P35462 (DRD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
D(3) dopamine receptor

Alternative name(s):
Dopamine D3 receptor

Gene names

Name:

DRD3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	400 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation. Ref.9
Subunit structure	Interacts with CLIC6 By similarity. Interacts with GRK4. Interacts with PALM. Ref.8 Ref.9
Subcellular location	Cell membrane; Multi-pass membrane protein. Note: Both membrane-bound and scattered in the cytoplasm during basal conditions. Receptor stimulation results in the rapid internalization and sequestration of the receptors at the perinuclear area (5 and 15 minutes), followed by the dispersal of the receptors to the membrane (30 minutes). DRD3 and GRK4 co-localize in lipid rafts of renal proximal tubule cells. Ref.9
Tissue specificity	Brain.
Post-translational modification	Phosphorylated by GRK4 (GRK4-alpha and GRK4-gamma). Ref.9
Involvement in disease	Tremor, hereditary essential 1 (ETM1) [MIM:190300]: A common movement disorder mainly characterized by postural tremor of the arms. Head, legs, trunk, voice, jaw, and facial muscles also may be involved. The condition can be aggravated by emotions, hunger, fatigue and temperature extremes, and may cause a functional disability or even incapacitation. Inheritance is autosomal dominant. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.15 Ref.16
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Sequence caution	The sequence AAA03543.1 differs from that shown. Reason: Frameshift at position 288. The sequence AAA64369.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor internalization Inferred from direct assay PubMed 18424554. Source: BHF-UCL adenylate cyclase-activating dopamine receptor signaling pathway Inferred from direct assay PubMed 18424554. Source: BHF-UCL adenylate cyclase-inhibiting dopamine receptor signaling pathway Inferred from direct assay PubMed 18424554PubMed 7907363. Source: BHF-UCL arachidonic acid secretion Inferred from direct assay PubMed 8301582. Source: BHF-UCL behavioral response to cocaine Inferred from expression pattern PubMed 8815892. Source: BHF-UCL cellular calcium ion homeostasis Inferred from direct assay PubMed 7911712. 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 locomotory behavior Inferred from sequence or structural similarity. Source: BHF-UCL musculoskeletal movement, spinal reflex action Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of adenylate cyclase activity Inferred from direct assay PubMed 7907363. Source: BHF-UCL negative regulation of blood pressure Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of dopamine receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of oligodendrocyte differentiation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of protein kinase B signaling cascade 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 sodium:hydrogen antiporter activity Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of dopamine receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of mitosis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of renal sodium excretion Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara prepulse inhibition Inferred from mutant phenotype PubMed 18325483. Source: BHF-UCL regulation of blood volume by renin-angiotensin Inferred from electronic annotation. Source: Compara regulation of circadian sleep/wake cycle, sleep Inferred from electronic annotation. Source: Compara regulation of dopamine secretion Inferred from sequence or structural similarity. Source: BHF-UCL regulation of dopamine uptake involved in synaptic transmission Inferred by curator PubMed 8301582. Source: BHF-UCL regulation of lipid metabolic process Inferred from electronic annotation. Source: Compara regulation of locomotion Inferred from electronic annotation. Source: Compara regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara response to amphetamine Inferred from electronic annotation. Source: Compara 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 morphine Inferred from sequence or structural similarity. Source: BHF-UCL social behavior Non-traceable author statement PubMed 12860355. Source: BHF-UCL synaptic transmission, dopaminergic Inferred from electronic annotation. Source: Compara visual learning Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	apical part of cell Inferred from electronic annotation. Source: Compara cell projection Inferred from electronic annotation. Source: Compara endocytic vesicle Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from direct assay PubMed 8413587. Source: BHF-UCL
Molecular_function	dopamine binding Inferred from electronic annotation. Source: Compara dopamine neurotransmitter receptor activity, coupled via Gi/Go Inferred from direct assay PubMed 8301582. Source: BHF-UCL drug binding Inferred from direct assay PubMed 8413587. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P35462-1)

Also known as: D3;

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 3 (identifier: P35462-3)

The sequence of this isoform differs from the canonical sequence as follows:
     287-320: SPTIAPKLSLEVRKLSNGRLSTSLKLGPLQPRGV → M

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 400

400

D(3) dopamine receptor

PRO_0000069397

Regions

Topological domain

1 – 32

32

Extracellular Probable

Transmembrane

33 – 55

23

Helical; Name=1

Topological domain

56 – 65

10

Cytoplasmic Ref.10

Transmembrane

66 – 88

23

Helical; Name=2

Topological domain

89 – 104

16

Extracellular Ref.10

Transmembrane

105 – 126

22

Helical; Name=3

Topological domain

127 – 149

23

Cytoplasmic Ref.10

Transmembrane

150 – 170

21

Helical; Name=4

Topological domain

171 – 187

17

Extracellular Ref.10

Transmembrane

188 – 212

25

Helical; Name=5

Topological domain

213 – 329

117

Cytoplasmic Ref.10

Transmembrane

330 – 351

22

Helical; Name=6

Topological domain

352 – 366

15

Extracellular Ref.10

Transmembrane

367 – 388

22

Helical; Name=7

Topological domain

389 – 400

12

Cytoplasmic Ref.10

Region

189 – 196

8

Agonist binding

Region

342 – 350

9

Agonist binding

Sites

Binding site

110

1

Agonist

Amino acid modifications

Glycosylation

12

1

N-linked (GlcNAc...) Potential

Glycosylation

19

1

N-linked (GlcNAc...) Potential

Glycosylation

97

1

N-linked (GlcNAc...) Potential

Glycosylation

173

1

N-linked (GlcNAc...) Potential

Disulfide bond

103 ↔ 181

Ref.10

Disulfide bond

355 ↔ 358

Ref.10

Natural variations

Alternative sequence

287 – 320

34

SPTIA…QPRGV → M in isoform 3.

VSP_040570

Natural variant

9

1

S → G Associated with susceptibility to ETM1; gain of function. Ref.5 Ref.7 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
Corresponds to variant rs6280 [ dbSNP | Ensembl ].

VAR_003463

Experimental info

Sequence conflict

396

1

K → L in AAH95510. Ref.7

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

400

Helix Strand Turn

Details...

Helix

35 – 56

22

Helix

63 – 81

19

Helix

83 – 91

9

Helix

100 – 133

34

Helix

135 – 140

6

Beta strand

143 – 145

3

Helix

147 – 169

23

Turn

170 – 172

3

Helix

186 – 196

11

Helix

198 – 216

19

Helix

322 – 353

32

Helix

362 – 386

25

Helix

388 – 398

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (D3) [UniParc]. Last modified November 1, 1995. Version 2. Checksum: 2CDA789D78378DDA	FASTA	400	44,225
	10 20 30 40 50 60 MASLSQLSSH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL 70 80 90 100 110 120 QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN 130 140 150 160 170 180 LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV 190 200 210 220 230 240 CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ 250 260 270 280 290 300 QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLSPTI APKLSLEVRK 310 320 330 340 350 360 LSNGRLSTSL KLGPLQPRGV PLREKKATQM VAIVLGAFIV CWLPFFLTHV LNTHCQTCHV 370 380 390 400 SPELYSATTW LGYVNSALNP VIYTTFNIEF RKAFLKILSC
	Isoform 3 [UniParc]. Checksum: 40F7FFA4519042FD	FASTA	367	40,760
	10 20 30 40 50 60 MASLSQLSSH LNYTCGAENS TGASQARPHA YYALSYCALI LAIVFGNGLV CMAVLKERAL 70 80 90 100 110 120 QTTTNYLVVS LAVADLLVAT LVMPWVVYLE VTGGVWNFSR ICCDVFVTLD VMMCTASILN 130 140 150 160 170 180 LCAISIDRYT AVVMPVHYQH GTGQSSCRRV ALMITAVWVL AFAVSCPLLF GFNTTGDPTV 190 200 210 220 230 240 CSISNPDFVI YSSVVSFYLP FGVTVLVYAR IYVVLKQRRR KRILTRQNSQ CNSVRPGFPQ 250 260 270 280 290 300 QTLSPDPAHL ELKRYYSICQ DTALGGPGFQ ERGGELKREE KTRNSLMPLR EKKATQMVAI 310 320 330 340 350 360 VLGAFIVCWL PFFLTHVLNT HCQTCHVSPE LYSATTWLGY VNSALNPVIY TTFNIEFRKA FLKILSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene cloning of human dopaminergic D3 receptor and identification of its chromosome." Giros B., Martres M.-P., Sokoloff P., Schwartz J.-C. C. R. Acad. Sci. III, Sci. Vie 311:501-508(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Selective loss of dopamine D3-type receptor mRNA expression in parietal and motor cortices of patients with chronic schizophrenia." Schmauss C., Haroutunian V., Davis K.L., Davidson M. Proc. Natl. Acad. Sci. U.S.A. 90:8942-8946(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[3]	"On the origin of mRNA encoding the truncated dopamine D3-type receptor D3nf and detection of D3nf-like immunoreactivity in human brain." Liu K., Bergson C., Levenson R., Schmauss C. J. Biol. Chem. 269:29220-29226(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. Tissue: Brain.
[4]	Fishburn C.S., Park B.-H., Fuchs S. Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-9.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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), VARIANT GLY-9.
[8]	"Paralemmin interacts with D3 dopamine receptors: implications for membrane localization and cAMP signaling." Basile M., Lin R., Kabbani N., Karpa K., Kilimann M., Simpson I., Kester M. Arch. Biochem. Biophys. 446:60-68(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PALM.
[9]	"G protein-coupled receptor kinase 4 (GRK4) regulates the phosphorylation and function of the dopamine D3 receptor." Villar V.A.M., Jones J.E., Armando I., Palmes-Saloma C., Yu P., Pascua A.M., Keever L., Arnaldo F.B., Wang Z., Luo Y., Felder R.A., Jose P.A. J. Biol. Chem. 284:21425-21434(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY GRK4, SUBCELLULAR LOCATION, INTERACTION WITH GRK4, FUNCTION.
[10]	"Structure of the human dopamine D3 receptor in complex with a D2/D3 selective antagonist." Chien E.Y., Liu W., Zhao Q., Katritch V., Han G.W., Hanson M.A., Shi L., Newman A.H., Javitch J.A., Cherezov V., Stevens R.C. Science 330:1091-1095(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH THE ANTAGONIST ETICLOPRIDE, DISULFIDE BONDS, MEMBRANE TOPOLOGY.
[11]	"Amino-acid substitution in the dopamine D3 receptor as useful polymorphism for investigating psychiatric disorders." Lannfelt T., Sokoloff P., Martres M.-P., Pilon C., Giros B., Joensson E., Sedvall G., Schwartz J.-C. Psychiatr. Genet. 2:249-256(1992) Cited for: VARIANT GLY-9.
[12]	"Further evidence of no association between Ser9Gly polymorphism of dopamine D3 receptor gene and schizophrenia." Chen C.-H., Liu M.-Y., Wei F.-C., Koong F.-J., Hwu H.-G., Hsiao K.-J. Am. J. Med. Genet. 74:40-43(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-9.
[13]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-9.
[14]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[15]	"Linkage with the Ser9Gly DRD3 polymorphism in essential tremor families." Lucotte G., Lagarde J.-P., Funalot B., Sokoloff P. Clin. Genet. 69:437-440(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-9, INVOLVEMENT IN SUSCEPTIBILITY TO ETM1.
[16]	"A functional variant of the dopamine D3 receptor is associated with risk and age-at-onset of essential tremor." Jeanneteau F., Funalot B., Jankovic J., Deng H., Lagarde J.-P., Lucotte G., Sokoloff P. Proc. Natl. Acad. Sci. U.S.A. 103:10753-10758(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLY-9, CHARACTERIZATION OF VARIANT GLY-9, INVOLVEMENT IN SUSCEPTIBILITY TO ETM1.
+	Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L20469 mRNA. Translation: AAA03543.1. Frameshift.
AH003061 Genomic DNA. Translation: AAA64369.1. Sequence problems.
U32499 mRNA. Translation: AAA73929.1.
AC092896 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79610.1.
BC095510 mRNA. Translation: AAH95510.1.
BC128123 mRNA. Translation: AAI28124.1.

IPI

IPI00018843.
IPI00798154.

PIR

A48258.
A55419.
G01977.

RefSeq

NP_000787.2. NM_000796.3.
NP_387512.3. NM_033663.3.

UniGene

Hs.121478.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PBL	X-ray	2.89	A/B	2-400	[»]

ProteinModelPortal

P35462.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5976N.

STRING

9606.ENSP00000373169.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P35462.

Polymorphism databases

DMDM

1169206.

Proteomic databases

PaxDb

P35462.

PRIDE

P35462.

Protocols and materials databases

DNASU

1814.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000383673; ENSP00000373169; ENSG00000151577.
ENST00000460779; ENSP00000419402; ENSG00000151577.
ENST00000467632; ENSP00000420662; ENSG00000151577.

GeneID

1814.

KEGG

hsa:1814.

UCSC

uc003ebc.1. human.

Organism-specific databases

CTD

1814.

GeneCards

GC03M113847.

H-InvDB

HIX0030774.
HIX0163472.

HGNC

HGNC:3024. DRD3.

MIM

126451. gene.
190300. phenotype.

neXtProt

NX_P35462.

Orphanet

862. Hereditary essential tremor.

PharmGKB

PA27479.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309657.

HOGENOM

HOG000239242.

HOVERGEN

HBG106962.

InParanoid

P35462.

KO

K04146.

OrthoDB

EOG47M1Z5.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P35462.

Bgee

P35462.

CleanEx

HS_DRD3.

Genevestigator

P35462.

GermOnline

ENSG00000151577. Homo sapiens.

Family and domain databases

InterPro

IPR001620. Dopa_D3_rcpt.
IPR000929. Dopamine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

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

PRINTS

PR00568. DOPAMINED3R.
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

BindingDB

P35462.

ChEMBL

CHEMBL234.

DrugBank

DB00714. Apomorphine.
DB01239. Chlorprothixene.
DB00907. Cocaine.
DB01403. Methotrimeprazine.
DB00334. Olanzapine.
DB00413. Pramipexole.
DB00268. Ropinirole.
DB00246. Ziprasidone.

GenomeRNAi

1814.

NextBio

7395.

SOURCE

Search...

Entry information

Entry name

DRD3_HUMAN

Accession

Primary (citable) accession number: P35462
Secondary accession number(s): A1A4V5, Q4VBM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.