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UniProtKB/Swiss-Prot entry P14416


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DRD2_HUMAN
Primary accession number P14416
Secondary accession numbers Q9NZR3 Q9UPA9
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on April 1, 1990 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 120)
Name and origin of the protein
Protein name D(2) dopamine receptor
Synonym Dopamine D2 receptor
Gene name
Name: DRD2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2533064 [NCBI, ExPASy, EBI, Israel, Japan]
Selbie L.A., Hayes G., Shine J.;
"The major dopamine D2 receptor: molecular analysis of the human D2A subtype.";
DNA 8:683-689(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
PubMed=2531656 [NCBI, ExPASy, EBI, Israel, Japan]
Dal-Toso R., Sommer B., Ewert M., Herb A., Pritchett D.B., Bach A., Shivers B.D., Seeburg P.H.;
"The dopamine D2 receptor: two molecular forms generated by alternative splicing.";
EMBO J. 8:4025-4034(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
DOI=10.1093/nar/18.5.1299; PubMed=2138729 [NCBI, ExPASy, EBI, Israel, Japan]
Robakis N.K., Mohamadi M., Fu D.Y., Sambamurti K., Refolo L.M.;
"Human retina D2 receptor cDNAs have multiple polyadenylation sites and differ from a pituitary clone at the 5' non-coding region.";
Nucleic Acids Res. 18:1299-1299(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1073/pnas.86.24.9762; PubMed=2532362 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cloning of the cDNA and gene for a human D2 dopamine receptor.";
Proc. Natl. Acad. Sci. U.S.A. 86:9762-9766(1989).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
PubMed=2137193 [NCBI, ExPASy, EBI, Israel, Japan]
Stormann T.M., Gdula D.C., Weiner D.M., Brann M.R.;
"Molecular cloning and expression of a dopamine D2 receptor from human retina.";
Mol. Pharmacol. 37:1-6(1990).
[6]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=2144985 [NCBI, ExPASy, EBI, Israel, Japan]
Selbie L.A., Hayes G., Shine J.;
"DNA homology screening: isolation and characterization of the human D2A dopamine receptor subtype.";
Adv. Second Messenger Phosphoprotein Res. 24:9-14(1990).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1016/0197-0186(92)90071-X; PubMed=1363862 [NCBI, ExPASy, EBI, Israel, Japan]
Araki K., Kuwano R., Morii K., Hayashi S., Minoshima S., Shimizu N., Katagiri T., Usui H., Kumanishi T., Takahashi Y.;
"Structure and expression of human and rat D2 dopamine receptor genes.";
Neurochem. Int. 21:91-98(1992).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Retina;
DOI=10.1007/BF00734808; PubMed=1835903 [NCBI, ExPASy, EBI, Israel, Japan]
Dearry A., Falardeau P., Shores C., Caron M.G.;
"D2 dopamine receptors in the human retina: cloning of cDNA and localization of mRNA.";
Cell. Mol. Neurobiol. 11:437-453(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=8471125 [NCBI, ExPASy, EBI, Israel, Japan]
Seeman P., Ohara K., Ulpian C., Seeman M.V., Jellinger K., Tol H.H., Niznik H.B.;
"Schizophrenia: normal sequence in the dopamine D2 receptor region that couples to G-proteins. DNA polymorphisms in D2.";
Neuropsychopharmacology 8:137-142(1993).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Corpus striatum;
DOI=10.1016/S0169-328X(99)00343-5; PubMed=10719223 [NCBI, ExPASy, EBI, Israel, Japan]
Seeman P., Nam D., Ulpian C., Liu I.S.C., Tallerico T.;
"New dopamine receptor, D2(Longer), with unique TG splice site, in human brain.";
Brain Res. Mol. Brain Res. 76:132-141(2000).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
Kidd K.K.;
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
INTERACTION WITH CADPS AND CADPS2.
DOI=10.1016/j.bcp.2005.02.015; PubMed=15857609 [NCBI, ExPASy, EBI, Israel, Japan]
Binda A.V., Kabbani N., Levenson R.;
"Regulation of dense core vesicle release from PC12 cells by interaction between the D2 dopamine receptor and calcium-dependent activator protein for secretion (CAPS).";
Biochem. Pharmacol. 69:1451-1461(2005).
[15]
VARIANT CYS-311.
DOI=10.1006/bbrc.1993.2404; PubMed=7902708 [NCBI, ExPASy, EBI, Israel, Japan]
Itokawa M., Arinami T., Futamura N., Hamaguchi H., Toru M.;
"A structural polymorphism of human dopamine D2 receptor, D2(Ser311->Cys).";
Biochem. Biophys. Res. Commun. 196:1369-1375(1993).
[16]
VARIANT DYT11 ILE-154.
DOI=10.1073/pnas.96.9.5173; PubMed=10220438 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Association of a missense change in the D2 dopamine receptor with myoclonus dystonia.";
Proc. Natl. Acad. Sci. U.S.A. 96:5173-5176(1999).
[17]
INVOLVEMENT IN SUSCEPTIBILITY TO ALCOHOLISM.
DOI=10.1002/ajmg.b.30085; PubMed=15389757 [NCBI, ExPASy, EBI, Israel, Japan]
Johann M., Putzhammer A., Eichhammer P., Wodarz N.;
"Association of the -141C Del variant of the dopamine D2 receptor (DRD2) with positive family history and suicidality in German alcoholics.";
Am. J. Med. Genet. B Neuropsychiatr. Genet. 132:46-49(2005).
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: Interacts with GPRASP1, PPP1R9B and CLIC6 (By similarity). Interacts with CADPS and CADPS2.
  • SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    SynonymsD2(Long)
    Isoform IDP14416-1
    This is the isoform sequence displayed in this entry.
    Name2
    SynonymsD2(Short)
    Isoform IDP14416-2
    Features which should be applied to build the isoform sequence: VSP_001870.
    Name3
    SynonymsD2(Longer)
    Isoform IDP14416-3
    Features which should be applied to build the isoform sequence: VSP_026455.
  • 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.
  • DISEASE: It has been suggested that DRD2 is involved in psychiatric disorders; especially in schizophrenia.
  • 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.
  • SIMILARITY: Belongs to the G-protein coupled receptor 1 family [view classification].
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=DRD2";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M30625; AAA88024.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51645; CAB56463.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51646; CAB37869.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X51362; CAA35746.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29066; AAA52761.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S62137; AAB26819.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S69899; AAB20571.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S58589; AAB26274.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S58577; AAB26274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S58584; AAB26274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S58586; AAB26274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S58588; AAB26274.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF176812; AAF61479.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB065860; BAC06078.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF050737; AAC78779.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC021195; AAH21195.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00026590; -.
IPI00219367; -.
IPI00375079; -.
PIR S08417; DYHUD2.
RefSeq NP_000786.1; -.
NP_057658.2; -.
UniGene Hs.73893
3D structure databases
PDB
1I15; Model; -; A=34-58, B=72-97, C=108-129, D=153-172, E=190-210, F=371-396, G=403-426.[ExPASy / RCSB / EBI]
2HLB; X-ray; 2.20 A; C=208-226.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1I15; -.
2HLB; -.
ModBase P14416.
Protein-protein interaction databases
DIP DIP:5977N; -.
Protein family/group databases
GPCRDB P14416; DRD2_HUMAN.
PTM databases
PhosphoSite P14416; -.
Organism-specific databases
GeneCards GC11M112785; -.
H-InvDB HIX0010135; -.
HGNC HGNC:3023; DRD2.
GenAtlas DRD2.
HPA HPA015691; -.
MIM 103780; phenotype. [NCBI / EBI]
126450; gene. [NCBI / EBI]
159900; phenotype. [NCBI / EBI]
608516; phenotype. [NCBI / EBI]
Orphanet 36899; Myoclonic dystonia.
PharmGKB PA27478; -.
Gene expression databases
ArrayExpress P14416; -.
Bgee P14416; -.
CleanEx HS_DRD2; -.
GermOnline ENSG00000149295; Homo sapiens.
Ontologies
GO
GO:0030424; Cellular component: axon (inferred from sequence or structural similarity from UniProtKB).
GO:0030425; Cellular component: dendrite (inferred from sequence or structural similarity from UniProtKB).
GO:0005887; Cellular component: integral to plasma membrane (inferred from direct assay from UniProtKB).
GO:0001670; Molecular function: dopamine D2 receptor activity (inferred from direct assay from UniProtKB).
GO:0008144; Molecular function: drug binding (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0060158; Biological process: activation of phospholipase C activity by dopamine receptor signaling pathway (inferred from genetic interaction from MGI).
GO:0021984; Biological process: adenohypophysis development (inferred from sequence or structural similarity from UniProtKB).
GO:0007628; Biological process: adult walking behavior (inferred from sequence or structural similarity from UniProtKB).
GO:0050482; Biological process: arachidonic acid secretion (inferred from direct assay from UniProtKB).
GO:0008306; Biological process: associative learning (inferred from sequence or structural similarity from UniProtKB).
GO:0007409; Biological process: axonogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0048148; Biological process: behavioral response to cocaine (inferred from sequence or structural similarity from UniProtKB).
GO:0048149; Biological process: behavioral response to ethanol (inferred from sequence or structural similarity from UniProtKB).
GO:0048755; Biological process: branching morphogenesis of a nerve (inferred from sequence or structural similarity from UniProtKB).
GO:0021853; Biological process: cerebral cortex GABAergic interneuron migration (inferred from sequence or structural similarity from UniProtKB).
GO:0032922; Biological process: circadian regulation of gene expression (inferred from sequence or structural similarity from UniProtKB).
GO:0030146; Biological process: diuresis (inferred from sequence or structural similarity from UniProtKB).
GO:0042417; Biological process: dopamine metabolic process (inferred by curator from UniProtKB).
GO:0030147; Biological process: natriuresis (inferred from sequence or structural similarity from UniProtKB).
GO:0045776; Biological process: negative regulation of blood pressure (inferred from sequence or structural similarity from UniProtKB).
GO:0030336; Biological process: negative regulation of cell migration (inferred from sequence or structural similarity from UniProtKB).
GO:0008285; Biological process: negative regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0060160; Biological process: negative regulation of dopamine receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
GO:0051898; Biological process: negative regulation of protein kinase B signaling cascade (inferred from sequence or structural similarity from UniProtKB).
GO:0050709; Biological process: negative regulation of protein secretion (inferred from direct assay from UniProtKB).
GO:0051967; Biological process: negative regulation of synaptic transmission, glutamatergic (inferred from sequence or structural similarity from UniProtKB).
GO:0007270; Biological process: nerve-nerve synaptic transmission (inferred from sequence or structural similarity from UniProtKB).
GO:0001976; Biological process: neurological system process involved in regulation of systemic arterial blood pressure (inferred from sequence or structural similarity from UniProtKB).
GO:0030432; Biological process: peristalsis (inferred from sequence or structural similarity from UniProtKB).
GO:0030384; Biological process: phosphoinositide metabolic process (inferred from sequence or structural similarity from UniProtKB).
GO:0051586; Biological process: positive regulation of dopamine uptake (inferred from sequence or structural similarity from UniProtKB).
GO:0060124; Biological process: positive regulation of growth hormone secretion (inferred from sequence or structural similarity from UniProtKB).
GO:0002052; Biological process: positive regulation of neuroblast proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0060134; Biological process: prepulse inhibition (inferred from sequence or structural similarity from UniProtKB).
GO:0008104; Biological process: protein localization (inferred from sequence or structural similarity from UniProtKB).
GO:0030814; Biological process: regulation of cAMP metabolic process (inferred from direct assay from UniProtKB).
GO:0002027; Biological process: regulation of heart rate (inferred from sequence or structural similarity from UniProtKB).
GO:0048169; Biological process: regulation of long-term neuronal synaptic plasticity (inferred from sequence or structural similarity from UniProtKB).
GO:0043266; Biological process: regulation of potassium ion transport (inferred from sequence or structural similarity from UniProtKB).
GO:0002028; Biological process: regulation of sodium ion transport (inferred from sequence or structural similarity from UniProtKB).
GO:0032228; Biological process: regulation of synaptic transmission, GABAergic (inferred from sequence or structural similarity from UniProtKB).
GO:0051209; Biological process: release of sequestered calcium ion into cytosol (inferred from sequence or structural similarity from UniProtKB).
GO:0001975; Biological process: response to amphetamine (inferred from sequence or structural similarity from UniProtKB).
GO:0042493; Biological process: response to drug (inferred from sequence or structural similarity from UniProtKB).
GO:0034776; Biological process: response to histamine (inferred from direct assay from UniProtKB).
GO:0043278; Biological process: response to morphine (inferred from sequence or structural similarity from UniProtKB).
GO:0007608; Biological process: sensory perception of smell (inferred from sequence or structural similarity from UniProtKB).
GO:0007416; Biological process: synaptogenesis (inferred from sequence or structural similarity from UniProtKB).
GO:0001659; Biological process: temperature homeostasis (inferred from sequence or structural similarity from UniProtKB).
GO:0008542; Biological process: visual learning (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000276; 7TM_GPCR_Rhodpsn.
IPR001922; Dopa_D2_rcpt.
IPR000929; Dopamine_rcpt.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.
PANTHER PTHR19266:SF52; Dopa_D2_rcpt; 1.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00567; DOPAMINED2R.
PR00242; DOPAMINER.
PR00237; GPCRRHODOPSN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P14416; -.
Genome annotation databases
Ensembl ENSG00000149295; Homo sapiens. [Contig view]
GeneID 1813; -.
KEGG hsa:1813; -.
Phylogenomic databases
HOVERGEN P14416; -.
OMA P14416; LNLSWYD.
Other
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 DRD2; Homo sapiens.
GPCRDB-Snakes P14416.
ProtoNet P14416.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell membrane; Disease mutation; Disulfide bond; Dystonia; G-protein coupled receptor; Glycoprotein; Membrane; Polymorphism; Receptor; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   443  443     D(2) dopamine receptor. PRO_0000069387
TOPO_DOM   1    37  37     Extracellular (Potential). 
TRANSMEM   38    60  23     1 (Potential). 
TOPO_DOM   61    71  11     Cytoplasmic (Potential). 
TRANSMEM   72    97  26     2 (Potential). 
TOPO_DOM   98   108  11     Extracellular (Potential). 
TRANSMEM   109   130  22     3 (Potential). 
TOPO_DOM   131   151  21     Cytoplasmic (Potential). 
TRANSMEM   152   174  23     4 (Potential). 
TOPO_DOM   175   186  12     Extracellular (Potential). 
TRANSMEM   187   210  24     5 (Potential). 
TOPO_DOM   211   373  163     Cytoplasmic (Potential). 
TRANSMEM   374   397  24     6 (Potential). 
TOPO_DOM   398   405  8     Extracellular (Potential). 
TRANSMEM   406   429  24     7 (Potential). 
TOPO_DOM   430   443  14     Cytoplasmic (Potential). 
REGION   211   373  163     Interaction with PPP1R9B (By similarity). 
SITE   193   193  1     Implicated in catechol agonist binding (By similarity). 
SITE   194   194  1     Implicated in receptor activation (By similarity). 
SITE   197   197  1     Implicated in receptor activation (By similarity). 
CARBOHYD   5     5        N-linked (GlcNAc...) (Potential). 
CARBOHYD   17    17        N-linked (GlcNAc...) (Potential). 
CARBOHYD   23    23        N-linked (GlcNAc...) (Potential). 
DISULFID   107   182        By similarity. 
VAR_SEQ   242   270        Missing (in isoform 2). VSP_001870
VAR_SEQ   270   270        V -> VVQ (in isoform 3). VSP_026455
VARIANT   154   154  1     V -> I (in DYT11; the contribution to this phenotype is unclear). VAR_017143 
VARIANT   310   310  1     P -> S (in dbSNP:rs1800496 [NCBI]). VAR_014674 
VARIANT   311   311  1     S -> C (associated with schizophrenia; dbSNP:rs1801028 [NCBI]). VAR_003462 
CONFLICT   40    40        L -> R (in Ref. 7; AAB26819). 
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      
Sequence information
Length: 443 AA [This is the length of the unprocessed precursor] Molecular weight: 50619 Da [This is the MW of the unprocessed precursor] CRC64: 9BF8EA36C988A2E2 [This is a checksum on the sequence]
        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 

P14416 in FASTA format

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