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Protein

Beta-arrestin-1

Gene

Arrb1

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. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. 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). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. 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). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. 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. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. 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. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) (By similarity). Involved in IL8-mediated granule release in neutrophils. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity).By similarity20 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei250 – 2501Inositol hexakisphosphateBy similarity
Binding sitei255 – 2551Inositol hexakisphosphateBy similarity
Binding sitei324 – 3241Inositol hexakisphosphateBy similarity
Binding sitei326 – 3261Inositol hexakisphosphateBy similarity

GO - Molecular functioni

  • alpha-1A adrenergic receptor binding Source: RGD
  • alpha-1B adrenergic receptor binding Source: RGD
  • AP-2 adaptor complex binding Source: BHF-UCL
  • clathrin adaptor activity Source: BHF-UCL
  • clathrin binding Source: RGD
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: Ensembl
  • estrogen receptor binding Source: RGD
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein coupled receptor binding Source: RGD
  • GTPase activator activity Source: Ensembl
  • ion channel binding Source: RGD
  • phosphoprotein binding Source: UniProtKB
  • protein phosphorylated amino acid binding Source: RGD
  • transcription regulatory region DNA binding Source: Ensembl
  • V2 vasopressin receptor binding Source: RGD

GO - Biological processi

  • activation of MAPK activity Source: RGD
  • adenylate cyclase-modulating G-protein coupled receptor signaling pathway Source: RGD
  • desensitization of G-protein coupled receptor protein signaling pathway by arrestin 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 ERK1 and ERK2 cascade Source: RGD
  • negative regulation of GTPase activity Source: RGD
  • negative regulation of interleukin-6 production Source: Ensembl
  • negative regulation of interleukin-8 production Source: Ensembl
  • negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  • negative regulation of protein phosphorylation Source: RGD
  • negative regulation of protein ubiquitination Source: Ensembl
  • phototransduction Source: Ensembl
  • positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • positive regulation of ERK1 and ERK2 cascade Source: RGD
  • positive regulation of histone H4 acetylation Source: Ensembl
  • positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: Ensembl
  • positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  • positive regulation of protein binding Source: Ensembl
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of protein ubiquitination Source: RGD
  • positive regulation of receptor internalization Source: UniProtKB
  • positive regulation of Rho protein signal transduction Source: Ensembl
  • positive regulation of smooth muscle cell apoptotic process Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  • protein transport Source: UniProtKB-KW
  • protein ubiquitination 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
  • sensory perception of pain Source: RGD
  • sensory perception of touch Source: RGD
  • stress fiber assembly Source: Ensembl
  • transcription from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiR-RNO-418555. G alpha (s) signalling events.
R-RNO-432720. Lysosome Vesicle Biogenesis.
R-RNO-432722. Golgi Associated Vesicle Biogenesis.
R-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-arrestin-1
Alternative name(s):
Arrestin beta-1
Gene namesi
Name:Arrb1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi2156. Arrb1.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: RGD
  • chromatin Source: Ensembl
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: RGD
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytosol Source: RGD
  • dendritic spine Source: RGD
  • nucleoplasm Source: Ensembl
  • nucleus Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: RGD
  • pseudopodium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi53 – 531V → D: Inhibits internalization of EDNRA, EDNRB and ADRB2. No effect on interaction with SRC; impairs ADRB2- and HTR1A-mediated ERK phosphorylation; impairs sequestration of ADRB2. 3 Publications
Mutagenesisi91 – 911P → G: Impairs interaction with SRC; impairs ADRB2- and HTR1A-mediated ERK phosphorylation; no effect on sequestration of ADRB2; when associated with E-121. 1 Publication
Mutagenesisi121 – 1211P → E: Impairs interaction with SRC; impairs ADRB2- and HTR1A-mediated ERK phosphorylation; no effect on sequestration of ADRB2; when associated with G-91. 1 Publication
Mutagenesisi412 – 4121S → A: Abolishes phosphorylation and inhibits ADRB2 endocytosis; no effect on interaction with ADRB2. 3 Publications
Mutagenesisi412 – 4121S → D: Impairs interaction with SRC; impairs ADRB2-mediated ERK phosphorylation and IGFR1-mediated MAP kinase phosphorylation of GAB1; impairs sequestration of ADRB2 and IGFR1; abolishes interaction with clathrin; no effect on interaction with ADRB2 and IGFR1. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Beta-arrestin-1PRO_0000205197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471PhosphotyrosineBy similarity
Modified residuei412 – 4121PhosphoserineCombined sources1 Publication
Modified residuei412 – 4121Phosphoserine; by GRK5By similarity

Post-translational modificationi

Constitutively phosphorylated at Ser-412 in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and beta-2 adrenergic receptor/ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated.1 Publication
The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. 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 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP29066.
PRIDEiP29066.

PTM databases

iPTMnetiP29066.
PhosphoSiteiP29066.

Expressioni

Tissue specificityi

Predominantly localized in neuronal tissues and in the spleen.

Gene expression databases

GenevisibleiP29066. RN.

Interactioni

Subunit structurei

Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated at 'Tyr-737'); phosphorylation of AP2B1 at 'Tyr-737' disrupts the interaction. Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2 and ADRBK1. Interacts with CRR5. Interacts with PTAFR (phosphorylated on serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and the protein kinase domain); the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with TACR1. Interacts with RAF1. Interacts with CHUK, IKBKB and MAP3K14. Interacts with DVL1; the interaction is enhanced by phosphorylation of DVL1. Interacts with DVL2; the interaction is enhanced by phosphorylation of DVL2. Interacts with IGF1R. Associates with MAP kinase p38. Part of a MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3 (activated). Interacts with GPR143 (By similarity). Interacts with MAP2K4/MKK4 (By similarity). Interacts with HCK and CXCR1 (phosphorylated). Interacts with ACKR3 and ACKR4 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LIMK1P536672EBI-4303019,EBI-444403From a different organism.
PDXPQ96GD02EBI-4303019,EBI-4303060From a different organism.

GO - Molecular functioni

  • alpha-1A adrenergic receptor binding Source: RGD
  • alpha-1B adrenergic receptor binding Source: RGD
  • AP-2 adaptor complex binding Source: BHF-UCL
  • clathrin adaptor activity Source: BHF-UCL
  • clathrin binding Source: RGD
  • estrogen receptor binding Source: RGD
  • follicle-stimulating hormone receptor binding Source: RGD
  • G-protein coupled receptor binding Source: RGD
  • ion channel binding Source: RGD
  • phosphoprotein binding Source: UniProtKB
  • protein phosphorylated amino acid binding Source: RGD
  • V2 vasopressin receptor binding Source: RGD

Protein-protein interaction databases

BioGridi247425. 7 interactions.
DIPiDIP-40808N.
IntActiP29066. 5 interactions.
MINTiMINT-89355.
STRINGi10116.ENSRNOP00000046069.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 126Combined sources
Beta strandi16 – 238Combined sources
Beta strandi25 – 295Combined sources
Beta strandi37 – 437Combined sources
Turni45 – 473Combined sources
Beta strandi53 – 6311Combined sources
Beta strandi73 – 8715Combined sources
Helixi99 – 10810Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi127 – 1293Combined sources
Beta strandi141 – 15010Combined sources
Beta strandi152 – 1565Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 1719Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi197 – 2048Combined sources
Beta strandi206 – 2083Combined sources
Beta strandi214 – 2229Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi228 – 25831Combined sources
Beta strandi266 – 2749Combined sources
Beta strandi288 – 2903Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi315 – 32915Combined sources
Turni334 – 3385Combined sources
Beta strandi343 – 3519Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JQIX-ray2.60A2-393[»]
ProteinModelPortaliP29066.
SMRiP29066. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 163163Interaction with SRCAdd
BLAST
Regioni45 – 8642Interaction with CHRM2By similarityAdd
BLAST
Regioni318 – 418101Interaction with TRAF6By similarityAdd
BLAST

Domaini

The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. Binding to phosphorylated GPCRs induces a conformationanl change that exposes the motif to the surface (By similarity).By similarity
The N-terminus binds InsP6 with low affinity.
The C-terminus binds InsP6 with high affinity.

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP29066.
KOiK04439.
OMAiMQLERPM.
OrthoDBiEOG79W954.
PhylomeDBiP29066.
TreeFamiTF314260.

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.

P29066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE
60 70 80 90 100
RRVYVTLTCA FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL
110 120 130 140 150
QERLIKKLGE HAYPFTFEIP PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC
160 170 180 190 200
AENLEEKIHK RNSVRLVIRK VQYAPERPGP QPTAETTRQF LMSDKPLHLE
210 220 230 240 250
ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD ICLFNTAQYK
260 270 280 290 300
CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL
310 320 330 340 350
ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT
360 370 380 390 400
LMHPKPKEEP PHREVPESET PVDTNLIELD TNDDDIVFED FARQRLKGMK
410
DDKDEEDDGT GSPHLNNR
Length:418
Mass (Da):47,020
Last modified:December 1, 1992 - v1
Checksum:i0A3C07D71B7ABC55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91589 mRNA. Translation: AAA74459.1.
PIRiB43404.
RefSeqiNP_037042.1. NM_012910.2.
UniGeneiRn.34876.

Genome annotation databases

EnsembliENSRNOT00000043554; ENSRNOP00000046069; ENSRNOG00000030404.
GeneIDi25387.
KEGGirno:25387.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M91589 mRNA. Translation: AAA74459.1.
PIRiB43404.
RefSeqiNP_037042.1. NM_012910.2.
UniGeneiRn.34876.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JQIX-ray2.60A2-393[»]
ProteinModelPortaliP29066.
SMRiP29066. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247425. 7 interactions.
DIPiDIP-40808N.
IntActiP29066. 5 interactions.
MINTiMINT-89355.
STRINGi10116.ENSRNOP00000046069.

PTM databases

iPTMnetiP29066.
PhosphoSiteiP29066.

Proteomic databases

PaxDbiP29066.
PRIDEiP29066.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000043554; ENSRNOP00000046069; ENSRNOG00000030404.
GeneIDi25387.
KEGGirno:25387.

Organism-specific databases

CTDi408.
RGDi2156. Arrb1.

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP29066.
KOiK04439.
OMAiMQLERPM.
OrthoDBiEOG79W954.
PhylomeDBiP29066.
TreeFamiTF314260.

Enzyme and pathway databases

ReactomeiR-RNO-418555. G alpha (s) signalling events.
R-RNO-432720. Lysosome Vesicle Biogenesis.
R-RNO-432722. Golgi Associated Vesicle Biogenesis.
R-RNO-456926. Thrombin signalling through proteinase activated receptors (PARs).

Miscellaneous databases

PROiP29066.

Gene expression databases

GenevisibleiP29066. 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. "Role of beta-arrestin in mediating agonist-promoted G protein-coupled receptor internalization."
    Ferguson S.S.G., Downey W.E. III, Colapietro A.-M., Barak L.S., Menard L., Caron M.G.
    Science 271:363-366(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF ADRB2, MUTAGENESIS OF VAL-53.
  3. "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: FUNCTION IN DESENSITIZATION, FUNCTION IN INTERNALIZATION OF ADBR2, PHOSPHORYLATION AT SER-412, INTERACTION WITH ADRB2 AND CLTC, MUTAGENESIS OF SER-412.
  4. "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: FUNCTION IN INTERNALIZATION OF IGFR1, FUNCTION IN MAPK SIGNALING, INTERACTION WITH IGF1R, MUTAGENESIS OF SER-412.
  5. "Regulation of muscarinic acetylcholine receptor sequestration and function by beta-arrestin."
    Voegler O., Nolte B., Voss M., Schmidt M., Jakobs K.H., van Koppen C.J.
    J. Biol. Chem. 274:12333-12338(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF CHRM1; CHRM3 AND CHRM4.
  6. Cited for: FUNCTION IN INTERNALIZATION OF IL8RA, SUBCELLULAR LOCATION.
  7. "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: INTERACTION WITH AP2B1, SUBCELLULAR LOCATION.
  8. Cited for: FUNCTION IN MAPK SIGNALING, SUBCELLULAR LOCATION, INTERACTION WITH SRC, MUTAGENESIS OF VAL-53; PRO-91; PRO-121 AND SER-412.
  9. "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.
  10. "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-53.
  11. "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: INTERACTION WITH AP2B1 AND CLTC, SUBCELLULAR LOCATION.
  12. "beta-arrestin-dependent endocytosis of proteinase-activated receptor 2 is required for intracellular targeting of activated ERK1/2."
    DeFea K.A., Zalevsky J., Thoma M.S., Dery O., Mullins R.D., Bunnett N.W.
    J. Cell Biol. 148:1267-1281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAPK SIGNALING, INTERACTION WITH RAF1, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH F2RL1; MAPK1; MAPK3 AND RAF1.
  13. "Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
    Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
    Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCK AND CXCR1.
  14. "The proliferative and antiapoptotic effects of substance P are facilitated by formation of a beta -arrestin-dependent scaffolding complex."
    DeFea K.A., Vaughn Z.D., O'Bryan E.M., Nishijima D., Dery O., Bunnett N.W.
    Proc. Natl. Acad. Sci. U.S.A. 97:11086-11091(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MAPK SIGNALING, SUBCELLULAR LOCATION, INTERACTION WITH SRC AND TACR1, IDENTIFICATION IN A COMPLEX WITH SRC; MAPK1; MAPK3 AND TACR1.
  15. "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins."
    Chen W., Hu L.A., Semenov M.V., Yanagawa S., Kikuchi A., Lefkowitz R.J., Miller W.E.
    Proc. Natl. Acad. Sci. U.S.A. 98:14889-14894(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH DVL1 AND DVL2.
  16. "Association of beta-Arrestin 1 with the type 1A angiotensin II receptor involves phosphorylation of the receptor carboxyl terminus and correlates with receptor internalization."
    Qian H., Pipolo L., Thomas W.G.
    Mol. Endocrinol. 15:1706-1719(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION INTERNALIZATION OF AGTR1, INTERACTION WITH AGTR1.
  17. "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.
  18. "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.
  19. "alpha-Thrombin induces rapid and sustained Akt phosphorylation by beta-arrestin1-dependent and -independent mechanisms, and only the sustained Akt phosphorylation is essential for G1 phase progression."
    Goel R., Phillips-Mason P.J., Raben D.M., Baldassare J.J.
    J. Biol. Chem. 277:18640-18648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AKT1 SIGNALING.
  20. "Targeting of cyclic AMP degradation to beta 2-adrenergic receptors by beta-arrestins."
    Perry S.J., Baillie G.S., Kohout T.A., McPhee I., Magiera M.M., Ang K.L., Miller W.E., McLean A.J., Conti M., Houslay M.D., Lefkowitz R.J.
    Science 298:834-836(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CAMP DEGRADATION, INTERACTION WITH PDE4D.
  21. "Role of G protein-coupled receptor kinase 4 and beta-arrestin 1 in agonist-stimulated metabotropic glutamate receptor 1 internalization and activation of mitogen-activated protein kinases."
    Iacovelli L., Salvatore L., Capobianco L., Picascia A., Barletta E., Storto M., Mariggio S., Sallese M., Porcellini A., Nicoletti F., De Blasi A.
    J. Biol. Chem. 278:12433-12442(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF GRM1.
  22. "A beta-arrestin-dependent scaffold is associated with prolonged MAPK activation in pseudopodia during protease-activated receptor-2-induced chemotaxis."
    Ge L., Ly Y., Hollenberg M., DeFea K.
    J. Biol. Chem. 278:34418-34426(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOSKELETAL REARRANGEMENT AND CHEMOTAXIS, SUBCELLULAR LOCATION.
  23. "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: FUNCTION IN REGULATION OF NF-KAPPA-B, INTERACTION WITH CHUK; IKBKB AND MAP3K14.
  24. "{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.
  25. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "The role of beta-arrestins in the formyl peptide receptor-like 1 internalization and signaling."
    Huet E., Boulay F., Barral S., Rabiet M.J.
    Cell. Signal. 19:1939-1948(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF FPR1.
  27. "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.
  28. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARRB1_RAT
AccessioniPrimary (citable) accession number: P29066
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: June 8, 2016
This is version 125 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.