Variant position: 43 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:
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 LLSAECTVFLDHENANKILN RPKRYNSGKLEEFVQGNLERE
Chimpanzee LLSAECTVFLDHENANKILN RPKRYNSGKLEEFVQGNLERE
Mouse LLSTECAVFLDRENATKILT RPKRYNSGKLEEFVRGNLERE
Rat LLSTECAVFLDRENATKILT RPKRYNSGKLEEFVQGNLERE
Bovine LLSAECTVFLDRENATKILH RPKRYNSGKLEEFVRGNLERE
Cat LLGADCTVFLDHEDATKVLS RPKRYNSGKLEEFVQGNLERE
Chicken FLGAESTVFIENKEASTVLS RTRRGNSNRLEELIPGNLERE
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
29 – 46
47 – 47 Calcium 1; via carbonyl oxygen
48 – 48 Calcium 2
53 – 53 Calcium 1; via 4-carboxyglutamate
53 – 53 Calcium 2; via 4-carboxyglutamate
54 – 54 Calcium 2; via 4-carboxyglutamate
54 – 54 Calcium 3; via 4-carboxyglutamate
61 – 61 Calcium 4; via 4-carboxyglutamate
61 – 61 Magnesium 1; via 4-carboxyglutamate
63 – 63 Calcium 1; via 4-carboxyglutamate
63 – 63 Calcium 2; via 4-carboxyglutamate
63 – 63 Calcium 3; via 4-carboxyglutamate
53 – 53 4-carboxyglutamate
54 – 54 4-carboxyglutamate
61 – 61 4-carboxyglutamate
63 – 63 4-carboxyglutamate
Modification of the N-terminus of human factor IX by defective propeptide cleavage or acetylation results in a destabilized calcium-induced conformation: effects on phospholipid binding and activation by factor XIa.
Wojcik E.G.; Van Den Berg M.; Poort S.R.; Bertina R.M.;
Biochem. J. 323:629-636(1997)
Cited for: PROTEIN SEQUENCE OF 47-52; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS HEMB GLN-43; LEU-43 AND TRP-43; CALCIUM-BINDING; PROTEOLYTIC CLEAVAGE;
Germline mutations in Peruvian patients with hemophilia B: pattern of mutation in Amerindians is similar to the putative endogenous germline pattern.
Heit J.A.; Thorland E.C.; Ketterling R.P.; Lind T.J.; Daniels T.M.; Zapata R.E.; Ordonez S.M.; Kasper C.K.; Sommer S.S.;
Hum. Mutat. 11:372-376(1998)
Cited for: VARIANTS HEMB GLN-43; TRP-43; THR-46; SER-106; CYS-115; PHE-155; GLN-379; GLU-387; VAL-432 AND CYS-450;
Molecular analyses in hemophilia B families: identification of six new mutations in the factor IX gene.
Espinos C.; Casana P.; Haya S.; Cid A.R.; Aznar J.A.;
Cited for: VARIANTS HEMB TRP-43; ARG-84; ARG-125; VAL-125; PHE-170; ARG-302; MET-342; LEU-344; LEU-395; THR-414; TYR-435; GLU-442 AND TRP-449;
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.