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P29274

- AA2AR_HUMAN

UniProt

P29274 - AA2AR_HUMAN

Protein

Adenosine receptor A2a

Gene

ADORA2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

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

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. G-protein coupled adenosine receptor activity Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of adenylate cyclase activity Source: Reactome
    2. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: ProtInc
    3. apoptotic process Source: ProtInc
    4. astrocyte activation Source: Ensembl
    5. blood circulation Source: ProtInc
    6. blood coagulation Source: ProtInc
    7. cAMP biosynthetic process Source: ProtInc
    8. cell-cell signaling Source: ProtInc
    9. cellular defense response Source: ProtInc
    10. central nervous system development Source: ProtInc
    11. eating behavior Source: Ensembl
    12. inflammatory response Source: ProtInc
    13. locomotory behavior Source: Ensembl
    14. negative regulation of alpha-beta T cell activation Source: Ensembl
    15. negative regulation of cell proliferation Source: Ensembl
    16. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    17. negative regulation of inflammatory response Source: Ensembl
    18. negative regulation of locomotion Source: Ensembl
    19. negative regulation of neuron apoptotic process Source: Ensembl
    20. negative regulation of protein kinase activity Source: Ensembl
    21. negative regulation of vascular permeability Source: Ensembl
    22. neuron projection morphogenesis Source: Ensembl
    23. neurotrophin TRK receptor signaling pathway Source: Reactome
    24. phagocytosis Source: ProtInc
    25. positive regulation of acetylcholine secretion, neurotransmission Source: Ensembl
    26. positive regulation of adenylate cyclase activity involved in G-protein coupled receptor signaling pathway Source: UniProtKB
    27. positive regulation of apoptotic signaling pathway Source: Ensembl
    28. positive regulation of circadian sleep/wake cycle, sleep Source: Ensembl
    29. positive regulation of glutamate secretion Source: Ensembl
    30. positive regulation of protein secretion Source: Ensembl
    31. positive regulation of renal sodium excretion Source: Ensembl
    32. positive regulation of synaptic transmission, GABAergic Source: Ensembl
    33. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    34. positive regulation of urine volume Source: Ensembl
    35. prepulse inhibition Source: Ensembl
    36. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    37. regulation of calcium ion transport Source: Ensembl
    38. regulation of excitatory postsynaptic membrane potential Source: Ensembl
    39. regulation of inhibitory postsynaptic membrane potential Source: Ensembl
    40. regulation of mitochondrial membrane potential Source: Ensembl
    41. regulation of norepinephrine secretion Source: Ensembl
    42. regulation of synaptic plasticity Source: Ensembl
    43. regulation of transcription, DNA-templated Source: Ensembl
    44. response to amphetamine Source: Ensembl
    45. response to caffeine Source: Ensembl
    46. response to drug Source: Ensembl
    47. sensory perception Source: ProtInc
    48. synaptic transmission, cholinergic Source: Ensembl
    49. synaptic transmission, dopaminergic Source: Ensembl
    50. synaptic transmission, glutamatergic Source: Ensembl
    51. transmembrane receptor protein tyrosine kinase signaling pathway Source: Reactome
    52. vasodilation Source: Ensembl

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Enzyme and pathway databases

    ReactomeiREACT_11046. NGF-independant TRKA activation.
    REACT_18288. Adenosine P1 receptors.
    REACT_19327. G alpha (s) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenosine receptor A2a
    Gene namesi
    Name:ADORA2A
    Synonyms:ADORA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:263. ADORA2A.

    Subcellular locationi

    GO - Cellular componenti

    1. asymmetric synapse Source: Ensembl
    2. axolemma Source: Ensembl
    3. dendrite Source: Ensembl
    4. endomembrane system Source: Ensembl
    5. integral component of plasma membrane Source: UniProtKB
    6. membrane Source: ProtInc
    7. neuronal cell body Source: Ensembl
    8. plasma membrane Source: UniProtKB
    9. postsynaptic density Source: Ensembl
    10. postsynaptic membrane Source: Ensembl
    11. presynaptic active zone Source: Ensembl
    12. presynaptic membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti363549. Acute encephalopathy with biphasic seizures and late reduced diffusion.
    PharmGKBiPA24584.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Adenosine receptor A2aPRO_0000068999Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 1591 PublicationPROSITE-ProRule annotation
    Disulfide bondi74 ↔ 1461 PublicationPROSITE-ProRule annotation
    Disulfide bondi77 ↔ 1661 PublicationPROSITE-ProRule annotation
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi259 ↔ 2621 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    Ubiquitinated. Deubiquitinated by USP4; leading to stabilization and expression at the cell surface.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP29274.
    PRIDEiP29274.

    PTM databases

    PhosphoSiteiP29274.

    Expressioni

    Gene expression databases

    BgeeiP29274.
    CleanExiHS_ADORA2A.
    GenevestigatoriP29274.

    Interactioni

    Subunit structurei

    Interacts (via cytoplasmic C-terminal domain) with USP4; the interaction is direct. May interact with DRD4.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself6EBI-2902702,EBI-2902702
    ADORA1P305424EBI-2902702,EBI-2903663
    CALM3P621583EBI-2902702,EBI-397435
    CYTH2Q994186EBI-2902702,EBI-448974
    DRD2P144162EBI-2902702,EBI-2928178
    Grm5P31424-13EBI-2902702,EBI-2902778From a different organism.
    NECAB2Q7Z6G35EBI-2902702,EBI-950070
    USP4Q131074EBI-2902702,EBI-723290

    Protein-protein interaction databases

    BioGridi106647. 8 interactions.
    IntActiP29274. 9 interactions.
    MINTiMINT-4823612.
    STRINGi9606.ENSP00000336630.

    Structurei

    Secondary structure

    1
    412
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 3332
    Helixi35 – 373
    Helixi40 – 5718
    Helixi59 – 679
    Beta strandi71 – 733
    Helixi74 – 10734
    Helixi109 – 1157
    Helixi118 – 13619
    Helixi138 – 1414
    Helixi145 – 1473
    Helixi151 – 1566
    Beta strandi163 – 1653
    Helixi168 – 1714
    Helixi174 – 1796
    Helixi180 – 1867
    Helixi187 – 20822
    Beta strandi213 – 2164
    Helixi219 – 25840
    Beta strandi260 – 2623
    Helixi267 – 29125
    Helixi293 – 30513
    Turni308 – 3103
    Helixi312 – 3176

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP29274.
    SMRiP29274. Positions 2-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP29274.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 77Extracellular1 Publication
    Topological domaini33 – 4210Cytoplasmic1 Publication
    Topological domaini67 – 7711Extracellular1 PublicationAdd
    BLAST
    Topological domaini101 – 12020Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini144 – 17330Extracellular1 PublicationAdd
    BLAST
    Topological domaini199 – 23436Cytoplasmic1 PublicationAdd
    BLAST
    Topological domaini259 – 2668Extracellular1 Publication
    Topological domaini291 – 412122Cytoplasmic1 PublicationAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei8 – 3225Helical; Name=1Add
    BLAST
    Transmembranei43 – 6624Helical; Name=2Add
    BLAST
    Transmembranei78 – 10023Helical; Name=3Add
    BLAST
    Transmembranei121 – 14323Helical; Name=4Add
    BLAST
    Transmembranei174 – 19825Helical; Name=5Add
    BLAST
    Transmembranei235 – 25824Helical; Name=6Add
    BLAST
    Transmembranei267 – 29024Helical; Name=7Add
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni168 – 17710Agonist binding
    Regioni246 – 2538Agonist binding
    Regioni264 – 27411Agonist bindingAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG287824.
    HOGENOMiHOG000015770.
    HOVERGENiHBG106962.
    InParanoidiP29274.
    KOiK04266.
    OMAiPGVWANG.
    TreeFamiTF325296.

    Family and domain databases

    Gene3Di1.20.1070.10. 1 hit.
    InterProiIPR001513. Adeno_A2A_rcpt.
    IPR001634. Adenosn_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view]
    PfamiPF00001. 7tm_1. 1 hit.
    [Graphical view]
    PRINTSiPR00553. ADENOSINA2AR.
    PR00424. ADENOSINER.
    PR00237. GPCRRHODOPSN.
    PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P29274-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPIMGSSVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA    50
    ADIAVGVLAI PFAITISTGF CAACHGCLFI ACFVLVLTQS SIFSLLAIAI 100
    DRYIAIRIPL RYNGLVTGTR AKGIIAICWV LSFAIGLTPM LGWNNCGQPK 150
    EGKNHSQGCG EGQVACLFED VVPMNYMVYF NFFACVLVPL LLMLGVYLRI 200
    FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG LFALCWLPLH 250
    IINCFTFFCP DCSHAPLWLM YLAIVLSHTN SVVNPFIYAY RIREFRQTFR 300
    KIIRSHVLRQ QEPFKAAGTS ARVLAAHGSD GEQVSLRLNG HPPGVWANGS 350
    APHPERRPNG YALGLVSGGS AQESQGNTGL PDVELLSHEL KGVCPEPPGL 400
    DDPLAQDGAG VS 412
    Length:412
    Mass (Da):44,707
    Last modified:June 1, 1994 - v2
    Checksum:i9438E9D64A6BE61B
    GO

    Sequence cautioni

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

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501A → V.1 Publication
    Corresponds to variant rs4530 [ dbSNP | Ensembl ].
    VAR_011835
    Natural varianti300 – 3001R → H.
    Corresponds to variant rs4990 [ dbSNP | Ensembl ].
    VAR_011836
    Natural varianti392 – 3921G → R.
    VAR_003451

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13826.1.
    PIRiA48978.
    RefSeqiNP_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.
    UniGeneiHs.197029.

    Genome annotation databases

    EnsembliENST00000337539; ENSP00000336630; ENSG00000128271.
    GeneIDi135.
    KEGGihsa:135.
    UCSCiuc002zzx.3. human.

    Polymorphism databases

    DMDMi543740.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS13826.1.
    PIRi A48978.
    RefSeqi NP_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.
    UniGenei Hs.197029.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MMH model - 1 6-36 [» ]
    2 42-69 [» ]
    3 78-102 [» ]
    4 117-143 [» ]
    5 175-203 [» ]
    6 233-260 [» ]
    7 264-296 [» ]
    1UPE model - A 1-304 [» ]
    2YDO X-ray 3.00 A 1-317 [» ]
    2YDV X-ray 2.60 A 1-317 [» ]
    3EML X-ray 2.60 A 2-208 [» ]
    A 222-316 [» ]
    3PWH X-ray 3.30 A 1-317 [» ]
    3QAK X-ray 2.71 A 2-208 [» ]
    A 222-316 [» ]
    3REY X-ray 3.31 A 1-317 [» ]
    3RFM X-ray 3.60 A 1-317 [» ]
    3UZA X-ray 3.27 A 1-317 [» ]
    3UZC X-ray 3.34 A 1-317 [» ]
    3VG9 X-ray 2.70 A 1-316 [» ]
    3VGA X-ray 3.10 A 1-316 [» ]
    4EIY X-ray 1.80 A 2-208 [» ]
    A 219-316 [» ]
    ProteinModelPortali P29274.
    SMRi P29274. Positions 2-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106647. 8 interactions.
    IntActi P29274. 9 interactions.
    MINTi MINT-4823612.
    STRINGi 9606.ENSP00000336630.

    Chemistry

    BindingDBi P29274.
    ChEMBLi CHEMBL2111329.
    DrugBanki DB00201. Caffeine.
    DB04932. Defibrotide.
    DB00061. Pegademase bovine.
    DB00277. Theophylline.
    GuidetoPHARMACOLOGYi 19.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei P29274.

    Polymorphism databases

    DMDMi 543740.

    Proteomic databases

    PaxDbi P29274.
    PRIDEi P29274.

    Protocols and materials databases

    DNASUi 135.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337539 ; ENSP00000336630 ; ENSG00000128271 .
    GeneIDi 135.
    KEGGi hsa:135.
    UCSCi uc002zzx.3. human.

    Organism-specific databases

    CTDi 135.
    GeneCardsi GC22P024813.
    HGNCi HGNC:263. ADORA2A.
    MIMi 102776. gene.
    neXtProti NX_P29274.
    Orphaneti 363549. Acute encephalopathy with biphasic seizures and late reduced diffusion.
    PharmGKBi PA24584.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287824.
    HOGENOMi HOG000015770.
    HOVERGENi HBG106962.
    InParanoidi P29274.
    KOi K04266.
    OMAi PGVWANG.
    TreeFami TF325296.

    Enzyme and pathway databases

    Reactomei REACT_11046. NGF-independant TRKA activation.
    REACT_18288. Adenosine P1 receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    EvolutionaryTracei P29274.
    GeneWikii Adenosine_A2A_receptor.
    GenomeRNAii 135.
    NextBioi 543.
    PROi P29274.
    SOURCEi Search...

    Gene expression databases

    Bgeei P29274.
    CleanExi HS_ADORA2A.
    Genevestigatori P29274.

    Family and domain databases

    Gene3Di 1.20.1070.10. 1 hit.
    InterProi IPR001513. Adeno_A2A_rcpt.
    IPR001634. Adenosn_rcpt.
    IPR000276. GPCR_Rhodpsn.
    IPR017452. GPCR_Rhodpsn_7TM.
    [Graphical view ]
    Pfami PF00001. 7tm_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00553. ADENOSINA2AR.
    PR00424. ADENOSINER.
    PR00237. GPCRRHODOPSN.
    PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
    PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. Cited for: VARIANT VAL-50.

    Entry informationi

    Entry nameiAA2AR_HUMAN
    AccessioniPrimary (citable) accession number: P29274
    Secondary accession number(s): B2R7E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 157 of the entry and version 2 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, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human chromosome 22
      Human chromosome 22: 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