Sequence information
Variant position: 82 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:
NAFLEELRPGSLERECKEEQ
C SFEEAREIFKDAERTKLFWI
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 NAFLEELRPGSLERECKEEQC SFEEAREIFKDAERTKLFWI
Chimpanzee NAFLEELRPGSLERECKEEQC SFEEAREIFKDLERTKLFWI
Mouse NSLLEELWPGSLERECNEEQC SFEEAREIFKSPERTKQFWI
Rat NSLLEELWSSSLERECNEERC SFEEAREIFKSPERTKQFWT
Bovine NGFLEELLPGSLERECREELC SFEEAHEIFRNEERTRQFWV
Rabbit NSFLEELRPGSLERECKEELC SFEEAREVFQSTERTKQFWI
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
61 – 212
Factor VII light chain
Domain
61 – 105
Gla
Modified residue
66 – 66
4-carboxyglutamate
Modified residue
67 – 67
4-carboxyglutamate
Modified residue
74 – 74
4-carboxyglutamate
Modified residue
76 – 76
4-carboxyglutamate
Modified residue
79 – 79
4-carboxyglutamate
Modified residue
80 – 80
4-carboxyglutamate
Modified residue
85 – 85
4-carboxyglutamate
Modified residue
86 – 86
4-carboxyglutamate
Modified residue
89 – 89
4-carboxyglutamate
Modified residue
95 – 95
4-carboxyglutamate
Disulfide bond
77 – 82
Literature citations
Factor VII deficiency: clinical manifestation of 717 subjects from Europe and Latin America with mutations in the factor 7 gene.
Herrmann F.H.; Wulff K.; Auerswald G.; Schulman S.; Astermark J.; Batorova A.; Kreuz W.; Pollmann H.; Ruiz-Saez A.; De Bosch N.; Salazar-Sanchez L.;
Haemophilia 15:267-280(2009)
Cited for: VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88; PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157; ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194; THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254; TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298; GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307; MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343; SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363; GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387; SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413; MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND PHE-437;
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.