Sequence information
Variant position: 79 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:
NLERECMEEKCSFEEAREVF
E NTERTTEFWKQYVDGDQCES
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 NLERECMEEKCSFEEAREVFE NTERTTEFWKQYVDGDQCES
NLERECIEEKCSFEEAREVFE NTEKTTEFWKQYVDGDQCES
Chimpanzee NLERECMEEKCSFEEAREVFE NTERTTEFWKQYVDGDQCES
Mouse NLERECIEERCSFEEAREVFE NTEKTTEFWKQYVDGDQCES
Rat NLERECIEERCSFEEAREVFE NTEKTTEFWKQYVDGDQCES
Bovine NLERECKEEKCSFEEAREVFE NTEKTTEFWKQYVDGDQCES
Cat NLERECMEEKCSFEEAREVFE NTEKTTEFWKQYVDGDQCES
Chicken NLERECIEEKCSFEEAREVFE NTEKTMEFWKIYIDGDQCNS
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
47 – 461
Coagulation factor IX
Chain
47 – 191
Coagulation factor IXa light chain
Domain
47 – 92
Gla
Metal binding
61 – 61
Calcium 4; via 4-carboxyglutamate
Metal binding
61 – 61
Magnesium 1; via 4-carboxyglutamate
Metal binding
63 – 63
Calcium 1; via 4-carboxyglutamate
Metal binding
63 – 63
Calcium 2; via 4-carboxyglutamate
Metal binding
63 – 63
Calcium 3; via 4-carboxyglutamate
Metal binding
66 – 66
Calcium 4; via 4-carboxyglutamate
Metal binding
66 – 66
Magnesium 1; via 4-carboxyglutamate
Metal binding
67 – 67
Calcium 1; via 4-carboxyglutamate
Metal binding
72 – 72
Calcium 5; via 4-carboxyglutamate
Metal binding
72 – 72
Magnesium 2; via 4-carboxyglutamate
Metal binding
73 – 73
Calcium 2; via 4-carboxyglutamate
Metal binding
73 – 73
Calcium 3; via 4-carboxyglutamate
Metal binding
76 – 76
Calcium 3; via 4-carboxyglutamate
Metal binding
76 – 76
Calcium 5; via 4-carboxyglutamate
Metal binding
76 – 76
Magnesium 2; via 4-carboxyglutamate
Metal binding
82 – 82
Calcium 6; via 4-carboxyglutamate
Metal binding
82 – 82
Magnesium 3; via 4-carboxyglutamate
Metal binding
86 – 86
Calcium 6; via 4-carboxyglutamate
Metal binding
86 – 86
Magnesium 3; via 4-carboxyglutamate
Metal binding
93 – 93
Calcium 7
Metal binding
94 – 94
Calcium 7; via carbonyl oxygen
Metal binding
96 – 96
Calcium 7
Modified residue
61 – 61
4-carboxyglutamate
Modified residue
63 – 63
4-carboxyglutamate
Modified residue
66 – 66
4-carboxyglutamate
Modified residue
67 – 67
4-carboxyglutamate
Modified residue
72 – 72
4-carboxyglutamate
Modified residue
73 – 73
4-carboxyglutamate
Modified residue
76 – 76
4-carboxyglutamate
Modified residue
79 – 79
4-carboxyglutamate
Modified residue
82 – 82
4-carboxyglutamate
Modified residue
86 – 86
4-carboxyglutamate
Glycosylation
85 – 85
O-linked (GalNAc...) threonine
Glycosylation
99 – 99
O-linked (Glc...) serine
Beta strand
78 – 80
Literature citations
Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG.
Koeberl D.D.; Bottema C.D.; Buerstedde J.-M.; Sommer S.S.;
Am. J. Hum. Genet. 45:448-457(1989)
Cited for: VARIANTS HEMB GLN-75; ASP-79; TRP-268; THR-279; SER-306; MET-342; ARG-357 AND ARG-453; VARIANT PHE-7;
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.