Variant position: 294 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 KITVVAGEHNIEETEHTEQK RNVIRIIPHHNYNAAINKYNH
Chimpanzee KITVVAGEHNIEETEHTEQK RNVIRIIPHHNYNAAINKYNH
Mouse KIEVVAGEYNIDKKEDTEQR RNVIRTIPHHQYNATINKYSH
Rat KIEVVAGEHNIDEKEDTEQR RNVIRTIPHHQYNATINKYSH
Bovine KITVVAGEHNTEKPEPTEQK RNVIRAIPYHSYNASINKYSH
Cat EITVVAGEHNTEETEHTEQK RNVIRTILHHSYNASVNKYSH
Chicken NVTAVAGEYNTKEDDHTEQR RQVVKILPYPTYNRTRNKHHN
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
227 – 461 Coagulation factor IXa heavy chain
227 – 459 Peptidase S1
281 – 281 Calcium 8
283 – 283 Calcium 8; via carbonyl oxygen
286 – 286 Calcium 8; via carbonyl oxygen
288 – 288 Calcium 8
291 – 291 Calcium 8
178 – 335 Interchain (between light and heavy chains)
305 – 305 Y -> F. Strongly increases enzyme activity with a synthetic peptide substrate; when associated with T-311; A-365 and T-391.
311 – 311 K -> T. Strongly increases enzyme activity with a synthetic peptide substrate; when associated with F-305; A-365 and T-391.
312 – 312 Y -> A. Strongly decreases enzyme activity with a synthetic peptide substrate.
292 – 301
Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins.
Chen S.H.; Thompson A.R.; Zhang M.; Scott C.R.;
J. Clin. Invest. 84:113-118(1989)
Cited for: VARIANTS HEMB LYS-73; SER-106 AND GLN-294;
Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX.
Ludwig M.; Sabharwal A.K.; Brackmann H.H.; Olek K.; Smith K.J.; Birktoft J.J.; Bajaj S.P.;
Cited for: VARIANTS HEMB VAL-291; GLN-294; HIS-410; GLY-411 AND ILE-411;
Single-strand conformation polymorphism (SSCP) analysis of the molecular pathology of hemophilia B.
David D.; Rosa H.A.V.; Pemberton S.; Diniz M.J.; Campos M.; Lavinha J.;
Hum. Mutat. 2:355-361(1993)
Cited for: VARIANTS HEMB ARG-253; GLN-294; GLN-379; PRO-426 AND ILE-TYR-THR-445 INS;
Identification of mutations in four hemophilia B patients of Turkish origin, including a novel deletion of base 6411.
Caglayan S.H.; Vielhaber E.; Guersel T.; Aktuglu G.; Sommer S.S.;
Hum. Mutat. 4:163-165(1994)
Cited for: VARIANTS HEMB GLN-294 AND ARG-413;
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.