UniProtKB/Swiss-Prot P09172: Variant p.Arg549Cys

Dopamine beta-hydroxylase
Gene: DBH
Feedback?

Variant information Variant position:

549 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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 Arginine (R) to Cysteine (C) at position 549 (R549C, p.Arg549Cys). 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 large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-3 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
Polymorphism:

There are two main alleles of DBH: DBH-A with Ala-318 and DBH-B with Ser-318 (PubMed:10391209, PubMed:10391210, PubMed:10490716). Additional information on the polymorphism described.
Other resources:

Links to websites of interest for the variant.

Variant rs6271 [ dbSNP | Ensembl ]

Sequence information Variant position:

549 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

617 The length of the canonical sequence.
Location on the sequence:

TCPQASVSQQFTSVPWNSFN R DVLKALYSFAPISMHCNKSS 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                         TCPQ----------------ASVSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSS

                              TCPQASGTTCPQASGTTCPRASVPEQFASVPWNSFSRVVLK

Mouse                         TCPQ----------------ASVPQQFSSVPWNSFNRDMLK

Rat                           TCPQ----------------ASVPQQFASVPWNSFNRDMLK

Bovine                        TCPQ----------------ASVPEQFASVPWNSFNREVLK

Horse                         TCPQ----------------ASVPEQFATVPWNSFNRQVLS

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	1 – 617	Dopamine beta-hydroxylase
Chain	40 – 617	Soluble dopamine beta-hydroxylase
Topological domain	38 – 617	Intragranular
Glycosylation	566 – 566	N-linked (GlcNAc...) asparagine
Disulfide bond	154 – 596
Disulfide bond	394 – 565
Disulfide bond	530 – 530	Interchain (with C-528)
Helix	546 – 558

Literature citations
The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme.
Lamouroux A.; Vigny A.; Faucon Biguet N.; Darmon M.C.; Franck R.; Henry J.-P.; Mallet J.;
EMBO J. 6:3931-3937(1987)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-617; PARTIAL PROTEIN SEQUENCE; VARIANTS THR-211 AND CYS-549; CATALYTIC ACTIVITY; FUNCTION; PATHWAY; Characterization of single-nucleotide polymorphisms in coding regions of human genes.
Cargill M.; Altshuler D.; Ireland J.; Sklar P.; Ardlie K.; Patil N.; Shaw N.; Lane C.R.; Lim E.P.; Kalyanaraman N.; Nemesh J.; Ziaugra L.; Friedland L.; Rolfe A.; Warrington J.; Lipshutz R.; Daley G.Q.; Lander E.S.;
Nat. Genet. 22:231-238(1999)
Cited for: VARIANTS SER-318 AND CYS-549;

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.