UniProtKB/SwissProt variant VAR

Variant information

Variant position:

76

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 Asparagine (N) to Aspartate (D) at position 76 (N76D, p.Asn76Asp).

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 polar (N) to medium size and acidic (D)

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:

In SMDMDM.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs786203989 [ dbSNP | Ensembl ]

Sequence information

Variant position:

76

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

Protein sequence length:

125

The length of the canonical sequence.

Location on the sequence:

LQEAQQILNVSKLSPEEVQK N YEHLFKVNDKSVGGSFYLQS

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                         LQEAQQILNVSK----LSPEEVQKNYEHLFKVNDKSVGGSFYLQS

Mouse                         LQEAQQILNVSK----LSPEEVQKNYEHLFKVNDKSVGGSF

Rat                           LQEAQQILNISK----LSPEEVQ-NYEHLFKVNDKSVGDSF

Xenopus tropicalis            LQEAQQILNVSK----LTPEEIQKNYEHLFKVNDKEVGGSF

Zebrafish                     LQEAQQILNIST----LTPEEIQKNYEHLFKVNDKAVGGSF

Caenorhabditis elegans        LEESLQILNVKTP---LNREEVEKHYEHLFNINDKSKGGTL

Drosophila                    LEEAKQILNIDDP---KNVDAITKNYEHLFQVNERSKGGSF

Slime mold                    PIEARKILGLENVE-TVSKEDIDKKYNELLTINDPKDGGSE

Baker's yeast                 LDESCKILNIEESKGDLNMDKINNRFNYLFEVNDKEKGGSF

Fission yeast                 IQEAGSILNIKPES--LEEGELEKRFQKMFEINDPKKGGSF

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	1 – 125	Mitochondrial import inner membrane translocase subunit TIM16
Region	58 – 110	J-like
Modified residue	69 – 69	Phosphoserine
Mutagenesis	62 – 62	I -> AQW. Substantial loss of protein translocation into mitochondria in a heterologous system.
Mutagenesis	92 – 92	F -> G. Partial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of protein translocation into mitochondria in a heterologous system; when associated with G-93. Partial loss of DNAJC19-binding. Loss of DNAJC19-binding; when associated with G-93. Partial loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity. Complete loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity; when associated with G-93.
Mutagenesis	93 – 93	Y -> G. Partial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of protein translocation into mitochondria in a heterologous system; when associated with G-92. Loss of DNAJC19-binding; when associated with G-92. Complete loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity; when associated with G-92.
Mutagenesis	94 – 94	L -> A. No effect on protein translocation into mitochondria in a heterologous system.
Mutagenesis	94 – 94	L -> Q. Substantial loss of protein translocation into mitochondria in a heterologous system. Substantial loss of DNAJC19-binding. Partial loss of inhibition of DNAJC19 stimulation of HSPA9 ATPase activity.

Literature citations

The impairment of MAGMAS function in human is responsible for a severe skeletal dysplasia.
Mehawej C.; Delahodde A.; Legeai-Mallet L.; Delague V.; Kaci N.; Desvignes J.P.; Kibar Z.; Capo-Chichi J.M.; Chouery E.; Munnich A.; Cormier-Daire V.; Megarbane A.;
PLoS Genet. 10:E1004311-E1004311(2014)
Cited for: INVOLVEMENT IN SMDMDM; VARIANT SMDMDM ASP-76;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y3D7: Variant p.Asn76Asp