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:
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 EKGEKGDPGLIGPKGDIGET GVPGAEGPRGFPGIQGRKGEP
Mouse EKGEKGDAGLLGPKGETGDV GMTGAEGPRGFPGTPGRKGEP
Bovine EKGEKGDPGLVGPKGDTGET GITGIEGPRGFPGTPGRKGEP
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
19 – 244 Adiponectin
42 – 107 Collagen-like
40 – 101 Disordered
86 – 86 Not hydroxylated
104 – 104 Not hydroxylated
65 – 65 5-hydroxylysine
68 – 68 5-hydroxylysine
71 – 71 4-hydroxyproline; partial
76 – 76 4-hydroxyproline; partial
77 – 77 5-hydroxylysine
91 – 91 4-hydroxyproline
95 – 95 4-hydroxyproline; partial
101 – 101 5-hydroxylysine
65 – 65 O-linked (Gal...) hydroxylysine; partial
68 – 68 O-linked (Gal...) hydroxylysine; partial
77 – 77 O-linked (Gal...) hydroxylysine; partial
101 – 101 O-linked (Gal...) hydroxylysine; partial
65 – 65 K -> R. Impaired formation of HMW multimers; when associated with R-68.
68 – 68 K -> R. Impaired formation of HMW multimers; when associated with R-65.
77 – 77 K -> R. Impaired formation of HMW multimers; when associated with R-101.
101 – 101 K -> R. Impaired formation of HMW multimers; when associated with R-77.
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.;
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;
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