Sequence information
Variant position: 125 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:
GGSCKDDINSYECWCPFGFE
G KNCELDVTCNIKNGRCEQFC
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 GGSCKDDINSYECWCPFGFEG KNCELDVTCNIKNGRCEQFC
DGVCKDDINSYECWCRAGFEG KNCELDVTCNIKNGRCKQFC
Chimpanzee GGSCKDDINSYECWCPFGFEG KNCELDVTCNIKNGRCEQFC
Mouse GGICKDDISSYECWCQVGFEG RNCELDATCNIKNGRCKQFC
Rat GGICKDDINSYECWCQAGFEG RNCELDATCSIKNGRCKQFC
Bovine GGMCKDDINSYECWCQAGFEG TNCELDATCSIKNGRCKQFC
Cat GGICKDDINSYECWCQTGFEG KNCELDVTCNIKNGRCKQFC
Chicken GAVCKDGVSSYECMCPPGYGG RNCEIDSTCATKNGGCEHFC
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
93 – 129
EGF-like 1; calcium-binding
Metal binding
110 – 110
Calcium 7
Metal binding
111 – 111
Calcium 7; via carbonyl oxygen
Modified residue
110 – 110
(3R)-3-hydroxyaspartate
Modified residue
114 – 114
Phosphoserine
Glycosylation
107 – 107
O-linked (Fuc...) serine
Disulfide bond
119 – 128
Alternative sequence
93 – 130
Missing. In isoform 2.
Turn
125 – 128
Literature citations
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.;
Haematologica 88:235-236(2003)
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;
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.