Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P08913 (ADA2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 166. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-2A adrenergic receptor
Alternative name(s):
Alpha-2 adrenergic receptor subtype C10
Alpha-2A adrenoreceptor
Short name=Alpha-2A adrenoceptor
Short name=Alpha-2AAR
Gene names
Name:ADRA2A
Synonyms:ADRA2R, ADRAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol. Ref.16

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.16.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRA2A sub-subfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: Ensembl

G-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity PubMed 19965390. Source: BHF-UCL

Ras protein signal transduction

Traceable author statement PubMed 8226727. Source: ProtInc

Rho protein signal transduction

Traceable author statement PubMed 9624180. Source: ProtInc

actin cytoskeleton organization

Traceable author statement PubMed 9624180. Source: ProtInc

activation of MAPK activity by adrenergic receptor signaling pathway

Inferred from direct assay Ref.4. Source: BHF-UCL

activation of protein kinase B activity

Inferred from direct assay PubMed 17215105. Source: BHF-UCL

activation of protein kinase activity

Inferred from direct assay PubMed 15653687. Source: BHF-UCL

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

adenylate cyclase-inhibiting adrenergic receptor signaling pathway

Inferred from direct assay Ref.4. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 9624180. Source: ProtInc

cellular response to hormone stimulus

Inferred from genetic interaction PubMed 10948198. Source: BHF-UCL

energy reserve metabolic process

Traceable author statement. Source: Reactome

epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 17215105PubMed 17655843. Source: BHF-UCL

fear response

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from mutant phenotype PubMed 10952463. Source: BHF-UCL

intestinal absorption

Traceable author statement PubMed 17655843. Source: BHF-UCL

negative regulation of adenylate cyclase activity

Inferred from sequence or structural similarity PubMed 1354394. Source: BHF-UCL

negative regulation of adrenergic receptor signaling pathway

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

negative regulation of cAMP biosynthetic process

Inferred from direct assay PubMed 16531006. Source: BHF-UCL

negative regulation of calcium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 1354394. Source: BHF-UCL

negative regulation of calcium ion transport

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

negative regulation of calcium ion-dependent exocytosis

Inferred by curator PubMed 19965390. Source: BHF-UCL

negative regulation of epinephrine secretion

Non-traceable author statement PubMed 16531006. Source: BHF-UCL

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 10952463. Source: BHF-UCL

negative regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from mutant phenotype PubMed 19965390. Source: BHF-UCL

negative regulation of lipid catabolic process

Inferred from genetic interaction PubMed 10948198. Source: BHF-UCL

negative regulation of norepinephrine secretion

Non-traceable author statement PubMed 16531006. Source: BHF-UCL

negative regulation of uterine smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

phospholipase C-activating adrenergic receptor signaling pathway

Inferred from direct assay Ref.4. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 19477270. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype PubMed 17655843. Source: BHF-UCL

positive regulation of cell proliferation

Traceable author statement PubMed 10896916. Source: ProtInc

positive regulation of cytokine production

Inferred from direct assay PubMed 17655843. Source: BHF-UCL

positive regulation of epidermal growth factor-activated receptor activity

Inferred from direct assay PubMed 17655843. Source: BHF-UCL

positive regulation of membrane protein ectodomain proteolysis

Inferred from direct assay PubMed 17655843. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from sequence or structural similarity PubMed 1354394. Source: BHF-UCL

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

positive regulation of wound healing

Inferred from mutant phenotype PubMed 17655843. Source: BHF-UCL

regulation of insulin secretion

Traceable author statement. Source: Reactome

regulation of vasoconstriction

Inferred from electronic annotation. Source: InterPro

signal transduction

Traceable author statement PubMed 10896916Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

thermoception

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasolateral plasma membrane

Traceable author statement PubMed 17655843. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 19477270. Source: BHF-UCL

integral component of plasma membrane

Inferred from direct assay Ref.4PubMed 10948198Ref.1. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay Ref.4. Source: BHF-UCL

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalpha-1B adrenergic receptor binding

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

alpha-2C adrenergic receptor binding

Inferred from physical interaction PubMed 16605244. Source: BHF-UCL

alpha2-adrenergic receptor activity

Inferred from direct assay Ref.4. Source: BHF-UCL

epinephrine binding

Inferred from direct assay Ref.4Ref.1. Source: BHF-UCL

heterotrimeric G-protein binding

Inferred from direct assay Ref.4. Source: BHF-UCL

norepinephrine binding

Inferred from direct assay Ref.1. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 16531006. Source: BHF-UCL

protein heterodimerization activity

Inferred from physical interaction PubMed 16605244. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 16605244. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction PubMed 15653687. Source: BHF-UCL

thioesterase binding

Inferred from physical interaction PubMed 19477270. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Alpha-2A adrenergic receptor
PRO_0000069080

Regions

Topological domain1 – 3333Extracellular By similarity
Transmembrane34 – 5926Helical; Name=1; By similarity
Topological domain60 – 7011Cytoplasmic By similarity
Transmembrane71 – 9626Helical; Name=2; By similarity
Topological domain97 – 10610Extracellular By similarity
Transmembrane107 – 12923Helical; Name=3; By similarity
Topological domain130 – 15122Cytoplasmic By similarity
Transmembrane152 – 17221Helical; Name=4; By similarity
Topological domain173 – 19422Extracellular By similarity
Transmembrane195 – 21723Helical; Name=5; By similarity
Topological domain218 – 374157Cytoplasmic By similarity
Transmembrane375 – 39521Helical; Name=6; By similarity
Topological domain396 – 40914Extracellular By similarity
Transmembrane410 – 42920Helical; Name=7; By similarity
Topological domain430 – 45021Cytoplasmic By similarity

Sites

Site1131Implicated in ligand binding
Site2001Implicated in catechol agonist binding and receptor activation
Site2041Implicated in catechol agonist binding and receptor activation

Amino acid modifications

Lipidation4421S-palmitoyl cysteine By similarity
Glycosylation101N-linked (GlcNAc...) Potential
Glycosylation141N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 188 By similarity

Natural variations

Natural variant2511N → K Rare polymorphism; frequency in Caucasians 0.004 and in African-Americans 0.05; 40% increase in agonist-promoted Gi coupling. Ref.4 Ref.5 Ref.9
Corresponds to variant rs1800035 [ dbSNP | Ensembl ].
VAR_014957
Natural variant4011C → S.
Corresponds to variant rs35658213 [ dbSNP | Ensembl ].
VAR_055908

Experimental info

Mutagenesis791D → N: No change in binding affinity. eliminates guanine nucleotide-sensitive agonist binding. Ref.15
Mutagenesis1131D → N: No binding to yohimbine. Increase in adenylate cyclase activity. Ref.15
Mutagenesis1301D → N: Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding. Ref.15
Mutagenesis2001S → A: Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding. Ref.15
Mutagenesis2041S → A: Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding. Ref.15
Mutagenesis4121F → N: 350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol. Ref.14 Ref.15
Sequence conflict1041A → T in AAA51664. Ref.1
Sequence conflict1241L → P Ref.13
Sequence conflict1571V → C in AAA51664. Ref.1
Sequence conflict333 – 36533PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51664. Ref.1
Sequence conflict333 – 36533PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51665. Ref.2
Sequence conflict3681R → L in AAA51664. Ref.1

Secondary structure

...... 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08913 [UniParc].

Last modified February 1, 1996. Version 3.
Checksum: A703CF262F04E8AC

FASTA45048,957
        10         20         30         40         50         60 
MGSLQPDAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLLTVFG NVLVIIAVFT 

        70         80         90        100        110        120 
SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKAWCEIYL ALDVLFCTSS 

       130        140        150        160        170        180 
IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIITVWVI SAVISFPPLI SIEKKGGGGG 

       190        200        210        220        230        240 
PQPAEPRCEI NDQKWYVISS CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAVA 

       250        260        270        280        290        300 
APPGGTERRP NGLGPERSAG PGGAEAEPLP TQLNGAPGEP APAGPRDTDA LDLEESSSSD 

       310        320        330        340        350        360 
HAERPPGPRR PERGPRGKGK ARASQVKPGD SLPRRGPGAT GIGTPAAGPG EERVGAAKAS 

       370        380        390        400        410        420 
RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG CSVPRTLFKF FFWFGYCNSS 

       430        440        450 
LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and expression of the gene coding for the human platelet alpha 2-adrenergic receptor."
Kobilka B.K., Matsui H., Kobilka T.S., Yang-Feng T.L., Francke U., Caron M.G., Lefkowitz R.J., Regan J.W.
Science 238:650-656(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Platelet.
[2]"Cloning, sequence analysis, and permanent expression of a human alpha 2-adrenergic receptor in Chinese hamster ovary cells. Evidence for independent pathways of receptor coupling to adenylate cyclase attenuation and activation."
Fraser C.M., Arakawa S., McCombie W.R., Venter J.C.
J. Biol. Chem. 264:11754-11761(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning, sequencing, and expression of the gene encoding the porcine alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and amiloride analogs."
Guyer C.A., Horstman D.A., Wilson A.L., Clark J.D., Kragoe E.J. Jr., Limbird L.E.
J. Biol. Chem. 265:17307-17317(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 333-365.
[4]"An Asn to Lys polymorphism in the third intracellular loop of the human alpha 2A-adrenergic receptor imparts enhanced agonist-promoted Gi coupling."
Small K.M., Forbes S.L., Brown K.M., Liggett S.B.
J. Biol. Chem. 275:38518-38523(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-251.
[5]"Complex haplotypes derived from noncoding polymorphisms of the intronless alpha-2A-adrenergic gene diversify receptor expression."
Small K.M., Brown K.M., Seman C.A., Theiss C.T., Liggett S.B.
Proc. Natl. Acad. Sci. U.S.A. 103:5472-5477(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-251.
[6]"Cloning and expression of human alpha-2A adrenergic receptor in SY5Y cells."
Mao Z.-M., Tang K., Li B.-M., Jing N.-H.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"A search for genetic variability in the human alpha-2 adrenergic receptor on chromosome 10."
Castellano M., Giacche' M., Rossi F., Rivadossi F., Perani C., Beschi M., Agabiti Rosei E.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Human alpha-2A adrenergic receptor gene and the genotype of -1296 nucleotide and motionsickness."
Liu L., Yuan L.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]SeattleSNPs variation discovery resource
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-251.
[10]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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].
Tissue: PNS and Testis.
[13]"Identification of an additional gene belonging to the alpha 2 adrenergic receptor family in the human genome by PCR."
Chhajlani V., Rangel N., Uhlen S., Wikberg J.E.S.
FEBS Lett. 280:241-244(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-209.
[14]"A point mutation in the seventh hydrophobic domain of the alpha 2 adrenergic receptor increases its affinity for a family of beta receptor antagonists."
Suryanarayana S., Daunt D.A., von Zastrow M., Kobilka B.K.
J. Biol. Chem. 266:15488-15492(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF PHE-412.
[15]"Site-directed mutagenesis of alpha 2a-adrenergic receptors: Identification of amino acids involved in ligand binding and receptor activation by agonists."
Wang C.-D., Buck M.A., Fraser C.M.
Mol. Pharmacol. 40:168-179(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASPARTIC ACID AND SERINE RESIDUES.
[16]"Rab26 modulates the cell surface transport of alpha2-adrenergic receptors from the Golgi."
Li C., Fan Y., Lan T.H., Lambert N.A., Wu G.
J. Biol. Chem. 287:42784-42794(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]"NMR structure of the second intracellular loop of the alpha 2A adrenergic receptor: evidence for a novel cytoplasmic helix."
Chung D.A., Zuiderweg E.R.P., Fowler C.B., Soyer O.S., Mosberg H.I., Neubig R.R.
Biochemistry 41:3596-3604(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 118-149, PROBABLE MEMBRANE TOPOLOGY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18415 Genomic DNA. Translation: AAA51664.1.
M23533 Genomic DNA. Translation: AAA51665.1.
AF281308 Genomic DNA. Translation: AAF91441.1.
AF316894 Genomic DNA. Translation: AAK01634.1.
DQ149926 Genomic DNA. Translation: AAZ73101.1.
AF284095 mRNA. Translation: AAK26743.1.
AF262016 Genomic DNA. Translation: AAG00447.2.
AY032736 Genomic DNA. Translation: AAK51162.1.
DQ285607 Genomic DNA. Translation: ABB72683.1.
EU332846 Genomic DNA. Translation: ABY87535.1.
AL158163 Genomic DNA. Translation: CAH72817.1.
BC035047 mRNA. Translation: AAH35047.1.
BC050414 mRNA. Translation: AAH50414.4.
PIRA34169.
RefSeqNP_000672.3. NM_000681.3.
UniGeneHs.249159.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLLNMR-A118-149[»]
1HO9NMR-A118-149[»]
1HODNMR-A118-149[»]
1HOFNMR-A118-149[»]
ProteinModelPortalP08913.
SMRP08913. Positions 39-442.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106659. 8 interactions.
STRING9606.ENSP00000280155.

Chemistry

BindingDBP08913.
ChEMBLCHEMBL2331074.
DrugBankDB00321. Amitriptyline.
DB00182. Amphetamine.
DB00964. Apraclonidine.
DB00865. Benzphetamine.
DB00217. Bethanidine.
DB00484. Brimonidine.
DB00575. Clonidine.
DB04840. Debrisoquin.
DB00633. Dexmedetomidine.
DB00449. Dipivefrin.
DB00751. Epinastine.
DB00696. Ergotamine.
DB00800. Fenoldopam.
DB00629. Guanabenz.
DB00226. Guanadrel Sulfate.
DB01170. Guanethidine.
DB01018. Guanfacine.
DB04948. Lofexidine.
DB00968. Methyldopa.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB00368. Norepinephrine.
DB00935. Oxymetazoline.
DB00692. Phentolamine.
DB00397. Phenylpropanolamine.
DB00852. Pseudoephedrine.
DB00697. Tizanidine.
DB00656. Trazodone.
DB01392. Yohimbine.
GuidetoPHARMACOLOGY25.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP08913.

Polymorphism databases

DMDM1351829.

Proteomic databases

PaxDbP08913.
PRIDEP08913.

Protocols and materials databases

DNASU150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280155; ENSP00000280155; ENSG00000150594.
GeneID150.
KEGGhsa:150.
UCSCuc001kzo.3. human.

Organism-specific databases

CTD150.
GeneCardsGC10P112826.
H-InvDBHIX0190540.
HGNCHGNC:281. ADRA2A.
MIM104210. gene.
neXtProtNX_P08913.
PharmGKBPA35.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249628.
HOGENOMHOG000239242.
HOVERGENHBG106962.
InParanoidP08913.
KOK04138.
OrthoDBEOG7J9VPT.
PhylomeDBP08913.
TreeFamTF316350.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.
SignaLinkP08913.

Gene expression databases

BgeeP08913.
CleanExHS_ADRA2A.
GenevestigatorP08913.

Family and domain databases

Gene3D1.20.1070.10. 2 hits.
InterProIPR002233. ADR_fam.
IPR001946. ADRA2A_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24248:SF24. PTHR24248:SF24. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01103. ADRENERGICR.
PR00558. ADRENRGCA2AR.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08913.
GeneWikiAlpha-2A_adrenergic_receptor.
GenomeRNAi150.
NextBio595.
PROP08913.
SOURCESearch...

Entry information

Entry nameADA2A_HUMAN
AccessionPrimary (citable) accession number: P08913
Secondary accession number(s): B0LPF6 expand/collapse secondary AC list , Q2I8G2, Q2XN99, Q86TH8, Q9BZK1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 166 of the entry and version 3 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 10

Human chromosome 10: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries