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Q91YI4

- ARRB2_MOUSE

UniProt

Q91YI4 - ARRB2_MOUSE

Protein

Beta-arrestin-2

Gene

Arrb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein kinase B binding Source: UniProtKB

    GO - Biological processi

    1. adult walking behavior Source: UniProtKB
    2. apoptotic DNA fragmentation Source: Ensembl
    3. brain development Source: Ensembl
    4. cell chemotaxis Source: Ensembl
    5. desensitization of G-protein coupled receptor protein signaling pathway by arrestin Source: Ensembl
    6. detection of temperature stimulus involved in sensory perception of pain Source: Ensembl
    7. follicle-stimulating hormone signaling pathway Source: Ensembl
    8. G-protein coupled receptor internalization Source: Ensembl
    9. negative regulation of GTPase activity Source: Ensembl
    10. negative regulation of interleukin-12 production Source: UniProtKB
    11. negative regulation of interleukin-1 beta production Source: UniProtKB
    12. negative regulation of interleukin-6 production Source: UniProtKB
    13. negative regulation of natural killer cell mediated cytotoxicity Source: Ensembl
    14. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    15. negative regulation of protein ubiquitination Source: Ensembl
    16. negative regulation of smooth muscle cell apoptotic process Source: Ensembl
    17. negative regulation of toll-like receptor signaling pathway Source: UniProtKB
    18. negative regulation of tumor necrosis factor production Source: UniProtKB
    19. positive regulation of apoptotic process Source: Ensembl
    20. positive regulation of calcium ion transport Source: Ensembl
    21. positive regulation of DNA biosynthetic process Source: Ensembl
    22. positive regulation of ERK1 and ERK2 cascade Source: Ensembl
    23. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    24. positive regulation of protein kinase B signaling Source: UniProtKB
    25. positive regulation of protein ubiquitination Source: Ensembl
    26. positive regulation of receptor internalization Source: UniProtKB
    27. positive regulation of release of cytochrome c from mitochondria Source: Ensembl
    28. positive regulation of synaptic transmission, dopaminergic Source: UniProtKB
    29. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    30. protein transport Source: UniProtKB-KW
    31. protein ubiquitination Source: Ensembl
    32. regulation of androgen receptor signaling pathway Source: Ensembl
    33. regulation of G-protein coupled receptor protein signaling pathway Source: MGI
    34. regulation of protein phosphorylation Source: MGI
    35. transcription from RNA polymerase II promoter Source: Ensembl
    36. transforming growth factor beta receptor signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Signal transduction inhibitor

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-arrestin-2
    Alternative name(s):
    Arrestin beta-2
    Gene namesi
    Name:Arrb2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:99474. Arrb2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication. Cell membrane 1 Publication. Membraneclathrin-coated pit By similarity. Cytoplasmic vesicle By similarity
    Note: Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. coated pit Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB
    4. dendritic spine Source: Ensembl
    5. endocytic vesicle Source: UniProtKB
    6. intracellular Source: MGI
    7. nucleus Source: UniProtKB-SubCell
    8. postsynaptic density Source: Ensembl
    9. postsynaptic membrane Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    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.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi395 – 3951L → A: Nuclear localization. Causes nuclear relocalization of MAPK10. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 410410Beta-arrestin-2PRO_0000205200Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei48 – 481Phosphotyrosine1 Publication
    Modified residuei176 – 1761Hydroxyproline; by PHD2By similarity
    Modified residuei181 – 1811Hydroxyproline; by PHD2By similarity
    Modified residuei361 – 3611PhosphoserineBy similarity
    Modified residuei383 – 3831PhosphothreonineBy similarity

    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

    MaxQBiQ91YI4.
    PaxDbiQ91YI4.
    PRIDEiQ91YI4.

    PTM databases

    PhosphoSiteiQ91YI4.

    Expressioni

    Tissue specificityi

    Predominantly localized in neuronal tissues and in the spleen.

    Gene expression databases

    ArrayExpressiQ91YI4.
    BgeeiQ91YI4.
    CleanExiMM_ARRB2.
    GenevestigatoriQ91YI4.

    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 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.By similarityCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ffar4Q7TMA44EBI-994161,EBI-2912413

    Protein-protein interaction databases

    BioGridi229812. 2 interactions.
    DIPiDIP-36064N.
    IntActiQ91YI4. 4 interactions.
    STRINGi10090.ENSMUSP00000078065.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91YI4.
    SMRiQ91YI4. Positions 6-394.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni241 – 410170Interaction with TRAF6By similarityAdd
    BLAST
    Regioni364 – 41047Interaction with AP2B1By similarityAdd
    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

    eggNOGiNOG302111.
    GeneTreeiENSGT00390000013152.
    HOGENOMiHOG000231319.
    HOVERGENiHBG002399.
    KOiK04439.
    OMAiKPHDHIT.
    PhylomeDBiQ91YI4.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q91YI4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK    50
    DRKVFVTLTC AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR 100
    LQDRLLKKLG QHAHPFFFTI PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF 150
    CAKSIEEKSH KRNSVRLIIR KVQFAPETPG PQPSAETTRH FLMSDRRSLH 200
    LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY ADICLFSTAQ 250
    YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT 300
    NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP 350
    HDHITLPRPQ SAPRETDVPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM 400
    KDDDCDDQFC 410
    Length:410
    Mass (Da):46,314
    Last modified:December 1, 2001 - v1
    Checksum:i0DFA73A1C532AE03
    GO
    Isoform 2 (identifier: Q91YI4-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:421
    Mass (Da):47,440
    Checksum:iD814F7259E59B528
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111K → R in BAE41934. (PubMed:16141072)Curated
    Sequence conflicti59 – 591T → N in BAE41934. (PubMed:16141072)Curated
    Sequence conflicti75 – 751S → Y in BAE41934. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei360 – 3601Q → QSAPIHPPLLCP in isoform 2. 1 PublicationVSP_020652

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS24946.1. [Q91YI4-1]
    CCDS70226.1. [Q91YI4-2]
    RefSeqiNP_001258287.1. NM_001271358.1. [Q91YI4-2]
    NP_001258288.1. NM_001271359.1. [Q91YI4-2]
    NP_001258289.1. NM_001271360.1. [Q91YI4-1]
    NP_663404.1. NM_145429.5. [Q91YI4-1]
    UniGeneiMm.203747.

    Genome annotation databases

    EnsembliENSMUST00000079056; ENSMUSP00000078065; ENSMUSG00000060216. [Q91YI4-2]
    ENSMUST00000102563; ENSMUSP00000099623; ENSMUSG00000060216. [Q91YI4-1]
    ENSMUST00000102564; ENSMUSP00000099624; ENSMUSG00000060216. [Q91YI4-1]
    ENSMUST00000108568; ENSMUSP00000104208; ENSMUSG00000060216. [Q91YI4-2]
    GeneIDi216869.
    KEGGimmu:216869.
    UCSCiuc007jur.1. mouse. [Q91YI4-1]
    uc007jus.1. mouse. [Q91YI4-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS24946.1. [Q91YI4-1 ]
    CCDS70226.1. [Q91YI4-2 ]
    RefSeqi NP_001258287.1. NM_001271358.1. [Q91YI4-2 ]
    NP_001258288.1. NM_001271359.1. [Q91YI4-2 ]
    NP_001258289.1. NM_001271360.1. [Q91YI4-1 ]
    NP_663404.1. NM_145429.5. [Q91YI4-1 ]
    UniGenei Mm.203747.

    3D structure databases

    ProteinModelPortali Q91YI4.
    SMRi Q91YI4. Positions 6-394.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229812. 2 interactions.
    DIPi DIP-36064N.
    IntActi Q91YI4. 4 interactions.
    STRINGi 10090.ENSMUSP00000078065.

    PTM databases

    PhosphoSitei Q91YI4.

    Proteomic databases

    MaxQBi Q91YI4.
    PaxDbi Q91YI4.
    PRIDEi Q91YI4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079056 ; ENSMUSP00000078065 ; ENSMUSG00000060216 . [Q91YI4-2 ]
    ENSMUST00000102563 ; ENSMUSP00000099623 ; ENSMUSG00000060216 . [Q91YI4-1 ]
    ENSMUST00000102564 ; ENSMUSP00000099624 ; ENSMUSG00000060216 . [Q91YI4-1 ]
    ENSMUST00000108568 ; ENSMUSP00000104208 ; ENSMUSG00000060216 . [Q91YI4-2 ]
    GeneIDi 216869.
    KEGGi mmu:216869.
    UCSCi uc007jur.1. mouse. [Q91YI4-1 ]
    uc007jus.1. mouse. [Q91YI4-2 ]

    Organism-specific databases

    CTDi 409.
    MGIi MGI:99474. Arrb2.

    Phylogenomic databases

    eggNOGi NOG302111.
    GeneTreei ENSGT00390000013152.
    HOGENOMi HOG000231319.
    HOVERGENi HBG002399.
    KOi K04439.
    OMAi KPHDHIT.
    PhylomeDBi Q91YI4.
    TreeFami TF314260.

    Enzyme and pathway databases

    Reactomei REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_220322. Thrombin signalling through proteinase activated receptors (PARs).
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Miscellaneous databases

    NextBioi 375424.
    PROi Q91YI4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91YI4.
    Bgeei Q91YI4.
    CleanExi MM_ARRB2.
    Genevestigatori Q91YI4.

    Family and domain databases

    Gene3Di 2.60.40.640. 1 hit.
    2.60.40.840. 1 hit.
    InterProi 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 ]
    PANTHERi PTHR11792. PTHR11792. 1 hit.
    Pfami PF02752. Arrestin_C. 1 hit.
    PF00339. Arrestin_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00309. ARRESTIN.
    SMARTi SM01017. Arrestin_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81296. SSF81296. 2 hits.
    PROSITEi PS00295. ARRESTINS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiARRB2_MOUSE
    AccessioniPrimary (citable) accession number: Q91YI4
    Secondary accession number(s): Q3TCM2, Q5F2D8, Q5F2E0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 112 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3