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UniProtKB - P09172 (DOPO_HUMAN)

Entry version 219 (29 Sep 2021)
Sequence version 3 (24 Jul 2007)
Previous versions | rss
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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 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P09172

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

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000123454

<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

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

Orthostatic hypotension 1 (ORTHYP1)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of orthostatic hypotension due to congenital dopamine beta-hydroxylase deficiency. Orthostatic hypotension, also known as postural hypotension, is a finding defined as a 20-mm Hg decrease in systolic pressure or a 10-mm Hg decrease in diastolic pressure occurring 3 minutes after a person has risen from supine to standing. Symptoms include dizziness, blurred vision, and sometimes syncope. ORTHYP1 is an autosomal recessive condition apparent from infancy or early childhood and characterized by low plasma and urinary levels of norepinephrine and epinephrine, and episodic hypoglycemia.
Related information in OMIM
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 ORTHYP1. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.1
Natural variantiVAR_022759114D → E in ORTHYP1. 1 PublicationCorresponds to variant dbSNP:rs77576840EnsemblClinVar.1
Natural variantiVAR_022760345D → N in ORTHYP1. 1 PublicationCorresponds to variant dbSNP:rs267606761EnsemblClinVar.1

Keywords - Diseasei

Disease variant

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

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P09172, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3102

Drug and drug target database

More...DrugBanki		DB00126, Ascorbic acid
DB06774, Capsaicin
DB09130, Copper
DB05394, Corticorelin
DB00822, Disulfiram
DB00988, Dopamine
DB00550, Propylthiouracil

DrugCentral

More...DrugCentrali		P09172

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2486

Genetic variation 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 or proteolytic cleavage.<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

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P09172

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: a multi-organism proteome resource

More...ProteomicsDBi		52205

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1933, 9 N-Linked glycans (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P09172, 4 sites, 9 N-linked glycans (1 site)

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 adrenal gland and 114 other tissues

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		ENSG00000123454, Group enriched (adrenal gland, brain, liver)

<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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107989, 13 interactors

Protein interaction database and analysis system

More...IntActi		P09172, 21 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P09172, protein

<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

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

More...SMRi		P09172

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni590 – 617DisorderedSequence analysisAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi591 – 606Polar residuesSequence analysisAdd BLAST16

<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

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063085

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_017939_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09172

Identification of Orthologs from Complete Genome Data

More...OMAi		CAPEMDN

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
IPR000945, DBH-like
IPR005018, DOMON_domain
IPR008977, PHM/PNGase_F_dom_sf
IPR028460, Tbh/DBH

The PANTHER Classification System

More...PANTHERi		PTHR10157, PTHR10157, 1 hit

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>. The information is filed in different subsections. The current subsections and their content are listed below:<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:3 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. Truncated N-terminus.Curated
The sequence CAA31631 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAA31632 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence CAA68285 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.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 ORTHYP1. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.1
Natural variantiVAR_022759114D → E in ORTHYP1. 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 ORTHYP1. 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

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

<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

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[»]
SMRiP09172
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107989, 13 interactors
IntActiP09172, 21 interactors
MINTiP09172
STRINGi9606.ENSP00000376776

Chemistry databases

BindingDBiP09172
ChEMBLiCHEMBL3102
DrugBankiDB00126, Ascorbic acid
DB06774, Capsaicin
DB09130, Copper
DB05394, Corticorelin
DB00822, Disulfiram
DB00988, Dopamine
DB00550, Propylthiouracil
DrugCentraliP09172
GuidetoPHARMACOLOGYi2486

PTM databases

GlyConnecti1933, 9 N-Linked glycans (1 site)
GlyGeniP09172, 4 sites, 9 N-linked glycans (1 site)
iPTMnetiP09172
PhosphoSitePlusiP09172

Genetic variation databases

BioMutaiDBH
DMDMi158517849

Proteomic databases

MassIVEiP09172
PaxDbiP09172
PeptideAtlasiP09172
PRIDEiP09172
ProteomicsDBi52205

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		881, 537 antibodies

The DNASU plasmid repository

More...DNASUi		1621

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1621
DisGeNETi1621

GeneCards: human genes, protein and diseases

More...GeneCardsi		DBH
GeneReviewsiDBH
HGNCiHGNC:2689, DBH
HPAiENSG00000123454, Group enriched (adrenal gland, brain, liver)
MalaCardsiDBH
MIMi223360, phenotype
609312, gene
neXtProtiNX_P09172
OpenTargetsiENSG00000123454
Orphaneti230, Dopamine beta-hydroxylase deficiency
PharmGKBiPA136
VEuPathDBiHostDB:ENSG00000123454

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3568, Eukaryota
GeneTreeiENSGT00530000063085
HOGENOMiCLU_017939_3_0_1
InParanoidiP09172
OMAiCAPEMDN
OrthoDBi1472750at2759
PhylomeDBiP09172
TreeFamiTF320698

Enzyme and pathway databases

UniPathwayiUPA00748;UER00735
BioCyciMetaCyc:MONOMER66-381
BRENDAi1.14.17.1, 2681
PathwayCommonsiP09172
ReactomeiR-HSA-209905, Catecholamine biosynthesis
SignaLinkiP09172
SIGNORiP09172

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1621, 2 hits in 1006 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		DBH, human

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
PharosiP09172, Tchem

Protein Ontology

More...PROi		PR:P09172
RNActiP09172, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000123454, Expressed in adrenal gland and 114 other tissues
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
IPR000945, DBH-like
IPR005018, DOMON_domain
IPR008977, PHM/PNGase_F_dom_sf
IPR028460, Tbh/DBH
PANTHERiPTHR10157, PTHR10157, 1 hit
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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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: September 29, 2021
This is version 219 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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. SIMILARITY comments
    Index of protein domains and families
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