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P29274 (AA2AR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenosine receptor A2a
Gene names
Name:ADORA2A
Synonyms:ADORA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Subunit structure

Interacts (via cytoplasmic C-terminal domain) with USP4; the interaction is direct. May interact with DRD4. Ref.11 Ref.13

Subcellular location

Cell membrane; Multi-pass membrane protein.

Domain

The cytoplasmic C-terminal domain is necessary for targeting the non-ubiquitinated form of this protein to the cell surface. Ref.12

Post-translational modification

Ubiquitinated. Deubiquitinated by USP4; leading to stabilization and expression at the cell surface. Ref.13

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence caution

The sequence AAA58356.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of adenylate cyclase activity

Traceable author statement. Source: Reactome

adenylate cyclase-modulating G-protein coupled receptor signaling pathway

Traceable author statement PubMed 10899090. Source: ProtInc

apoptotic process

Traceable author statement PubMed 7818494. Source: ProtInc

astrocyte activation

Inferred from electronic annotation. Source: Ensembl

blood circulation

Traceable author statement PubMed 9262401. Source: ProtInc

blood coagulation

Traceable author statement PubMed 10899090. Source: ProtInc

cAMP biosynthetic process

Traceable author statement PubMed 10899090. Source: ProtInc

cell-cell signaling

Traceable author statement PubMed 7818494. Source: ProtInc

cellular defense response

Traceable author statement PubMed 10051547. Source: ProtInc

central nervous system development

Traceable author statement PubMed 10945659. Source: ProtInc

eating behavior

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 8360491. Source: ProtInc

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of alpha-beta T cell activation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

negative regulation of locomotion

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

phagocytosis

Traceable author statement PubMed 8360491. Source: ProtInc

positive regulation of acetylcholine secretion, neurotransmission

Inferred from electronic annotation. Source: Ensembl

positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 21393508. Source: UniProtKB

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of circadian sleep/wake cycle, sleep

Inferred from electronic annotation. Source: Ensembl

positive regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of renal sodium excretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, GABAergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of urine volume

Inferred from electronic annotation. Source: Ensembl

prepulse inhibition

Inferred from electronic annotation. Source: Ensembl

protein kinase C-activating G-protein coupled receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of excitatory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of inhibitory postsynaptic membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of norepinephrine secretion

Inferred from electronic annotation. Source: Ensembl

regulation of synaptic plasticity

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

response to amphetamine

Inferred from electronic annotation. Source: Ensembl

response to caffeine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

sensory perception

Traceable author statement PubMed 9262401. Source: ProtInc

synaptic transmission, cholinergic

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

transmembrane receptor protein tyrosine kinase signaling pathway

Traceable author statement. Source: Reactome

vasodilation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentasymmetric synapse

Inferred from electronic annotation. Source: Ensembl

axolemma

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

endomembrane system

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from mutant phenotype PubMed 21393508. Source: UniProtKB

membrane

Traceable author statement PubMed 10051547. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.13. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

presynaptic active zone

Inferred from electronic annotation. Source: Ensembl

presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled adenosine receptor activity

Inferred from direct assay PubMed 21393508PubMed 21593763. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.13. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 18675812PubMed 19013155. Source: IntAct

protein binding

Inferred from physical interaction PubMed 11571652. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412Adenosine receptor A2a
PRO_0000068999

Regions

Topological domain1 – 77Extracellular Ref.14
Transmembrane8 – 3225Helical; Name=1
Topological domain33 – 4210Cytoplasmic Ref.14
Transmembrane43 – 6624Helical; Name=2
Topological domain67 – 7711Extracellular Ref.14
Transmembrane78 – 10023Helical; Name=3
Topological domain101 – 12020Cytoplasmic Ref.14
Transmembrane121 – 14323Helical; Name=4
Topological domain144 – 17330Extracellular Ref.14
Transmembrane174 – 19825Helical; Name=5
Topological domain199 – 23436Cytoplasmic Ref.14
Transmembrane235 – 25824Helical; Name=6
Topological domain259 – 2668Extracellular Ref.14
Transmembrane267 – 29024Helical; Name=7
Topological domain291 – 412122Cytoplasmic Ref.14
Region168 – 17710Agonist binding
Region246 – 2538Agonist binding
Region264 – 27411Agonist binding

Amino acid modifications

Glycosylation1541N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 159 Ref.14
Disulfide bond74 ↔ 146 Ref.14
Disulfide bond77 ↔ 166 Ref.14
Disulfide bond259 ↔ 262 Ref.14

Natural variations

Natural variant501A → V. Ref.15
Corresponds to variant rs4530 [ dbSNP | Ensembl ].
VAR_011835
Natural variant3001R → H.
Corresponds to variant rs4990 [ dbSNP | Ensembl ].
VAR_011836
Natural variant3921G → R.
VAR_003451

Secondary structure

............................................ 412
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29274 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 9438E9D64A6BE61B

FASTA41244,707
        10         20         30         40         50         60 
MPIMGSSVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA ADIAVGVLAI 

        70         80         90        100        110        120 
PFAITISTGF CAACHGCLFI ACFVLVLTQS SIFSLLAIAI DRYIAIRIPL RYNGLVTGTR 

       130        140        150        160        170        180 
AKGIIAICWV LSFAIGLTPM LGWNNCGQPK EGKNHSQGCG EGQVACLFED VVPMNYMVYF 

       190        200        210        220        230        240 
NFFACVLVPL LLMLGVYLRI FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG 

       250        260        270        280        290        300 
LFALCWLPLH IINCFTFFCP DCSHAPLWLM YLAIVLSHTN SVVNPFIYAY RIREFRQTFR 

       310        320        330        340        350        360 
KIIRSHVLRQ QEPFKAAGTS ARVLAAHGSD GEQVSLRLNG HPPGVWANGS APHPERRPNG 

       370        380        390        400        410 
YALGLVSGGS AQESQGNTGL PDVELLSHEL KGVCPEPPGL DDPLAQDGAG VS 

« Hide

References

« Hide 'large scale' references
[1]Tiffany H.L., Murphy P.M.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Salvatore C.A., Luneau C.J., Johnson R.G., Jacobson M.
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Molecular characterization of a human brain adenosine A2 receptor."
Furlong T.J., Pierce K.D., Selbie L.A., Shine J.
Brain Res. Mol. Brain Res. 15:62-66(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hippocampus.
[4]"Characterization and chromosomal localization of the human A2a adenosine receptor gene: ADORA2A."
Le F., Townsend-Nicholson A., Baker E., Sutherland G.R., Schofield P.R.
Biochem. Biophys. Res. Commun. 223:461-467(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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: Lymph.
[11]"The dopamine D(4) receptor, the ultimate disordered protein."
Woods A.S.
J. Recept. Signal Transduct. 30:331-336(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE INTERACTION WITH DRD4.
[12]"Site-directed mutagenesis identifies residues involved in ligand recognition in the human A2a adenosine receptor."
Kim J., Wess J., van Rhee A.M., Schoneberg T., Jacobson K.A.
J. Biol. Chem. 270:13987-13997(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF TRANSMEMBRANE DOMAINS.
[13]"The ubiquitin-specific protease Usp4 regulates the cell surface level of the A2A receptor."
Milojevic T., Reiterer V., Stefan E., Korkhov V.M., Dorostkar M.M., Ducza E., Ogris E., Boehm S., Freissmuth M., Nanoff C.
Mol. Pharmacol. 69:1083-1094(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP4, UBIQUITINATION, DEUBIQUITINATION BY USP4.
[14]"The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist."
Jaakola V.-P., Griffith M.T., Hanson M.A., Cherezov V., Chien E.Y.T., Lane J.R., Ijzerman A.P., Stevens R.C.
Science 322:1211-1217(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-316 IN COMPLEX WITH ANTAGONIST, TOPOLOGY, DISULFIDE BONDS.
[15]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-50.
[16]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97370 mRNA. Translation: AAA58356.1. Different initiation.
X68486 mRNA. Translation: CAA48504.1.
S46950 mRNA. Translation: AAB23956.1.
U40771, U40770 Genomic DNA. Translation: AAA83270.1.
AY136747 mRNA. Translation: AAN01273.1.
CR456367 mRNA. Translation: CAG30253.1.
BT006999 mRNA. Translation: AAP35645.1.
AK312946 mRNA. Translation: BAG35787.1.
CH471095 Genomic DNA. Translation: EAW59658.1.
BC013780 mRNA. Translation: AAH13780.1.
CCDSCCDS13826.1.
PIRA48978.
RefSeqNP_000666.2. NM_000675.5.
NP_001265426.1. NM_001278497.1.
NP_001265427.1. NM_001278498.1.
NP_001265428.1. NM_001278499.1.
NP_001265429.1. NM_001278500.1.
UniGeneHs.197029.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MMHmodel-16-36[»]
242-69[»]
378-102[»]
4117-143[»]
5175-203[»]
6233-260[»]
7264-296[»]
1UPEmodel-A1-304[»]
2YDOX-ray3.00A1-317[»]
2YDVX-ray2.60A1-317[»]
3EMLX-ray2.60A2-208[»]
A222-316[»]
3PWHX-ray3.30A1-317[»]
3QAKX-ray2.71A2-208[»]
A222-316[»]
3REYX-ray3.31A1-317[»]
3RFMX-ray3.60A1-317[»]
3UZAX-ray3.27A1-317[»]
3UZCX-ray3.34A1-317[»]
3VG9X-ray2.70A1-316[»]
3VGAX-ray3.10A1-316[»]
4EIYX-ray1.80A2-208[»]
A219-316[»]
ProteinModelPortalP29274.
SMRP29274. Positions 2-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106647. 8 interactions.
IntActP29274. 9 interactions.
MINTMINT-4823612.
STRING9606.ENSP00000336630.

Chemistry

BindingDBP29274.
ChEMBLCHEMBL2111329.
DrugBankDB00201. Caffeine.
DB04932. Defibrotide.
DB00061. Pegademase bovine.
DB00277. Theophylline.
GuidetoPHARMACOLOGY19.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP29274.

Polymorphism databases

DMDM543740.

Proteomic databases

PaxDbP29274.
PRIDEP29274.

Protocols and materials databases

DNASU135.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337539; ENSP00000336630; ENSG00000128271.
GeneID135.
KEGGhsa:135.
UCSCuc002zzx.3. human.

Organism-specific databases

CTD135.
GeneCardsGC22P024813.
HGNCHGNC:263. ADORA2A.
MIM102776. gene.
neXtProtNX_P29274.
Orphanet363549. Acute encephalopathy with biphasic seizures and late reduced diffusion.
PharmGKBPA24584.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287824.
HOGENOMHOG000015770.
HOVERGENHBG106962.
InParanoidP29274.
KOK04266.
OMAPGVWANG.
TreeFamTF325296.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP29274.
CleanExHS_ADORA2A.
GenevestigatorP29274.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001513. Adeno_A2A_rcpt.
IPR001634. Adenosn_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00553. ADENOSINA2AR.
PR00424. ADENOSINER.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29274.
GeneWikiAdenosine_A2A_receptor.
GenomeRNAi135.
NextBio543.
PROP29274.
SOURCESearch...

Entry information

Entry nameAA2AR_HUMAN
AccessionPrimary (citable) accession number: P29274
Secondary accession number(s): B2R7E0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 155 of the entry and version 2 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 22

Human chromosome 22: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries