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UniProtKB - P09172 (DOPO_HUMAN)

Protein

Dopamine beta-hydroxylase

Gene

DBH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Conversion of dopamine to noradrenaline.4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Cu2+1 Publication1 PublicationNote: Binds 2 copper ions per subunit.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.8 mM for tyramine1 Publication

    pH dependencei

    Optimum pH is 5.2.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-noradrenaline biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.3 Publications
    Proteins known to be involved in this subpathway in this organism are:
    1. Dopamine beta-hydroxylase (DBH)
    This subpathway is part of the pathway (R)-noradrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-noradrenaline from dopamine, the pathway (R)-noradrenaline biosynthesis and in Catecholamine biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei230Sequence analysis1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi262Copper ABy similarity1
    Metal bindingi263Copper ABy similarity1
    Metal bindingi333Copper ABy similarity1
    Active sitei412Sequence analysis1
    Metal bindingi412Copper BCombined sources1 Publication1
    Metal bindingi414Copper BCombined sources1 Publication1
    Metal bindingi487Copper BCombined sources1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionMonooxygenase, Oxidoreductase
    Biological processCatecholamine biosynthesis
    LigandCopper, Metal-binding, Vitamin C

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:MONOMER66-381

    BRENDA Comprehensive Enzyme Information System

    More...    BRENDAi    		1.14.17.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-HSA-209905 Catecholamine biosynthesis

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...    SignaLinki    		P09172

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P09172

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi
    UPA00748;UER00735

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Dopamine beta-hydroxylase (EC:1.14.17.13 Publications)
    Alternative name(s):
    Dopamine beta-monooxygenase
    Cleaved into the following chain:
    Soluble dopamine beta-hydroxylase
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:DBH
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000123454.10

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:2689 DBH

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		609312 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P09172

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 16CytoplasmicSequence analysisAdd BLAST16
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei17 – 37Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
    Topological domaini38 – 617IntragranularSequence analysisAdd BLAST580

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Membrane, Secreted

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Dopamine beta-hydroxylase deficiency (DBH deficiency)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionCharacterized by profound deficits in autonomic and cardiovascular function, but apparently only subtle signs, if any, of central nervous system dysfunction.
    See also OMIM:223360
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022758101V → M in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.1
    Natural variantiVAR_022759114D → E in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs77576840EnsemblClinVar.1
    Natural variantiVAR_022760345D → N in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606761EnsemblClinVar.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		1621

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...    GeneReviewsi    		DBH

    MalaCards human disease database

    More...    MalaCardsi    		DBH
    MIMi223360 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000123454

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...    Orphaneti    		230 Dopamine beta-hydroxylase deficiency

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA136

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL3102

    Drug and drug target database

    More...    DrugBanki    		DB06774 Capsaicin
    DB05394 corticotropin-releasing factor
    DB00822 Disulfiram
    DB00988 Dopamine
    DB00550 Propylthiouracil
    DB00126 Vitamin C

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		2486

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		DBH

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		158517849

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000063561 – 617Dopamine beta-hydroxylaseAdd BLAST617
    ChainiPRO_000030820940 – 617Soluble dopamine beta-hydroxylaseAdd BLAST578

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi64N-linked (GlcNAc...) asparagineSequence analysisCombined sources1 Publication1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi154 ↔ 596Combined sources1 Publication
    Glycosylationi184N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications1
    Disulfide bondi232 ↔ 283Combined sources1 Publication
    Disulfide bondi269 ↔ 295Combined sources1 Publication
    Disulfide bondi390 ↔ 503Combined sources1 Publication
    Disulfide bondi394 ↔ 565Combined sources1 Publication
    Disulfide bondi466 ↔ 488Combined sources1 Publication
    Disulfide bondi528Interchain (with C-530)Combined sources1 Publication
    Disulfide bondi530Interchain (with C-528)Combined sources1 Publication
    Glycosylationi566N-linked (GlcNAc...) asparagineCombined sources1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    N-glycosylated.2 Publications
    Proteolytic cleavage after the membrane-anchor leads to the release of the soluble form.By similarity

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei39 – 40CleavageBy similarity2

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		P09172

    PeptideAtlas

    More...    PeptideAtlasi    		P09172

    PRoteomics IDEntifications database

    More...    PRIDEi    		P09172

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		52205

    PTM databases

    GlyConnect protein glycosylation platform

    More...    GlyConnecti    		1933

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P09172

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...    PhosphoSitePlusi    		P09172

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Activity is enhanced by nerve growth factor (in superior cervical ganglia and adrenal medulla). Trans-synaptic stimulation with reserpine, acetylcholine and glucocorticoids.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000123454 Expressed in 77 organ(s), highest expression level in right adrenal gland

    CleanEx database of gene expression profiles

    More...    CleanExi    		HS_DBH

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P09172 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P09172 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		HPA002130
    HPA005960
    HPA070789

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer; composed of two disulfide-linked dimers.1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...    BioGridi    		107989, 6 interactors

    Protein interaction database and analysis system

    More...    IntActi    		P09172, 2 interactors

    Molecular INTeraction database

    More...    MINTi    		P09172

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000376776

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P09172

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1617
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...    PDBei

    Protein Data Bank RCSB

    More...    RCSB PDBi

    Protein Data Bank Japan

    More...    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		P09172

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...    SMRi    		P09172

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini57 – 173DOMONPROSITE-ProRule annotationAdd BLAST117

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the copper type II ascorbate-dependent monooxygenase family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG3568 Eukaryota
    ENOG410XR89 LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00530000063085

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000063669

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...    HOVERGENi    		HBG005519

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P09172

    KEGG Orthology (KO)

    More...    KOi    		K00503

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		MYEPIVT

    Database of Orthologous Groups

    More...    OrthoDBi    		1472750at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P09172

    TreeFam database of animal gene trees

    More...    TreeFami    		TF320698

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		2.60.120.230, 1 hit
    2.60.120.310, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR014784 Cu2_ascorb_mOase-like_C
    IPR020611 Cu2_ascorb_mOase_CS-1
    IPR014783 Cu2_ascorb_mOase_CS-2
    IPR000323 Cu2_ascorb_mOase_N
    IPR036939 Cu2_ascorb_mOase_N_sf
    IPR024548 Cu2_monoox_C
    IPR005018 DOMON_domain
    IPR008977 PHM/PNGase_F_dom_sf
    IPR028460 Tbh/DBH

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF03712 Cu2_monoox_C, 1 hit
    PF01082 Cu2_monooxygen, 1 hit
    PF03351 DOMON, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00767 DBMONOXGNASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00664 DoH, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF49742 SSF49742, 2 hits

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS00084 CU2_MONOOXYGENASE_1, 1 hit
    PS00085 CU2_MONOOXYGENASE_2, 1 hit
    PS50836 DOMON, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    P09172-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPALSRWASL PGPSMREAAF MYSTAVAIFL VILVAALQGS APRESPLPYH 
            60         70         80         90        100
    IPLDPEGSLE LSWNVSYTQE AIHFQLLVRR LKAGVLFGMS DRGELENADL 
           110        120        130        140        150
    VVLWTDGDTA YFADAWSDQK GQIHLDPQQD YQLLQVQRTP EGLTLLFKRP 
           160        170        180        190        200
    FGTCDPKDYL IEDGTVHLVY GILEEPFRSL EAINGSGLQM GLQRVQLLKP 
           210        220        230        240        250
    NIPEPELPSD ACTMEVQAPN IQIPSQETTY WCYIKELPKG FSRHHIIKYE 
           260        270        280        290        300
    PIVTKGNEAL VHHMEVFQCA PEMDSVPHFS GPCDSKMKPD RLNYCRHVLA 
           310        320        330        340        350
    AWALGAKAFY YPEEAGLAFG GPGSSRYLRL EVHYHNPLVI EGRNDSSGIR 
           360        370        380        390        400
    LYYTAKLRRF NAGIMELGLV YTPVMAIPPR ETAFILTGYC TDKCTQLALP 
           410        420        430        440        450
    PSGIHIFASQ LHTHLTGRKV VTVLVRDGRE WEIVNQDNHY SPHFQEIRML 
           460        470        480        490        500
    KKVVSVHPGD VLITSCTYNT EDRELATVGG FGILEEMCVN YVHYYPQTQL 
           510        520        530        540        550
    ELCKSAVDAG FLQKYFHLIN RFNNEDVCTC PQASVSQQFT SVPWNSFNRD 
           560        570        580        590        600
    VLKALYSFAP ISMHCNKSSA VRFQGEWNLQ PLPKVISTLE EPTPQCPTSQ 
           610 
    GRSPAGPTVV SIGGGKG
    Length:617
    Mass (Da):69,065
    Last modified:July 24, 2007 - v3
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4D5586F0E358885D
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    Q5T382Q5T382_HUMAN
    Dopamine beta-hydroxylase
    DBH
    		256Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAH17174 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA31631 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA31632 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAA68285 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti505S → T in CAA68285 (PubMed:3443096).Curated1
    Sequence conflicti505S → T in CAA31631 (PubMed:2922261).Curated1
    Sequence conflicti505S → T in CAA31632 (PubMed:2922261).Curated1

    <p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

    There are two main alleles of DBH: DBH-A with Ala-318 and DBH-B with Ser-318 (PubMed:10490716, PubMed:10391209, PubMed:10391210).3 Publications

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04883812G → S. Corresponds to variant dbSNP:rs5318Ensembl.1
    Natural variantiVAR_022758101V → M in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.1
    Natural variantiVAR_022759114D → E in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs77576840EnsemblClinVar.1
    Natural variantiVAR_014706181E → Q. Corresponds to variant dbSNP:rs5319Ensembl.1
    Natural variantiVAR_013947211A → T2 PublicationsCorresponds to variant dbSNP:rs5320EnsemblClinVar.1
    Natural variantiVAR_014707239K → N. Corresponds to variant dbSNP:rs5321Ensembl.1
    Natural variantiVAR_014708250E → Q. Corresponds to variant dbSNP:rs5323Ensembl.1
    Natural variantiVAR_014709290D → N. Corresponds to variant dbSNP:rs5324EnsemblClinVar.1
    Natural variantiVAR_014710317L → P. Corresponds to variant dbSNP:rs5325Ensembl.1
    Natural variantiVAR_002196318A → S in allele DBH-B. 3 PublicationsCorresponds to variant dbSNP:rs4531EnsemblClinVar.1
    Natural variantiVAR_022760345D → N in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606761EnsemblClinVar.1
    Natural variantiVAR_013948549R → C2 PublicationsCorresponds to variant dbSNP:rs6271EnsemblClinVar.1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		AL365494 Genomic DNA No translation available.
    Y00096 mRNA Translation: CAA68285.1 Different initiation.
    BC017174 mRNA Translation: AAH17174.1 Different initiation.
    X13255 mRNA Translation: CAA31631.1 Different initiation.
    X13256 mRNA Translation: CAA31632.1 Different initiation.

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS6977.2

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S03020

    NCBI Reference Sequences

    More...    RefSeqi    		NP_000778.3, NM_000787.3

    UniGene gene-oriented nucleotide sequence clusters

    More...    UniGenei    		Hs.591890

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000393056; ENSP00000376776; ENSG00000123454

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		1621

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:1621

    UCSC genome browser

    More...    UCSCi    		uc004cel.4 human

    Keywords - Coding sequence diversityi

    Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Wikipedia

    Dopamine beta hydroxylase entry

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		AL365494 Genomic DNA No translation available.
    Y00096 mRNA Translation: CAA68285.1 Different initiation.
    BC017174 mRNA Translation: AAH17174.1 Different initiation.
    X13255 mRNA Translation: CAA31631.1 Different initiation.
    X13256 mRNA Translation: CAA31632.1 Different initiation.
    CCDSiCCDS6977.2
    PIRiS03020
    RefSeqiNP_000778.3, NM_000787.3
    UniGeneiHs.591890

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    		PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4ZELX-ray2.90A/B40-617[»]
    ProteinModelPortaliP09172
    SMRiP09172
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107989, 6 interactors
    IntActiP09172, 2 interactors
    MINTiP09172
    STRINGi9606.ENSP00000376776

    Chemistry databases

    BindingDBiP09172
    ChEMBLiCHEMBL3102
    DrugBankiDB06774 Capsaicin
    DB05394 corticotropin-releasing factor
    DB00822 Disulfiram
    DB00988 Dopamine
    DB00550 Propylthiouracil
    DB00126 Vitamin C
    GuidetoPHARMACOLOGYi2486

    PTM databases

    GlyConnecti1933
    iPTMnetiP09172
    PhosphoSitePlusiP09172

    Polymorphism and mutation databases

    BioMutaiDBH
    DMDMi158517849

    Proteomic databases

    PaxDbiP09172
    PeptideAtlasiP09172
    PRIDEiP09172
    ProteomicsDBi52205

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		1621
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000393056; ENSP00000376776; ENSG00000123454
    GeneIDi1621
    KEGGihsa:1621
    UCSCiuc004cel.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		1621
    DisGeNETi1621
    EuPathDBiHostDB:ENSG00000123454.10

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		DBH
    GeneReviewsiDBH

    H-Invitational Database, human transcriptome db

    More...    H-InvDBi    		HIX0008510
    HGNCiHGNC:2689 DBH
    HPAiHPA002130
    HPA005960
    HPA070789
    MalaCardsiDBH
    MIMi223360 phenotype
    609312 gene
    neXtProtiNX_P09172
    OpenTargetsiENSG00000123454
    Orphaneti230 Dopamine beta-hydroxylase deficiency
    PharmGKBiPA136

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG3568 Eukaryota
    ENOG410XR89 LUCA
    GeneTreeiENSGT00530000063085
    HOGENOMiHOG000063669
    HOVERGENiHBG005519
    InParanoidiP09172
    KOiK00503
    OMAiMYEPIVT
    OrthoDBi1472750at2759
    PhylomeDBiP09172
    TreeFamiTF320698

    Enzyme and pathway databases

    UniPathwayi
    UPA00748;UER00735

    BioCyciMetaCyc:MONOMER66-381
    BRENDAi1.14.17.1 2681
    ReactomeiR-HSA-209905 Catecholamine biosynthesis
    SignaLinkiP09172
    SIGNORiP09172

    Miscellaneous databases

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		Dopamine_beta_hydroxylase

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...    GenomeRNAii    		1621

    Protein Ontology

    More...    PROi    		PR:P09172

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000123454 Expressed in 77 organ(s), highest expression level in right adrenal gland
    CleanExiHS_DBH
    ExpressionAtlasiP09172 baseline and differential
    GenevisibleiP09172 HS

    Family and domain databases

    Gene3Di2.60.120.230, 1 hit
    2.60.120.310, 1 hit
    InterProiView protein in InterPro
    IPR014784 Cu2_ascorb_mOase-like_C
    IPR020611 Cu2_ascorb_mOase_CS-1
    IPR014783 Cu2_ascorb_mOase_CS-2
    IPR000323 Cu2_ascorb_mOase_N
    IPR036939 Cu2_ascorb_mOase_N_sf
    IPR024548 Cu2_monoox_C
    IPR005018 DOMON_domain
    IPR008977 PHM/PNGase_F_dom_sf
    IPR028460 Tbh/DBH
    PfamiView protein in Pfam
    PF03712 Cu2_monoox_C, 1 hit
    PF01082 Cu2_monooxygen, 1 hit
    PF03351 DOMON, 1 hit
    PRINTSiPR00767 DBMONOXGNASE
    SMARTiView protein in SMART
    SM00664 DoH, 1 hit
    SUPFAMiSSF49742 SSF49742, 2 hits
    PROSITEiView protein in PROSITE
    PS00084 CU2_MONOOXYGENASE_1, 1 hit
    PS00085 CU2_MONOOXYGENASE_2, 1 hit
    PS50836 DOMON, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDOPO_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09172
    Secondary accession number(s): Q5T381, Q96AG2
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 24, 2007
    Last modified: January 16, 2019
    This is version 199 of the entry and version 3 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
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