P08913 (ADA2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	450 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: Compara 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 acute inflammatory response Inferred from electronic annotation. Source: Compara adenylate cyclase-inhibiting adrenergic receptor signaling pathway Inferred from direct assay Ref.4. Source: BHF-UCL 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: Compara female pregnancy Inferred from electronic annotation. Source: Compara 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 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 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: Compara 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 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 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: Compara positive regulation of wound healing Inferred from mutant phenotype PubMed 17655843. Source: BHF-UCL small molecule metabolic process Traceable author statement. Source: Reactome thermoception Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Traceable author statement PubMed 17655843. Source: BHF-UCL cytoplasm Inferred from direct assay PubMed 19477270. Source: BHF-UCL integral to plasma membrane Inferred from direct assay Ref.4PubMed 10948198Ref.1. Source: BHF-UCL receptor complex Inferred from direct assay Ref.4. Source: BHF-UCL synapse Inferred from electronic annotation. Source: Compara
Molecular_function	alpha-1B adrenergic receptor binding Inferred from sequence or structural similarity. 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 heterodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL protein homodimerization activity Inferred from direct assay PubMed 16605244. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Alpha-2A adrenergic receptor

PRO_0000069080

Regions

Topological domain

1 – 33

33

Extracellular By similarity

Transmembrane

34 – 59

26

Helical; Name=1; By similarity

Topological domain

60 – 70

11

Cytoplasmic By similarity

Transmembrane

71 – 96

26

Helical; Name=2; By similarity

Topological domain

97 – 106

10

Extracellular By similarity

Transmembrane

107 – 129

23

Helical; Name=3; By similarity

Topological domain

130 – 151

22

Cytoplasmic By similarity

Transmembrane

152 – 172

21

Helical; Name=4; By similarity

Topological domain

173 – 194

22

Extracellular By similarity

Transmembrane

195 – 217

23

Helical; Name=5; By similarity

Topological domain

218 – 374

157

Cytoplasmic By similarity

Transmembrane

375 – 395

21

Helical; Name=6; By similarity

Topological domain

396 – 409

14

Extracellular By similarity

Transmembrane

410 – 429

20

Helical; Name=7; By similarity

Topological domain

430 – 450

21

Cytoplasmic By similarity

Sites

Site

113

1

Implicated in ligand binding

Site

200

1

Implicated in catechol agonist binding and receptor activation

Site

204

1

Implicated in catechol agonist binding and receptor activation

Amino acid modifications

Lipidation

442

1

S-palmitoyl cysteine By similarity

Glycosylation

10

1

N-linked (GlcNAc...) Potential

Glycosylation

14

1

N-linked (GlcNAc...) Potential

Disulfide bond

106 ↔ 188

By similarity

Natural variations

Natural variant

251

1

N → 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 variant

401

1

C → S.
Corresponds to variant rs35658213 [ dbSNP | Ensembl ].

VAR_055908

Experimental info

Mutagenesis

79

1

D → N: No change in binding affinity. eliminates guanine nucleotide-sensitive agonist binding. Ref.15

Mutagenesis

113

1

D → N: No binding to yohimbine. Increase in adenylate cyclase activity. Ref.15

Mutagenesis

130

1

D → N: Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding. Ref.15

Mutagenesis

200

1

S → A: Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding. Ref.15

Mutagenesis

204

1

S → A: Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding. Ref.15

Mutagenesis

412

1

F → N: 350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol. Ref.14 Ref.15

Sequence conflict

104

1

A → T in AAA51664. Ref.1

Sequence conflict

124

1

L → P Ref.13

Sequence conflict

157

1

V → C in AAA51664. Ref.1

Sequence conflict

333 – 365

33

PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51664. Ref.1

Sequence conflict

333 – 365

33

PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51665. Ref.2

Sequence conflict

368

1

R → L in AAA51664. Ref.1

Secondary structure

1

.

.

.

.

.

.

450

Helix Strand Turn

Details...

Helix

119 – 128

10

Helix

130 – 139

10

Helix

140 – 142

3

Sequences

	Sequence		Length	Mass (Da)
	P08913 [UniParc]. Last modified February 1, 1996. Version 3. Checksum: A703CF262F04E8AC	FASTA	450	48,957
	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

References

	« Hide 'large scale' referencesShow '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. , 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

SeattleSNPs

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.

IPI

IPI00797870.

PIR

A34169.

RefSeq

NP_000672.3. NM_000681.3.

UniGene

Hs.249159.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HLL	NMR	-	A	118-149	[»]
1HO9	NMR	-	A	118-149	[»]
1HOD	NMR	-	A	118-149	[»]
1HOF	NMR	-	A	118-149	[»]

ProteinModelPortal

P08913.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000280155.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P08913.

Polymorphism databases

DMDM

1351829.

Proteomic databases

PaxDb

P08913.

PRIDE

P08913.

Protocols and materials databases

DNASU

150.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000280155; ENSP00000280155; ENSG00000150594.

GeneID

150.

KEGG

hsa:150.

UCSC

uc001kzo.3. human.

Organism-specific databases

CTD

150.

GeneCards

GC10P112826.

H-InvDB

HIX0190540.

HGNC

HGNC:281. ADRA2A.

MIM

104210. gene.

neXtProt

NX_P08913.

PharmGKB

PA35.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG249628.

HOGENOM

HOG000239242.

HOVERGEN

HBG106962.

InParanoid

P08913.

KO

K04138.

OrthoDB

EOG4R502W.

PhylomeDB

P08913.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_604. Hemostasis.

SignaLink

P08913.

Gene expression databases

Bgee

P08913.

CleanEx

HS_ADRA2A.

Genevestigator

P08913.

GermOnline

ENSG00000150594. Homo sapiens.

Family and domain databases

InterPro

IPR001946. Adren_rcpt_A2A.
IPR002233. Adrnrgc_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

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

PRINTS

PR01103. ADRENERGICR.
PR00558. ADRENRGCA2AR.
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

P08913.

ChEMBL

CHEMBL1867.

DrugBank

DB00321. 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.

EvolutionaryTrace

P08913.

GenomeRNAi

150.

NextBio

595.

SOURCE

Search...

Entry information

Entry name

ADA2A_HUMAN

Accession

Primary (citable) accession number: P08913
Secondary accession number(s): B0LPF6 , Q2I8G2, Q2XN99, Q86TH8, Q9BZK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 156 of the entry and version 3 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.