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P09172

- DOPO_HUMAN

UniProt

P09172 - DOPO_HUMAN

Protein

Dopamine beta-hydroxylase

Gene

DBH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (24 Jul 2007)
      Previous versions | rss
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    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

    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. chromaffin granule lumen Source: UniProtKB-SubCell
    2. chromaffin granule membrane Source: UniProtKB-SubCell
    3. cytoplasm Source: ProtInc
    4. extracellular region Source: UniProtKB
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane Source: ProtInc
    7. secretory granule lumen Source: Reactome
    8. transport vesicle membrane Source: UniProtKB-SubCell

    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

    ArrayExpressiP09172.
    BgeeiP09172.
    CleanExiHS_DBH.
    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.
    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

    MPALSRWASL PGPSMREAAF MYSTAVAIFL VILVAALQGS APRESPLPYH    50
    IPLDPEGSLE LSWNVSYTQE AIHFQLLVRR LKAGVLFGMS DRGELENADL 100
    VVLWTDGDTA YFADAWSDQK GQIHLDPQQD YQLLQVQRTP EGLTLLFKRP 150
    FGTCDPKDYL IEDGTVHLVY GILEEPFRSL EAINGSGLQM GLQRVQLLKP 200
    NIPEPELPSD ACTMEVQAPN IQIPSQETTY WCYIKELPKG FSRHHIIKYE 250
    PIVTKGNEAL VHHMEVFQCA PEMDSVPHFS GPCDSKMKPD RLNYCRHVLA 300
    AWALGAKAFY YPEEAGLAFG GPGSSRYLRL EVHYHNPLVI EGRNDSSGIR 350
    LYYTAKLRRF NAGIMELGLV YTPVMAIPPR ETAFILTGYC TDKCTQLALP 400
    PSGIHIFASQ LHTHLTGRKV VTVLVRDGRE WEIVNQDNHY SPHFQEIRML 450
    KKVVSVHPGD VLITSCTYNT EDRELATVGG FGILEEMCVN YVHYYPQTQL 500
    ELCKSAVDAG FLQKYFHLIN RFNNEDVCTC PQASVSQQFT SVPWNSFNRD 550
    VLKALYSFAP ISMHCNKSSA VRFQGEWNLQ PLPKVISTLE EPTPQCPTSQ 600
    GRSPAGPTVV SIGGGKG 617
    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 DB00988. Dopamine.
    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.
    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

    ArrayExpressi P09172.
    Bgeei P09172.
    CleanExi HS_DBH.
    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

    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 1, 2014
    This is version 164 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