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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96AY3: Variant p.Arg115Gln

Peptidyl-prolyl cis-trans isomerase FKBP10
Gene: FKBP10
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Variant information Variant position: help 115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Glutamine (Q) at position 115 (R115Q, p.Arg115Gln). 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: help Change from large size and basic (R) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In BRKS1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 115 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 582 The length of the canonical sequence.
Location on the sequence: help VGRLITGMDRGLMGMCVNER R RLIVPPHLGYGSIGLAGLIP 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         VGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGLAGLIP

Mouse                         VGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGVAGLIP

Bovine                        VGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGVAGLIP
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 27 – 582 Peptidyl-prolyl cis-trans isomerase FKBP10
Domain 62 – 150 PPIase FKBP-type 1
Alternative sequence 2 – 177 Missing. In isoform 2.



Literature citations
Mutations in FKBP10 cause recessive osteogenesis imperfecta and Bruck syndrome.
Kelley B.P.; Malfait F.; Bonafe L.; Baldridge D.; Homan E.; Symoens S.; Willaert A.; Elcioglu N.; Van Maldergem L.; Verellen-Dumoulin C.; Gillerot Y.; Napierala D.; Krakow D.; Beighton P.; Superti-Furga A.; De Paepe A.; Lee B.;
J. Bone Miner. Res. 26:666-672(2011)
Cited for: VARIANT BRKS1 GLN-115; INVOLVEMENT IN OI11; Mutations in FKBP10, which result in Bruck syndrome and recessive forms of osteogenesis imperfecta, inhibit the hydroxylation of telopeptide lysines in bone collagen.
Schwarze U.; Cundy T.; Pyott S.M.; Christiansen H.E.; Hegde M.R.; Bank R.A.; Pals G.; Ankala A.; Conneely K.; Seaver L.; Yandow S.M.; Raney E.; Babovic-Vuksanovic D.; Stoler J.; Ben-Neriah Z.; Segel R.; Lieberman S.; Siderius L.; Al-Aqeel A.; Hannibal M.; Hudgins L.; McPherson E.; Clemens M.; Sussman M.D.; Steiner R.D.; Mahan J.; Smith R.; Anyane-Yeboa K.; Wynn J.; Chong K.; Uster T.; Aftimos S.; Sutton V.R.; Davis E.C.; Kim L.S.; Weis M.A.; Eyre D.; Byers P.H.;
Hum. Mol. Genet. 22:1-17(2013)
Cited for: VARIANTS BRKS1 LYS-113; GLN-115 AND LEU-136; INVOLVEMENT IN OI11;
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.