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.
Location on the sequence:
EKGEKGDPGLIGPKGDIGET
G VPGAEGPRGFPGIQGRKGEP
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 EKGEKGDPGLIGPKGDIGETG VPGAEGPRGFPGIQGRKGEP
Mouse EKGEKGDAGLLGPKGETGDVG MTGAEGPRGFPGTPGRKGEP
Bovine EKGEKGDPGLVGPKGDTGETG ITGIEGPRGFPGTPGRKGEP
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.
Type Positions Description
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)
Cited for: SUBUNIT; DISULFIDE BOND; MUTAGENESIS OF CYS-36; CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164;
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.