Variant position: 891 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1487 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 APGPQGPTGVTGPKGARGAQ GPPGATGFPGAAGRVGPPGSN
Mouse APGPQGPTGVTGPKGARGAQ GPPGATGFPGAAGRVGPPGAN
Rat APGPQGPTGVTGPKGARGAQ GPPGATGFPGAAGRVGPPGSN
Bovine APGPQGPTGVTGPKGARGAQ GPPGATGFPGAAGRVGPPGSN
Xenopus laevis APGPQGPTGVFGPKGARGAQ GPAGATGFPGAAGRVGTPGPN
Xenopus tropicalis APGPQGPTGVNGPKGARGAQ GPPGATGFPGAAGRVGPPGPN
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
182 – 1241 Collagen alpha-1(II) chain
97 – 1237 Disordered
201 – 1214 Triple-helical region
907 – 907 3-hydroxyproline
908 – 908 4-hydroxyproline
1 – 1219 Missing. In isoform 3.
A radiographic, morphologic, biochemical and molecular analysis of a case of achondrogenesis type II resulting from substitution for a glycine residue (Gly691-->Arg) in the type II collagen trimer.
Mortier G.R.; Wilkin D.J.; Wilcox W.R.; Rimoin D.L.; Lachman R.S.; Eyre D.R.; Cohn D.H.;
Hum. Mol. Genet. 4:285-288(1995)
Cited for: VARIANT ACG2 ARG-891;
Three new point mutations in type II procollagen (COL2A1) and identification of a fourth family with the COL2A1 Arg519-->Cys base substitution using conformation sensitive gel electrophoresis.
Williams C.J.; Rock M.; Considine E.L.; McCarron S.; Gow P.; Ladda R.; McLain D.; Michels V.M.; Murphy W.; Prockop D.J.; Ganguly A.;
Hum. Mol. Genet. 4:309-312(1995)
Cited for: VARIANT CZECHD CYS-275; VARIANT SEDC SER-1176; VARIANT OSCDP CYS-719; VARIANT HYPOCHONDROGENESIS ARG-891; VARIANT ACG2 ARG-1188;
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.