Sequence information
Variant position: 226 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:
EAETILDNITQSTQSFNDFT
R VVGGEDAKPGQFPWQVVLNG
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 EAETILDNITQSTQS-------------FNDFTR VVGGEDAKPGQFPWQV-VLNG
EVEKILDNVTQP----------------LNDFTR VVGGKDA
Chimpanzee EAETILDNITQSTQS-------------FNDFTR VVGGEDA
Mouse TDGAILNNVTESSES-------------LNDFTR VVGGENA
Rat TNSTILDNLTENSEP-------------INDFTR VVGGENA
Bovine EAEIIWDNVTQSNQS-------------FDEFSR VVGGEDA
Cat EAEKNVDNVTQP----------------LNDLTR IVGGKTA
Chicken HDEAL--DITEPPPPPTTSAAPAKIVPITKNDTR VVGGYDS
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
Propeptide
192 – 226
Activation peptide
Site
226 – 227
Cleavage; by factor XIa
Glycosylation
213 – 213
N-linked (GlcNAc...) asparagine
Glycosylation
215 – 215
O-linked (GalNAc...) threonine
Glycosylation
225 – 225
O-linked (GalNAc...) threonine
Disulfide bond
178 – 335
Interchain (between light and heavy chains)
Literature citations
Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo.
Monroe D.M.; McCord D.M.; Huang M.N.; High K.A.; Lundblad R.L.; Kasper C.K.; Roberts H.R.;
Blood 73:1540-1544(1989)
Cited for: VARIANT HEMB GLN-226;
Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX.
Bertina R.M.; van der Linden I.K.; Mannucci P.M.; Reinalda-Poot H.H.; Cupers R.; Poort S.R.; Reitsma P.H.;
J. Biol. Chem. 265:10876-10883(1990)
Cited for: VARIANTS HEMB GLN-226; TRP-226; PHE-227 AND THR-414;
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;
Comprehensive analysis of phenotypes and genetics in 21 Chinese families with haemophilia B: characterization of five novel mutations.
Guo Z.P.; Yang L.H.; Qin X.Y.; Liu X.E.; Chen J.F.; Zhang Y.F.;
Haemophilia 20:859-865(2014)
Cited for: VARIANTS HEMB SER-20; TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138; GLN-226; ILE-284 DEL; MET-296; LYS-328; TYR-328; THR-414 AND TYR-THR-LYS-VAL-447 INS; CHARACTERIZATION OF VARIANTS HEMB SER-20; TYR-28; SER-46; ASP-54; GLU-58; ARG-84; HIS-138; GLN-226; ILE-284 DEL; MET-296; LYS-328; TYR-328; THR-414 AND TYR-THR-LYS-VAL-447 INS;
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.