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UniProtKB/Swiss-Prot P09172: Variant p.Arg549Cys

Dopamine beta-hydroxylase
Gene: DBH
Variant information

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

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

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:10490716, PubMed:10391209, PubMed:10391210).
Additional information on the polymorphism described.

Other resources:  
Links to websites of interest for the variant.



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                         TCPQAS----------------VSQQFTSVPWNSFNRDVLKALYSFAPISMHCNKSS

                              TCPQASGTTCPQASGTTCPRASVPEQFASVPWNSFSRVVLK

Mouse                         TCPQAS----------------VPQQFSSVPWNSFNRDMLK

Rat                           TCPQAS----------------VPQQFASVPWNSFNRDMLK

Bovine                        TCPQAS----------------VPEQFASVPWNSFNREVLK

Horse                         TCPQAS----------------VPEQFATVPWNSFNRQVLS

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 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.