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P14416 (DRD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D(2) dopamine receptor
Alternative name(s):
Dopamine D2 receptor
Gene names
Name:DRD2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase By similarity. Ref.17 Ref.18

Subunit structure

Forms homo- and heterooligomers with DRD4. The interaction with DRD4 may modulate agonist-induced downstream signaling. Interacts with GPRASP1, PPP1R9B and CLIC6 By similarity. Interacts with CADPS and CADPS2. Interacts with ARRB2 By similarity. Interacts with GNAI1. Interacts with GNAI2 isoform sGi2 the interaction allows the creation of an intracellular pool of DRD2 that can be released to cell surface upon agonist stimulation. Interacts with HTR2A. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.17.

Polymorphism

Genetic variations in DRD2 may determine the genetic susceptibility to alcoholism [MIM:103780]. Genetic variations in DRD2 might be a protective factor against the development of withdrawal symptoms but might also be a risk factor in a highly burdened subgroup of alcoholics with a paternal and grandpaternal history of alcoholism and might contribute to suicide risk in alcoholics.

Involvement in disease

Dystonia 11 (DYT11) [MIM:159900]: A myoclonic dystonia. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT11 is characterized by involuntary lightning jerks and dystonic movements and postures alleviated by alcohol. Inheritance is autosomal dominant. The age of onset, pattern of body involvement, presence of myoclonus and response to alcohol are all variable.
Note: The gene represented in this entry may be involved in disease pathogenesis. DRD2 mutations in myoclonic dystonia patients are rare, and their contribution to disease phenotype is unclear (Ref.23). Ref.21 Ref.23

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dystonia
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor internalization

Inferred from electronic annotation. Source: Ensembl

Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

adenohypophysis development

Inferred from sequence or structural similarity. Source: BHF-UCL

adenylate cyclase-inhibiting dopamine receptor signaling pathway

Inferred from direct assay PubMed 1331329Ref.2PubMed 1331329. Source: BHF-UCL

adult walking behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

arachidonic acid secretion

Inferred from direct assay PubMed 8301582. Source: BHF-UCL

associative learning

Inferred from sequence or structural similarity. Source: BHF-UCL

auditory behavior

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

behavioral response to cocaine

Inferred from sequence or structural similarity. Source: BHF-UCL

behavioral response to ethanol

Inferred from sequence or structural similarity. Source: BHF-UCL

branching morphogenesis of a nerve

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular calcium ion homeostasis

Inferred by curator PubMed 7921596. Source: BHF-UCL

cerebral cortex GABAergic interneuron migration

Inferred from sequence or structural similarity. Source: BHF-UCL

circadian regulation of gene expression

Inferred from sequence or structural similarity. Source: BHF-UCL

dopamine metabolic process

Inferred by curator PubMed 8301582. Source: BHF-UCL

feeding behavior

Inferred from electronic annotation. Source: Ensembl

grooming behavior

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from direct assay PubMed 1331329PubMed 1331329. Source: BHF-UCL

locomotory behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

long-term memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of adenylate cyclase activity

Inferred from direct assay Ref.2. Source: BHF-UCL

negative regulation of blood pressure

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell migration

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of circadian sleep/wake cycle, sleep

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

negative regulation of dopamine receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of dopamine secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein secretion

Inferred from direct assay PubMed 16839358. Source: BHF-UCL

negative regulation of synaptic transmission, glutamatergic

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of voltage-gated calcium channel activity

Inferred from direct assay PubMed 7921596. Source: BHF-UCL

neurological system process involved in regulation of systemic arterial blood pressure

Inferred from sequence or structural similarity. Source: BHF-UCL

neuron-neuron synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

orbitofrontal cortex development

Inferred from electronic annotation. Source: Ensembl

peristalsis

Inferred from sequence or structural similarity. Source: BHF-UCL

phosphatidylinositol metabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

phospholipase C-activating dopamine receptor signaling pathway

Inferred from genetic interaction PubMed 17194762. Source: MGI

pigmentation

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of G-protein coupled receptor protein signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytokinesis

Inferred from mutant phenotype PubMed 22888021. Source: UniProt

positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway

Inferred from direct assay PubMed 1331329PubMed 1331329. Source: BHF-UCL

positive regulation of dopamine uptake involved in synaptic transmission

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of growth hormone secretion

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of long-term synaptic potentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of receptor internalization

Inferred from electronic annotation. Source: Ensembl

positive regulation of renal sodium excretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of urine volume

Inferred from electronic annotation. Source: Ensembl

prepulse inhibition

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cAMP metabolic process

Inferred from direct assay PubMed 8666994. Source: BHF-UCL

regulation of dopamine uptake involved in synaptic transmission

Inferred by curator PubMed 8301582. Source: BHF-UCL

regulation of heart rate

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of locomotion involved in locomotory behavior

Inferred from electronic annotation. Source: Ensembl

regulation of long-term neuronal synaptic plasticity

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

regulation of potassium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of sodium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of synapse structural plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic transmission, GABAergic

Inferred from sequence or structural similarity. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

response to amphetamine

Inferred from sequence or structural similarity. Source: BHF-UCL

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to cocaine

Inferred from sequence or structural similarity. Source: BHF-UCL

response to drug

Inferred from sequence or structural similarity. Source: BHF-UCL

response to histamine

Inferred from direct assay PubMed 16839358. Source: BHF-UCL

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to inactivity

Inferred from electronic annotation. Source: Ensembl

response to iron ion

Inferred from electronic annotation. Source: Ensembl

response to light stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

response to morphine

Inferred from sequence or structural similarity. Source: BHF-UCL

response to nicotine

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

sensory perception of smell

Inferred from sequence or structural similarity. Source: BHF-UCL

striatum development

Inferred from electronic annotation. Source: Ensembl

synapse assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

temperature homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

visual learning

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentacrosomal vesicle

Inferred from electronic annotation. Source: Ensembl

axon

Inferred from sequence or structural similarity. Source: BHF-UCL

axon terminus

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from sequence or structural similarity. Source: BHF-UCL

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred by curator Ref.2. Source: BHF-UCL

lateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

perikaryon

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

sperm flagellum

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionadrenergic receptor activity

Inferred from electronic annotation. Source: InterPro

dopamine binding

Inferred from electronic annotation. Source: Ensembl

dopamine neurotransmitter receptor activity, coupled via Gi/Go

Inferred from direct assay PubMed 8301582Ref.2. Source: BHF-UCL

drug binding

Inferred from direct assay PubMed 8413587. Source: BHF-UCL

identical protein binding

Inferred from physical interaction PubMed 18668123. Source: IntAct

potassium channel regulator activity

Non-traceable author statement PubMed 12297500. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P14416-1)

Also known as: D2(Long);

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P14416-2)

Also known as: D2(Short);

The sequence of this isoform differs from the canonical sequence as follows:
     242-270: Missing.
Isoform 3 (identifier: P14416-3)

Also known as: D2(Longer);

The sequence of this isoform differs from the canonical sequence as follows:
     270-270: V → VVQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443D(2) dopamine receptor
PRO_0000069387

Regions

Topological domain1 – 3737Extracellular By similarity
Transmembrane38 – 6023Helical; Name=1; By similarity
Topological domain61 – 7010Cytoplasmic By similarity
Transmembrane71 – 9323Helical; Name=2; By similarity
Topological domain94 – 10815Extracellular By similarity
Transmembrane109 – 13022Helical; Name=3; By similarity
Topological domain131 – 15121Cytoplasmic By similarity
Transmembrane152 – 17221Helical; Name=4; By similarity
Topological domain173 – 18816Extracellular By similarity
Transmembrane189 – 21325Helical; Name=5; By similarity
Topological domain214 – 373160Cytoplasmic By similarity
Transmembrane374 – 39522Helical; Name=6; By similarity
Topological domain396 – 40914Extracellular By similarity
Transmembrane410 – 43122Helical; Name=7; By similarity
Topological domain432 – 44312Cytoplasmic By similarity
Region190 – 1978Agonist binding By similarity
Region211 – 373163Interaction with PPP1R9B By similarity
Region386 – 3949Agonist binding By similarity

Sites

Binding site1141Agonist By similarity
Site1941Important for receptor activation By similarity
Site1971Important for receptor activation By similarity

Amino acid modifications

Glycosylation51N-linked (GlcNAc...) Potential
Glycosylation171N-linked (GlcNAc...) Potential
Glycosylation231N-linked (GlcNAc...) Potential
Disulfide bond107 ↔ 182 By similarity
Disulfide bond399 ↔ 401 By similarity

Natural variations

Alternative sequence242 – 27029Missing in isoform 2.
VSP_001870
Alternative sequence2701V → VVQ in isoform 3.
VSP_026455
Natural variant1541V → I in DYT11; uncertain pathological significance; the mutation does not affect functional properties. Ref.21 Ref.23
Corresponds to variant rs104894220 [ dbSNP | Ensembl ].
VAR_017143
Natural variant3101P → S.
Corresponds to variant rs1800496 [ dbSNP | Ensembl ].
VAR_014674
Natural variant3111S → C May be associated with a higher risk for schizophrenia. Ref.20
Corresponds to variant rs1801028 [ dbSNP | Ensembl ].
VAR_003462
Natural variant3271K → E. Ref.24
Corresponds to variant rs71653614 [ dbSNP | Ensembl ].
VAR_064579

Experimental info

Sequence conflict401L → R in AAB26819. Ref.7

Secondary structure

... 443
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (D2(Long)) [UniParc].

Last modified April 1, 1990. Version 2.
Checksum: 9BF8EA36C988A2E2

FASTA44350,619
        10         20         30         40         50         60 
MDPLNLSWYD DDLERQNWSR PFNGSDGKAD RPHYNYYATL LTLLIAVIVF GNVLVCMAVS 

        70         80         90        100        110        120 
REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA 

       130        140        150        160        170        180 
SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMISIVW VLSFTISCPL LFGLNNADQN 

       190        200        210        220        230        240 
ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRRRR KRVNTKRSSR AFRAHLRAPL 

       250        260        270        280        290        300 
KGNCTHPEDM KLCTVIMKSN GSFPVNRRRV EAARRAQELE MEMLSSTSPP ERTRYSPIPP 

       310        320        330        340        350        360 
SHHQLTLPDP SHHGLHSTPD SPAKPEKNGH AKDHPKIAKI FEIQTMPNGK TRTSLKTMSR 

       370        380        390        400        410        420 
RKLSQQKEKK ATQMLAIVLG VFIICWLPFF ITHILNIHCD CNIPPVLYSA FTWLGYVNSA 

       430        440 
VNPIIYTTFN IEFRKAFLKI LHC 

« Hide

Isoform 2 (D2(Short)) [UniParc].

Checksum: BFC25AC601DFDC7F
Show »

FASTA41447,347
Isoform 3 (D2(Longer)) [UniParc].

Checksum: 111674E96E087FD6
Show »

FASTA44550,847

References

« Hide 'large scale' references
[1]"The major dopamine D2 receptor: molecular analysis of the human D2A subtype."
Selbie L.A., Hayes G., Shine J.
DNA 8:683-689(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The dopamine D2 receptor: two molecular forms generated by alternative splicing."
Dal-Toso R., Sommer B., Ewert M., Herb A., Pritchett D.B., Bach A., Shivers B.D., Seeburg P.H.
EMBO J. 8:4025-4034(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
[3]"Human retina D2 receptor cDNAs have multiple polyadenylation sites and differ from a pituitary clone at the 5' non-coding region."
Robakis N.K., Mohamadi M., Fu D.Y., Sambamurti K., Refolo L.M.
Nucleic Acids Res. 18:1299-1299(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[4]"Cloning of the cDNA and gene for a human D2 dopamine receptor."
Grandy D.K., Marchionni M.A., Makam H., Stofko R.E., Alfano M., Frothingham L., Fischer J.B., Burke-Howie K.J., Bunzow J.R., Server A.C., Civelli O.
Proc. Natl. Acad. Sci. U.S.A. 86:9762-9766(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Molecular cloning and expression of a dopamine D2 receptor from human retina."
Stormann T.M., Gdula D.C., Weiner D.M., Brann M.R.
Mol. Pharmacol. 37:1-6(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[6]"DNA homology screening: isolation and characterization of the human D2A dopamine receptor subtype."
Selbie L.A., Hayes G., Shine J.
Adv. Second Messenger Phosphoprotein Res. 24:9-14(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[7]"Structure and expression of human and rat D2 dopamine receptor genes."
Araki K., Kuwano R., Morii K., Hayashi S., Minoshima S., Shimizu N., Katagiri T., Usui H., Kumanishi T., Takahashi Y.
Neurochem. Int. 21:91-98(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]"D2 dopamine receptors in the human retina: cloning of cDNA and localization of mRNA."
Dearry A., Falardeau P., Shores C., Caron M.G.
Cell. Mol. Neurobiol. 11:437-453(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[9]"Schizophrenia: normal sequence in the dopamine D2 receptor region that couples to G-proteins. DNA polymorphisms in D2."
Seeman P., Ohara K., Ulpian C., Seeman M.V., Jellinger K., Tol H.H., Niznik H.B.
Neuropsychopharmacology 8:137-142(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Tissue: Brain.
[10]"New dopamine receptor, D2(Longer), with unique TG splice site, in human brain."
Seeman P., Nam D., Ulpian C., Liu I.S.C., Tallerico T.
Brain Res. Mol. Brain Res. 76:132-141(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Corpus striatum.
[11]"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
[12]Kidd K.K.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[13]"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] (ISOFORM 1).
Tissue: Lung.
[14]"Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS)."
Binda A.V., Kabbani N., Levenson R.
Biochem. Pharmacol. 69:1451-1461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CADPS AND CADPS2.
[15]"Role of a Galphai2 protein splice variant in the formation of an intracellular dopamine D2 receptor pool."
Lopez-Aranda M.F., Acevedo M.J., Gutierrez A., Koulen P., Khan Z.U.
J. Cell Sci. 120:2171-2178(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GNAI2.
[16]"Dopamine D2 and D4 receptor heteromerization and its allosteric receptor-receptor interactions."
Borroto-Escuela D.O., Van Craenenbroeck K., Romero-Fernandez W., Guidolin D., Woods A.S., Rivera A., Haegeman G., Agnati L.F., Tarakanov A.O., Fuxe K.
Biochem. Biophys. Res. Commun. 404:928-934(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMOOLIGOMERIZATION, INTERACTION WITH DRD4.
[17]"Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine D2 receptors."
Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.
Neuropharmacology 61:770-777(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HTR2A, FUNCTION, SUBCELLULAR LOCATION.
[18]"Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity."
Johnston C.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 104:2001-2006(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 208-226 IN COMPLEX WITH GNAI1, INTERACTION WITH GNAI1, FUNCTION.
[19]Erratum
Johnston C.A., Siderovski D.P.
Proc. Natl. Acad. Sci. U.S.A. 109:1808-1808(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: RETRACTION.
[20]"A structural polymorphism of human dopamine D2 receptor, D2(Ser311->Cys)."
Itokawa M., Arinami T., Futamura N., Hamaguchi H., Toru M.
Biochem. Biophys. Res. Commun. 196:1369-1375(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-311.
[21]"Association of a missense change in the D2 dopamine receptor with myoclonus dystonia."
Klein C., Brin M.F., Kramer P., Sena-Esteves M., de Leon D., Doheny D., Bressman S., Fahn S., Breakefield X.O., Ozelius L.J.
Proc. Natl. Acad. Sci. U.S.A. 96:5173-5176(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DYT11 ILE-154.
[22]"Association of the -141C Del variant of the dopamine D2 receptor (DRD2) with positive family history and suicidality in German alcoholics."
Johann M., Putzhammer A., Eichhammer P., Wodarz N.
Am. J. Med. Genet. B Neuropsychiatr. Genet. 132:46-49(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
[23]"Evaluation of the role of the D2 dopamine receptor in myoclonus dystonia."
Klein C., Gurvich N., Sena-Esteves M., Bressman S., Brin M.F., Ebersole B.J., Fink S., Forsgren L., Friedman J., Grimes D., Holmgren G., Kyllerman M., Lang A.E., de Leon D., Leung J., Prioleau C., Raymond D., Sanner G. expand/collapse author list , Saunders-Pullman R., Vieregge P., Wahlstrom J., Breakefield X.O., Kramer P.L., Ozelius L.J., Sealfon S.C.
Ann. Neurol. 47:369-373(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT DYT11 ILE-154.
[24]"A population-specific HTR2B stop codon predisposes to severe impulsivity."
Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., Peltonen L., Virkkunen M., Goldman D.
Nature 468:1061-1066(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GLU-327.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30625 mRNA. Translation: AAA88024.1.
X51645 mRNA. Translation: CAB56463.1.
X51646 Genomic DNA. Translation: CAB37869.1.
X51362 mRNA. Translation: CAA35746.1.
M29066 mRNA. Translation: AAA52761.1.
S62137 mRNA. Translation: AAB26819.1.
S69899 mRNA. Translation: AAB20571.1.
S58589 expand/collapse EMBL AC list , S58577, S58584, S58586, S58588 Genomic DNA. Translation: AAB26274.1.
AF176812 mRNA. Translation: AAF61479.1.
AB065860 Genomic DNA. Translation: BAC06078.1.
AF050737 Genomic DNA. Translation: AAC78779.1.
BC021195 mRNA. Translation: AAH21195.1.
PIRDYHUD2. S08417.
RefSeqNP_000786.1. NM_000795.3.
NP_057658.2. NM_016574.3.
XP_005271482.1. XM_005271425.2.
UniGeneHs.73893.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1I15model-A34-58[»]
B72-97[»]
C108-129[»]
D153-172[»]
E190-210[»]
F371-396[»]
G403-426[»]
2YOUX-ray2.19B/C430-443[»]
ProteinModelPortalP14416.
SMRP14416. Positions 7-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108147. 11 interactions.
DIPDIP-5977N.
IntActP14416. 4 interactions.
MINTMINT-201447.
STRING9606.ENSP00000354859.

Chemistry

BindingDBP14416.
ChEMBLCHEMBL2111460.
DrugBankDB01063. Acetophenazine.
DB00915. Amantadine.
DB00714. Apomorphine.
DB01238. Aripiprazole.
DB01200. Bromocriptine.
DB00490. Buspirone.
DB00248. Cabergoline.
DB01038. Carphenazine.
DB00477. Chlorpromazine.
DB01239. Chlorprothixene.
DB00568. Cinnarizine.
DB00363. Clozapine.
DB01184. Domperidone.
DB00450. Droperidol.
DB00696. Ergotamine.
DB00875. Flupenthixol.
DB00623. Fluphenazine.
DB04842. Fluspirilene.
DB00502. Haloperidol.
DB01235. Levodopa.
DB00589. Lisuride.
DB00408. Loxapine.
DB00933. Mesoridazine.
DB01233. Metoclopramide.
DB00805. Minaprine.
DB01618. Molindone.
DB00334. Olanzapine.
DB01267. Paliperidone.
DB01186. Pergolide.
DB00850. Perphenazine.
DB01100. Pimozide.
DB00413. Pramipexole.
DB00433. Prochlorperazine.
DB00420. Promazine.
DB01069. Promethazine.
DB00777. Propiomazine.
DB01224. Quetiapine.
DB00409. Remoxipride.
DB00734. Risperidone.
DB00268. Ropinirole.
DB06144. Sertindole.
DB00391. Sulpiride.
DB00372. Thiethylperazine.
DB00679. Thioridazine.
DB00752. Tranylcypromine.
DB00831. Trifluoperazine.
DB00508. Triflupromazine.
DB00246. Ziprasidone.
DB01624. Zuclopenthixol.
GuidetoPHARMACOLOGY215.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP14416.

Polymorphism databases

DMDM118206.

Proteomic databases

PaxDbP14416.
PRIDEP14416.

Protocols and materials databases

DNASU1813.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346454; ENSP00000278597; ENSG00000149295. [P14416-2]
ENST00000355319; ENSP00000347474; ENSG00000149295. [P14416-3]
ENST00000362072; ENSP00000354859; ENSG00000149295. [P14416-1]
ENST00000538967; ENSP00000438215; ENSG00000149295. [P14416-3]
ENST00000542968; ENSP00000442172; ENSG00000149295. [P14416-1]
GeneID1813.
KEGGhsa:1813.
UCSCuc001pnz.3. human. [P14416-1]
uc001pob.4. human. [P14416-2]

Organism-specific databases

CTD1813.
GeneCardsGC11M113280.
HGNCHGNC:3023. DRD2.
HPAHPA015691.
MIM103780. phenotype.
126450. gene.
159900. phenotype.
neXtProtNX_P14416.
Orphanet36899. Myoclonus-dystonia syndrome.
PharmGKBPA27478.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG309657.
HOVERGENHBG106962.
KOK04145.
OMANSVKHSR.
OrthoDBEOG769ZMG.
PhylomeDBP14416.
TreeFamTF334382.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP14416.

Gene expression databases

ArrayExpressP14416.
BgeeP14416.
CleanExHS_DRD2.
GenevestigatorP14416.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR002233. ADR_fam.
IPR001922. Dopamine_D2_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24248. PTHR24248. 1 hit.
PTHR24248:SF13. PTHR24248:SF13. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00567. DOPAMINED2R.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14416.
GeneWikiDopamine_receptor_D2.
GenomeRNAi1813.
NextBio7389.
PROP14416.
SOURCESearch...

Entry information

Entry nameDRD2_HUMAN
AccessionPrimary (citable) accession number: P14416
Secondary accession number(s): Q9NZR3, Q9UPA9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 1, 1990
Last modified: April 16, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries