<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	113 – 113	1	Agonist or antagonist
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	118 – 118	1	Agonist or antagonist

<div> <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. beta2-adrenergic receptor activity Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

2. norepinephrine binding Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

3. potassium channel regulator activity Source: BHF-UCL

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 12297500

4. protein binding Source: UniProtKB

   <div> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex). </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ipi">GO evidence code guide</a>.</p> </div> Inferred from physical interactionⁱ

   • 19424180
   • 19584355
   • 20733053
   • 9560162

5. protein homodimerization activity Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

<div> <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. activation of adenylate cyclase activity Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

2. activation of transmembrane receptor protein tyrosine kinase activity Source: ProtInc

   <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

   • 10734107

3. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: Ensembl
4. adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: ProtInc

   <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

   • 2823249

5. adrenergic receptor signaling pathway Source: GOC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

6. bone resorption Source: Ensembl
7. brown fat cell differentiation Source: Ensembl
8. cell surface receptor signaling pathway Source: ProtInc

   <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

   • 1371121

9. desensitization of G-protein coupled receptor protein signaling pathway by arrestin Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

10. diet induced thermogenesis Source: Ensembl
11. endosome to lysosome transport Source: ProtInc

    <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

    • 9507004

12. heat generation Source: Ensembl
13. negative regulation of multicellular organism growth Source: Ensembl
14. negative regulation of smooth muscle contraction Source: Ensembl
15. positive regulation of bone mineralization Source: Ensembl
16. positive regulation of MAPK cascade Source: HGNC

    <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

    • 15123695

17. positive regulation of protein ubiquitination Source: BHF-UCL

    <div> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#imp">GO evidence code guide</a>.</p> </div> Inferred from mutant phenotypeⁱ

    • 19372219

18. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
19. receptor-mediated endocytosis Source: HGNC

    <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

    • 15123695

20. regulation of sodium ion transport Source: Ensembl
21. regulation of vasodilation Source: InterPro
22. response to cold Source: Ensembl
23. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: Ensembl

<div> <p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Molecular functionⁱ

Enzyme and pathway databases

Protein family/group databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	1 – 34	34	Extracellular3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	35 – 58	24	Helical; Name=1			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	59 – 71	13	Cytoplasmic3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	72 – 95	24	Helical; Name=2			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	96 – 106	11	Extracellular3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	107 – 129	23	Helical; Name=3			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	130 – 150	21	Cytoplasmic3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	151 – 174	24	Helical; Name=4			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	175 – 196	22	Extracellular3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	197 – 220	24	Helical; Name=5			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	221 – 274	54	Cytoplasmic3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	275 – 298	24	Helical; Name=6			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	299 – 305	7	Extracellular3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	306 – 329	24	Helical; Name=7			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	330 – 413	84	Cytoplasmic3 Publications Manual assertion based on experiment in: Ref.29 "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor." Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K. Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.			Add BLAST

<div> <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. apical plasma membrane Source: Ensembl
2. endosome Source: ProtInc

   <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

   • 10734107

3. integral component of plasma membrane Source: BHF-UCL

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 12297500

4. lysosome Source: ProtInc

   <div> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#tas">GO evidence code guide</a>.</p> </div> Traceable author statementⁱ

   • 9507004

5. nucleus Source: Ensembl
6. plasma membrane Source: MGI

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 9235896

7. receptor complex Source: HGNC

   <div> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term. </p> <p>More information in the <a href="http://www.geneontology.org/GO.evidence.shtml#ida">GO evidence code guide</a>.</p> </div> Inferred from direct assayⁱ

   • 15123695

<div> <p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	79 – 79	1	D → N: Affects binding of catecholamines, and produces an uncoupling between the receptor and stimulatory G proteins. 2 Publications Manual assertion based on experiment in: Ref.15 "Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation." Chung F.-Z., Wang C.-D., Potter P.C., Venter J.C., Fraser C.M. J. Biol. Chem. 263:4052-4055(1988) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASP-79. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	141 – 141	1	Y → F: Abolishes insulin-induced tyrosine phosphorylation and insulin-induced receptor supersensitization. 2 Publications Manual assertion based on experiment in: Ref.17 "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	341 – 341	1	C → G: Uncoupled receptor. 2 Publications Manual assertion based on experiment in: Ref.16 "Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor." O'Dowd B.F., Hnatowich M., Caron M.G., Lefkowitz R.J., Bouvier M. J. Biol. Chem. 264:7564-7569(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-341, MUTAGENESIS OF CYS-341. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	345 – 346	2	SS → AA: Delayed agonist-promoted desensitization. 1 Publication Manual assertion based on experiment in: Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	350 – 350	1	Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications Manual assertion based on experiment in: Ref.17 "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	354 – 354	1	Y → A: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications Manual assertion based on experiment in: Ref.17 "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	366 – 366	1	Y → F: Does not affect insulin-induced tyrosine phosphorylation or insulin-induced receptor supersensitization. 2 Publications Manual assertion based on experiment in: Ref.17 "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 413	413	Beta-2 adrenergic receptor		PRO_0000069130	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	6 – 6	1	N-linked (GlcNAc...) Inferred
<p>Specifies the position and type of each covalently attached glycan group (mono-, di- , or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	15 – 15	1	N-linked (GlcNAc...) Inferred
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	106 ↔ 191		2 Publications Manual assertion based on experiment in: Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	141 – 141	1	Phosphotyrosine1 Publication Manual assertion based on experiment in: Ref.17 "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor." Valiquette M., Parent S., Loisel T.P., Bouvier M. EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141.
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	184 ↔ 190		2 Publications Manual assertion based on experiment in: Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	246 – 246	1	Phosphoserine1 Publication Manual assertion based on experiment in: Ref.24 "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	261 – 261	1	Phosphoserine; by PKA Reviewed prediction
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	262 – 262	1	Phosphoserine; by PKA Reviewed prediction
<p>Specifies the position(s) and the type of covalently attached lipid group(s).</p><p><a href='../manual/lipid' target='_top'>More...</a></p>Lipidationi	341 – 341	1	S-palmitoyl cysteine4 Publications Manual assertion based on experiment in: Ref.16 "Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor." O'Dowd B.F., Hnatowich M., Caron M.G., Lefkowitz R.J., Bouvier M. J. Biol. Chem. 264:7564-7569(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-341, MUTAGENESIS OF CYS-341. Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346. Ref.30 "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor." Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C. Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341. Ref.31 "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor." Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C. Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	345 – 345	1	Phosphoserine; by PKA1 Publication Manual assertion based on experiment in: Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	346 – 346	1	Phosphoserine; by PKA1 Publication Manual assertion based on experiment in: Ref.22 "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization." Moffett S., Rousseau G., Lagace M., Bouvier M. J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	355 – 355	1	Phosphoserine; by BARK Inferred
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	356 – 356	1	Phosphoserine; by BARK Inferred
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	382 – 382	1	4-hydroxyproline1 Publication Manual assertion based on experiment in: Ref.26 "Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL." Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S. Sci. Signal. 2:RA33-RA33(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EGLN3 AND VHL, SUBCELLULAR LOCATION, INDUCTION, UBIQUITINATION, HYDROXYLATION AT PRO-382 AND PRO-395, IDENTIFICATION BY MASS SPECTROMETRY.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	395 – 395	1	4-hydroxyproline1 Publication Manual assertion based on experiment in: Ref.26 "Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL." Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S. Sci. Signal. 2:RA33-RA33(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EGLN3 AND VHL, SUBCELLULAR LOCATION, INDUCTION, UBIQUITINATION, HYDROXYLATION AT PRO-382 AND PRO-395, IDENTIFICATION BY MASS SPECTROMETRY.

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<div> <p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	25 – 27	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	31 – 60	30
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	62 – 64	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	67 – 85	19
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	87 – 96	10
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	102 – 136	35
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	137 – 139	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	147 – 170	24
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	171 – 174	4
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	179 – 186	8
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	187 – 189	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	197 – 207	11
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	209 – 229	21
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	235 – 239	5
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	263 – 265	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	267 – 298	32
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	299 – 303	5
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	305 – 317	13
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	318 – 320	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	322 – 325	4
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	326 – 328	3
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	330 – 339	10
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	345 – 347	3

3D structure databases

Miscellaneous databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	193 – 207	15	Agonist and antagonist binding			Add BLAST
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	286 – 293	8	Agonist and antagonist binding
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	312 – 316	5	Agonist and antagonist binding

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.</p><p><a href='../manual/motif' target='_top'>More...</a></p>Motifi	410 – 413	4	PDZ-binding

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<div> <p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

MGQPGNGSAF LLAPNGSHAP DHDVTQERDE VWVVGMGIVM SLIVLAIVFG    50
NVLVITAIAK FERLQTVTNY FITSLACADL VMGLAVVPFG AAHILMKMWT   100
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYFAITSPFK YQSLLTKNKA   150
RVIILMVWIV SGLTSFLPIQ MHWYRATHQE AINCYANETC CDFFTNQAYA   200
IASSIVSFYV PLVIMVFVYS RVFQEAKRQL QKIDKSEGRF HVQNLSQVEQ   250
DGRTGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIQD   300
NLIRKEVYIL LNWIGYVNSG FNPLIYCRSP DFRIAFQELL CLRRSSLKAY   350
GNGYSSNGNT GEQSGYHVEQ EKENKLLCED LPGTEDFVGH QGTVPSDNID   400
SQGRNCSTND SLL                                           413

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

<p>Provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="/manual/involvement_in_disease">‘Involvement in disease’</a> subsection.</p><p><a href='../manual/polymorphism' target='_top'>More...</a></p>Polymorphismⁱ

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	15 – 15	1	N → S. Corresponds to variant rs33973603 [ dbSNP | Ensembl ].		VAR_049373
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	16 – 16	1	G → R Common polymorphism. 8 Publications Manual assertion based on experiment in: Ref.2 "Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions." Kobilka B.K., Frielle T., Dohlman H.G., Bolanowski M.A., Dixon R.A.F., Keller P., Caron M.G., Lefkowitz R.J. J. Biol. Chem. 262:7321-7327(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27. Ref.3 "Primary structure of the human beta-adrenergic receptor gene." Schofield P.R., Rhee L.M., Peralta E.G. Nucleic Acids Res. 15:3636-3636(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27. Ref.4 "cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor." Kobilka B.K., Dixon R.A.F., Frielle T., Dohlman H.G., Bolanowski M.A., Sigal I.S., Yang-Feng T.L., Francke U., Caron M.G., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 84:46-50(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-16 AND GLN-27. Ref.6 "Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects." Reihsaus E., Innis M., Macintyre N., Liggett S.B. Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164. Ref.8 "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], VARIANTS ARG-16 AND GLN-27. Ref.14 "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], VARIANTS ARG-16 AND GLN-27. Ref.32 "Amino-terminal polymorphisms of the human beta 2-adrenergic receptor impart distinct agonist-promoted regulatory properties." Green S.A., Turki J., Innis M., Ligget S.B. Biochemistry 33:9414-9419(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-16 AND GLN-27, CHARACTERIZATION. Ref.33 "Genetic polymorphisms of the beta 2-adrenergic receptor in nocturnal and nonnocturnal asthma. Evidence that Gly16 correlates with the nocturnal phenotype." Turki J., Pak J., Green S.A., Martin R.J., Liggett S.B. J. Clin. Invest. 95:1635-1641(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-16, POLYMORPHISM. Corresponds to variant rs1042713 [ dbSNP | Ensembl ].		VAR_003452
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	27 – 27	1	E → Q.13 Publications Manual assertion based on experiment in: Ref.1 "Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors." Chung F.-Z., Lentes K.-U., Gocayne J.D., Fitzgerald M.G., Robinson D.A., Kerlavage A.R., Fraser C.M., Venter J.C. FEBS Lett. 211:200-206(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-27. Ref.2 "Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions." Kobilka B.K., Frielle T., Dohlman H.G., Bolanowski M.A., Dixon R.A.F., Keller P., Caron M.G., Lefkowitz R.J. J. Biol. Chem. 262:7321-7327(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27. Ref.3 "Primary structure of the human beta-adrenergic receptor gene." Schofield P.R., Rhee L.M., Peralta E.G. Nucleic Acids Res. 15:3636-3636(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27. Ref.4 "cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor." Kobilka B.K., Dixon R.A.F., Frielle T., Dohlman H.G., Bolanowski M.A., Sigal I.S., Yang-Feng T.L., Francke U., Caron M.G., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 84:46-50(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-16 AND GLN-27. Ref.5 "Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization." Emorine L.J., Marullo S., Delavier-Klutchko C., Kaveri S.V., Durieu-Trautmann O., Strosberg A.D. Proc. Natl. Acad. Sci. U.S.A. 84:6995-6999(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-27. Ref.6 "Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects." Reihsaus E., Innis M., Macintyre N., Liggett S.B. Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164. Ref.7 "Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population." Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W. Ann. Hum. Genet. 64:135-143(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375. Ref.8 "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], VARIANTS ARG-16 AND GLN-27. Ref.10 Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-27. Ref.11 SeattleSNPs variation discovery resource Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27 AND CYS-220. Ref.12 NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-27. Ref.14 "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], VARIANTS ARG-16 AND GLN-27. Ref.32 "Amino-terminal polymorphisms of the human beta 2-adrenergic receptor impart distinct agonist-promoted regulatory properties." Green S.A., Turki J., Innis M., Ligget S.B. Biochemistry 33:9414-9419(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ARG-16 AND GLN-27, CHARACTERIZATION. Corresponds to variant rs1042714 [ dbSNP | Ensembl ].		VAR_003453
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	34 – 34	1	V → M.1 Publication Manual assertion based on experiment in: Ref.6 "Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects." Reihsaus E., Innis M., Macintyre N., Liggett S.B. Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164.		VAR_003454
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	159 – 159	1	I → F.1 Publication Manual assertion based on experiment in: Ref.7 "Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population." Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W. Ann. Hum. Genet. 64:135-143(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375.		VAR_009125
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	159 – 159	1	I → L.1 Publication Manual assertion based on experiment in: Ref.7 "Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population." Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W. Ann. Hum. Genet. 64:135-143(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375.		VAR_009124
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	164 – 164	1	T → I.1 Publication Manual assertion based on experiment in: Ref.6 "Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects." Reihsaus E., Innis M., Macintyre N., Liggett S.B. Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164. Corresponds to variant rs1800888 [ dbSNP | Ensembl ].		VAR_003455
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	220 – 220	1	S → C.1 Publication Manual assertion based on experiment in: Ref.11 SeattleSNPs variation discovery resource Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27 AND CYS-220. Corresponds to variant rs3729943 [ dbSNP | Ensembl ].		VAR_025101
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	375 – 375	1	K → R.1 Publication Manual assertion based on experiment in: Ref.7 "Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population." Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W. Ann. Hum. Genet. 64:135-143(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375.		VAR_009394

Sequence conflict

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	71 – 71	1	F → L in BAG35969. 1 Publication Ref.9 "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].
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	216 – 216	1	V → A in AAN01267. 1 Publication Ref.8 "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], VARIANTS ARG-16 AND GLN-27.
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	261 – 261	1	S → P in BAD96745. 1 Publication Ref.10 Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-27.
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	402 – 402	1	Q → P in AAH12481. 1 Publication Ref.14 "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], VARIANTS ARG-16 AND GLN-27.

Sequence databases

Genome annotation databases

Polymorphism databases

<div> <p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityⁱ

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

<p>Provides links to various web resources that are relevant for a specific protein.</p><p><a href='../manual/web_resource' target='_top'>More...</a></p> Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors."
   Chung F.-Z., Lentes K.-U., Gocayne J.D., Fitzgerald M.G., Robinson D.A., Kerlavage A.R., Fraser C.M., Venter J.C.
   FEBS Lett. 211:200-206(1987) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-27.
   Tissue: Brain.
   
2. "Delineation of the intronless nature of the genes for the human and hamster beta 2-adrenergic receptor and their putative promoter regions."
   Kobilka B.K., Frielle T., Dohlman H.G., Bolanowski M.A., Dixon R.A.F., Keller P., Caron M.G., Lefkowitz R.J.
   J. Biol. Chem. 262:7321-7327(1987) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27.
3. "Primary structure of the human beta-adrenergic receptor gene."
   Schofield P.R., Rhee L.M., Peralta E.G.
   Nucleic Acids Res. 15:3636-3636(1987) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16 AND GLN-27.
4. "cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor."
   Kobilka B.K., Dixon R.A.F., Frielle T., Dohlman H.G., Bolanowski M.A., Sigal I.S., Yang-Feng T.L., Francke U., Caron M.G., Lefkowitz R.J.
   Proc. Natl. Acad. Sci. U.S.A. 84:46-50(1987) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-16 AND GLN-27.
5. "Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization."
   Emorine L.J., Marullo S., Delavier-Klutchko C., Kaveri S.V., Durieu-Trautmann O., Strosberg A.D.
   Proc. Natl. Acad. Sci. U.S.A. 84:6995-6999(1987) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-27.
6. "Mutations in the gene encoding for the beta 2-adrenergic receptor in normal and asthmatic subjects."
   Reihsaus E., Innis M., Macintyre N., Liggett S.B.
   Am. J. Respir. Cell Mol. Biol. 8:334-339(1993) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-16; GLN-27; MET-34 AND ILE-164.
7. "Beta2-adrenergic receptor allele frequencies in the Quechua, a high altitude native population."
   Rupert J.L., Monsalve M.V., Devine D.V., Hochachka P.W.
   Ann. Hum. Genet. 64:135-143(2000) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27; LEU-159; PHE-159 AND ARG-375.
   Tissue: Blood.
   
8. "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], VARIANTS ARG-16 AND GLN-27.
   Tissue: Heart.
   
9. "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: Brain.
   
10. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLN-27.
    Tissue: Thyroid.
    
11. SeattleSNPs variation discovery resource
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-27 AND CYS-220.
12. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-27.
13. 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.

    , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
14. "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], VARIANTS ARG-16 AND GLN-27.
    Tissue: Fetal brain, Leukocyte and Prostate.
    
15. "Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation."
    Chung F.-Z., Wang C.-D., Potter P.C., Venter J.C., Fraser C.M.
    J. Biol. Chem. 263:4052-4055(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-79.
16. "Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor."
    O'Dowd B.F., Hnatowich M., Caron M.G., Lefkowitz R.J., Bouvier M.
    J. Biol. Chem. 264:7564-7569(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-341, MUTAGENESIS OF CYS-341.
17. "Mutation of tyrosine-141 inhibits insulin-promoted tyrosine phosphorylation and increased responsiveness of the human beta 2-adrenergic receptor."
    Valiquette M., Parent S., Loisel T.P., Bouvier M.
    EMBO J. 14:5542-5549(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-141; TYR-350; TYR-354 AND TYR-366, PHOSPHORYLATION AT TYR-141.
18. "Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors."
    Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M., Sterne-Marr R., Hosey M.M., Benovic J.L.
    J. Biol. Chem. 270:720-731(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
19. "Clathrin-mediated endocytosis of the beta-adrenergic receptor is regulated by phosphorylation/dephosphorylation of beta-arrestin1."
    Lin F.-T., Krueger K.M., Kendall H.E., Daaka Y., Fredericks Z.L., Pitcher J.A., Lefkowitz R.J.
    J. Biol. Chem. 272:31051-31057(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1.
20. "A kinase-regulated PDZ-domain interaction controls endocytic sorting of the beta2-adrenergic receptor."
    Cao T.T., Deacon H.W., Reczek D., Bretscher A., von Zastrow M.
    Nature 401:286-290(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLC9A3R1.
21. "Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes."
    Luttrell L.M., Ferguson S.S.G., Daaka Y., Miller W.E., Maudsley S., Della Rocca G.J., Lin F.-T., Kawakatsu H., Owada K., Luttrell D.K., Caron M.G., Lefkowitz R.J.
    Science 283:655-661(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC AND ARRB1.
22. "The palmitoylation state of the beta(2)-adrenergic receptor regulates the synergistic action of cyclic AMP-dependent protein kinase and beta-adrenergic receptor kinase involved in its phosphorylation and desensitization."
    Moffett S., Rousseau G., Lagace M., Bouvier M.
    J. Neurochem. 76:269-279(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT OF PALMITOYLATION, PHOSPHORYLATION AT SER-345 AND SER-346, MUTAGENESIS OF 345-SER-SER-346.
23. "Modulation of postendocytic sorting of G protein-coupled receptors."
    Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P., Murray S.R., Von Zastrow M.
    Science 297:615-620(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPRASP1.
24. "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
    Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
    Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
    
25. "The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization."
    Berthouze M., Venkataramanan V., Li Y., Shenoy S.K.
    EMBO J. 28:1684-1696(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP20 AND USP33, INTERACTION WITH USP20 AND USP33.
26. "Oxygen-regulated beta(2)-adrenergic receptor hydroxylation by EGLN3 and ubiquitylation by pVHL."
    Xie L., Xiao K., Whalen E.J., Forrester M.T., Freeman R.S., Fong G., Gygi S.P., Lefkowitz R.J., Stamler J.S.
    Sci. Signal. 2:RA33-RA33(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EGLN3 AND VHL, SUBCELLULAR LOCATION, INDUCTION, UBIQUITINATION, HYDROXYLATION AT PRO-382 AND PRO-395, IDENTIFICATION BY MASS SPECTROMETRY.
27. "SNX27 mediates PDZ-directed sorting from endosomes to the plasma membrane."
    Lauffer B.E., Melero C., Temkin P., Lei C., Hong W., Kortemme T., von Zastrow M.
    J. Cell Biol. 190:565-574(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX27.
28. "SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors."
    Temkin P., Lauffer B., Jager S., Cimermancic P., Krogan N.J., von Zastrow M.
    Nat. Cell Biol. 13:715-721(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX27.
29. "Crystal structure of the human beta2 adrenergic G-protein-coupled receptor."
    Rasmussen S.G.F., Choi H.-J., Rosenbaum D.M., Kobilka T.S., Thian F.S., Edwards P.C., Burghammer M., Ratnala V.R.P., Sanishvili R., Fischetti R.F., Schertler G.F.X., Weis W.I., Kobilka B.K.
    Nature 450:383-387(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL, TOPOLOGY.
30. "High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor."
    Cherezov V., Rosenbaum D.M., Hanson M.A., Rasmussen S.G.F., Thian F.S., Kobilka T.S., Choi H.-J., Kuhn P., Weis W.I., Kobilka B.K., Stevens R.C.
    Science 318:1258-1265(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-365 IN COMPLEX WITH CARAZOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
31. "A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor."
    Hanson M.A., Cherezov V., Griffith M.T., Roth C.B., Jaakola V.P., Chien E.Y., Velasquez J., Kuhn P., Stevens R.C.
    Structure 16:897-905(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-365 IN COMPLEX WITH TIMOLOL AND CHOLESTEROL, DISULFIDE BONDS, TOPOLOGY, PALMITOYLATION AT CYS-341.
32. "Amino-terminal polymorphisms of the human beta 2-adrenergic receptor impart distinct agonist-promoted regulatory properties."
    Green S.A., Turki J., Innis M., Ligget S.B.
    Biochemistry 33:9414-9419(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-16 AND GLN-27, CHARACTERIZATION.
33. "Genetic polymorphisms of the beta 2-adrenergic receptor in nocturnal and nonnocturnal asthma. Evidence that Gly16 correlates with the nocturnal phenotype."
    Turki J., Pak J., Green S.A., Martin R.J., Liggett S.B.
    J. Clin. Invest. 95:1635-1641(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-16, POLYMORPHISM.

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Documents

1. 7-transmembrane G-linked receptors
   List of 7-transmembrane G-linked receptor entries
2. Human chromosome 5
   Human chromosome 5: 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

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
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