Sequence information
Variant position: 139 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:
GSCKDQLQSYICFCLPAFEG
R NCETHKDDQLICVNENGGCE
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 GSCKDQLQSYICFCLPAFEGR NCETHKDDQLICVNENGGCE
Chimpanzee GSCKDQLQSYICFCLPAFEGR NCETYKDDQLICVNENGGCE
Mouse GTCQDHLKSYVCFCLLDFEGR NCEKSKNEQLICANENGDCD
Rat GTCQDHLKSYVCFCPLDFEGR NCEKNKNEQLICANENGDCD
Bovine GSCEDQLRSYICFCPDGFEGR NCETDKQSQLICANDNGGCE
Rabbit GSCEDQIQSYICFCLADFEGR NCEKNKNDQLICMYENGGCE
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
106 – 142
EGF-like 1; calcium-binding
Modified residue
123 – 123
(3R)-3-hydroxyaspartate
Glycosylation
120 – 120
O-linked (Fuc) serine
Disulfide bond
132 – 141
Literature citations
Detection of missense mutations by single-strand conformational polymorphism (SSCP) analysis in five dysfunctional variants of coagulation factor VII.
Takamiya O.; Kemball-Cook G.; Martin D.M.A.; Cooper D.N.; von Felten A.; Meili E.; Hahn I.; Prangnell D.R.; Lumley H.; Tuddenham E.G.D.; McVey J.H.;
Hum. Mol. Genet. 2:1355-1359(1993)
Cited for: VARIANTS FA7D GLN-139; TRP-139; ARG-160; GLU-197 AND GLN-364;
Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor.
Chaing S.; Clarke B.; Sridhara S.; Chu K.; Friedman P.; Vandusen W.; Roberts H.R.; Blajchman M.; Monroe D.M.; High K.A.;
Blood 83:3524-3535(1994)
Cited for: VARIANTS FA7D GLN-139 AND GLN-212;
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.