Variant position: 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 466 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 SDGDQCASSPCQNGGSCKDQ LQSYICFCLPAFEGRNCETHK
Chimpanzee SDGDQCASSPCQNGGSCKDQ LQSYICFCLPAFEGRNCETYK
Mouse SDGDQCASNPCQNGGTCQDH LKSYVCFCLLDFEGRNCEKSK
Rat SDGDQCASNPCQNGGTCQDH LKSYVCFCPLDFEGRNCEKNK
Bovine NDGDQCASSPCQNGGSCEDQ LRSYICFCPDGFEGRNCETDK
Rabbit NDGDQCASNPCQNGGSCEDQ IQSYICFCLADFEGRNCEKNK
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
61 – 212 Factor VII light chain
106 – 142 EGF-like 1; calcium-binding
113 – 113 Important for S-112 for O-xylosylation
123 – 123 (3R)-3-hydroxyaspartate
112 – 112 O-linked (Glc...) serine; alternate
112 – 112 O-linked (Xyl...) serine; alternate
120 – 120 O-linked (Fuc) serine
115 – 130
112 – 112 S -> A. Complete loss of O-glycosylation and O-xylosylation by POGLUT1.
113 – 113 S -> A. No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation.
Molecular analysis of the genotype-phenotype relationship in factor VII deficiency.
Millar D.S.; Kemball-Cook G.; McVey J.H.; Tuddenham E.G.D.; Mumford A.D.; Attock G.B.; Reverter J.C.; Lanir N.; Parapia L.A.; Reynaud J.; Meili E.; von Felton A.; Martinowitz U.; Prangnell D.R.; Krawczak M.; Cooper D.N.;
Hum. Genet. 107:327-342(2000)
Cited for: VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435;
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.