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UniProtKB/Swiss-Prot Q6NUK1: Variant p.Arg217His

Calcium-binding mitochondrial carrier protein SCaMC-1
Gene: SLC25A24
Variant information

Variant position:  217
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Histidine (H) at position 217 (R217H, p.Arg217His).
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 large size and basic (R) to medium size and polar (H)
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

Involvement in disease:  Fontaine progeroid syndrome (FPS) [MIM:612289]: An autosomal dominant progeroid disorder characterized by prenatal and postnatal growth retardation, decreased subcutaneous fat tissue, wrinkled skin, an aged appearance since birth, an abnormal scalp hair pattern, sparse hair, hypoplastic distal phalanges with hypoplastic nails, a widely open anterior fontanel, facial dysmorphisms, and craniosynostosis. Early death is observed in some patients. {ECO:0000269|PubMed:29100093}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In FPS; no effect on protein abundance; no effect on localization to the mitochondrion; altered mitochondrial ATP transport; increased sensitivity to oxidative stress that leads to mitochondrial swelling.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  217
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  477
The length of the canonical sequence.

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.







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.

Chain 1 – 477 Calcium-binding mitochondrial carrier protein SCaMC-1
Topological domain 216 – 252 Mitochondrial matrix
Repeat 192 – 278 Solcar 1

Literature citations

De Novo Mutations in SLC25A24 Cause a Craniosynostosis Syndrome with Hypertrichosis, Progeroid Appearance, and Mitochondrial Dysfunction.
Ehmke N.; Graul-Neumann L.; Smorag L.; Koenig R.; Segebrecht L.; Magoulas P.; Scaglia F.; Kilic E.; Hennig A.F.; Adolphs N.; Saha N.; Fauler B.; Kalscheuer V.M.; Hennig F.; Altmueller J.; Netzer C.; Thiele H.; Nuernberg P.; Yigit G.; Jaeger M.; Hecht J.; Krueger U.; Mielke T.; Krawitz P.M.; Horn D.; Schuelke M.; Mundlos S.; Bacino C.A.; Bonnen P.E.; Wollnik B.; Fischer-Zirnsak B.; Kornak U.;
Am. J. Hum. Genet. 101:833-843(2017)

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.