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UniProtKB/Swiss-Prot P17936: Variant p.Ala32Gly

Insulin-like growth factor-binding protein 3
Gene: IGFBP3
Variant information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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:  From Alanine (A) to Glycine (G) at position 32 (A32G, p.Ala32Gly).
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 small size and hydrophobic (A) to glycine (G)
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

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



Sequence information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  291
The length of the canonical sequence.

Location on the sequence:   ALTLLVLLRGPPVARAGASS  A GLGPVVRCEPCDARALAQCA
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.

Human                         ALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCA

Mouse                         ALTALTLLRGPPVARAGAGAVGAGPVVRCEPCDARALSQCA

Rat                           ALTALTLLRGPPVARAGAGAVGAGPVVRCEPCDARALAQCA

Pig                           ALIALALLRGPPAARAGSGAAGTGPVVRCEPCDARALAQCA

Bovine                        ALTALTLLRGPPAARAGAGTMGAGPVVRCEPCDARAVAQCA

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.

TypePositionsDescription
Chain 28 – 291 Insulin-like growth factor-binding protein 3
Region 28 – 134 IGF-binding


Literature citations

Cloning and expression of the growth hormone-dependent insulin-like growth factor-binding protein.
Wood W.I.; Cachianes G.; Henzel W.J.; Winslow G.A.; Spencer S.A.; Hellmiss R.; Martin J.L.; Baxter R.C.;
Mol. Endocrinol. 2:1176-1185(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLY-32;

Insulin-like growth factor binding protein-3. Organization of the human chromosomal gene and demonstration of promoter activity.
Cubbage M.L.; Suwanichkul A.; Powell D.R.;
J. Biol. Chem. 265:12642-12649(1990)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1); VARIANT GLY-32;

Analysis of the primary structure of insulin-like growth factor binding protein-3 cDNA from Werner syndrome fibroblasts.
Thweatt R.; Fleischmann R.; Goldstein S.;
DNA Seq. 4:43-46(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANT GLY-32;

Purification from human cerebrospinal fluid of insulin-like growth factor binding proteins (IGFBPs). Isolation of IGFBP-2, an altered form of IGFBP-3 and a new IGFBP species.
Roghani M.; Segovia B.; Whitechurch O.; Binoux M.;
Growth Regul. 1:125-130(1991)
Cited for: PROTEIN SEQUENCE OF 28-45; INTERACTION WITH IGF2; VARIANT GLY-32;

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.