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Protein

Beta-arrestin-2

Gene

Arrb2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires ADRBK1. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity).By similarity10 Publications

GO - Molecular functioni

  • 14-3-3 protein binding Source: RGD
  • alpha-1A adrenergic receptor binding Source: RGD
  • alpha-1B adrenergic receptor binding Source: RGD
  • clathrin binding Source: RGD
  • D1 dopamine receptor binding Source: RGD
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein coupled receptor binding Source: RGD
  • mitogen-activated protein kinase binding Source: RGD
  • platelet activating factor receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • type 1 angiotensin receptor binding Source: RGD
  • type 2A serotonin receptor binding Source: RGD

GO - Biological processi

  • adult walking behavior Source: Ensembl
  • brain development Source: RGD
  • cell chemotaxis Source: Ensembl
  • desensitization of G-protein coupled receptor protein signaling pathway by arrestin Source: RGD
  • detection of temperature stimulus involved in sensory perception of pain Source: RGD
  • endocytosis Source: RGD
  • follicle-stimulating hormone signaling pathway Source: RGD
  • G-protein coupled receptor internalization Source: Ensembl
  • G-protein coupled receptor signaling pathway Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • negative regulation of GTPase activity Source: RGD
  • negative regulation of interleukin-12 production Source: Ensembl
  • negative regulation of interleukin-1 beta production Source: Ensembl
  • negative regulation of interleukin-6 production Source: Ensembl
  • negative regulation of natural killer cell mediated cytotoxicity Source: Ensembl
  • negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  • negative regulation of protein ubiquitination Source: RGD
  • negative regulation of release of cytochrome c from mitochondria Source: RGD
  • negative regulation of smooth muscle cell apoptotic process Source: RGD
  • negative regulation of toll-like receptor signaling pathway Source: Ensembl
  • negative regulation of tumor necrosis factor production Source: Ensembl
  • positive regulation of calcium ion transport Source: RGD
  • positive regulation of DNA biosynthetic process Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: RGD
  • positive regulation of peptidyl-serine phosphorylation Source: RGD
  • positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
  • positive regulation of protein kinase B signaling Source: RGD
  • positive regulation of protein phosphorylation Source: RGD
  • positive regulation of protein ubiquitination Source: Ensembl
  • positive regulation of receptor internalization Source: RGD
  • positive regulation of synaptic transmission, dopaminergic Source: Ensembl
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  • protein transport Source: UniProtKB-KW
  • protein ubiquitination Source: Ensembl
  • regulation of androgen receptor signaling pathway Source: Ensembl
  • regulation of cAMP biosynthetic process Source: RGD
  • regulation of cAMP catabolic process Source: RGD
  • regulation of G-protein coupled receptor protein signaling pathway Source: RGD
  • transcription from RNA polymerase II promoter Source: Ensembl
  • transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-RNO-5099900. WNT5A-dependent internalization of FZD4.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-arrestin-2
Alternative name(s):
Arrestin beta-2
Gene namesi
Name:Arrb2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2157. Arrb2.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: RGD
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • dendritic spine Source: RGD
  • endocytic vesicle Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 122KK → RR: Transient ubiquitination; no stable endocytic complexes with AGTR1; impaired in scaffolding-activated ERK1/2. 1 Publication
Mutagenesisi18 – 181K → R: Promotes agonist-stimulated down-regulation of CHRM2 and CHRM1; no effect on internalization of CHRM2; when associated with R-107, R-108, R-207 and R-296. 1 Publication
Mutagenesisi54 – 541V → A: Inhibits internalization of EDNRA and EDNRB. 1 Publication
Mutagenesisi107 – 1071K → R: Promotes agonist-stimulated down-regulation of CHRM2 and CHRM1; no effect on internalization of CHRM2; when associated with R-18, R-108, R-207 and R-296. 1 Publication
Mutagenesisi108 – 1081K → R: Promotes agonist-stimulated down-regulation of CHRM2 and CHRM1; no effect on internalization of CHRM2; when associated with R-18, R-107, R-207 and R-296. 1 Publication
Mutagenesisi198 – 1981S → P: Greatly reduces interaction with MAPK10. 1 Publication
Mutagenesisi207 – 2071K → R: Promotes agonist-stimulated down-regulation of CHRM2 and CHRM1; no effect on internalization of CHRM2; when associated with R-18, R-107, R-108 and R-296. 1 Publication
Mutagenesisi296 – 2961K → R: Promotes agonist-stimulated down-regulation of CHRM2 and CHRM1; no effect on internalization of CHRM2; when associated with R-18, R-107, R-108 and R-207. 1 Publication
Mutagenesisi361 – 3611S → D: Almost abolishes phosphorylation; inhibits internalization of ADRB2; when associated with D-383. 1 Publication
Mutagenesisi361 – 3611S → D: Reduces interaction with CLTC. 1 Publication
Mutagenesisi374 – 3774LIEF → AAEA: Abolishes interaction with CLTC; reduces interaction with AP2B1. 1 Publication
Mutagenesisi383 – 3831T → D: Almost abolishes phosphorylation; inhibits internalization of ADRB2; when associated with D-361. 1 Publication
Mutagenesisi383 – 3831T → D: Reduces interaction with CLTC. 1 Publication
Mutagenesisi394 – 3941R → A: Abolishes interaction with AP2B1; no effect on interaction with clathrin.
Mutagenesisi396 – 3961R → A: Abolishes interaction with AP2B1. 1 Publication
Mutagenesisi398 – 3981K → A: No effect on interaction with AP2B1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410Beta-arrestin-2PRO_0000205201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphotyrosineBy similarity
Modified residuei176 – 1761Hydroxyproline; by PHD2By similarity
Modified residuei181 – 1811Hydroxyproline; by PHD2By similarity
Modified residuei361 – 3611Phosphoserine1 Publication
Modified residuei383 – 3831Phosphothreonine; by CaMK21 Publication

Post-translational modificationi

Phosphorylated at Thr-383 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1 (By similarity).By similarity
The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occurr GPCR-specifc. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33. Stimulation of a class B GPCR promotes a sustained ubiquitination (By similarity).By similarity
Hydroxylation by PHD2 modulates the rate of internalization by slowing down recruitment to the plasma membrane and inhibiting subsequent co-internalization with class A receptors.By similarity

Keywords - PTMi

Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29067.
PRIDEiP29067.

PTM databases

iPTMnetiP29067.
PhosphoSiteiP29067.

Expressioni

Tissue specificityi

Predominantly localized in neuronal tissues and in the spleen.

Gene expression databases

GenevisibleiP29067. RN.

Interactioni

Subunit structurei

Homooligomer; the self-association is mediated by InsP6-binding (Probable). Heterooligomer with ARRB1; the association is mediated by InsP6-binding. Interacts with ADRB2 AND CHRM2. Interacts with PDE4A. Interacts with PDE4D. Interacts with MAPK10, MAPK1 and MAPK3. Interacts with DRD2. Interacts with FSHR. Interacts with CLTC. Interacts with HTR2C. Interacts with CCR5. Interacts with CXCR4. Interacts with SRC. Interacts with DUSP16; the interaction is interrupted by stimulation of AGTR1 and activation of MAPK10. Interacts with CHUK; the interaction is enhanced stimulation of ADRB2. Interacts with RELA. Interacts with MDM2; the interaction is enhanced by activation of GPCRs. Interacts with SLC9A5. Interacts with TRAF6. Interacts with IGF1R. Interacts with ENG. Interacts with KIR2DL1, KIR2DL3 and KIR2DL4. Interacts with LDLR. Interacts with AP2B1. Interacts with C5AR1. Interacts with RAF1. Interacts with MAP2K1. Interacts with MAPK1. Interacts with MAPK10; the interaction enhances MAPK10 activation by MAP3K5. Interacts with MAP2K4; the interaction is enhanced by presence of MAP3K5 and MAPK10. Interacts with MAP3K5. Interacts with AKT1. Interacts with IKBKB and MAP3K14. Interacts with SMO (activated). Interacts with GSK3A and GSK3B. Associates with protein phosphatase 2A (PP2A). Interacts with CXCR4; the interaction is dependent on C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with GPR143. Interacts with HCK and CXCR1 (phosphorylated) (By similarity). Interacts with ACKR3 and ACKR4 (By similarity).By similarityCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-1636616,EBI-296087From a different organism.
LIMK1P536672EBI-1636616,EBI-444403From a different organism.

GO - Molecular functioni

  • 14-3-3 protein binding Source: RGD
  • alpha-1A adrenergic receptor binding Source: RGD
  • alpha-1B adrenergic receptor binding Source: RGD
  • clathrin binding Source: RGD
  • D1 dopamine receptor binding Source: RGD
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein coupled receptor binding Source: RGD
  • mitogen-activated protein kinase binding Source: RGD
  • platelet activating factor receptor binding Source: RGD
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • type 1 angiotensin receptor binding Source: RGD
  • type 2A serotonin receptor binding Source: RGD

Protein-protein interaction databases

BioGridi247426. 8 interactions.
DIPiDIP-40507N.
IntActiP29067. 14 interactions.
MINTiMINT-151424.
STRINGi10116.ENSRNOP00000026207.

Structurei

3D structure databases

ProteinModelPortaliP29067.
SMRiP29067. Positions 6-394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni241 – 410170Interaction with TRAF6By similarityAdd
BLAST
Regioni378 – 41033Interaction with AP2B1Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi386 – 39611[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motifBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP29067.
KOiK04439.
OMAiHSKPQSA.
OrthoDBiEOG79W954.
PhylomeDBiP29067.

Family and domain databases

Gene3Di2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProiIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11792. PTHR11792. 1 hit.
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSiPR00309. ARRESTIN.
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.
PROSITEiPS00295. ARRESTINS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29067-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK
60 70 80 90 100
DRKVFVTLTC AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR
110 120 130 140 150
LQDRLLKKLG QHAHPFFFTI PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF
160 170 180 190 200
CAKSIEEKSH KRNSVRLIIR KVQFAPETPG PQPSAETTRH FLMSDRRSLH
210 220 230 240 250
LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY ADICLFSTAQ
260 270 280 290 300
YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT
310 320 330 340 350
NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP
360 370 380 390 400
HDHITLPRPQ SAPREIDIPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM
410
KDDDCDDQFC
Length:410
Mass (Da):46,340
Last modified:December 1, 1992 - v1
Checksum:i0DFA6A897C2B86BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91590 mRNA. Translation: AAA74460.1.
BC087578 mRNA. Translation: AAH87578.1.
U03627 mRNA. Translation: AAA17551.1.
AF051457 Genomic DNA. Translation: AAC28617.1.
PIRiA59279.
RefSeqiNP_037043.1. NM_012911.1.
UniGeneiRn.32973.

Genome annotation databases

EnsembliENSRNOT00000026207; ENSRNOP00000026207; ENSRNOG00000019308.
GeneIDi25388.
KEGGirno:25388.
UCSCiRGD:2157. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91590 mRNA. Translation: AAA74460.1.
BC087578 mRNA. Translation: AAH87578.1.
U03627 mRNA. Translation: AAA17551.1.
AF051457 Genomic DNA. Translation: AAC28617.1.
PIRiA59279.
RefSeqiNP_037043.1. NM_012911.1.
UniGeneiRn.32973.

3D structure databases

ProteinModelPortaliP29067.
SMRiP29067. Positions 6-394.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247426. 8 interactions.
DIPiDIP-40507N.
IntActiP29067. 14 interactions.
MINTiMINT-151424.
STRINGi10116.ENSRNOP00000026207.

PTM databases

iPTMnetiP29067.
PhosphoSiteiP29067.

Proteomic databases

PaxDbiP29067.
PRIDEiP29067.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000026207; ENSRNOP00000026207; ENSRNOG00000019308.
GeneIDi25388.
KEGGirno:25388.
UCSCiRGD:2157. rat.

Organism-specific databases

CTDi409.
RGDi2157. Arrb2.

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP29067.
KOiK04439.
OMAiHSKPQSA.
OrthoDBiEOG79W954.
PhylomeDBiP29067.

Enzyme and pathway databases

ReactomeiR-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).
R-RNO-5099900. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

NextBioi606447.
PROiP29067.

Gene expression databases

GenevisibleiP29067. RN.

Family and domain databases

Gene3Di2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProiIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11792. PTHR11792. 1 hit.
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSiPR00309. ARRESTIN.
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.
PROSITEiPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family."
    Attramadal H., Arriza J.L., Aoki C., Dawson T.M., Codina J., Kwatra M.M., Snyder S.H., Caron M.G., Lefkowitz R.J.
    J. Biol. Chem. 267:17882-17890(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "Cone arrestin identified by targeting expression of a functional family."
    Craft C.M., Whitmore D.H., Wiechmann A.F.
    J. Biol. Chem. 269:4613-4619(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 295-410.
    Tissue: Pineal gland.
  4. "Differential expression of alternative splice variants of beta-arrestin-1 and -2 in rat central nervous system and peripheral tissues."
    Komori N., Cain S.D., Roch J.-M., Miller K.E., Matsumoto H.
    Eur. J. Neurosci. 10:2607-2616(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-386.
    Strain: Sprague-Dawley.
    Tissue: Retina.
  5. "beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor."
    Lin F.-T., Daaka Y., Lefkowitz R.J.
    J. Biol. Chem. 273:31640-31643(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGF1R.
  6. "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis."
    Laporte S.A., Oakley R.H., Zhang J., Holt J.A., Ferguson S.S.G., Caron M.G., Barak L.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:3712-3717(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF ADRB2, INTERACTION WITH CLTC AND AP2B1, MUTAGENESIS OF 374-LEU--PHE-377, SUBCELLULAR LOCATION.
  7. "beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis."
    Miller W.E., Maudsley S., Ahn S., Khan K.D., Luttrell L.M., Lefkowitz R.J.
    J. Biol. Chem. 275:11312-11319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRC.
  8. "Regulation and intracellular trafficking pathways of the endothelin receptors."
    Bremnes T., Paasche J.D., Mehlum A., Sandberg C., Bremnes B., Attramadal H.
    J. Biol. Chem. 275:17596-17604(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF EDNRA AND EDNRB, MUTAGENESIS OF VAL-54.
  9. "The interaction of beta-arrestin with the AP-2 adaptor is required for the clustering of beta 2-adrenergic receptor into clathrin-coated pits."
    Laporte S.A., Oakley R.H., Holt J.A., Barak L.S., Caron M.G.
    J. Biol. Chem. 275:23120-23126(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AP2B1 AND CLTC, MUTAGENESIS OF ARG-396 AND LYS-398.
  10. "Selective recruitment of arrestin-3 to clathrin coated pits upon stimulation of G protein-coupled receptors."
    Santini F., Penn R.B., Gagnon A.W., Benovic J.L., Keen J.H.
    J. Cell Sci. 113:2463-2470(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3."
    McDonald P.H., Chow C.W., Miller W.E., Laporte S.A., Field M.E., Lin F.-T., Davis R.J., Lefkowitz R.J.
    Science 290:1574-1577(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAPK SIGNALING, INTERACTION WITH MAPK10; MAP2K4 AND MAP3K5.
  12. "Characterization of sequence determinants within the carboxyl-terminal domain of chemokine receptor CCR5 that regulate signaling and receptor internalization."
    Kraft K., Olbrich H., Majoul I., Mack M., Proudfoot A., Oppermann M.
    J. Biol. Chem. 276:34408-34418(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCR5.
  13. "Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds."
    Luttrell L.M., Roudabush F.L., Choy E.W., Miller W.E., Field M.E., Pierce K.L., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 98:2449-2454(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAPK SIGNALING, INTERACTION WITH RAF1; MAP2K1 AND MAPK1.
  14. "Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin."
    Shenoy S.K., McDonald P.H., Kohout T.A., Lefkowitz R.J.
    Science 294:1307-1313(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH MDM2.
  15. "Phosphorylation of beta-arrestin2 regulates its function in internalization of beta(2)-adrenergic receptors."
    Lin F.-T., Chen W., Shenoy S., Cong M., Exum S.T., Lefkowitz R.J.
    Biochemistry 41:10692-10699(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-361 AND THR-383, INTERACTION WITH CLTC, MUTAGENESIS OF SER-361 AND THR-383.
  16. "beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: identification of a beta-arrestin binding site in beta 2-adaptin."
    Laporte S.A., Miller W.E., Kim K.-M., Caron M.G.
    J. Biol. Chem. 277:9247-9254(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.
  17. "beta-Arrestin scaffolding of the ERK cascade enhances cytosolic ERK activity but inhibits ERK-mediated transcription following angiotensin AT1a receptor stimulation."
    Tohgo A., Pierce K.L., Choy E.W., Lefkowitz R.J., Luttrell L.M.
    J. Biol. Chem. 277:9429-9436(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ERK SIGNALING.
  18. "Phosphorylation of key serine residues is required for internalization of the complement 5a (C5a) anaphylatoxin receptor via a beta-arrestin, dynamin, and clathrin-dependent pathway."
    Braun L., Christophe T., Boulay F.
    J. Biol. Chem. 278:4277-4285(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF C5AR1, SUBCELLULAR LOCATION, INTERACTION WITH C5AR1.
  19. "The adaptor protein beta-arrestin2 enhances endocytosis of the low density lipoprotein receptor."
    Wu J.-H., Peppel K., Nelson C.D., Lin F.-T., Kohout T.A., Miller W.E., Exum S.T., Freedman N.J.
    J. Biol. Chem. 278:44238-44245(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LDLR.
  20. "The unique amino-terminal region of the PDE4D5 cAMP phosphodiesterase isoform confers preferential interaction with beta-arrestins."
    Bolger G.B., McCahill A., Huston E., Cheung Y.F., McSorley T., Baillie G.S., Houslay M.D.
    J. Biol. Chem. 278:49230-49238(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE4D.
  21. "beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha."
    Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHUK; IKBKB AND MAP3K14.
  22. "Activity-dependent internalization of smoothened mediated by beta-arrestin 2 and GRK2."
    Chen W., Ren X.R., Nelson C.D., Barak L.S., Chen J.K., Beachy P.A., de Sauvage F., Lefkowitz R.J.
    Science 306:2257-2260(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMO.
  23. "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic neurotransmission and behavior."
    Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J., Gainetdinov R.R., Caron M.G.
    Cell 122:261-273(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AKT1; GSK3A AND GSK3B.
  24. "Receptor-specific ubiquitination of beta-arrestin directs assembly and targeting of seven-transmembrane receptor signalosomes."
    Shenoy S.K., Lefkowitz R.J.
    J. Biol. Chem. 280:15315-15324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, MUTAGENESIS OF 11-LYS-LYS-12.
  25. "{beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase."
    Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R.J., Larsson O.
    J. Biol. Chem. 280:24412-24419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF IGF1R.
  26. "Identification and characterization of PDE4A11, a novel, widely expressed long isoform encoded by the human PDE4A cAMP phosphodiesterase gene."
    Wallace D.A., Johnston L.A., Huston E., Macmaster D., Houslay T.M., Cheung Y.-F., Campbell L., Millen J.E., Smith R.A., Gall I., Knowles R.G., Sullivan M., Houslay M.D.
    Mol. Pharmacol. 67:1920-1934(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE4A.
  27. "Ubiquitination of beta-arrestin links seven-transmembrane receptor endocytosis and ERK activation."
    Shenoy S.K., Barak L.S., Xiao K., Ahn S., Berthouze M., Shukla A.K., Luttrell L.M., Lefkowitz R.J.
    J. Biol. Chem. 282:29549-29562(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  28. "Role of beta-arrestin-mediated desensitization and signaling in the control of angiotensin AT1a receptor-stimulated transcription."
    Lee M.-H., El-Shewy H.M., Luttrell D.K., Luttrell L.M.
    J. Biol. Chem. 283:2088-2097(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DESENSITIZATION OF AGTR1, FUNCTION IN AGTR1-MEDIATED ERK SIGNALING.
  29. "The beta-arrestin-2 scaffold protein promotes c-Jun N-terminal kinase-3 activation by binding to its nonconserved N terminus."
    Guo C., Whitmarsh A.J.
    J. Biol. Chem. 283:15903-15911(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAPK SIGNALING, INTERACTION WITH MAPK10 AND MAP3K5, MUTAGENESIS OF SER-198.
  30. "Differential role of beta-arrestin ubiquitination in agonist-promoted down-regulation of M1 vs M2 muscarinic acetylcholine receptors."
    Mosser V.A., Jones K.T., Hoffman K.M., McCarty N.A., Jackson D.A.
    J. Mol. Signal. 3:20-20(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF CHRM1 AND CHRM2, MUTAGENESIS OF LYS-18; LYS-107; LYS-108; LYS-207 AND LYS-296.

Entry informationi

Entry nameiARRB2_RAT
AccessioniPrimary (citable) accession number: P29067
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: May 11, 2016
This is version 132 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.