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P18762

- ADRB2_MOUSE

UniProt

P18762 - ADRB2_MOUSE

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Protein

Beta-2 adrenergic receptor

Gene

Adrb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei113 – 1131Agonist or antagonistBy similarity
Binding sitei118 – 1181Agonist or antagonistBy similarity

GO - Molecular functioni

  1. adenylate cyclase binding Source: BHF-UCL
  2. beta2-adrenergic receptor activity Source: MGI
  3. enzyme binding Source: BHF-UCL
  4. norepinephrine binding Source: HGNC
  5. potassium channel regulator activity Source: Ensembl
  6. protein homodimerization activity Source: HGNC

GO - Biological processi

  1. activation of adenylate cyclase activity Source: HGNC
  2. adenylate cyclase-activating G-protein coupled receptor signaling pathway Source: MGI
  3. adrenergic receptor signaling pathway Source: GOC
  4. bone resorption Source: MGI
  5. brown fat cell differentiation Source: MGI
  6. desensitization of G-protein coupled receptor protein signaling pathway by arrestin Source: HGNC
  7. diet induced thermogenesis Source: MGI
  8. heat generation Source: MGI
  9. negative regulation of multicellular organism growth Source: MGI
  10. negative regulation of smooth muscle contraction Source: MGI
  11. positive regulation of bone mineralization Source: MGI
  12. positive regulation of MAPK cascade Source: HGNC
  13. positive regulation of protein ubiquitination Source: Ensembl
  14. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  15. receptor-mediated endocytosis Source: HGNC
  16. regulation of sodium ion transport Source: MGI
  17. regulation of systemic arterial blood pressure by norepinephrine-epinephrine Source: MGI
  18. regulation of vasodilation Source: InterPro
  19. response to cold Source: MGI
  20. vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_242871. G alpha (s) signalling events.
REACT_255413. Adrenoceptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-2 adrenergic receptor
Alternative name(s):
Beta-2 adrenoreceptor
Short name:
Beta-2 adrenoceptor
Gene namesi
Name:Adrb2
Synonyms:Adrb2r
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:87938. Adrb2.

Subcellular locationi

Cell membrane By similarity; Multi-pass membrane protein By similarity
Note: Colocalizes with VHL on cell membranes.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3434ExtracellularBy similarityAdd
BLAST
Transmembranei35 – 5824Helical; Name=1By similarityAdd
BLAST
Topological domaini59 – 7113CytoplasmicBy similarityAdd
BLAST
Transmembranei72 – 9524Helical; Name=2By similarityAdd
BLAST
Topological domaini96 – 10611ExtracellularBy similarityAdd
BLAST
Transmembranei107 – 12923Helical; Name=3By similarityAdd
BLAST
Topological domaini130 – 15021CytoplasmicBy similarityAdd
BLAST
Transmembranei151 – 17424Helical; Name=4By similarityAdd
BLAST
Topological domaini175 – 19622ExtracellularBy similarityAdd
BLAST
Transmembranei197 – 22024Helical; Name=5By similarityAdd
BLAST
Topological domaini221 – 27454CytoplasmicBy similarityAdd
BLAST
Transmembranei275 – 29824Helical; Name=6By similarityAdd
BLAST
Topological domaini299 – 3057ExtracellularBy similarity
Transmembranei306 – 32924Helical; Name=7By similarityAdd
BLAST
Topological domaini330 – 41889CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: MGI
  2. integral component of plasma membrane Source: Ensembl
  3. membrane Source: MGI
  4. nucleus Source: MGI
  5. plasma membrane Source: MGI
  6. receptor complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Beta-2 adrenergic receptorPRO_0000069134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi6 – 61N-linked (GlcNAc...)Curated
Glycosylationi15 – 151N-linked (GlcNAc...)Curated
Disulfide bondi106 ↔ 191PROSITE-ProRule annotation
Modified residuei141 – 1411PhosphotyrosineBy similarity
Disulfide bondi184 ↔ 190PROSITE-ProRule annotation
Modified residuei246 – 2461PhosphoserineBy similarity
Modified residuei261 – 2611Phosphoserine; by PKASequence Analysis
Modified residuei262 – 2621Phosphoserine; by PKASequence Analysis
Lipidationi341 – 3411S-palmitoyl cysteineBy similarity
Modified residuei345 – 3451Phosphoserine; by PKABy similarity
Modified residuei346 – 3461Phosphoserine; by PKABy similarity
Modified residuei355 – 3551Phosphoserine; by BARKCurated
Modified residuei356 – 3561Phosphoserine; by BARKCurated
Modified residuei387 – 38714-hydroxyprolineBy similarity
Modified residuei400 – 40014-hydroxyprolineBy similarity

Post-translational modificationi

Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity).By similarity
Phosphorylated by PKA and BARK upon agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.
Phosphorylation of Tyr-141 is induced by insulin and leads to supersensitization of the receptor.By similarity
Polyubiquitinated. Agonist-induced ubiquitination leads to sort internalized receptors to the lysosomes for degradation. Deubiquitination by USP20 and USP33, leads to ADRB2 recycling and resensitization after prolonged agonist stimulation. USP20 and USP33 are constitutively associated and are dissociated immediately after agonist stimulation. Ubiquitination by the VHL-E3 ligase complex is oxygen-dependent (By similarity).By similarity
Hydroxylation by EGLN3 occurs only under normoxia and increases the interaction with VHL and the subsequent ubiquitination and degradation of ADRB2.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP18762.

PTM databases

PhosphoSiteiP18762.

Expressioni

Gene expression databases

BgeeiP18762.
CleanExiMM_ADRB2.
ExpressionAtlasiP18762. baseline and differential.
GenevestigatoriP18762.

Interactioni

Subunit structurei

Binds SLC9A3R1 and GPRASP1. Interacts with ARRB1 and ARRB2. Interacts with SRC, USP20 and USP33. Interacts with VHL; the interaction, which is increased on hydroxylation of ADRB2, ubiquitinates ADRB2 leading to its degradation. Interacts with EGLN3; the interaction hydroxylates ADRB2 facilitating VHL-E3 ligase-mediated ubiquitination. Interacts (via PDZ-binding motif) with SNX27 (via PDZ domain); the interaction is required when endocytosed to prevent degradation in lysosomes and promote recycling to the plasma membrane (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-59568N.
IntActiP18762. 5 interactions.
MINTiMINT-1793203.

Structurei

3D structure databases

ProteinModelPortaliP18762.
SMRiP18762. Positions 7-342.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 20715Agonist and antagonist bindingBy similarityAdd
BLAST
Regioni286 – 2938Agonist and antagonist bindingBy similarity
Regioni312 – 3165Agonist and antagonist bindingBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi415 – 4184PDZ-binding

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Adrenergic receptor subfamily. ADRB2 sub-subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG262978.
GeneTreeiENSGT00760000118774.
HOGENOMiHOG000239242.
HOVERGENiHBG106962.
InParanoidiP18762.
KOiK04142.
OMAiRVFQVAK.
OrthoDBiEOG7BS4BS.
TreeFamiTF316350.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24248:SF21. PTHR24248:SF21. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18762-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGPHGNDSDF LLAPNGSRAP DHDVTQERDE AWVVGMAILM SVIVLAIVFG
60 70 80 90 100
NVLVITAIAK FERLQTVTNY FIISLACADL VMGLAVVPFG ASHILMKMWN
110 120 130 140 150
FGNFWCEFWT SIDVLCVTAS IETLCVIAVD RYVAITSPFK YQSLLTKNKA
160 170 180 190 200
RVVILMVWIV SGLTSFLPIQ MHWYRATHKK AIDCYTEETC CDFFTNQAYA
210 220 230 240 250
IASSIVSFYV PLVVMVFVYS RVFQVAKRQL QKIDKSEGRF HAQNLSQVEQ
260 270 280 290 300
DGRSGHGLRR SSKFCLKEHK ALKTLGIIMG TFTLCWLPFF IVNIVHVIRD
310 320 330 340 350
NLIPKEVYIL LNWLGYVNSA FNPLIYCRSP DFRIAFQELL CLRRSSSKTY
360 370 380 390 400
GNGYSSNSNG RTDYTGEPNT CQLGQEREQE LLCEDPPGME GFVNCQGTVP
410
SLSVDSQGRN CSTNDSPL
Length:418
Mass (Da):46,998
Last modified:July 27, 2011 - v2
Checksum:i51D1EC73D7619D58
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211D → H in CAA33664. (PubMed:2549959)Curated
Sequence conflicti94 – 952IL → TS in CAA33664. (PubMed:2549959)Curated
Sequence conflicti254 – 2541S → T in CAA33664. (PubMed:2549959)Curated
Sequence conflicti347 – 3482SK → FE in CAA33664. (PubMed:2549959)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15643 Genomic DNA. Translation: CAA33664.1.
AK080241 mRNA. Translation: BAC37856.1.
CH466528 Genomic DNA. Translation: EDL09746.1.
BC032883 mRNA. Translation: AAH32883.1.
CCDSiCCDS29289.1.
PIRiS00260.
RefSeqiNP_031446.2. NM_007420.3.
UniGeneiMm.5598.

Genome annotation databases

EnsembliENSMUST00000053640; ENSMUSP00000062256; ENSMUSG00000045730.
GeneIDi11555.
KEGGimmu:11555.
UCSCiuc008fcy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15643 Genomic DNA. Translation: CAA33664.1 .
AK080241 mRNA. Translation: BAC37856.1 .
CH466528 Genomic DNA. Translation: EDL09746.1 .
BC032883 mRNA. Translation: AAH32883.1 .
CCDSi CCDS29289.1.
PIRi S00260.
RefSeqi NP_031446.2. NM_007420.3.
UniGenei Mm.5598.

3D structure databases

ProteinModelPortali P18762.
SMRi P18762. Positions 7-342.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59568N.
IntActi P18762. 5 interactions.
MINTi MINT-1793203.

Chemistry

ChEMBLi CHEMBL2111395.
GuidetoPHARMACOLOGYi 29.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P18762.

Proteomic databases

PRIDEi P18762.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000053640 ; ENSMUSP00000062256 ; ENSMUSG00000045730 .
GeneIDi 11555.
KEGGi mmu:11555.
UCSCi uc008fcy.1. mouse.

Organism-specific databases

CTDi 154.
MGIi MGI:87938. Adrb2.

Phylogenomic databases

eggNOGi NOG262978.
GeneTreei ENSGT00760000118774.
HOGENOMi HOG000239242.
HOVERGENi HBG106962.
InParanoidi P18762.
KOi K04142.
OMAi RVFQVAK.
OrthoDBi EOG7BS4BS.
TreeFami TF316350.

Enzyme and pathway databases

Reactomei REACT_242871. G alpha (s) signalling events.
REACT_255413. Adrenoceptors.

Miscellaneous databases

NextBioi 279054.
PROi P18762.
SOURCEi Search...

Gene expression databases

Bgeei P18762.
CleanExi MM_ADRB2.
ExpressionAtlasi P18762. baseline and differential.
Genevestigatori P18762.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR002233. ADR_fam.
IPR000332. ADRB2_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24248:SF21. PTHR24248:SF21. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR01103. ADRENERGICR.
PR00562. ADRENRGCB2AR.
PR00237. GPCRRHODOPSN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isoproterenol response following transfection of the mouse beta 2-adrenergic receptor gene into Y1 cells."
    Allen J.M., Baetge E.E., Abrass I.B., Palmiter R.D.
    EMBO J. 7:133-138(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genetic regulation of beta 2-adrenergic receptors in 3T3-L1 fibroblasts."
    Nakada M.T., Haskell K.M., Ecker D.J., Stadel J.M., Crooke S.T.
    Biochem. J. 260:53-59(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.

Entry informationi

Entry nameiADRB2_MOUSE
AccessioniPrimary (citable) accession number: P18762
Secondary accession number(s): Q8BH38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3