P29066 (ARRB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-arrestin-1

Alternative name(s):
Arrestin beta-1

Gene names

Name:

Arrb1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27
Subunit structure	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). Ref.3 Ref.4 Ref.7 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.20 Ref.23
Subcellular location	Cytoplasm. Nucleus. Cell membrane. Membrane › clathrin-coated pit Probable. Cell projection › pseudopodium. Cytoplasmic vesicle. Note: Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in the nucleus. The oligomeric form is located in the cytoplasm. Translocates to the nucleus upon stimulation of OPRD1 By similarity. Ref.6 Ref.7 Ref.8 Ref.11 Ref.12 Ref.14 Ref.22
Tissue specificity	Predominantly localized in neuronal tissues and in the spleen.
Domain	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. The N-terminus binds InsP6 with low affinity. The C-terminus binds InsP6 with high affinity.
Post-translational modification	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. Ref.3 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.
Sequence similarities	Belongs to the arrestin family.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cell membrane Cell projection Coated pit Cytoplasm Cytoplasmic vesicle Membrane Nucleus
Molecular function	Signal transduction inhibitor
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of MAPK activity Inferred from direct assay PubMed 12167719Ref.21. Source: RGD adenylate cyclase-modulating G-protein coupled receptor signaling pathway Traceable author statement Ref.21. Source: RGD desensitization of G-protein coupled receptor protein signaling pathway by arrestin Traceable author statement PubMed 15514408. Source: RGD endocytosis Inferred from direct assay Ref.21. Source: RGD follicle-stimulating hormone signaling pathway Inferred from direct assay PubMed 16899567. Source: RGD negative regulation of GTPase activity Inferred from direct assay Ref.1. Source: RGD negative regulation of protein phosphorylation Inferred from mutant phenotype PubMed 19254952. Source: RGD positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype PubMed 19289825. Source: RGD positive regulation of protein ubiquitination Inferred from mutant phenotype PubMed 20650893. Source: RGD positive regulation of smooth muscle cell apoptotic process Inferred from mutant phenotype PubMed 19171933. Source: RGD positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16325578. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of cAMP biosynthetic process Traceable author statement Ref.20. Source: RGD regulation of cAMP catabolic process Traceable author statement Ref.20. Source: RGD sensory perception of pain Traceable author statement PubMed 14519533. Source: RGD sensory perception of touch Traceable author statement PubMed 14519533. Source: RGD transcription from RNA polymerase II promoter Inferred from direct assay Ref.15. Source: UniProtKB
Cellular_component	basolateral plasma membrane Inferred from direct assay PubMed 16899567. Source: RGD coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 15514408. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from direct assay Ref.1. Source: RGD postsynaptic membrane Inferred from direct assay Ref.1. Source: RGD pseudopodium Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	AP-2 adaptor complex binding Inferred from direct assay PubMed 15728179. Source: BHF-UCL V2 vasopressin receptor binding Inferred from mutant phenotype PubMed 17513300. Source: RGD alpha-1B adrenergic receptor binding Inferred from direct assay PubMed 18523139. Source: RGD clathrin adaptor activity Inferred from direct assay PubMed 15728179. Source: BHF-UCL protein phosphorylated amino acid binding Inferred from mutant phenotype PubMed 17513300. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LIMK1	P53667	2	EBI-4303019,EBI-444403	From a different organism.
PDXP	Q96GD0	2	EBI-4303019,EBI-4303060	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Beta-arrestin-1		PRO_0000205197
Regions
	Region	1 – 163	163	Interaction with SRC
	Region	45 – 86	42	Interaction with CHRM2 By similarity
	Region	318 – 418	101	Interaction with TRAF6 By similarity
Sites
	Binding site	250	1	Inositol hexakisphosphate By similarity
	Binding site	255	1	Inositol hexakisphosphate By similarity
	Binding site	324	1	Inositol hexakisphosphate By similarity
	Binding site	326	1	Inositol hexakisphosphate By similarity
Amino acid modifications
	Modified residue	47	1	Phosphotyrosine By similarity
	Modified residue	410	1	Phosphothreonine Ref.25
	Modified residue	412	1	Phosphoserine; by GRK5 By similarity
Experimental info
	Mutagenesis	53	1	V → 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. Ref.2 Ref.8 Ref.10
	Mutagenesis	91	1	P → G: Impairs interaction with SRC; impairs ADRB2- and HTR1A-mediated ERK phosphorylation; no effect on sequestration of ADRB2; when associated with E-121. Ref.8
	Mutagenesis	121	1	P → E: Impairs interaction with SRC; impairs ADRB2- and HTR1A-mediated ERK phosphorylation; no effect on sequestration of ADRB2; when associated with G-91. Ref.8
	Mutagenesis	412	1	S → A: Abolishes phosphorylation and inhibits ADRB2 endocytosis; no effect on interaction with ADRB2. Ref.3 Ref.4 Ref.8
	Mutagenesis	412	1	S → 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. Ref.3 Ref.4 Ref.8

Sequences

	Sequence		Length	Mass (Da)
	P29066 [UniParc]. Last modified December 1, 1992. Version 1. Checksum: 0A3C07D71B7ABC55	FASTA	418	47,020
	10 20 30 40 50 60 MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA 70 80 90 100 110 120 FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HAYPFTFEIP 130 140 150 160 170 180 PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP 190 200 210 220 230 240 QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD 250 260 270 280 290 300 ICLFNTAQYK CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL 310 320 330 340 350 360 ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP 370 380 390 400 410 PHREVPESET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKDEEDDGT GSPHLNNR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"beta-arrestins regulate interleukin-8-induced CXCR1 internalization." Barlic J., Khandaker M.H., Mahon E., Andrews J., DeVries M.E., Mitchell G.B., Rahimpour R., Tan C.M., Ferguson S.S.G., Kelvin D.J. J. Biol. Chem. 274:16287-16294(1999) [PubMed] [Europe PMC] [Abstract] 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]	"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: 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 THR-410 AND SER-412, MASS SPECTROMETRY. Tissue: Renal collecting duct.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M91589 mRNA. Translation: AAA74459.1.
IPI	IPI00200580.
PIR	B43404.
RefSeq	NP_037042.1. NM_012910.2.
UniGene	Rn.34876.
3D structure databases
ProteinModelPortal	P29066.
SMR	P29066. Positions 5-393.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-40808N.
IntAct	P29066. 3 interactions.
STRING	10116.ENSRNOP00000046069.
PTM databases
PhosphoSite	P29066.
Proteomic databases
PaxDb	P29066.
PRIDE	P29066.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000043554; ENSRNOP00000046069; ENSRNOG00000030404.
GeneID	25387.
KEGG	rno:25387.
Organism-specific databases
CTD	408.
RGD	2156. Arrb1.
Phylogenomic databases
eggNOG	NOG302111.
GeneTree	ENSGT00390000013152.
HOGENOM	HOG000231319.
HOVERGEN	HBG002399.
InParanoid	P29066.
KO	K04439.
OrthoDB	EOG4MCX0K.
Gene expression databases
ArrayExpress	P29066.
Genevestigator	P29066.
GermOnline	ENSRNOG00000030404. Rattus norvegicus.
Family and domain databases
Gene3D	2.60.40.640. 1 hit. 2.60.40.840. 1 hit.
InterPro	IPR000698. Arrestin. IPR011021. Arrestin-like_N. IPR014752. Arrestin_C. IPR011022. Arrestin_C-like. IPR017864. Arrestin_CS. IPR014753. Arrestin_N. IPR014756. Ig_E-set. [Graphical view]
PANTHER	PTHR11792. PTHR11792. 1 hit.
Pfam	PF02752. Arrestin_C. 1 hit. PF00339. Arrestin_N. 1 hit. [Graphical view]
PRINTS	PR00309. ARRESTIN.
SMART	SM01017. Arrestin_C. 1 hit. [Graphical view]
SUPFAM	SSF81296. Ig_E-set. 2 hits.
PROSITE	PS00295. ARRESTINS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	606443.

Entry information

Entry name

ARRB1_RAT

Accession

Primary (citable) accession number: P29066

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program