Variant position: 102 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1663 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 HMGNVTFTIPANREFKSEKG RNKFVTVQATFGTQVVEKVVL
Mouse HLRSVSIKIPASKEFNSDKE GHKYVTVVANFGETVVEKAVM
Rat HLNRVFIKIPASKEFNADK- GHKYVTVVANFGATVVEKAVL
Pig YLSTVNIKIPASKEFKSEK- GHKFVTVQALFGNVQVEKVVL
Bovine YLSTVTIKIPASKELKSDK- GHKFVTVVATFGNVQVEKVVL
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
23 – 1663 Complement C3
23 – 667 Complement C3 beta chain
85 – 85 N-linked (GlcNAc...) asparagine
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS GLY-102; LEU-314; LYS-863; ASP-1224 AND THR-1367;
Molecular basis of polymorphisms of human complement component C3.
Botto M.; Yong Fong K.; So A.K.; Koch C.; Walport M.J.;
J. Exp. Med. 172:1011-1017(1990)
Cited for: VARIANTS GLY-102 AND LEU-314;
Complement C3 variant and the risk of age-related macular degeneration.
Yates J.R.W.; Sepp T.; Matharu B.K.; Khan J.C.; Thurlby D.A.; Shahid H.; Clayton D.G.; Hayward C.; Morgan J.; Wright A.F.; Armbrecht A.M.; Dhillon B.; Deary I.J.; Redmond E.; Bird A.C.; Moore A.T.;
N. Engl. J. Med. 357:553-561(2007)
Cited for: ASSOCIATION OF VARIANT GLY-102 WITH ARMD9;
Common polymorphisms in C3, factor B, and factor H collaborate to determine systemic complement activity and disease risk.
Heurich M.; Martinez-Barricarte R.; Francis N.J.; Roberts D.L.; Rodriguez de Cordoba S.; Morgan B.P.; Harris C.L.;
Proc. Natl. Acad. Sci. U.S.A. 108:8761-8766(2011)
Cited for: CHARACTERIZATION OF VARIANT GLY-102;
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