Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09172

- DOPO_HUMAN

UniProt

P09172 - DOPO_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Dopamine beta-hydroxylase

Gene

DBH

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 PQQ per subunit.
Binds 2 copper ions per subunit.

Pathwayi

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

  1. catalytic activity Source: ProtInc
  2. copper ion binding Source: InterPro
  3. dopamine beta-monooxygenase activity Source: Reactome
  4. L-ascorbic acid binding Source: UniProtKB-KW

GO - Biological processi

  1. behavioral response to ethanol Source: Ensembl
  2. blood vessel remodeling Source: Ensembl
  3. catecholamine biosynthetic process Source: Reactome
  4. cellular nitrogen compound metabolic process Source: Reactome
  5. cytokine production Source: Ensembl
  6. dopamine catabolic process Source: Ensembl
  7. fear response Source: Ensembl
  8. glucose homeostasis Source: Ensembl
  9. homoiothermy Source: Ensembl
  10. leukocyte mediated immunity Source: Ensembl
  11. leukocyte migration Source: Ensembl
  12. locomotory behavior Source: Ensembl
  13. maternal behavior Source: Ensembl
  14. memory Source: Ensembl
  15. norepinephrine biosynthetic process Source: UniProtKB-UniPathway
  16. positive regulation of vasoconstriction Source: Ensembl
  17. regulation of cell proliferation Source: Ensembl
  18. regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  19. response to amphetamine Source: Ensembl
  20. response to pain Source: Ensembl
  21. small molecule metabolic process Source: Reactome
  22. synaptic transmission Source: ProtInc
  23. visual learning Source: Ensembl
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.
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:2689. DBH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. extracellular region Source: UniProtKB
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: ProtInc
  5. secretory granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

Dopamine beta-hydroxylase deficiency (DBH deficiency) [MIM:223360]: Characterized by profound deficits in autonomic and cardiovascular function, but apparently only subtle signs, if any, of central nervous system dysfunction.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.

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.
GenevestigatoriP09172.

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...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini38 – 617580IntragranularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei17 – 3721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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.
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.
PfamiPF01082. 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.
The sequence CAA31631.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA31632.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA68285.1 differs from that shown. Reason: Erroneous initiation.

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:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi158517849.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Dopamine beta hydroxylase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS6977.2.
PIRi S03020.
RefSeqi NP_000778.3. NM_000787.3.
UniGenei Hs.591890.

3D structure databases

ProteinModelPortali P09172.
SMRi P09172. Positions 205-502.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107989. 2 interactions.
IntActi P09172. 1 interaction.
MINTi MINT-2843963.
STRINGi 9606.ENSP00000376776.

Chemistry

BindingDBi P09172.
ChEMBLi CHEMBL3102.
DrugBanki DB00822. Disulfiram.
DB00988. Dopamine.
DB00550. Propylthiouracil.
DB00126. Vitamin C.
GuidetoPHARMACOLOGYi 2486.

PTM databases

PhosphoSitei P09172.

Polymorphism databases

DMDMi 158517849.

Proteomic databases

PaxDbi P09172.
PRIDEi P09172.

Protocols and materials databases

DNASUi 1621.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000393056 ; ENSP00000376776 ; ENSG00000123454 .
GeneIDi 1621.
KEGGi hsa:1621.
UCSCi uc004cel.3. human.

Organism-specific databases

CTDi 1621.
GeneCardsi GC09P136501.
GeneReviewsi DBH.
H-InvDB HIX0008510.
HGNCi HGNC:2689. DBH.
HPAi HPA005960.
MIMi 223360. phenotype.
609312. gene.
neXtProti NX_P09172.
Orphaneti 230. Dopamine beta-hydroxylase deficiency.
PharmGKBi PA136.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG286384.
GeneTreei ENSGT00530000063085.
HOGENOMi HOG000063669.
HOVERGENi HBG005519.
InParanoidi P09172.
KOi K00503.
OMAi SYFGDAW.
OrthoDBi EOG78WKR4.
PhylomeDBi P09172.
TreeFami TF320698.

Enzyme and pathway databases

UniPathwayi UPA00748 ; UER00735 .
BioCyci MetaCyc:MONOMER66-381.
Reactomei REACT_15551. Catecholamine biosynthesis.
SignaLinki P09172.

Miscellaneous databases

GeneWikii Dopamine_beta_hydroxylase.
GenomeRNAii 1621.
NextBioi 6654.
PROi P09172.
SOURCEi Search...

Gene expression databases

Bgeei P09172.
CleanExi HS_DBH.
ExpressionAtlasi P09172. baseline and differential.
Genevestigatori P09172.

Family and domain databases

Gene3Di 2.60.120.230. 1 hit.
2.60.120.310. 1 hit.
InterProi IPR014784. Cu2_ascorb_mOase-like_C.
IPR020611. Cu2_ascorb_mOase_CS-1.
IPR014783. Cu2_ascorb_mOase_CS-2.
IPR000323. Cu2_ascorb_mOase_N.
IPR000945. DBH-rel.
IPR005018. DOMON_domain.
IPR008977. PHM/PNGase_F_dom.
IPR028460. Tbh/DBH.
[Graphical view ]
PANTHERi PTHR10157. PTHR10157. 1 hit.
PTHR10157:SF4. PTHR10157:SF4. 1 hit.
Pfami PF01082. Cu2_monooxygen. 1 hit.
PF03351. DOMON. 1 hit.
[Graphical view ]
PRINTSi PR00767. DBMONOXGNASE.
SMARTi SM00664. DoH. 1 hit.
[Graphical view ]
SUPFAMi SSF49742. SSF49742. 2 hits.
PROSITEi PS00084. CU2_MONOOXYGENASE_1. 1 hit.
PS00085. CU2_MONOOXYGENASE_2. 1 hit.
PS50836. DOMON. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 165 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