Protein Information: Adenosine receptor A2a
Cannonical Uniprot Accesion Number: P29274
10 20 30 40 50
MPIMGSSVYI TVELAIAVLA ILGNVLVCWA VWLNSNLQNV TNYFVVSLAA
60 70 80 90 100
ADIAVGVLAI PFAITISTGF CAACHGCLFI ACFVLVLTQS SIFSLLAIAI
110 120 130 140 150
DRYIAIRIPL RYNGLVTGTR AKGIIAICWV LSFAIGLTPM LGWNNCGQPK
160 170 180 190 200
EGKNHSQGCG EGQVACLFED VVPMNYMVYF NFFACVLVPL LLMLGVYLRI
210 220 230 240 250
FLAARRQLKQ MESQPLPGER ARSTLQKEVH AAKSLAIIVG LFALCWLPLH
260 270 280 290 300
IINCFTFFCP DCSHAPLWLM YLAIVLSHTN SVVNPFIYAY RIREFRQTFR
310 320 330 340 350
KIIRSHVLRQ QEPFKAAGTS ARVLAAHGSD GEQVSLRLNG HPPGVWANGS
360 370 380 390 400
APHPERRPNG YALGLVSGGS AQESQGNTGL PDVELLSHEL KGVCPEPPGL
410
DDPLAQDGAG VS
Scientific name: Homo sapiens
Is this protein a mutant? False
Alternative names:
Adenosine receptor A2a
Corresponding Cannonical Protein:
Protein ID: 35
You can find this protein in the following complex structures:
Complex Structure ID: 34 Complex Structure ID: 46 Complex Structure ID: 27 Complex Structure ID: 32 Complex Structure ID: 48 Complex Structure ID: 4 Complex Structure ID: 28 Complex Structure ID: 43 Complex Structure ID: 45 Complex Structure ID: 36 Complex Structure ID: 42 Complex Structure ID: 31 Complex Structure ID: 38 Complex Structure ID: 44 Complex Structure ID: 49 Complex Structure ID: 50 Complex Structure ID: 40 Complex Structure ID: 29 Complex Structure ID: 51 Complex Structure ID: 30 Complex Structure ID: 33 Complex Structure ID: 39 Complex Structure ID: 41 Complex Structure ID: 47 Complex Structure ID: 281 Complex Structure ID: 286 Complex Structure ID: 282 Complex Structure ID: 276 Complex Structure ID: 275 Complex Structure ID: 290 Complex Structure ID: 347 Complex Structure ID: 307 Complex Structure ID: 334 Complex Structure ID: 314 Complex Structure ID: 377 Complex Structure ID: 379 Complex Structure ID: 405 Complex Structure ID: 416 Complex Structure ID: 424 Complex Structure ID: 432 Complex Structure ID: 477 Complex Structure ID: 481 Complex Structure ID: 514 Complex Structure ID: 493 Complex Structure ID: 495 Complex Structure ID: 512 Complex Structure ID: 520 Complex Structure ID: 710 Complex Structure ID: 541 Complex Structure ID: 565 Complex Structure ID: 577 Complex Structure ID: 1211 Complex Structure ID: 621 Complex Structure ID: 625 Complex Structure ID: 636 Complex Structure ID: 644 Complex Structure ID: 658 Complex Structure ID: 623 Complex Structure ID: 1139 Complex Structure ID: 686 Complex Structure ID: 668 Complex Structure ID: 674 Complex Structure ID: 700 Complex Structure ID: 871 Complex Structure ID: 1065 Complex Structure ID: 1229 Complex Structure ID: 1119 Complex Structure ID: 1012 Complex Structure ID: 1231 Complex Structure ID: 787 Complex Structure ID: 1215 Complex Structure ID: 716 Complex Structure ID: 797 Complex Structure ID: 841 Complex Structure ID: 1046 Complex Structure ID: 989 Complex Structure ID: 1027 Complex Structure ID: 767 Complex Structure ID: 1218 Complex Structure ID: 849 Complex Structure ID: 1034 Complex Structure ID: 699 Complex Structure ID: 920 Complex Structure ID: 944 Complex Structure ID: 1226 Complex Structure ID: 728 Complex Structure ID: 827 Complex Structure ID: 848 Complex Structure ID: 867 Complex Structure ID: 1332 Complex Structure ID: 936 Complex Structure ID: 963 Complex Structure ID: 967 Complex Structure ID: 995 Complex Structure ID: 1001 Complex Structure ID: 1005 Complex Structure ID: 1014 Complex Structure ID: 1023 Complex Structure ID: 1025 Complex Structure ID: 1030 Complex Structure ID: 35 Complex Structure ID: 37 Complex Structure ID: 293 Complex Structure ID: 367 Complex Structure ID: 381 Complex Structure ID: 1114 Complex Structure ID: 597 Complex Structure ID: 680 Complex Structure ID: 4 Complex Structure ID: 28 Complex Structure ID: 43 Complex Structure ID: 45 Complex Structure ID: 30 Complex Structure ID: 33 Complex Structure ID: 39 Complex Structure ID: 41 Complex Structure ID: 47 Complex Structure ID: 35 Complex Structure ID: 37
References in which this protein is mentioned:
The UniProt Consortium. 2014. UniProt: a hub for protein information. Nucleic Acids Research 43 (None). doi: https://doi.org/10.1093/nar/gku989. Available in: Pubmed Link
R. Guixà-González, J. L. Albasanz, I. Rodriguez-Espigares, M. Pastor, F. Sanz, M. Martí-Solano, M. Manna, H. Martinez-Seara, P. W. Hildebrand, M. Martín, J. Selent. 2017. Membrane cholesterol access into a G-protein-coupled receptor. Nature Communications 8 (). doi: doi:10.1038/ncomms14505. Available in: Pubmed Link
Ismael Rodríguez-Espigares, Mariona Torrens-Fontanals, et al.. 2020. GPCRmd uncovers the dynamics of the 3D-GPCRome. Nature methods 17 (8). doi: 10.1038/s41592-020-0884-y. Available in: Pubmed Link
