Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00451: Variant p.Arg1800His

Coagulation factor VIII
Gene: F8
Feedback?
Variant information Variant position: help 1800 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change: help From Arginine (R) to Histidine (H) at position 1800 (R1800H, p.Arg1800His). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description: help In HEMA; moderate/severe. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 1800 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 2351 The length of the canonical sequence.
Location on the sequence: help PYIRAEVEDNIMVTFRNQAS R PYSFYSSLISYEEDQRQGAE 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human                         PYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGAE

                              PYIRAEVEDNIVVTFKNQASRPYSFYSSLISYDEDEGQGAE

Mouse                         PYIRAEVEDNIMVTFKNQASRPYSFYSSLISYKEDQR-GEE

Pig                           PYIRAEVEDNIMVTFKNQASRPYSFYSSLISYPDDQEQGAE

Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 20 – 2351 Coagulation factor VIII
Chain 1668 – 2351 Factor VIIIa light chain
Domain 1713 – 2040 F5/8 type A 3
Domain 1713 – 1877 Plastocyanin-like 5
Alternative sequence 9 – 2143 Missing. In isoform 2.
Beta strand 1798 – 1800



Literature citations
Molecular characterization of severe hemophilia A suggests that about half the mutations are not within the coding regions and splice junctions of the factor VIII gene.
Higuchi M.; Kazazian H.H. Jr.; Kasch L.; Warren T.C.; McGinniss M.J.; Phillips J.A. III; Kasper C.; Janco R.; Antonarakis S.E.;
Proc. Natl. Acad. Sci. U.S.A. 88:7405-7409(1991)
Cited for: VARIANTS HEMA THR-108; VAL-110; GLY-285; HIS-301; SER-312; ARG-444; HIS-492; GLY-561; CYS-612; THR-723; PHE-1699; HIS-1800; TYR-1803; ASP-1941; SER-1941; HIS-2169; GLN-2228 AND CYS-2323; Mutational analysis of ectopic factor VIII transcripts from hemophilia A patients: identification of cryptic splice site, exon skipping and novel point mutations.
Tavassoli K.; Eigel A.; Pollmann H.; Horst J.;
Hum. Genet. 100:508-511(1997)
Cited for: VARIANTS HEMA GLY-33; CYS-639; HIS-1800; LEU-1908 AND ARG-2106; A domain mutations in 65 haemophilia A families and molecular modelling of dysfunctional factor VIII proteins.
Liu M.; Murphy M.E.P.; Thompson A.R.;
Br. J. Haematol. 103:1051-1060(1998)
Cited for: VARIANTS HEMA LYS-98; GLY-101; CYS-133; HIS-145; ALA-159; LYS-163; ASP-164; PRO-179; MET-181; LYS-291; ALA-297; GLU-303; SER-312; HIS-391; ILE-427; TRP-437; ASN-450; ILE-454; LEU-470; SER-541; TRP-546; CYS-550; HIS-550; PRO-553; THR-560; ALA-578; ARG-603; ILE-633; ASN-683; LEU-721; CYS-742; THR-1698; GLY-1715; ARG-1779; THR-1791; HIS-1800; ALA-1801; PHE-1901; GLN-1960; GLN-1985; ILE-2007; TRP-2016; ASP-2022; ASN-2030 AND SER-2038; Protein truncation test: detection of severe haemophilia a mutation and analysis of factor VIII transcripts.
Maugard C.; Tuffery S.; Aguilar-Martinez P.; Schved J.-F.; Gris J.-C.; Demaille J.; Claustres M.;
Hum. Mutat. 11:18-22(1998)
Cited for: VARIANTS HEMA VAL-129; LYS-631 AND HIS-1800; Start of UK confidential haemophilia A database: analysis of 142 patients by solid phase fluorescent chemical cleavage of mismatch.
Waseem N.H.; Bagnall R.; Green P.M.; Giannelli F.;
Thromb. Haemost. 81:900-905(1999)
Cited for: VARIANTS HEMA CYS-24; ARG-26; TYR-113; SER-121; TRP-172; PRO-176; MET-181; VAL-214; THR-219; LYS-291; ALA-314; VAL-315; LYS-340; PHE-405; GLY-412; THR-470; GLU-474; ASN-478; CYS-484; GLY-490; ARG-498; TRP-546; CYS-550; HIS-561; ARG-584; THR-585; GLY-588; ASP-601; LYS-601; GLY-602; HIS-605; CYS-612; TRP-717; CYS-1708; GLN-1751; HIS-1800; CYS-1802; THR-1853; GLU-1864; PRO-1882; ILE-1888; LEU-1973; TRP-2016; ALA-2035; TYR-2040; CYS-2120; CYS-2145; HIS-2169; CYS-2178; HIS-2182; VAL-2183; VAL-2198; CYS-2248 AND GLY-2326; Non-inversion factor VIII mutations in 80 hemophilia A families including 24 with alloimmune responses.
Liu M.-L.; Nakaya S.; Thompson A.R.;
Thromb. Haemost. 87:273-276(2002)
Cited for: VARIANTS HEMA GLU-67; 84-ARG-PRO-85 DEL; PRO-85 DEL; MET-181; TYR-186; GLY-220; LEU-262; ARG-412; PHE-438; ASP-439; ARG-470; SER-513; SER-541; CYS-550; GLY-554; SER-583; GLN-594; ILE-609; CYS-612; ASN-635; THR-699; ILE-701; ILE-721; ARG-1779; LEU-1780; THR-1791; PRO-1798; HIS-1800; GLY-1848; ARG-1907; CYS-1907; THR-1939; VAL-1939; ILE-1982; GLN-1985; CYS-2015; TRP-2016; SER-2038; HIS-2169; ILE-2192 AND LEU-2326; Thirty-four novel mutations detected in factor VIII gene by multiplex CSGE: modeling of 13 novel amino acid substitutions.
Habart D.; Kalabova D.; Novotny M.; Vorlova Z.;
J. Thromb. Haemost. 1:773-781(2003)
Cited for: VARIANTS HEMA ARG-26; PRO-326; PHE-329; HIS-391; GLY-401; TYR-522; THR-540; TRP-546; TYR-588; CYS-683; SER-720; TYR-1066; HIS-1768; PRO-1771; HIS-1800; ASP-1904; PRO-1980; CYS-2169; HIS-2169; ASP-2174; CYS-2178; HIS-2178; CYS-2182; GLY-2228; PHE-2229; LEU-2319; CYS-2323; HIS-2323 AND SER-2345; Small FVIII gene rearrangements in 18 hemophilia A patients: five novel mutations.
Bicocchi M.P.; Pasino M.; Lanza T.; Bottini F.; Molinari A.C.; Caprino D.; Rosano C.; Acquila M.;
Am. J. Hematol. 78:117-122(2005)
Cited for: VARIANTS HEMA THR-111; ASP-450; CYS-612; HIS-1800; CYS-1802 AND ALA-2251;
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.