DBH

Functionⁱ

Conversion of dopamine to noradrenaline.4 Publications

Catalytic activityⁱ

3,4-dihydroxyphenethylamine + ascorbate + O₂ = noradrenaline + dehydroascorbate + H₂O.3 Publications

Cofactorⁱ

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

Kineticsⁱ

K_M=
1.8 mM for tyramine
1 Publication
Manual assertion based on experiment inⁱ
- Ref.5
  "Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells."
  Li B., Tsing S., Kosaka A.H., Nguyen B., Osen E.G., Bach C., Chan H., Barnett J.
  Biochem. J. 313:57-64(1996) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 40-48, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, SUBCELLULAR LOCATION, GLYCOSYLATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

pH dependenceⁱ

Optimum pH is 5.2.1 Publication

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:

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 key	Position(s)	DescriptionActions	Length
Active siteⁱ	230	Sequence analysis	1
Metal bindingⁱ	262	Copper ABy similarity	1
Metal bindingⁱ	263	Copper ABy similarity	1
Metal bindingⁱ	333	Copper ABy similarity	1
Active siteⁱ	412	Sequence analysis	1
Metal bindingⁱ	412	Copper BCombined sources1 Publication	1
Metal bindingⁱ	414	Copper BCombined sources1 Publication	1
Metal bindingⁱ	487	Copper BCombined sources1 Publication	1

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

behavioral response to ethanol Source: Ensembl
blood vessel remodeling Source: Ensembl
catecholamine biosynthetic process Source: Reactome
chemical synaptic transmission
Source: ProtInc
Traceable author statementⁱ
- 2880016
cytokine production Source: Ensembl
dopamine catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 3443096
- 7961964
fear response Source: Ensembl
glucose homeostasis Source: Ensembl
homoiothermy Source: Ensembl
leukocyte mediated immunity Source: Ensembl
leukocyte migration Source: Ensembl
locomotory behavior Source: Ensembl
maternal behavior Source: Ensembl
memory Source: Ensembl
norepinephrine biosynthetic process
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 27148966
octopamine biosynthetic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
positive regulation of cold-induced thermogenesis
Source: YuBioLab
Inferred from sequence or structural similarityⁱ
- 9139828
positive regulation of vasoconstriction Source: Ensembl
regulation of cell proliferation Source: Ensembl
regulation of extrinsic apoptotic signaling pathway Source: Ensembl
response to amphetamine Source: Ensembl
response to pain Source: Ensembl
visual learning Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Monooxygenase, Oxidoreductase
Biological process	Catecholamine biosynthesis
Ligand	Copper, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER66-381
BRENDAⁱ	1.14.17.1 2681
Reactomeⁱ	R-HSA-209905 Catecholamine biosynthesis
SignaLinkⁱ	P09172
SIGNORⁱ	P09172
UniPathwayⁱ	UPA00748;UER00735

Names & Taxonomyⁱ

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
Gene namesⁱ	Name:DBH
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 9

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000123454.10
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:2689 DBH
MIMⁱ	609312 gene
neXtProtⁱ	NX_P09172

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 16	CytoplasmicSequence analysisAdd BLAST	16
Transmembraneⁱ	17 – 37	Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST	21
Topological domainⁱ	38 – 617	IntragranularSequence analysisAdd BLAST	580

Keywords - Cellular componentⁱ

Cytoplasmic vesicle, Membrane, Secreted

Pathology & Biotechⁱ

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.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_022758	101	V → M in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.	1
Natural variantⁱVAR_022759	114	D → E in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs77576840EnsemblClinVar.	1
Natural variantⁱVAR_022760	345	D → N in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606761EnsemblClinVar.	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1621
GeneReviewsⁱ	DBH
MalaCards human disease database More...MalaCardsⁱ	DBH
MIMⁱ	223360 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000123454
Orphanetⁱ	230 Dopamine beta-hydroxylase deficiency
PharmGKBⁱ	PA136

Chemistry databases

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

BioMutaⁱ	DBH
DMDMⁱ	158517849

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000006356	1 – 617	Dopamine beta-hydroxylaseAdd BLAST		617
ChainⁱPRO_0000308209	40 – 617	Soluble dopamine beta-hydroxylaseAdd BLAST		578

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Glycosylationⁱ	64	N-linked (GlcNAc...) asparagineSequence analysisCombined sources1 Publication	1
Disulfide bondⁱ	154 ↔ 596	Combined sources1 Publication
Glycosylationⁱ	184	N-linked (GlcNAc...) (complex) asparagineCombined sources3 Publications	1
Disulfide bondⁱ	232 ↔ 283	Combined sources1 Publication
Disulfide bondⁱ	269 ↔ 295	Combined sources1 Publication
Disulfide bondⁱ	390 ↔ 503	Combined sources1 Publication
Disulfide bondⁱ	394 ↔ 565	Combined sources1 Publication
Disulfide bondⁱ	466 ↔ 488	Combined sources1 Publication
Disulfide bondⁱ	528	Interchain (with C-530)Combined sources1 Publication
Disulfide bondⁱ	530	Interchain (with C-528)Combined sources1 Publication
Glycosylationⁱ	566	N-linked (GlcNAc...) asparagineCombined sources1 Publication	1

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 key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	39 – 40	CleavageBy similarity		2

Keywords - PTMⁱ

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbⁱ	P09172
PeptideAtlas More...PeptideAtlasⁱ	P09172
PRIDEⁱ	P09172
ProteomicsDBⁱ	52205

PTM databases

iPTMnetⁱ	P09172
PhosphoSitePlusⁱ	P09172

Expressionⁱ

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

Bgeeⁱ	ENSG00000123454 Expressed in 77 organ(s), highest expression level in right adrenal gland
CleanExⁱ	HS_DBH
ExpressionAtlasⁱ	P09172 baseline and differential
Genevisibleⁱ	P09172 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA002130 HPA005960 HPA070789

HPAⁱ

HPA002130
HPA005960
HPA070789

Interactionⁱ

Subunit structureⁱ

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

Protein-protein interaction databases

BioGridⁱ	107989, 6 interactors
IntActⁱ	P09172, 2 interactors
Molecular INTeraction database More...MINTⁱ	P09172
STRINGⁱ	9606.ENSP00000376776

Chemistry databases

BindingDBⁱ

P09172

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	48 – 52	Combined sources	5
Beta strandⁱ	58 – 66	Combined sources	9
Turnⁱ	67 – 70	Combined sources	4
Beta strandⁱ	71 – 80	Combined sources	10
Beta strandⁱ	83 – 93	Combined sources	11
Beta strandⁱ	98 – 104	Combined sources	7
Beta strandⁱ	111 – 117	Combined sources	7
Beta strandⁱ	123 – 125	Combined sources	3
Beta strandⁱ	130 – 138	Combined sources	9
Beta strandⁱ	143 – 151	Combined sources	9
Beta strandⁱ	166 – 173	Combined sources	8
Beta strandⁱ	191 – 195	Combined sources	5
Beta strandⁱ	212 – 217	Combined sources	6
Beta strandⁱ	220 – 222	Combined sources	3
Beta strandⁱ	225 – 236	Combined sources	12
Beta strandⁱ	244 – 252	Combined sources	9
Turnⁱ	255 – 260	Combined sources	6
Beta strandⁱ	261 – 268	Combined sources	8
Beta strandⁱ	279 – 284	Combined sources	6
Beta strandⁱ	286 – 288	Combined sources	3
Beta strandⁱ	290 – 294	Combined sources	5
Beta strandⁱ	297 – 303	Combined sources	7
Beta strandⁱ	313 – 319	Combined sources	7
Beta strandⁱ	327 – 335	Combined sources	9
Beta strandⁱ	348 – 356	Combined sources	9
Beta strandⁱ	359 – 361	Combined sources	3
Beta strandⁱ	363 – 369	Combined sources	7
Beta strandⁱ	375 – 377	Combined sources	3
Beta strandⁱ	382 – 390	Combined sources	9
Helixⁱ	392 – 398	Combined sources	7
Beta strandⁱ	404 – 412	Combined sources	9
Beta strandⁱ	417 – 426	Combined sources	10
Beta strandⁱ	429 – 439	Combined sources	11
Beta strandⁱ	448 – 456	Combined sources	9
Beta strandⁱ	461 – 468	Combined sources	8
Beta strandⁱ	477 – 482	Combined sources	6
Beta strandⁱ	489 – 496	Combined sources	8
Beta strandⁱ	499 – 507	Combined sources	9
Helixⁱ	509 – 522	Combined sources	14
Helixⁱ	535 – 539	Combined sources	5
Helixⁱ	546 – 558	Combined sources	13
Beta strandⁱ	561 – 567	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P09172
SMRⁱ	P09172
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	57 – 173	DOMONPROSITE-ProRule annotationAdd BLAST		117

Sequence similaritiesⁱ

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

Keywords - Domainⁱ

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	KOG3568 Eukaryota ENOG410XR89 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063085
HOGENOMⁱ	HOG000063669
HOVERGENⁱ	HBG005519
InParanoidⁱ	P09172
KEGG Orthology (KO) More...KOⁱ	K00503
OMAⁱ	MYEPIVT
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03XS
PhylomeDBⁱ	P09172
TreeFamⁱ	TF320698

Family and domain databases

Gene3Dⁱ	2.60.120.230, 1 hit 2.60.120.310, 1 hit
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
PRINTSⁱ	PR00767 DBMONOXGNASE
SMARTⁱ	View protein in SMART SM00664 DoH, 1 hit
SUPFAMⁱ	SSF49742 SSF49742, 2 hits
PROSITEⁱ	View protein in PROSITE PS00084 CU2_MONOOXYGENASE_1, 1 hit PS00085 CU2_MONOOXYGENASE_2, 1 hit PS50836 DOMON, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

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 all Align All

P09172-1 [UniParc]FASTA Add 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

Checksum:ⁱ4D5586F0E358885D

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	Q5T382	Q5T382_HUMAN		Dopamine beta-hydroxylase Dopamine beta-hydroxylase	DBH	244	Annotation score:

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 key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	505	S → T in CAA68285 (PubMed:3443096).Curated	1
Sequence conflictⁱ	505	S → T in CAA31631 (PubMed:2922261).Curated	1
Sequence conflictⁱ	505	S → T in CAA31632 (PubMed:2922261).Curated	1

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 key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_048838	12	G → S. Corresponds to variant dbSNP:rs5318Ensembl.	1
Natural variantⁱVAR_022758	101	V → M in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606760EnsemblClinVar.	1
Natural variantⁱVAR_022759	114	D → E in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs77576840EnsemblClinVar.	1
Natural variantⁱVAR_014706	181	E → Q. Corresponds to variant dbSNP:rs5319Ensembl.	1
Natural variantⁱVAR_013947	211	A → T2 PublicationsCorresponds to variant dbSNP:rs5320EnsemblClinVar.	1
Natural variantⁱVAR_014707	239	K → N. Corresponds to variant dbSNP:rs5321Ensembl.	1
Natural variantⁱVAR_014708	250	E → Q. Corresponds to variant dbSNP:rs5323Ensembl.	1
Natural variantⁱVAR_014709	290	D → N. Corresponds to variant dbSNP:rs5324EnsemblClinVar.	1
Natural variantⁱVAR_014710	317	L → P. Corresponds to variant dbSNP:rs5325Ensembl.	1
Natural variantⁱVAR_002196	318	A → S in allele DBH-B. 3 PublicationsCorresponds to variant dbSNP:rs4531EnsemblClinVar.	1
Natural variantⁱVAR_022760	345	D → N in DBH deficiency. 1 PublicationCorresponds to variant dbSNP:rs267606761EnsemblClinVar.	1
Natural variantⁱVAR_013948	549	R → C2 PublicationsCorresponds to variant dbSNP:rs6271EnsemblClinVar.	1

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.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS6977.2
PIRⁱ	S03020
NCBI Reference Sequences More...RefSeqⁱ	NP_000778.3, NM_000787.3
UniGeneⁱ	Hs.591890

Genome annotation databases

Ensemblⁱ	ENST00000393056; ENSP00000376776; ENSG00000123454
GeneIDⁱ	1621
KEGGⁱ	hsa:1621
UCSC genome browser More...UCSCⁱ	uc004cel.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P09172	Uncharacterized protein		MACMU		620	UniRef90_P09172
Uncharacterized protein		COLAP		620
Uncharacterized protein		CERAT		620
Uncharacterized protein		PAPAN		620
Uncharacterized protein		MANLE		620
+19

Protein	Similar proteins		Species	Score	Length	Source
P09172	Dopamine beta-hydroxylase		BOVIN		610	UniRef50_P09172
Dopamine beta-hydroxylase		CANLF		625
Dopamine beta-hydroxylase		HORSE		610
Dopamine beta-hydroxylase	)	RAT		620
Dopamine beta-hydroxylase		MOUSE		622
+340

Cross-referencesⁱ

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.
CCDSⁱ	CCDS6977.2
PIRⁱ	S03020
RefSeqⁱ	NP_000778.3, NM_000787.3
UniGeneⁱ	Hs.591890

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 entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4ZEL	X-ray	2.90	A/B	40-617	[»]
ProteinModelPortalⁱ	P09172
SMRⁱ	P09172
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	107989, 6 interactors
IntActⁱ	P09172, 2 interactors
MINTⁱ	P09172
STRINGⁱ	9606.ENSP00000376776

Chemistry databases

BindingDBⁱ	P09172
ChEMBLⁱ	CHEMBL3102
DrugBankⁱ	DB06774 Capsaicin DB05394 corticotropin-releasing factor DB00822 Disulfiram DB00988 Dopamine DB00550 Propylthiouracil DB00126 Vitamin C
GuidetoPHARMACOLOGYⁱ	2486

PTM databases

iPTMnetⁱ	P09172
PhosphoSitePlusⁱ	P09172

Polymorphism and mutation databases

BioMutaⁱ	DBH
DMDMⁱ	158517849

Proteomic databases

PaxDbⁱ	P09172
PeptideAtlasⁱ	P09172
PRIDEⁱ	P09172
ProteomicsDBⁱ	52205

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	1621
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000393056; ENSP00000376776; ENSG00000123454
GeneIDⁱ	1621
KEGGⁱ	hsa:1621
UCSCⁱ	uc004cel.4 human

Organism-specific databases

CTDⁱ	1621
DisGeNETⁱ	1621
EuPathDBⁱ	HostDB:ENSG00000123454.10
GeneCardsⁱ	DBH
GeneReviewsⁱ	DBH
H-InvDBⁱ	HIX0008510
HGNCⁱ	HGNC:2689 DBH
HPAⁱ	HPA002130 HPA005960 HPA070789
MalaCardsⁱ	DBH
MIMⁱ	223360 phenotype 609312 gene
neXtProtⁱ	NX_P09172
OpenTargetsⁱ	ENSG00000123454
Orphanetⁱ	230 Dopamine beta-hydroxylase deficiency
PharmGKBⁱ	PA136
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3568 Eukaryota ENOG410XR89 LUCA
GeneTreeⁱ	ENSGT00530000063085
HOGENOMⁱ	HOG000063669
HOVERGENⁱ	HBG005519
InParanoidⁱ	P09172
KOⁱ	K00503
OMAⁱ	MYEPIVT
OrthoDBⁱ	EOG091G03XS
PhylomeDBⁱ	P09172
TreeFamⁱ	TF320698

Enzyme and pathway databases

UniPathwayⁱ	UPA00748;UER00735
BioCycⁱ	MetaCyc:MONOMER66-381
BRENDAⁱ	1.14.17.1 2681
Reactomeⁱ	R-HSA-209905 Catecholamine biosynthesis
SignaLinkⁱ	P09172
SIGNORⁱ	P09172

Miscellaneous databases

GeneWikiⁱ	Dopamine_beta_hydroxylase
GenomeRNAiⁱ	1621
Protein Ontology More...PROⁱ	PR:P09172
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000123454 Expressed in 77 organ(s), highest expression level in right adrenal gland
CleanExⁱ	HS_DBH
ExpressionAtlasⁱ	P09172 baseline and differential
Genevisibleⁱ	P09172 HS

Family and domain databases

Gene3Dⁱ	2.60.120.230, 1 hit 2.60.120.310, 1 hit
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
Pfamⁱ	View protein in Pfam PF03712 Cu2_monoox_C, 1 hit PF01082 Cu2_monooxygen, 1 hit PF03351 DOMON, 1 hit
PRINTSⁱ	PR00767 DBMONOXGNASE
SMARTⁱ	View protein in SMART SM00664 DoH, 1 hit
SUPFAMⁱ	SSF49742 SSF49742, 2 hits
PROSITEⁱ	View protein in PROSITE PS00084 CU2_MONOOXYGENASE_1, 1 hit PS00085 CU2_MONOOXYGENASE_2, 1 hit PS50836 DOMON, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DOPO_HUMAN
Accessionⁱ	P09172Primary (citable) accession number: P09172 Secondary accession number(s): Q5T381, Q96AG2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	July 24, 2007
	Last modified:	November 7, 2018
	This is version 197 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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.

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

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

UniProtKB

UniParc

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UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P09172 (DOPO_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Dopamine beta-hydroxylase

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<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

<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

pH dependencei

<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

Sites

<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

GO - Biological processi

Enzyme and pathway databases

<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

Organism-specific databases

<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

Other locations

Other locations

Cytoskeleton

Endoplasmic reticulum

Extracellular region or secreted

Other locations

Topology

Keywords - Cellular componenti

<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

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

<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

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<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

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

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Functionⁱ

Kineticsⁱ

pH dependenceⁱ

Pathwayⁱ: (R)-noradrenaline biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ