Sequence information
Variant position: 37 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 461 The length of the canonical sequence.
Location on the sequence:
ICLLGYLLSAECTVFLDHEN
A NKILNRPKRYNSGKLEEFVQ
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 ICLLGYLLSAECTVFLDHENA NKILNRPKRYNSGKLEEFVQ
VCLLGYLLSAECAVFLDRENA TKILSRPKRYNSGKLEEFVR
Chimpanzee ICLLGYLLSAECTVFLDHENA NKILNRPKRYNSGKLEEFVQ
Mouse IFLLGYLLSTECAVFLDRENA TKILTRPKRYNSGKLEEFVR
Rat IFLLGYLLSTECAVFLDRENA TKILTRPKRYNSGKLEEFVQ
Bovine ICLLGYLLSAECTVFLDRENA TKILHRPKRYNSGKLEEFVR
Cat ICLLGYLLGADCTVFLDHEDA TKVLSRPKRYNSGKLEEFVQ
Chicken FCLLEAFLGAESTVFIENKEA STVLSRTRRGNSNRLEELIP
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
Propeptide
29 – 46
Metal binding
47 – 47
Calcium 1; via carbonyl oxygen
Metal binding
48 – 48
Calcium 2
Metal binding
53 – 53
Calcium 1; via 4-carboxyglutamate
Metal binding
53 – 53
Calcium 2; via 4-carboxyglutamate
Metal binding
54 – 54
Calcium 2; via 4-carboxyglutamate
Metal binding
54 – 54
Calcium 3; via 4-carboxyglutamate
Modified residue
53 – 53
4-carboxyglutamate
Modified residue
54 – 54
4-carboxyglutamate
Literature citations
Missense mutations at ALA-10 in the factor IX propeptide: an insignificant variant in normal life but a decisive cause of bleeding during oral anticoagulant therapy.
Oldenburg J.; Quenzel E.M.; Harbrecht U.; Fregin A.; Kress W.; Mueller C.R.; Hertfelder H.J.; Schwaab R.; Brackmann H.H.; Hanfland P.;
Br. J. Haematol. 98:240-244(1997)
Cited for: VARIANTS WARFS THR-37 AND VAL-37;
Variants in FIX propeptide associated with vitamin K antagonist hypersensitivity: functional analysis and additional data confirming the common founder mutations.
Pezeshkpoor B.; Czogalla K.J.; Caspers M.; Berkemeier A.C.; Liphardt K.; Ghosh S.; Kellner M.; Ulrich S.; Pavlova A.; Oldenburg J.;
Ann. Hematol. 97:1061-1069(2018)
Cited for: VARIANTS WARFS THR-37 AND VAL-37; CHARACTERIZATION OF VARIANTS WARFS THR-37 AND VAL-37;
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.