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UniProtKB/Swiss-Prot Q15848: Variant p.Gly84Arg

Variant information

Variant position:  84
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 Glycine (G) to Arginine (R) at position 84 (G84R, p.Gly84Arg).
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 glycine (G) to large size and basic (R)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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

Polymorphism:  Genetic variations in ADIPOQ influence the variance in adiponectin serum levels and define the adiponectin serum levels quantitative trait locus 1 (ADIPQTL1) [MIM:612556].
Additional information on the polymorphism described.

Variant description:  Does not form high molecular weight multimers.
Any additional useful information about the variant.

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

Sequence information

Variant position:  84
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  244
The length of the canonical sequence.

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.




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.

Chain 19 – 244 Adiponectin
Domain 42 – 107 Collagen-like
Region 40 – 101 Disordered
Site 86 – 86 Not hydroxylated
Site 104 – 104 Not hydroxylated
Modified residue 65 – 65 5-hydroxylysine
Modified residue 68 – 68 5-hydroxylysine
Modified residue 71 – 71 4-hydroxyproline; partial
Modified residue 76 – 76 4-hydroxyproline; partial
Modified residue 77 – 77 5-hydroxylysine
Modified residue 91 – 91 4-hydroxyproline
Modified residue 95 – 95 4-hydroxyproline; partial
Modified residue 101 – 101 5-hydroxylysine
Glycosylation 65 – 65 O-linked (Gal...) hydroxylysine; partial
Glycosylation 68 – 68 O-linked (Gal...) hydroxylysine; partial
Glycosylation 77 – 77 O-linked (Gal...) hydroxylysine; partial
Glycosylation 101 – 101 O-linked (Gal...) hydroxylysine; partial
Mutagenesis 65 – 65 K -> R. Impaired formation of HMW multimers; when associated with R-68.
Mutagenesis 68 – 68 K -> R. Impaired formation of HMW multimers; when associated with R-65.
Mutagenesis 77 – 77 K -> R. Impaired formation of HMW multimers; when associated with R-101.
Mutagenesis 101 – 101 K -> R. Impaired formation of HMW multimers; when associated with R-77.

Literature citations

Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin.
Waki H.; Yamauchi T.; Kamon J.; Ito Y.; Uchida S.; Kita S.; Hara K.; Hada Y.; Vasseur F.; Froguel P.; Kimura S.; Nagai R.; Kadowaki T.;
J. Biol. Chem. 278:40352-40363(2003)

Genetic variation in the gene encoding adiponectin is associated with an increased risk of type 2 diabetes in the Japanese population.
Hara K.; Boutin P.; Mori Y.; Tobe K.; Dina C.; Yasuda K.; Yamauchi T.; Otabe S.; Okada T.; Eto K.; Kadowaki H.; Hagura R.; Akanuma Y.; Yazaki Y.; Nagai R.; Taniyama M.; Matsubara K.; Yoda M.; Nakano Y.; Kimura S.; Tomita M.; Kimura S.; Ito C.; Froguel P.; Kadowaki T.;
Diabetes 51:536-540(2002)
Cited for: VARIANTS ARG-84; MET-117; THR-164; SER-221 AND PRO-241;

Single-nucleotide polymorphism haplotypes in the both proximal promoter and exon 3 of the APM1 gene modulate adipocyte-secreted adiponectin hormone levels and contribute to the genetic risk for type 2 diabetes in French Caucasians.
Vasseur F.; Helbecque N.; Dina C.; Lobbens S.; Delannoy V.; Gaget S.; Boutin P.; Vaxillaire M.; Lepretre F.; Dupont S.; Hara K.; Clement K.; Bihain B.; Kadowaki T.; Froguel P.;
Hum. Mol. Genet. 11:2607-2614(2002)
Cited for: VARIANTS ARG-84; SER-90 AND HIS-111;

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.