Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y3C6: Variant p.Ala99Thr

Peptidyl-prolyl cis-trans isomerase-like 1
Gene: PPIL1
Feedback?
Variant information Variant position: help 99 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 Alanine (A) to Threonine (T) at position 99 (A99T, p.Ala99Thr). 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 small size and hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In PCH14; strongly reduced interaction with SNW1; strongly reduced protein levels in homozygous patient's fibroblasts compared to heterozygous or wild-type cells; in transgenic knockin mice, produces a pontocerebellar hypoplasia-like phenotype. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 99 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 166 The length of the canonical sequence.
Location on the sequence: help GKQFEDELHPDLKFTGAGIL A MANAGPDTNGSQFFVTLAPT 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                         GKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPT

Mouse                         GKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPT

Bovine                        GKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPT

Fission yeast                 GDKFDDEIHSDLHHTGAGILSMANAGPNTNSSQFFITLAPT
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 1 – 166 Peptidyl-prolyl cis-trans isomerase-like 1
Domain 10 – 164 PPIase cyclophilin-type
Binding site 99 – 104
Binding site 119 – 119
Beta strand 97 – 100



Literature citations
Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative Pontocerebellar Hypoplasia with Microcephaly.
Chai G.; Webb A.; Li C.; Antaki D.; Lee S.; Breuss M.W.; Lang N.; Stanley V.; Anzenberg P.; Yang X.; Marshall T.; Gaffney P.; Wierenga K.J.; Chung B.H.; Tsang M.H.; Pais L.S.; Lovgren A.K.; VanNoy G.E.; Rehm H.L.; Mirzaa G.; Leon E.; Diaz J.; Neumann A.; Kalverda A.P.; Manfield I.W.; Parry D.A.; Logan C.V.; Johnson C.A.; Bonthron D.T.; Valleley E.M.A.; Issa M.Y.; Abdel-Ghafar S.F.; Abdel-Hamid M.S.; Jennings P.; Zaki M.S.; Sheridan E.; Gleeson J.G.;
Neuron 109:241-256(2021)
Cited for: INVOLVEMENT IN PCH14; VARIANTS PCH14 45-ARG--GLY-166 DEL; CYS-78; SER-82; THR-99; ALA-ASN-ALA-GLY-PRO-ASP-106 INS; ALA-107; CYS-109; ALA-127 AND GLN-131; CHARACTERIZATION OF VARIANT PCH14 CYS-78; SER-82; THR-99; ALA-ASN-ALA-GLY-PRO-ASP-106 INS; ALA-107; ALA-127 AND GLN-131; FUNCTION; INTERACTION WITH CDC40; RBM22 AND SNW1; MUTAGENESIS OF ARG-55; CATALYTIC ACTIVITY;
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.