UniProtKB/Swiss-Prot Q969Y2: Variant p.Ala322Pro

tRNA modification GTPase GTPBP3, mitochondrial
Gene: GTPBP3
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Variant information Variant position:

322 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 Alanine (A) to Proline (P) at position 322 (A322P, p.Ala322Pro). 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 small size and hydrophobic (A) to medium size and hydrophobic (P) 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
Polymorphism:

Val-250 variation may influence aminoglycoside-induced deafness (AID) [MIM:580000]. AID is characterized by deafness, varying from profond congenital hearing loss to normal hearing, and is caused by homoplasmic A1555G mutation in the mitochondrial 12S rRNA. Val-250 may affect the accuracy of codon-anticodon interaction, leading to modulate the translational efficiency and thereby affecting the severity of deafness in patients homozygous for 12S rRNA A1555G mutation. Additional information on the polymorphism described.
Other resources:

Links to websites of interest for the variant.

Variant rs372174278 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

SDTAGLREGVGPVEQEGVRR A RERLEQADLILAMLDASDLA 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                         SDTAGLREGV-GPVEQEGVRRARERLEQADLILAMLDASDLA

Mouse                         SDTAGLREGV-GAVEQEGVRRARHRLEQADIILGVLDASDL

Rat                           SDTAGLREGA-GAVEQEGVRRARQRLEQADIILGMLDASDL

Zebrafish                     SDTAGLRDTS-DSVEQEGVRRARQRVEQADLSLVVVDLTQL

Slime mold                    GDTAGLRNSTNDQIEIEGIEMAKDRFNNSDIKLFLFDSFNL

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	82 – 492	tRNA modification GTPase GTPBP3, mitochondrial
Domain	249 – 416	TrmE-type G

Literature citations
Mutations in GTPBP3 cause a mitochondrial translation defect associated with hypertrophic cardiomyopathy, lactic acidosis, and encephalopathy.
Kopajtich R.; Nicholls T.J.; Rorbach J.; Metodiev M.D.; Freisinger P.; Mandel H.; Vanlander A.; Ghezzi D.; Carrozzo R.; Taylor R.W.; Marquard K.; Murayama K.; Wieland T.; Schwarzmayr T.; Mayr J.A.; Pearce S.F.; Powell C.A.; Saada A.; Ohtake A.; Invernizzi F.; Lamantea E.; Sommerville E.W.; Pyle A.; Chinnery P.F.; Crushell E.; Okazaki Y.; Kohda M.; Kishita Y.; Tokuzawa Y.; Assouline Z.; Rio M.; Feillet F.; Mousson de Camaret B.; Chretien D.; Munnich A.; Menten B.; Sante T.; Smet J.; Regal L.; Lorber A.; Khoury A.; Zeviani M.; Strom T.M.; Meitinger T.; Bertini E.S.; Van Coster R.; Klopstock T.; Rotig A.; Haack T.B.; Minczuk M.; Prokisch H.;
Am. J. Hum. Genet. 95:708-720(2014)
Cited for: INVOLVEMENT IN COXPD23; VARIANTS COXPD23 LEU-3; LYS-142; VAL-159; PRO-162; GLY-222; HIS-257; 312-GLY--VAL-319 DEL; HIS-337 AND LYS-459; VARIANTS LYS-225 AND PRO-322;

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.