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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00740: Variant p.Glu73Lys

Coagulation factor IX
Gene: F9
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Variant information Variant position: help 73 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 Glutamate (E) to Lysine (K) at position 73 (E73K, p.Glu73Lys). 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 medium size and acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 HEMB; severe; Seattle-3; Gla mutant. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 73 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 461 The length of the canonical sequence.
Location on the sequence: help EEFVQGNLERECMEEKCSFE E AREVFENTERTTEFWKQYVD 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                         EEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVD

                              EEFVRGNLERECIEEKCSFEEAREVFENTEKTTEFWKQYVD

Chimpanzee                    EEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVD

Mouse                         EEFVRGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVD

Rat                           EEFVQGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVD

Bovine                        EEFVRGNLERECKEEKCSFEEAREVFENTEKTTEFWKQYVD

Cat                           EEFVQGNLERECMEEKCSFEEAREVFENTEKTTEFWKQYVD

Chicken                       EELIPGNLERECIEEKCSFEEAREVFENTEKTMEFWKIYID

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 47 – 461 Coagulation factor IX
Chain 47 – 191 Coagulation factor IXa light chain
Domain 47 – 92 Gla
Binding site 53 – 53 via 4-carboxyglutamate
Binding site 53 – 53 via 4-carboxyglutamate
Binding site 54 – 54 via 4-carboxyglutamate
Binding site 54 – 54 via 4-carboxyglutamate
Binding site 61 – 61 via 4-carboxyglutamate
Binding site 61 – 61 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 63 – 63 via 4-carboxyglutamate
Binding site 66 – 66 via 4-carboxyglutamate
Binding site 66 – 66 via 4-carboxyglutamate
Binding site 67 – 67 via 4-carboxyglutamate
Binding site 72 – 72 via 4-carboxyglutamate
Binding site 72 – 72 via 4-carboxyglutamate
Binding site 73 – 73 via 4-carboxyglutamate
Binding site 73 – 73 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 76 – 76 via 4-carboxyglutamate
Binding site 82 – 82 via 4-carboxyglutamate
Binding site 82 – 82 via 4-carboxyglutamate
Binding site 86 – 86 via 4-carboxyglutamate
Binding site 86 – 86 via 4-carboxyglutamate
Binding site 93 – 93
Modified residue 53 – 53 4-carboxyglutamate
Modified residue 54 – 54 4-carboxyglutamate
Modified residue 61 – 61 4-carboxyglutamate
Modified residue 63 – 63 4-carboxyglutamate
Modified residue 66 – 66 4-carboxyglutamate
Modified residue 67 – 67 4-carboxyglutamate
Modified residue 72 – 72 4-carboxyglutamate
Modified residue 73 – 73 4-carboxyglutamate
Modified residue 76 – 76 4-carboxyglutamate
Modified residue 79 – 79 4-carboxyglutamate
Modified residue 82 – 82 4-carboxyglutamate
Modified residue 86 – 86 4-carboxyglutamate
Glycosylation 85 – 85 O-linked (GalNAc...) threonine
Helix 71 – 75



Literature citations
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;
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.