto N.; Neubauer B.A.; Simons C.; Vanderver A.;
Neurogenetics 18:185-194(2017)
Cited for: VARIANTS SEMDHL HIS-235; GLY-237 AND VAL-237; CHARACTERIZATION OF VARIANT SEMDHL HIS-235; INVOLVEMENT IN SEMDHL; TISSUE SPECIFICITY;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95831: Variant p.Gln235His