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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q969M3: Variant p.Ile98Ser

Protein YIPF5
Gene: YIPF5
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Variant information Variant position: help 98 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 Isoleucine (I) to Serine (S) at position 98 (I98S, p.Ile98Ser). 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 medium size and hydrophobic (I) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 MEDS2; no effect on differentiation and function of pancreatic beta cells; increased endoplasmic reticulum stress-induced apoptosis; decreased in C-peptide levels associated with increased proinsulin accumulation. Any additional useful information about the variant.


Sequence information Variant position: help 98 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 257 The length of the canonical sequence.
Location on the sequence: help PQPFYGNNFEDEPPLLEELG I NFDHIWQKTLTVLHPLKVAD 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                         PQPFYGNNFEDEPPLLEELGINFDHIWQKTLTVLHPLKVAD

Mouse                         PQPFYGDSFEEEPPLLEELGINFDHIWQKTLTVLHPLRAAD

Rat                           PQTFYGDSFEEEPPLLEELGINFDHIWQKTLTVLHPLRASD

Bovine                        PQPFYGNNFEDEPPLLEELGINFDHIWQKTLTVLHPLKVAD

Xenopus laevis                TESVYGSTFDDEPPLLEELGINFDHIWQKTLTVLHPLKVAD

Xenopus tropicalis            TDSVYGSTFDDEPPLLEELGINFDHIWQKTLTVLHPLKVAD

Zebrafish                     SQSMYSSSFEDEPPLLEELGINFDHIWQKTLTVLHPLKASD

Slime mold                    ------DSFDNELPLLEELGINFDHIRSKTLSVLNPLKKID
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 – 257 Protein YIPF5
Topological domain 1 – 124 Cytoplasmic
Region 75 – 106 Interaction with Sec23



Literature citations
YIPF5 mutations cause neonatal diabetes and microcephaly through endoplasmic reticulum stress.
De Franco E.; Lytrivi M.; Ibrahim H.; Montaser H.; Wakeling M.N.; Fantuzzi F.; Patel K.; Demarez C.; Cai Y.; Igoillo-Esteve M.; Cosentino C.; Lithovius V.; Vihinen H.; Jokitalo E.; Laver T.W.; Johnson M.B.; Sawatani T.; Shakeri H.; Pachera N.; Haliloglu B.; Ozbek M.N.; Unal E.; Yildirim R.; Godbole T.; Yildiz M.; Aydin B.; Bilheu A.; Suzuki I.; Flanagan S.E.; Vanderhaeghen P.; Senee V.; Julier C.; Marchetti P.; Eizirik D.L.; Ellard S.; Saarimaeki-Vire J.; Otonkoski T.; Cnop M.; Hattersley A.T.;
J. Clin. Invest. 130:6338-6353(2020)
Cited for: VARIANTS MEDS2 VAL-97; SER-98; LYS-106 DEL; VAL-181 AND ARG-218; CHARACTERIZATION OF VARIANT MEDS2 SER-98; TISSUE SPECIFICITY; DEVELOPMENTAL STAGE; FUNCTION;
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.