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Protein

Alpha-2A adrenergic receptor

Gene

ADRA2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei113 – 1131Implicated in ligand binding
Sitei200 – 2001Implicated in catechol agonist binding and receptor activation
Sitei204 – 2041Implicated in catechol agonist binding and receptor activation

GO - Molecular functioni

  • alpha-1B adrenergic receptor binding Source: BHF-UCL
  • alpha2-adrenergic receptor activity Source: BHF-UCL
  • alpha-2C adrenergic receptor binding Source: BHF-UCL
  • epinephrine binding Source: BHF-UCL
  • heterotrimeric G-protein binding Source: BHF-UCL
  • norepinephrine binding Source: BHF-UCL
  • protein heterodimerization activity Source: BHF-UCL
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • thioesterase binding Source: BHF-UCL

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • activation of MAPK activity by adrenergic receptor signaling pathway Source: BHF-UCL
  • activation of protein kinase activity Source: BHF-UCL
  • activation of protein kinase B activity Source: BHF-UCL
  • acute inflammatory response Source: Ensembl
  • adenylate cyclase-inhibiting adrenergic receptor signaling pathway Source: BHF-UCL
  • blood coagulation Source: Reactome
  • cell-cell signaling Source: GO_Central
  • cellular response to hormone stimulus Source: BHF-UCL
  • DNA replication Source: Ensembl
  • energy reserve metabolic process Source: Reactome
  • epidermal growth factor-activated receptor transactivation by G-protein coupled receptor signaling pathway Source: BHF-UCL
  • fear response Source: Ensembl
  • female pregnancy Source: Ensembl
  • glucose homeostasis Source: BHF-UCL
  • G-protein coupled receptor signaling pathway Source: BHF-UCL
  • intestinal absorption Source: BHF-UCL
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of adenylate cyclase activity Source: BHF-UCL
  • negative regulation of adrenergic receptor signaling pathway Source: BHF-UCL
  • negative regulation of calcium ion-dependent exocytosis Source: BHF-UCL
  • negative regulation of calcium ion transmembrane transporter activity Source: BHF-UCL
  • negative regulation of calcium ion transport Source: BHF-UCL
  • negative regulation of cAMP biosynthetic process Source: BHF-UCL
  • negative regulation of epinephrine secretion Source: BHF-UCL
  • negative regulation of insulin secretion Source: BHF-UCL
  • negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: BHF-UCL
  • negative regulation of lipid catabolic process Source: BHF-UCL
  • negative regulation of norepinephrine secretion Source: BHF-UCL
  • negative regulation of uterine smooth muscle contraction Source: Ensembl
  • phospholipase C-activating adrenergic receptor signaling pathway Source: BHF-UCL
  • platelet activation Source: Reactome
  • positive regulation of cell migration Source: BHF-UCL
  • positive regulation of cell proliferation Source: ProtInc
  • positive regulation of cytokine production Source: BHF-UCL
  • positive regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: BHF-UCL
  • positive regulation of membrane protein ectodomain proteolysis Source: BHF-UCL
  • positive regulation of potassium ion transport Source: BHF-UCL
  • positive regulation of vasodilation Source: Ensembl
  • positive regulation of wound healing Source: BHF-UCL
  • Ras protein signal transduction Source: ProtInc
  • regulation of insulin secretion Source: Reactome
  • regulation of vasoconstriction Source: InterPro
  • Rho protein signal transduction Source: ProtInc
  • signal transduction Source: ProtInc
  • small molecule metabolic process Source: Reactome
  • thermoception Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_16927. Adrenoceptors.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_19180. Adrenaline signalling through Alpha-2 adrenergic receptor.
REACT_19231. G alpha (i) signalling events.
REACT_19333. G alpha (z) signalling events.
SignaLinkiP08913.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ADRA2A
Synonyms:ADRA2R, ADRAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:281. ADRA2A.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3333ExtracellularBy similarityAdd
BLAST
Transmembranei34 – 5926Helical; Name=1By similarityAdd
BLAST
Topological domaini60 – 7011CytoplasmicBy similarityAdd
BLAST
Transmembranei71 – 9626Helical; Name=2By similarityAdd
BLAST
Topological domaini97 – 10610ExtracellularBy similarity
Transmembranei107 – 12923Helical; Name=3By similarityAdd
BLAST
Topological domaini130 – 15122CytoplasmicBy similarityAdd
BLAST
Transmembranei152 – 17221Helical; Name=4By similarityAdd
BLAST
Topological domaini173 – 19422ExtracellularBy similarityAdd
BLAST
Transmembranei195 – 21723Helical; Name=5By similarityAdd
BLAST
Topological domaini218 – 374157CytoplasmicBy similarityAdd
BLAST
Transmembranei375 – 39521Helical; Name=6By similarityAdd
BLAST
Topological domaini396 – 40914ExtracellularBy similarityAdd
BLAST
Transmembranei410 – 42920Helical; Name=7By similarityAdd
BLAST
Topological domaini430 – 45021CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: BHF-UCL
  • cytoplasm Source: BHF-UCL
  • integral component of plasma membrane Source: BHF-UCL
  • plasma membrane Source: Reactome
  • receptor complex Source: BHF-UCL
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791D → N: No change in binding affinity. eliminates guanine nucleotide-sensitive agonist binding. 1 Publication
Mutagenesisi113 – 1131D → N: No binding to yohimbine. Increase in adenylate cyclase activity. 1 Publication
Mutagenesisi130 – 1301D → N: Lower affinity for agonists. Eliminates guanine nucleotide-sensitive agonist binding. 1 Publication
Mutagenesisi200 – 2001S → A: Lower affinity for agonists. No change in guanine nucleotide-sensitive agonist binding. 1 Publication
Mutagenesisi204 – 2041S → A: Lower affinity for agonists. Reduced guanine nucleotide-sensitive agonist binding. 1 Publication
Mutagenesisi412 – 4121F → N: 350-fold reduced affinity for alpha-2 antagonist yohimbine, 3000-fold increase for beta-antagonist alprenolol. 1 Publication

Organism-specific databases

PharmGKBiPA35.

Chemistry

DrugBankiDB00321. Amitriptyline.
DB00543. Amoxapine.
DB00182. Amphetamine.
DB00714. Apomorphine.
DB00964. Apraclonidine.
DB01238. Aripiprazole.
DB06216. Asenapine.
DB00865. Benzphetamine.
DB00217. Bethanidine.
DB00484. Brimonidine.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB01136. Carvedilol.
DB00477. Chlorpromazine.
DB00575. Clonidine.
DB00363. Clozapine.
DB01151. Desipramine.
DB00633. Dexmedetomidine.
DB00320. Dihydroergotamine.
DB00449. Dipivefrin.
DB01142. Doxepin.
DB04855. Dronedarone.
DB06262. Droxidopa.
DB01363. Ephedra.
DB00751. Epinastine.
DB00668. Epinephrine.
DB01049. Ergoloid mesylate.
DB00696. Ergotamine.
DB00800. Fenoldopam.
DB06623. Flupirtine.
DB00629. Guanabenz.
DB01018. Guanfacine.
DB00589. Lisuride.
DB04948. Lofexidine.
DB00408. Loxapine.
DB08815. Lurasidone.
DB00934. Maprotiline.
DB01365. Mephentermine.
DB01577. Methamphetamine.
DB01403. Methotrimeprazine.
DB00968. Methyldopa.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB06711. Naphazoline.
DB01149. Nefazodone.
DB00368. Norepinephrine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB00935. Oxymetazoline.
DB01267. Paliperidone.
DB01186. Pergolide.
DB00925. Phenoxybenzamine.
DB00692. Phentolamine.
DB00397. Phenylpropanolamine.
DB00413. Pramipexole.
DB00457. Prazosin.
DB01608. Propericiazine.
DB00852. Pseudoephedrine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB00268. Ropinirole.
DB00697. Tizanidine.
DB00797. Tolazoline.
DB00656. Trazodone.
DB00726. Trimipramine.
DB06694. Xylometazoline.
DB01392. Yohimbine.
DB00246. Ziprasidone.
DB01624. Zuclopenthixol.

Polymorphism and mutation databases

BioMutaiADRA2A.
DMDMi1351829.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Alpha-2A adrenergic receptorPRO_0000069080Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi10 – 101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi14 – 141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi106 ↔ 188PROSITE-ProRule annotation
Lipidationi442 – 4421S-palmitoyl cysteineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiP08913.
PRIDEiP08913.

PTM databases

PhosphoSiteiP08913.

Expressioni

Gene expression databases

BgeeiP08913.
CleanExiHS_ADRA2A.
GenevisibleiP08913. HS.

Interactioni

Protein-protein interaction databases

BioGridi106659. 8 interactions.
IntActiP08913. 3 interactions.
STRINGi9606.ENSP00000280155.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi119 – 12810Combined sources
Helixi130 – 13910Combined sources
Helixi140 – 1423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLLNMR-A118-149[»]
1HO9NMR-A118-149[»]
1HODNMR-A118-149[»]
1HOFNMR-A118-149[»]
ProteinModelPortaliP08913.
SMRiP08913. Positions 39-442.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08913.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG249628.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP08913.
KOiK04138.
OrthoDBiEOG7J9VPT.
PhylomeDBiP08913.
TreeFamiTF316350.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR001946. ADRA2A_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF24. PTHR24248:SF24. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00558. ADRENRGCA2AR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08913-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSLQPDAGN ASWNGTEAPG GGARATPYSL QVTLTLVCLA GLLMLLTVFG
60 70 80 90 100
NVLVIIAVFT SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY
110 120 130 140 150
FGKAWCEIYL ALDVLFCTSS IVHLCAISLD RYWSITQAIE YNLKRTPRRI
160 170 180 190 200
KAIIITVWVI SAVISFPPLI SIEKKGGGGG PQPAEPRCEI NDQKWYVISS
210 220 230 240 250
CIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDAVA APPGGTERRP
260 270 280 290 300
NGLGPERSAG PGGAEAEPLP TQLNGAPGEP APAGPRDTDA LDLEESSSSD
310 320 330 340 350
HAERPPGPRR PERGPRGKGK ARASQVKPGD SLPRRGPGAT GIGTPAAGPG
360 370 380 390 400
EERVGAAKAS RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLTAVG
410 420 430 440 450
CSVPRTLFKF FFWFGYCNSS LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV
Length:450
Mass (Da):48,957
Last modified:February 1, 1996 - v3
Checksum:iA703CF262F04E8AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041A → T in AAA51664 (PubMed:2823383).Curated
Sequence conflicti124 – 1241L → P (PubMed:1849485).Curated
Sequence conflicti157 – 1571V → C in AAA51664 (PubMed:2823383).Curated
Sequence conflicti333 – 36533PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51664 (PubMed:2823383).CuratedAdd
BLAST
Sequence conflicti333 – 36533PRRGP…RWRGR → RGAGRGRRGSGRRLQGRGRS ASGLPRRRAGAGG in AAA51665 (PubMed:2568356).CuratedAdd
BLAST
Sequence conflicti368 – 3681R → L in AAA51664 (PubMed:2823383).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti251 – 2511N → K Rare polymorphism; frequency in Caucasians 0.004 and in African-Americans 0.05; 40% increase in agonist-promoted Gi coupling. 3 Publications
Corresponds to variant rs1800035 [ dbSNP | Ensembl ].
VAR_014957
Natural varianti401 – 4011C → S.
Corresponds to variant rs35658213 [ dbSNP | Ensembl ].
VAR_055908

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA34169.
RefSeqiNP_000672.3. NM_000681.3.
UniGeneiHs.249159.

Genome annotation databases

EnsembliENST00000280155; ENSP00000280155; ENSG00000150594.
GeneIDi150.
KEGGihsa:150.
UCSCiuc001kzo.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA34169.
RefSeqiNP_000672.3. NM_000681.3.
UniGeneiHs.249159.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HLLNMR-A118-149[»]
1HO9NMR-A118-149[»]
1HODNMR-A118-149[»]
1HOFNMR-A118-149[»]
ProteinModelPortaliP08913.
SMRiP08913. Positions 39-442.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106659. 8 interactions.
IntActiP08913. 3 interactions.
STRINGi9606.ENSP00000280155.

Chemistry

BindingDBiP08913.
ChEMBLiCHEMBL2095158.
DrugBankiDB00321. Amitriptyline.
DB00543. Amoxapine.
DB00182. Amphetamine.
DB00714. Apomorphine.
DB00964. Apraclonidine.
DB01238. Aripiprazole.
DB06216. Asenapine.
DB00865. Benzphetamine.
DB00217. Bethanidine.
DB00484. Brimonidine.
DB01200. Bromocriptine.
DB00248. Cabergoline.
DB01136. Carvedilol.
DB00477. Chlorpromazine.
DB00575. Clonidine.
DB00363. Clozapine.
DB01151. Desipramine.
DB00633. Dexmedetomidine.
DB00320. Dihydroergotamine.
DB00449. Dipivefrin.
DB01142. Doxepin.
DB04855. Dronedarone.
DB06262. Droxidopa.
DB01363. Ephedra.
DB00751. Epinastine.
DB00668. Epinephrine.
DB01049. Ergoloid mesylate.
DB00696. Ergotamine.
DB00800. Fenoldopam.
DB06623. Flupirtine.
DB00629. Guanabenz.
DB01018. Guanfacine.
DB00589. Lisuride.
DB04948. Lofexidine.
DB00408. Loxapine.
DB08815. Lurasidone.
DB00934. Maprotiline.
DB01365. Mephentermine.
DB01577. Methamphetamine.
DB01403. Methotrimeprazine.
DB00968. Methyldopa.
DB06148. Mianserin.
DB00370. Mirtazapine.
DB06711. Naphazoline.
DB01149. Nefazodone.
DB00368. Norepinephrine.
DB00540. Nortriptyline.
DB00334. Olanzapine.
DB00935. Oxymetazoline.
DB01267. Paliperidone.
DB01186. Pergolide.
DB00925. Phenoxybenzamine.
DB00692. Phentolamine.
DB00397. Phenylpropanolamine.
DB00413. Pramipexole.
DB00457. Prazosin.
DB01608. Propericiazine.
DB00852. Pseudoephedrine.
DB01224. Quetiapine.
DB00734. Risperidone.
DB00268. Ropinirole.
DB00697. Tizanidine.
DB00797. Tolazoline.
DB00656. Trazodone.
DB00726. Trimipramine.
DB06694. Xylometazoline.
DB01392. Yohimbine.
DB00246. Ziprasidone.
DB01624. Zuclopenthixol.
GuidetoPHARMACOLOGYi25.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP08913.

Polymorphism and mutation databases

BioMutaiADRA2A.
DMDMi1351829.

Proteomic databases

PaxDbiP08913.
PRIDEiP08913.

Protocols and materials databases

DNASUi150.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280155; ENSP00000280155; ENSG00000150594.
GeneIDi150.
KEGGihsa:150.
UCSCiuc001kzo.3. human.

Organism-specific databases

CTDi150.
GeneCardsiGC10P112826.
H-InvDBHIX0190540.
HGNCiHGNC:281. ADRA2A.
MIMi104210. gene.
neXtProtiNX_P08913.
PharmGKBiPA35.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG249628.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP08913.
KOiK04138.
OrthoDBiEOG7J9VPT.
PhylomeDBiP08913.
TreeFamiTF316350.

Enzyme and pathway databases

ReactomeiREACT_16927. Adrenoceptors.
REACT_18339. Adrenaline,noradrenaline inhibits insulin secretion.
REACT_19180. Adrenaline signalling through Alpha-2 adrenergic receptor.
REACT_19231. G alpha (i) signalling events.
REACT_19333. G alpha (z) signalling events.
SignaLinkiP08913.

Miscellaneous databases

EvolutionaryTraceiP08913.
GeneWikiiAlpha-2A_adrenergic_receptor.
GenomeRNAii150.
NextBioi595.
PROiP08913.
SOURCEiSearch...

Gene expression databases

BgeeiP08913.
CleanExiHS_ADRA2A.
GenevisibleiP08913. HS.

Family and domain databases

InterProiIPR002233. ADR_fam.
IPR001946. ADRA2A_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF24. PTHR24248:SF24. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00558. ADRENRGCA2AR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiADA2A_HUMAN
AccessioniPrimary (citable) accession number: P08913
Secondary accession number(s): B0LPF6
, Q2I8G2, Q2XN99, Q86TH8, Q9BZK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: June 24, 2015
This is version 176 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.