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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P06213: Variant p.Ile925Thr

Insulin receptor
Gene: INSR
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Variant information Variant position: help 925 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 Threonine (T) at position 925 (I925T, p.Ile925Thr). 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 medium size and polar (T) 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 LEPRCH; abolishes post-translational processing; abolishes insulin binding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 925 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1382 The length of the canonical sequence.
Location on the sequence: help FALERGCRLRGLSPGNYSVR I RATSLAGNGSWTEPTYFYVT 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                         FALERGCRLRGLSPGNYSVRIRATSLAGNGSWTEPTYFYVT

Mouse                         FALERGCRLRGLSPGNYSVRVRATSLAGNGSWTEPTYFYVT

Rat                           FALERGCRLRGLSPGNYSVRVRATSLAGNGSWTEPTYFYVT

Xenopus laevis                YNTDKGGKLRVLTPGNYSVKIRATSLAGNGSWTEQAYFQVP

Caenorhabditis elegans        STRNQGVLFQNLADGRYFVSVTATSVHGAGPEAESSDPIVV

Drosophila                    FNQTAGYLIK-LNEGLYSFRVRANSIAGYGDFTEVEHIKVE
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 763 – 1382 Insulin receptor subunit beta
Topological domain 763 – 956 Extracellular
Domain 853 – 947 Fibronectin type-III 3
Glycosylation 920 – 920 N-linked (GlcNAc...) asparagine
Glycosylation 933 – 933 N-linked (GlcNAc...) asparagine
Beta strand 918 – 931



Literature citations
Genotype-phenotype correlation in inherited severe insulin resistance.
Longo N.; Wang Y.; Smith S.A.; Langley S.D.; DiMeglio L.A.; Giannella-Neto D.;
Hum. Mol. Genet. 11:1465-1475(2002)
Cited for: CHARACTERIZATION OF VARIANTS LEPRCH PRO-113; VAL-119; ASN-308 DEL; THR-925 AND TRP-926; VARIANTS RMS THR-997; THR-1143; TRP-1158 AND TRP-1201; Structural Basis and Genotype-Phenotype Correlations of INSR Mutations Causing Severe Insulin Resistance.
Hosoe J.; Kadowaki H.; Miya F.; Aizu K.; Kawamura T.; Miyata I.; Satomura K.; Ito T.; Hara K.; Tanaka M.; Ishiura H.; Tsuji S.; Suzuki K.; Takakura M.; Boroevich K.A.; Tsunoda T.; Yamauchi T.; Shojima N.; Kadowaki T.;
Diabetes 66:2713-2723(2017)
Cited for: VARIANTS RMS CYS-256; LEU-635; ILE-835; VAL-842; LEU-874; SER-878 AND 999-TYR--SER-1382 DEL; VARIANTS IRAN TYPE A ASP-489 AND MET-1054; VARIANTS LEPRCH PHE-657; ARG-659 AND CYS-818; CHARACTERIZATION OF VARIANTS LEPRCH PHE-657; ARG-659; CYS-818; THR-925; TRP-926 AND MET-937; CHARACTERIZATION OF VARIANTS RMS LEU-635; ILE-835; VAL-842; LEU-874 AND SER-878;
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.