UniProtKB/SwissProt variant VAR

Variant information

Variant position:

419

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 Valine (V) to Glutamate (E) at position 419 (V419E, p.Val419Glu).

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 medium size and hydrophobic (V) to medium size and acidic (E)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-2

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; moderately severe.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs137852280 [ dbSNP | Ensembl ]

Sequence information

Variant position:

419

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:

FHEGGRDSCQGDSGGPHVTE V EGTSFLTGIISWGEECAMKG

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                         FHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKG

                              FHEGGKDSCQGDSGGPHVTEVEGISFLTGIISWGEECAMKG

Chimpanzee                    FHEGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKG

Mouse                         YREGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAMKG

Rat                           YREGGKDSCEGDSGGPHVTEVEGTSFLTGIISWGEECAMKG

Bovine                        YHEGGKDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKG

Cat                           FHEGGKDSCQGDSGGPHVTEVEGINFLTGIISWGEECAMKG

Chicken                       YTAGGKDTCGGDSGGPYTNSIGETWFLTGVTSWGEECAKPG

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
Chain	227 – 461	Coagulation factor IXa heavy chain
Domain	227 – 459	Peptidase S1
Active site	411 – 411	Charge relay system
Disulfide bond	407 – 435
Beta strand	414 – 419

Literature citations

Factor IX gene mutations causing haemophilia B: comparison of SSC screening versus systematic DNA sequencing and diagnostic applications.
Aguilar-Martinez P.; Romey M.-C.; Schved J.-F.; Gris J.-C.; Demaille J.; Claustres M.;
Hum. Genet. 94:287-290(1994)
Cited for: VARIANTS HEMB HIS-191; GLY-226; THR-279; GLN-379; GLU-419 AND GLN-449;

A novel mutation (Val-373 to Glu) in the catalytic domain of factor IX, resulting in moderately/severe hemophilia B in a southern French patient.
Aguilar-Martinez P.; Romey M.-C.; Gris J.-C.; Schved J.-F.; Demaille J.; Claustres M.;
Hum. Mutat. 3:156-158(1994)
Cited for: VARIANT HEMB GLU-419;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P00740: Variant p.Val419Glu