Variant position: 106 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 EFWKQYVDGDQCESNPCLNG GSCKDDINSYECWCPFGFEGK
Chimpanzee EFWKQYVDGDQCESNPCLNG GSCKDDINSYECWCPFGFEGK
Mouse EFWKQYVDGDQCESNPCLNG GICKDDISSYECWCQVGFEGR
Rat EFWKQYVDGDQCESNPCLNG GICKDDINSYECWCQAGFEGR
Bovine EFWKQYVDGDQCESNPCLNG GMCKDDINSYECWCQAGFEGT
Cat EFWKQYVDGDQCESNPCLNG GICKDDINSYECWCQTGFEGK
Chicken EFWKIYIDGDQCNSNPCKNG AVCKDGVSSYECMCPPGYGGR
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
47 – 461 Coagulation factor IX
47 – 191 Coagulation factor IXa light chain
93 – 129 EGF-like 1; calcium-binding
86 – 86 Calcium 6; via 4-carboxyglutamate
86 – 86 Magnesium 3; via 4-carboxyglutamate
93 – 93 Calcium 7
94 – 94 Calcium 7; via carbonyl oxygen
96 – 96 Calcium 7
110 – 110 Calcium 7
111 – 111 Calcium 7; via carbonyl oxygen
86 – 86 4-carboxyglutamate
110 – 110 (3R)-3-hydroxyaspartate
114 – 114 Phosphoserine
99 – 99 O-linked (Glc...) serine
107 – 107 O-linked (Fuc...) serine
97 – 108
102 – 117
93 – 130 Missing. In isoform 2.
Molecular pathology of haemophilia B in Turkish patients: identification of a large deletion and 33 independent point mutations.
Onay U.V.; Kavakli K.; Kilinc Y.; Gurgey A.; Aktuglu G.; Kemahli S.; Ozbek U.; Caglayan S.H.;
Br. J. Haematol. 120:656-659(2003)
Cited for: VARIANTS HEMB TYR-28; LEU-43; GLN-43; SER-52; ASP-106; LYS-124; TYR-134; GLN-226; GLY-226; TRP-226; LYS-241; TYR-252; GLN-294; PHE-316; ARG-318; GLY-379; ILE-383; PHE-383; ILE-395; PHE-396; ARG-407 AND GLU-412;
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.