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Q91YI4 (ARRB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-arrestin-2
Alternative name(s):
Arrestin beta-2
Gene names
Name:Arrb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13

Subunit structure

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 ARRB2. 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. 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. Associates with protein phosphatase 2A (PP2A). Interacts with ACKR3 and ACKR4 By similarity. Ref.7 Ref.10 Ref.13

Subcellular location

Cytoplasm. Nucleus. Cell membrane. Membraneclathrin-coated pit By similarity. Cytoplasmic vesicle By similarity. Note: Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. Ref.5

Tissue specificity

Predominantly localized in neuronal tissues and in the spleen.

Post-translational modification

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.

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.

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.

Disruption phenotype

Loss of beta-2 adrenergic receptor/ADRB2 ubiquitination. Reduction of dopamine-dependent behaviors, loss of Akt1 regulation by dopamine in the striatum and disruption of the dopamine-dependent interaction of Akt1 with its negative regulator, protein phosphatase 2A. Increased serum LDL-cholesterol levels upon high fat diet. Exacerbates insulin resistance. Elevated cytotoxicity of natural killer cells and lowered susceptibility to mouse cytomegalovirus infection. Ref.4 Ref.6 Ref.7 Ref.12 Ref.13

Sequence similarities

Belongs to the arrestin family.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Coated pit
Cytoplasm
Cytoplasmic vesicle
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   Molecular functionSignal transduction inhibitor
   PTMHydroxylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor internalization

Inferred from electronic annotation. Source: Ensembl

adult walking behavior

Inferred from mutant phenotype Ref.7. Source: UniProtKB

apoptotic DNA fragmentation

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

desensitization of G-protein coupled receptor protein signaling pathway by arrestin

Inferred from electronic annotation. Source: Ensembl

detection of temperature stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

follicle-stimulating hormone signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of GTPase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-1 beta production

Inferred from mutant phenotype PubMed 16378096. Source: UniProtKB

negative regulation of interleukin-12 production

Inferred from mutant phenotype PubMed 16378096. Source: UniProtKB

negative regulation of interleukin-6 production

Inferred from mutant phenotype PubMed 16378096. Source: UniProtKB

negative regulation of natural killer cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of toll-like receptor signaling pathway

Inferred from mutant phenotype PubMed 16378096. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from mutant phenotype PubMed 16378096. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from mutant phenotype Ref.7. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor internalization

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, dopaminergic

Inferred from mutant phenotype Ref.7. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

protein ubiquitination

Inferred from electronic annotation. Source: Ensembl

regulation of G-protein coupled receptor protein signaling pathway

Inferred from mutant phenotype PubMed 10617462PubMed 11130073PubMed 11171997. Source: MGI

regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein phosphorylation

Inferred from direct assay PubMed 15218143. Source: MGI

transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 11171997. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein kinase B binding

Inferred from physical interaction Ref.7. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ffar4Q7TMA44EBI-994161,EBI-2912413

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91YI4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q91YI4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     360-360: Q → QSAPIHPPLLCP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410Beta-arrestin-2
PRO_0000205200

Regions

Region241 – 410170Interaction with TRAF6 By similarity
Region364 – 41047Interaction with AP2B1 By similarity
Motif386 – 39611[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif By similarity

Amino acid modifications

Modified residue481Phosphotyrosine Ref.11
Modified residue1761Hydroxyproline; by PHD2 By similarity
Modified residue1811Hydroxyproline; by PHD2 By similarity
Modified residue3611Phosphoserine By similarity
Modified residue3831Phosphothreonine By similarity

Natural variations

Alternative sequence3601Q → QSAPIHPPLLCP in isoform 2.
VSP_020652

Experimental info

Mutagenesis3951L → A: Nuclear localization. Causes nuclear relocalization of MAPK10. Ref.5
Sequence conflict111K → R in BAE41934. Ref.1
Sequence conflict591T → N in BAE41934. Ref.1
Sequence conflict751S → Y in BAE41934. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0DFA73A1C532AE03

FASTA41046,314
        10         20         30         40         50         60 
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK DRKVFVTLTC 

        70         80         90        100        110        120 
AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR LQDRLLKKLG QHAHPFFFTI 

       130        140        150        160        170        180 
PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF CAKSIEEKSH KRNSVRLIIR KVQFAPETPG 

       190        200        210        220        230        240 
PQPSAETTRH FLMSDRRSLH LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY 

       250        260        270        280        290        300 
ADICLFSTAQ YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT 

       310        320        330        340        350        360 
NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP HDHITLPRPQ 

       370        380        390        400        410 
SAPRETDVPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM KDDDCDDQFC 

« Hide

Isoform 2 [UniParc].

Checksum: D814F7259E59B528
Show »

FASTA42147,440

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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] (ISOFORM 1).
[4]"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: DISRUPTION PHENOTYPE.
[5]"Differential nucleocytoplasmic shuttling of beta-arrestins. Characterization of a leucine-rich nuclear export signal in beta-arrestin2."
Scott M.G., Le Rouzic E., Perianin A., Pierotti V., Enslen H., Benichou S., Marullo S., Benmerah A.
J. Biol. Chem. 277:37693-37701(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING, MUTAGENESIS OF LEU-395.
[6]"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: FUNCTION IN ENDOCYTOSIS OF LDLR, DISRUPTION PHENOTYPE.
[7]"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: FUNCTION IN AKT1 SIGNALING, ASSOCIATION WITH PP2A, INTERACTION WITH AKT1; GSK3A AND GSK3B, DISRUPTION PHENOTYPE.
[8]"The interaction of endoglin with beta-arrestin2 regulates transforming growth factor-beta-mediated ERK activation and migration in endothelial cells."
Lee N.Y., Blobe G.C.
J. Biol. Chem. 282:21507-21517(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INTERNALIZATION OF ENG, FUNCTION IN TGF-BETA-MEDIATED ERK SIGNALING.
[9]"Beta-arrestins specifically constrain beta2-adrenergic receptor signaling and function in airway smooth muscle."
Deshpande D.A., Theriot B.S., Penn R.B., Walker J.K.
FASEB J. 22:2134-2141(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION.
[10]"Beta2-adrenergic receptor regulates Toll-like receptor-4-induced nuclear factor-kappaB activation through beta-arrestin 2."
Kizaki T., Izawa T., Sakurai T., Haga S., Taniguchi N., Tajiri H., Watanabe K., Day N.K., Toba K., Ohno H.
Immunology 124:348-356(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHUK.
[11]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[12]"An essential function for beta-arrestin 2 in the inhibitory signaling of natural killer cells."
Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L., Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.
Nat. Immunol. 9:898-907(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF INNATE IMMUNE RESPONSE, DISRUPTION PHENOTYPE.
[13]"Deficiency of a beta-arrestin-2 signal complex contributes to insulin resistance."
Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W., Kang J., Pei G.
Nature 457:1146-1149(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN INSULIN SIGNALING, INTERACTION WITH SRC; AKT1 AND INSR, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK154874 mRNA. Translation: BAE32894.1.
AK159317 mRNA. Translation: BAE34984.1.
AK170647 mRNA. Translation: BAE41934.1.
AK170889 mRNA. Translation: BAE42096.1.
AL596096 Genomic DNA. Translation: CAI51985.1.
AL596096 Genomic DNA. Translation: CAI51987.1.
BC016642 mRNA. Translation: AAH16642.1.
RefSeqNP_001258287.1. NM_001271358.1.
NP_001258288.1. NM_001271359.1.
NP_001258289.1. NM_001271360.1.
NP_663404.1. NM_145429.5.
UniGeneMm.203747.

3D structure databases

ProteinModelPortalQ91YI4.
SMRQ91YI4. Positions 6-394.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229812. 2 interactions.
DIPDIP-36064N.
IntActQ91YI4. 4 interactions.
STRING10090.ENSMUSP00000078065.

PTM databases

PhosphoSiteQ91YI4.

Proteomic databases

PaxDbQ91YI4.
PRIDEQ91YI4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079056; ENSMUSP00000078065; ENSMUSG00000060216. [Q91YI4-2]
ENSMUST00000102563; ENSMUSP00000099623; ENSMUSG00000060216. [Q91YI4-1]
ENSMUST00000102564; ENSMUSP00000099624; ENSMUSG00000060216. [Q91YI4-1]
ENSMUST00000108568; ENSMUSP00000104208; ENSMUSG00000060216. [Q91YI4-2]
GeneID216869.
KEGGmmu:216869.
UCSCuc007jur.1. mouse. [Q91YI4-1]
uc007jus.1. mouse. [Q91YI4-2]

Organism-specific databases

CTD409.
MGIMGI:99474. Arrb2.

Phylogenomic databases

eggNOGNOG302111.
GeneTreeENSGT00390000013152.
HOGENOMHOG000231319.
HOVERGENHBG002399.
KOK04439.
OMAKPHDHIT.
PhylomeDBQ91YI4.
TreeFamTF314260.

Gene expression databases

ArrayExpressQ91YI4.
BgeeQ91YI4.
CleanExMM_ARRB2.
GenevestigatorQ91YI4.

Family and domain databases

Gene3D2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR11792. PTHR11792. 1 hit.
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSPR00309. ARRESTIN.
SMARTSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 2 hits.
PROSITEPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio375424.
PROQ91YI4.
SOURCESearch...

Entry information

Entry nameARRB2_MOUSE
AccessionPrimary (citable) accession number: Q91YI4
Secondary accession number(s): Q3TCM2, Q5F2D8, Q5F2E0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot