Reviewed, UniProtKB/Swiss-Prot P14416 (DRD2_HUMAN)

Names and origin

Protein names

Recommended name:
D(2) dopamine receptor

Alternative name(s):
Dopamine D2 receptor

Gene names

Name:

DRD2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	443 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Subunit structure	Interacts with GPRASP1, PPP1R9B and CLIC6 By similarity. Interacts with CADPS and CADPS2. Interacts with ARRB2 By similarity. Ref.14
Subcellular location	Cell membrane; Multi-pass membrane protein.
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	Defects in DRD2 are associated with dystonia type 11 (DYT11) [MIM:159900]; also known as alcohol-responsive dystonia. DYT11 is 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. Ref.16
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dystonia
Domain	Transmembrane
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	activation of phospholipase C activity by dopamine receptor signaling pathway Inferred from genetic interaction. Source: MGI adenohypophysis development Inferred from sequence or structural similarity. Source: UniProtKB adult walking behavior Inferred from sequence or structural similarity. Source: UniProtKB arachidonic acid secretion Inferred from direct assay. Source: UniProtKB associative learning Inferred from sequence or structural similarity. Source: UniProtKB axonogenesis Inferred from sequence or structural similarity. Source: UniProtKB behavioral response to cocaine Inferred from sequence or structural similarity. Source: UniProtKB behavioral response to ethanol Inferred from sequence or structural similarity. Source: UniProtKB branching morphogenesis of a nerve Inferred from sequence or structural similarity. Source: UniProtKB cerebral cortex GABAergic interneuron migration Inferred from sequence or structural similarity. Source: UniProtKB circadian regulation of gene expression Inferred from sequence or structural similarity. Source: UniProtKB diuresis Inferred from sequence or structural similarity. Source: UniProtKB dopamine metabolic process Inferred by curator. Source: UniProtKB elevation of cytosolic calcium ion concentration during G-protein signaling, coupled to IP3 second messenger (phospholipase C activating) Inferred from direct assay. Source: UniProtKB inhibition of adenylate cyclase activity by dopamine receptor signaling pathway Inferred from direct assay. Source: UniProtKB natriuresis Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of calcium ion transport via voltage-gated calcium channel activity Inferred from direct assay. Source: UniProtKB negative regulation of cell migration Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of dopamine receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein kinase B signaling cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of protein secretion Inferred from direct assay. Source: UniProtKB negative regulation of synaptic transmission, glutamatergic Inferred from sequence or structural similarity. Source: UniProtKB nerve-nerve synaptic transmission Inferred from sequence or structural similarity. Source: UniProtKB neurological system process involved in regulation of systemic arterial blood pressure Inferred from sequence or structural similarity. Source: UniProtKB peristalsis Inferred from sequence or structural similarity. Source: UniProtKB phosphoinositide metabolic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of dopamine uptake Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of growth hormone secretion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neuroblast proliferation Inferred from sequence or structural similarity. Source: UniProtKB prepulse inhibition Inferred from sequence or structural similarity. Source: UniProtKB protein kinase cascade Inferred from direct assay. Source: UniProtKB protein localization Inferred from sequence or structural similarity. Source: UniProtKB regulation of cAMP metabolic process Inferred from direct assay. Source: UniProtKB regulation of heart rate Inferred from sequence or structural similarity. Source: UniProtKB regulation of long-term neuronal synaptic plasticity Inferred from sequence or structural similarity. Source: UniProtKB regulation of potassium ion transport Inferred from sequence or structural similarity. Source: UniProtKB regulation of sodium ion transport Inferred from sequence or structural similarity. Source: UniProtKB regulation of synaptic transmission, GABAergic Inferred from sequence or structural similarity. Source: UniProtKB release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to amphetamine Inferred from sequence or structural similarity. Source: UniProtKB response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to histamine Inferred from direct assay. Source: UniProtKB response to morphine Inferred from sequence or structural similarity. Source: UniProtKB sensory perception of smell Inferred from sequence or structural similarity. Source: UniProtKB synapse assembly Inferred from sequence or structural similarity. Source: UniProtKB temperature homeostasis Inferred from sequence or structural similarity. Source: UniProtKB visual learning Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	axon Inferred from sequence or structural similarity. Source: UniProtKB dendrite Inferred from sequence or structural similarity. Source: UniProtKB integral to plasma membrane Inferred by curator. Source: UniProtKB
Molecular function	dopamine D2 receptor activity Inferred from direct assay. Source: UniProtKB dopamine receptor activity, coupled via Gi/Go Inferred from direct assay. Source: UniProtKB drug binding Inferred from direct assay. Source: UniProtKB potassium channel regulator activity Non-traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 443

443

D(2) dopamine receptor

PRO_0000069387

Regions

Topological domain

1 – 37

37

Extracellular Potential

Transmembrane

38 – 60

23

1 Potential

Topological domain

61 – 71

11

Cytoplasmic Potential

Transmembrane

72 – 97

26

2 Potential

Topological domain

98 – 108

11

Extracellular Potential

Transmembrane

109 – 130

22

3 Potential

Topological domain

131 – 151

21

Cytoplasmic Potential

Transmembrane

152 – 174

23

4 Potential

Topological domain

175 – 186

12

Extracellular Potential

Transmembrane

187 – 210

24

5 Potential

Topological domain

211 – 373

163

Cytoplasmic Potential

Transmembrane

374 – 397

24

6 Potential

Topological domain

398 – 405

8

Extracellular Potential

Transmembrane

406 – 429

24

7 Potential

Topological domain

430 – 443

14

Cytoplasmic Potential

Region

211 – 373

163

Interaction with PPP1R9B By similarity

Sites

Site

193

1

Implicated in catechol agonist binding By similarity

Site

194

1

Implicated in receptor activation By similarity

Site

197

1

Implicated in receptor activation By similarity

Amino acid modifications

Glycosylation

5

1

N-linked (GlcNAc...) Potential

Glycosylation

17

1

N-linked (GlcNAc...) Potential

Glycosylation

23

1

N-linked (GlcNAc...) Potential

Disulfide bond

107 ↔ 182

By similarity

Natural variations

Alternative sequence

242 – 270

29

Missing in isoform 2.

VSP_001870

Alternative sequence

270

1

V → VVQ in isoform 3.

VSP_026455

Natural variant

154

1

V → I in DYT11; the contribution to this phenotype is unclear. Ref.16

VAR_017143

Natural variant

310

1

P → S: dbSNP rs1800496.

VAR_014674

Natural variant

311

1

S → C May be associated with a higher risk for schizophrenia. dbSNP rs1801028.

VAR_003462

Experimental info

Sequence conflict

40

1

L → R in AAB26819. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

443

Helix Strand Turn

Details...

Helix

35 – 56

22

Helix

73 – 96

24

Helix

109 – 128

20

Helix

154 – 171

18

Helix

191 – 209

19

Helix

372 – 395

24

Helix

404 – 425

22

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (D2(Long)) [UniParc]. Last modified April 1, 1990. Version 2. Checksum: 9BF8EA36C988A2E2	FASTA	443	50,619
	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
	Isoform 2 (D2(Short)). Checksum: BFC25AC601DFDC7F	FASTA	414	47,347
	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 KEAARRAQEL EMEMLSSTSP PERTRYSPIP PSHHQLTLPD PSHHGLHSTP DSPAKPEKNG 310 320 330 340 350 360 HAKDHPKIAK IFEIQTMPNG KTRTSLKTMS RRKLSQQKEK KATQMLAIVL GVFIICWLPF 370 380 390 400 410 FITHILNIHC DCNIPPVLYS AFTWLGYVNS AVNPIIYTTF NIEFRKAFLK ILHC
	Isoform 3 (D2(Longer)). Checksum: 111674E96E087FD6	FASTA	445	50,847
	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 VQEAARRAQE LEMEMLSSTS PPERTRYSPI 310 320 330 340 350 360 PPSHHQLTLP DPSHHGLHST PDSPAKPEKN GHAKDHPKIA KIFEIQTMPN GKTRTSLKTM 370 380 390 400 410 420 SRRKLSQQKE KKATQMLAIV LGVFIICWLP FFITHILNIH CDCNIPPVLY SAFTWLGYVN 430 440 SAVNPIIYTT FNIEFRKAFL KILHC

References

	« Hide 'large scale' referencesShow '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: 2533064] [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: 2531656] [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: 2138729] [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: 2532362] [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: 2137193] [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: 2144985] [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: 1363862] [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: 1835903] [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: 8471125] [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: 10719223] [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: 15489334] [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: 15857609] [Abstract] Cited for: INTERACTION WITH CADPS AND CADPS2.
[15]	"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: 7902708] [Abstract] Cited for: VARIANT CYS-311.
[16]	"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: 10220438] [Abstract] Cited for: VARIANT DYT11 ILE-154.
[17]	"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: 15389757] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
+	Additional computationally mapped references.

Web resources

GeneReviews

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 , 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.

IPI

IPI00026590.
IPI00219367.
IPI00375079.

PIR

DYHUD2. S08417.

RefSeq

NP_000786.1.
NP_057658.2.

UniGene

Hs.73893

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1I15	model	-	A	34-58	[»]
			B	72-97	[»]
			C	108-129	[»]
			D	153-172	[»]
			E	190-210	[»]
			F	371-396	[»]
			G	403-426	[»]
2HLB	X-ray	2.20	C	208-226	[»]

SMR

P14416. Positions 33-443.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5977N.

STRING

P14416.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P14416.

Proteomic databases

PRIDE

P14416.

Genome annotation databases

Ensembl

ENST00000362072; ENSP00000354859; ENSG00000149295; Homo sapiens. [Genome view]

GeneID

1813.

KEGG

hsa:1813.

UCSC

uc001pnz.1. human.
uc001pob.2. human.

Organism-specific databases

CTD

1813.

GeneCards

GC11M112785.

H-InvDB

HIX0010135.

HGNC

HGNC:3023. DRD2.

HPA

HPA015691.

MIM

103780. phenotype.
126450. gene.
159900. phenotype.

Orphanet

36899. Myoclonic dystonia.

PharmGKB

PA27478.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14714.

HOVERGEN

HBG106962.

OMA

WYDDDLE.

Enzyme and pathway databases

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

P14416.

Bgee

P14416.

CleanEx

HS_DRD2.

Genevestigator

P14416.

GermOnline

ENSG00000149295. Homo sapiens.

Family and domain databases

InterPro

IPR000276. 7TM_GPCR_Rhodpsn.
IPR001922. Dopa_D2_rcpt.
IPR000929. Dopamine_rcpt.
IPR017452. GPCR_Rhodpsn_supfam.
[Graphical view]

PANTHER

PTHR19266:SF52. Dopa_D2_rcpt. 1 hit.

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00567. DOPAMINED2R.
PR00242. DOPAMINER.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB01063. 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.

NextBio

7389.

SOURCE

Search...

Entry information

Entry name

DRD2_HUMAN

Accession

Primary (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:	March 2, 2010
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.