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Q91YI4

- ARRB2_MOUSE

UniProt

Q91YI4 - ARRB2_MOUSE

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Protein

Beta-arrestin-2

Gene

Arrb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. 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
Complete GO annotation...

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-KW
  3. cytoplasm Source: UniProtKB
  4. dendritic spine Source: Ensembl
  5. endocytic vesicle Source: UniProtKB
  6. intracellular Source: MGI
  7. nucleus Source: UniProtKB-KW
  8. postsynaptic density Source: Ensembl
  9. postsynaptic membrane Source: Ensembl
Complete GO annotation...

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

BgeeiQ91YI4.
CleanExiMM_ARRB2.
ExpressionAtlasiQ91YI4. baseline and differential.
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.
InParanoidiQ91YI4.
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

        10         20         30         40         50
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK
60 70 80 90 100
DRKVFVTLTC AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR
110 120 130 140 150
LQDRLLKKLG QHAHPFFFTI PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF
160 170 180 190 200
CAKSIEEKSH KRNSVRLIIR KVQFAPETPG PQPSAETTRH FLMSDRRSLH
210 220 230 240 250
LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY ADICLFSTAQ
260 270 280 290 300
YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT
310 320 330 340 350
NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP
360 370 380 390 400
HDHITLPRPQ SAPRETDVPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM
410
KDDDCDDQFC
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi Q91YI4.
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

ChiTaRSi Arrb2. mouse.
NextBioi 375424.
PROi Q91YI4.
SOURCEi Search...

Gene expression databases

Bgeei Q91YI4.
CleanExi MM_ARRB2.
ExpressionAtlasi Q91YI4. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 114 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