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Protein

Beta-arrestin-1

Gene

ARRB1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in IL8-mediated granule release in neutrophils. Binds phosphoinositides. Binds inositol hexakisphosphate (InsP6) (By similarity). Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity).By similarity4 Publications

Sites

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Protein transport, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-arrestin-1
Alternative name(s):
Arrestin beta-1
Arrestin-2
Gene namesi
Name:ARRB1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

  • chromatin Source: Ensembl
  • coated pit Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytoplasmic vesicle Source: UniProtKB
  • cytosol Source: Ensembl
  • nucleoplasm Source: Ensembl
  • plasma membrane Source: UniProtKB
  • pseudopodium Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi157 – 1571K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-160 and Q-161. 1 Publication
Mutagenesisi160 – 1601K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-157 and Q-161. 1 Publication
Mutagenesisi161 – 1611R → Q: Impairs InsP6-binding and oligomerization; when associated with Q-157 and Q-160. 1 Publication
Mutagenesisi232 – 2321K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-236, Q-250, Q-324 and Q-326. 1 Publication
Mutagenesisi236 – 2361R → Q: Impairs InsP6-binding and oligomerization; when associated with Q-232, Q-250, Q-324 and Q-326. 1 Publication
Mutagenesisi250 – 2501K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-232, Q-236, Q-324 and Q-326. 1 Publication
Mutagenesisi324 – 3241K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-232, Q-236, Q-250 and Q-326. 1 Publication
Mutagenesisi326 – 3261K → Q: Impairs InsP6-binding and oligomerization; when associated with Q-232, Q-236, Q-250 and Q-324. 1 Publication
Mutagenesisi391 – 3911F → A: Abolishes interaction with AP2B1; no effect on interaction with CLTC. 1 Publication
Mutagenesisi395 – 3951R → E: Abolishes interaction with AP2B1; impairs interaction with CLTC. 1 Publication
Mutagenesisi396 – 3961L → A: Impairs interaction with AP2B1; no effect on interaction with CLTC. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 418418Beta-arrestin-1PRO_0000205193Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Constitutively phosphorylated at Ser-412 in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated.
The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to occur GPCR-specific. Ubiquitinated by MDM2; the ubiquitination is required for rapid internalization of ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a dissociation of the beta-arrestin-GPCR complex. Stimulation of a class A GPCR, such as ADRB2, induces transient ubiquitination and subsequently promotes association with USP33 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP17870.
PRIDEiP17870.

Expressioni

Tissue specificityi

Beta-arrestin 1A is found in cortex, cerebellum, striatum, pineal gland, retina and heart. Beta-arrestin 1B is found in spleen, lung, pituitary and kidney.

Gene expression databases

ExpressionAtlasiP17870. baseline and differential.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-61028N.
STRINGi9913.ENSBTAP00000027296.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Beta strandi14 – 174Combined sources
Beta strandi19 – 235Combined sources
Beta strandi25 – 295Combined sources
Beta strandi31 – 344Combined sources
Beta strandi37 – 426Combined sources
Helixi45 – 484Combined sources
Beta strandi52 – 6413Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 8814Combined sources
Beta strandi91 – 933Combined sources
Helixi99 – 1079Combined sources
Beta strandi112 – 1176Combined sources
Beta strandi121 – 1233Combined sources
Beta strandi127 – 1304Combined sources
Helixi133 – 1386Combined sources
Beta strandi140 – 15314Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 17210Combined sources
Beta strandi185 – 1895Combined sources
Beta strandi191 – 1955Combined sources
Beta strandi197 – 2048Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi214 – 2229Combined sources
Beta strandi224 – 2263Combined sources
Beta strandi228 – 24114Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi247 – 25812Combined sources
Beta strandi266 – 2749Combined sources
Helixi278 – 2803Combined sources
Turni281 – 2833Combined sources
Beta strandi285 – 2917Combined sources
Beta strandi293 – 2953Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 32914Combined sources
Beta strandi333 – 3353Combined sources
Helixi336 – 3383Combined sources
Beta strandi342 – 35211Combined sources
Beta strandi355 – 3584Combined sources
Beta strandi386 – 3905Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4MX-ray1.90A/B1-393[»]
1G4RX-ray2.20A1-393[»]
1JSYX-ray2.90A1-418[»]
1ZSHX-ray2.90A1-418[»]
2WTRX-ray2.90A/B1-418[»]
3GC3X-ray2.20A1-393[»]
3GD1X-ray3.50C/E1-393[»]
DisProtiDP00390.
ProteinModelPortaliP17870.
SMRiP17870. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17870.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 163163Interaction with SRCBy similarityAdd
BLAST
Regioni45 – 8642Interaction with CHRM2Add
BLAST
Regioni318 – 418101Interaction with TRAF6By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi385 – 39511[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motifAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP17870.
KOiK04439.
OMAiMQLERPM.
OrthoDBiEOG79W954.
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. AlignAdd to basket

Isoform 1A (identifier: P17870-1) [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
MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVEPVDGV VLVDPEYLKE
60 70 80 90 100
RRVYVTLTCA FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL
110 120 130 140 150
QERLIKKLGE HAYPFTFEIP PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC
160 170 180 190 200
AENLEEKIHK RNSVRLVIRK VQYAPERPGP QPTAETTRQF LMSDKPLHLE
210 220 230 240 250
ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD ICLFNTAQYK
260 270 280 290 300
CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL
310 320 330 340 350
ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT
360 370 380 390 400
LMHPKPKEEP PHREVPEHET PVDTNLIELD TNDDDIVFED FARQRLKGMK
410
DDKEEEEDGT GSPRLNDR
Length:418
Mass (Da):47,132
Last modified:August 1, 1990 - v1
Checksum:i345302C620FA3360
GO
Isoform 1B (identifier: P17870-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     334-341: Missing.

Show »
Length:410
Mass (Da):46,375
Checksum:i61C47F9F7A7B0736
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei334 – 3418Missing in isoform 1B. CuratedVSP_000321

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33601 mRNA. Translation: AAA30387.1.
PIRiA34851.
RefSeqiNP_776668.1. NM_174243.3. [P17870-1]
UniGeneiBt.52082.

Genome annotation databases

EnsembliENSBTAT00000027296; ENSBTAP00000027296; ENSBTAG00000020485. [P17870-1]
GeneIDi281637.
KEGGibta:281637.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33601 mRNA. Translation: AAA30387.1.
PIRiA34851.
RefSeqiNP_776668.1. NM_174243.3. [P17870-1]
UniGeneiBt.52082.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G4MX-ray1.90A/B1-393[»]
1G4RX-ray2.20A1-393[»]
1JSYX-ray2.90A1-418[»]
1ZSHX-ray2.90A1-418[»]
2WTRX-ray2.90A/B1-418[»]
3GC3X-ray2.20A1-393[»]
3GD1X-ray3.50C/E1-393[»]
DisProtiDP00390.
ProteinModelPortaliP17870.
SMRiP17870. Positions 5-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61028N.
STRINGi9913.ENSBTAP00000027296.

Proteomic databases

PaxDbiP17870.
PRIDEiP17870.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027296; ENSBTAP00000027296; ENSBTAG00000020485. [P17870-1]
GeneIDi281637.
KEGGibta:281637.

Organism-specific databases

CTDi408.

Phylogenomic databases

eggNOGiKOG3865. Eukaryota.
ENOG410XR0F. LUCA.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP17870.
KOiK04439.
OMAiMQLERPM.
OrthoDBiEOG79W954.
TreeFamiTF314260.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP17870.

Gene expression databases

ExpressionAtlasiP17870. baseline and differential.

Family and domain databases

Gene3Di2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProiIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11792. PTHR11792. 1 hit.
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSiPR00309. ARRESTIN.
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.
PROSITEiPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Beta-arrestin: a protein that regulates beta-adrenergic receptor function."
    Lohse M.J., Benovic J.L., Codina J., Caron M.G., Lefkowitz R.J.
    Science 248:1547-1550(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems."
    Lohse M.J., Andexinger S., Pitcher J., Trukawinski S., Codina J., Faure J.P., Caron M.G., Lefkowitz R.J.
    J. Biol. Chem. 267:8558-8564(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION.
  3. "Polypeptide variants of beta-arrestin and arrestin3."
    Sterne-Marr R., Gurevich V.V., Goldsmith P., Bodine R.C., Sanders C., Donoso L.A., Benovic J.L.
    J. Biol. Chem. 268:15640-15648(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
    Tissue: Brain.
  4. "Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptors."
    Gurevich V.V., Dion S.B., Onorato J.J., Ptasienski J., Kim C.M., Sterne-Marr R., Hosey M.M., Benovic J.L.
    J. Biol. Chem. 270:720-731(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADRB2 AND CHRM2.
  5. "Arrestin function in G protein-coupled receptor endocytosis requires phosphoinositide binding."
    Gaidarov I., Krupnick J.G., Falck J.R., Benovic J.L., Keen J.H.
    EMBO J. 18:871-881(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOINOSITIDE-BINDING.
  6. "A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes."
    Mukherjee S., Palczewski K., Gurevich V.V., Benovic J.L., Banga J.P., Hunzicker-Dunn M.
    Proc. Natl. Acad. Sci. U.S.A. 96:493-498(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DESENSITIZATION OF LHCGR.
  7. "Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2."
    Mukherjee S., Gurevich V.V., Preninger A., Hamm H.E., Bader M.-F., Fazleabas A.T., Birnbaumer L., Hunzicker-Dunn M.
    J. Biol. Chem. 277:17916-17927(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LHCGR.
  8. "The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO ARF6 ELMO protein network."
    Bouschet T., Martin S., Kanamarlapudi V., Mundell S., Henley J.M.
    J. Cell Sci. 120:2489-2497(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CYTH2 AND CASR.
  9. "Agonist-selective, receptor-specific interaction of human P2Y receptors with beta-arrestin-1 and -2."
    Hoffmann C., Ziegler N., Reiner S., Krasel C., Lohse M.J.
    J. Biol. Chem. 283:30933-30941(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF P2Y PURINOCEPTORS, SUBCELLULAR LOCATION.
  10. "Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation."
    Han M., Gurevich V.V., Vishnivetskiy S.A., Sigler P.B., Schubert C.
    Structure 9:869-880(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 5-393, INTERACTION WITH CHRM2.
  11. "Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis."
    Milano S.K., Pace H.C., Kim Y.-M., Brenner C., Benovic J.L.
    Biochemistry 41:3321-3328(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), INTERACTION WITH AP2B1 AND CLTC, MUTAGENESIS OF PHE-391; ARG-395 AND LEU-396.
  12. "Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding."
    Milano S.K., Kim Y.-M., Stefano F.P., Benovic J.L., Brenner C.
    J. Biol. Chem. 281:9812-9823(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBUNIT, INSP6-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-157; LYS-160; ARG-161; LYS-232; ARG-236; LYS-250; LYS-324 AND LYS-326.

Entry informationi

Entry nameiARRB1_BOVIN
AccessioniPrimary (citable) accession number: P17870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 8, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.