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Protein

Dopamine beta-hydroxylase

Gene

DBH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conversion of dopamine to noradrenaline.

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

Pathway: (R)-noradrenaline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-noradrenaline from dopamine.
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei230 – 2301Sequence Analysis
Metal bindingi262 – 2621Copper ABy similarity
Metal bindingi263 – 2631Copper ABy similarity
Metal bindingi333 – 3331Copper ABy similarity
Active sitei412 – 4121Sequence Analysis
Metal bindingi412 – 4121Copper BBy similarity
Metal bindingi414 – 4141Copper BBy similarity
Metal bindingi487 – 4871Copper BBy similarity

GO - Molecular functioni

  • catalytic activity Source: ProtInc
  • copper ion binding Source: InterPro
  • dopamine beta-monooxygenase activity Source: Reactome
  • L-ascorbic acid binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

Copper, Metal-binding, PQQ, Vitamin C

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER66-381.
BRENDAi1.14.17.1. 2681.
ReactomeiREACT_15551. Catecholamine biosynthesis.
SignaLinkiP09172.
UniPathwayiUPA00748; UER00735.

Names & Taxonomyi

Protein namesi
Recommended name:
Dopamine beta-hydroxylase (EC:1.14.17.1)
Alternative name(s):
Dopamine beta-monooxygenase
Cleaved into the following chain:
Gene namesi
Name:DBH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2689. DBH.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini38 – 617580IntragranularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • chromaffin granule lumen Source: UniProtKB-SubCell
  • chromaffin granule membrane Source: UniProtKB-SubCell
  • cytoplasm Source: ProtInc
  • extracellular region Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: ProtInc
  • secretory granule lumen Source: Reactome
  • transport vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

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.

See also OMIM:223360
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti101 – 1011V → M in DBH deficiency. 1 Publication
VAR_022758
Natural varianti114 – 1141D → E in DBH deficiency. 1 Publication
VAR_022759
Natural varianti345 – 3451D → N in DBH deficiency. 1 Publication
VAR_022760

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi223360. phenotype.
Orphaneti230. Dopamine beta-hydroxylase deficiency.
PharmGKBiPA136.

Chemistry

DrugBankiDB00822. Disulfiram.
DB00988. Dopamine.
DB00550. Propylthiouracil.
DB00126. Vitamin C.

Polymorphism and mutation databases

BioMutaiDBH.
DMDMi158517849.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617Dopamine beta-hydroxylasePRO_0000006356Add
BLAST
Chaini40 – 617578Soluble dopamine beta-hydroxylasePRO_0000308209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi154 ↔ 596By similarity
Glycosylationi184 – 1841N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi232 ↔ 283By similarity
Disulfide bondi269 ↔ 295By similarity
Disulfide bondi390 ↔ 503By similarity
Disulfide bondi394 ↔ 565By similarity
Disulfide bondi466 ↔ 488By similarity
Disulfide bondi528 – 528InterchainBy similarity
Disulfide bondi530 – 530InterchainBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP09172.
PRIDEiP09172.

PTM databases

PhosphoSiteiP09172.

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

BgeeiP09172.
CleanExiHS_DBH.
ExpressionAtlasiP09172. baseline and differential.
GenevisibleiP09172. HS.

Organism-specific databases

HPAiHPA005960.

Interactioni

Subunit structurei

Homotetramer composed of two non-covalently bound disulfide-linked dimers.

Protein-protein interaction databases

BioGridi107989. 2 interactions.
IntActiP09172. 1 interaction.
MINTiMINT-2843963.
STRINGi9606.ENSP00000376776.

Structurei

3D structure databases

ProteinModelPortaliP09172.
SMRiP09172. Positions 205-502.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini57 – 173117DOMONPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 DOMON domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG286384.
GeneTreeiENSGT00530000063085.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiP09172.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG78WKR4.
PhylomeDBiP09172.
TreeFamiTF320698.

Family and domain databases

Gene3Di2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR024548. Cu2_monoox_C.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view]
PANTHERiPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF4. PTHR10157:SF4. 1 hit.
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSiPR00767. DBMONOXGNASE.
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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
Checksum:i4D5586F0E358885D
GO

Sequence cautioni

The sequence AAH17174.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA31631.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA31632.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA68285.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti505 – 5051S → T in CAA68285 (PubMed:3443096).Curated
Sequence conflicti505 – 5051S → T in CAA31631 (PubMed:2922261).Curated
Sequence conflicti505 – 5051S → T in CAA31632 (PubMed:2922261).Curated

Polymorphismi

There are two main alleles of DBH: DBH-A with Ala-318 and DBH-B with Ser-318.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121G → S.
Corresponds to variant rs5318 [ dbSNP | Ensembl ].
VAR_048838
Natural varianti101 – 1011V → M in DBH deficiency. 1 Publication
VAR_022758
Natural varianti114 – 1141D → E in DBH deficiency. 1 Publication
VAR_022759
Natural varianti181 – 1811E → Q.
Corresponds to variant rs5319 [ dbSNP | Ensembl ].
VAR_014706
Natural varianti211 – 2111A → T.2 Publications
Corresponds to variant rs5320 [ dbSNP | Ensembl ].
VAR_013947
Natural varianti239 – 2391K → N.
Corresponds to variant rs5321 [ dbSNP | Ensembl ].
VAR_014707
Natural varianti250 – 2501E → Q.
Corresponds to variant rs5323 [ dbSNP | Ensembl ].
VAR_014708
Natural varianti290 – 2901D → N.
Corresponds to variant rs5324 [ dbSNP | Ensembl ].
VAR_014709
Natural varianti317 – 3171L → P.
Corresponds to variant rs5325 [ dbSNP | Ensembl ].
VAR_014710
Natural varianti318 – 3181A → S in allele DBH-B. 3 Publications
Corresponds to variant rs4531 [ dbSNP | Ensembl ].
VAR_002196
Natural varianti345 – 3451D → N in DBH deficiency. 1 Publication
VAR_022760
Natural varianti549 – 5491R → C.2 Publications
Corresponds to variant rs6271 [ dbSNP | Ensembl ].
VAR_013948

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL365494 Genomic DNA. Translation: CAI13354.2.
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.

Genome annotation databases

EnsembliENST00000393056; ENSP00000376776; ENSG00000123454.
GeneIDi1621.
KEGGihsa:1621.
UCSCiuc004cel.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Dopamine beta hydroxylase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL365494 Genomic DNA. Translation: CAI13354.2.
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

ProteinModelPortaliP09172.
SMRiP09172. Positions 205-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107989. 2 interactions.
IntActiP09172. 1 interaction.
MINTiMINT-2843963.
STRINGi9606.ENSP00000376776.

Chemistry

BindingDBiP09172.
ChEMBLiCHEMBL3102.
DrugBankiDB00822. Disulfiram.
DB00988. Dopamine.
DB00550. Propylthiouracil.
DB00126. Vitamin C.
GuidetoPHARMACOLOGYi2486.

PTM databases

PhosphoSiteiP09172.

Polymorphism and mutation databases

BioMutaiDBH.
DMDMi158517849.

Proteomic databases

PaxDbiP09172.
PRIDEiP09172.

Protocols and materials databases

DNASUi1621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393056; ENSP00000376776; ENSG00000123454.
GeneIDi1621.
KEGGihsa:1621.
UCSCiuc004cel.3. human.

Organism-specific databases

CTDi1621.
GeneCardsiGC09P136501.
GeneReviewsiDBH.
H-InvDBHIX0008510.
HGNCiHGNC:2689. DBH.
HPAiHPA005960.
MIMi223360. phenotype.
609312. gene.
neXtProtiNX_P09172.
Orphaneti230. Dopamine beta-hydroxylase deficiency.
PharmGKBiPA136.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG286384.
GeneTreeiENSGT00530000063085.
HOGENOMiHOG000063669.
HOVERGENiHBG005519.
InParanoidiP09172.
KOiK00503.
OMAiSYFGDAW.
OrthoDBiEOG78WKR4.
PhylomeDBiP09172.
TreeFamiTF320698.

Enzyme and pathway databases

UniPathwayiUPA00748; UER00735.
BioCyciMetaCyc:MONOMER66-381.
BRENDAi1.14.17.1. 2681.
ReactomeiREACT_15551. Catecholamine biosynthesis.
SignaLinkiP09172.

Miscellaneous databases

GeneWikiiDopamine_beta_hydroxylase.
GenomeRNAii1621.
NextBioi6654.
PROiP09172.
SOURCEiSearch...

Gene expression databases

BgeeiP09172.
CleanExiHS_DBH.
ExpressionAtlasiP09172. baseline and differential.
GenevisibleiP09172. HS.

Family and domain databases

Gene3Di2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProiIPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR024548. Cu2_monoox_C.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view]
PANTHERiPTHR10157. PTHR10157. 1 hit.
PTHR10157:SF4. PTHR10157:SF4. 1 hit.
PfamiPF03712. Cu2_monoox_C. 1 hit.
PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view]
PRINTSiPR00767. DBMONOXGNASE.
SMARTiSM00664. DoH. 1 hit.
[Graphical view]
SUPFAMiSSF49742. SSF49742. 2 hits.
PROSITEiPS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme."
    Lamouroux A., Vigny A., Faucon Biguet N., Darmon M.C., Franck R., Henry J.-P., Mallet J.
    EMBO J. 6:3931-3937(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-617, PARTIAL PROTEIN SEQUENCE, VARIANTS THR-211 AND CYS-549.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-617.
    Tissue: Brain.
  4. "Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation."
    Kobayashi K., Kurosawa Y., Fukita K., Nagatsu T.
    Nucleic Acids Res. 17:1089-1102(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-617.
  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.
  6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184.
    Tissue: Plasma.
  7. Cited for: GLYCOSYLATION AT ASN-184.
  8. "No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH)."
    Williams H.J., Bray N., Murphy K.C., Cardno A.G., Jones L.A., Owen M.J.
    Am. J. Med. Genet. 88:557-559(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-318.
  9. Cited for: VARIANTS SER-318 AND CYS-549.
  10. "Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
    Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
    Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-211 AND SER-318.
  11. "Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency."
    Kim C.-H., Zabetian C.P., Cubells J.F., Cho S., Biaggioni I., Cohen B.M., Robertson D., Kim K.-S.
    Am. J. Med. Genet. 108:140-147(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DBH DEFICIENCY MET-101; GLU-114 AND ASN-345.

Entry informationi

Entry nameiDOPO_HUMAN
AccessioniPrimary (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: June 24, 2015
This is version 170 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.