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UniProtKB/Swiss-Prot P00740: Variant p.Gly106Asp

Coagulation factor IX
Gene: F9
Variant information

Variant position:  106
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Glycine (G) to Aspartate (D) at position 106 (G106D, p.Gly106Asp).
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:  Change from glycine (G) to medium size and acidic (D)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In HEMB.
Any additional useful information about the variant.



Sequence information

Variant position:  106
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:   EFWKQYVDGDQCESNPCLNG  G SCKDDINSYECWCPFGFEGK
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                         EFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGK

                              EFWKQYVDGDQCESNPCLNDGVCKDDINSYECWCRAGFEGK

Chimpanzee                    EFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCPFGFEGK

Mouse                         EFWKQYVDGDQCESNPCLNGGICKDDISSYECWCQVGFEGR

Rat                           EFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQAGFEGR

Bovine                        EFWKQYVDGDQCESNPCLNGGMCKDDINSYECWCQAGFEGT

Cat                           EFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQTGFEGK

Chicken                       EFWKIYIDGDQCNSNPCKNGAVCKDGVSSYECMCPPGYGGR

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.

TypePositionsDescription
Chain 47 – 461 Coagulation factor IX
Chain 47 – 191 Coagulation factor IXa light chain
Domain 93 – 129 EGF-like 1; calcium-binding
Metal binding 86 – 86 Calcium 6 or magnesium 3; via 4-carboxyglutamate
Metal binding 93 – 93 Calcium 7
Metal binding 94 – 94 Calcium 7; via carbonyl oxygen
Metal binding 96 – 96 Calcium 7
Metal binding 110 – 110 Calcium 7
Metal binding 111 – 111 Calcium 7; via carbonyl oxygen
Modified residue 86 – 86 4-carboxyglutamate
Modified residue 110 – 110 (3R)-3-hydroxyaspartate
Modified residue 114 – 114 Phosphoserine
Glycosylation 99 – 99 O-linked (Glc...) serine
Glycosylation 107 – 107 O-linked (Fuc...) serine
Disulfide bond 97 – 108
Disulfide bond 102 – 117
Alternative sequence 93 – 130 Missing. In isoform 2.


Literature citations

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;

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.