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P32121

- ARRB2_HUMAN

UniProt

P32121 - ARRB2_HUMAN

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Protein

Beta-arrestin-2

Gene

ARRB2

Organism
Homo sapiens (Human)
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 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 IL8-mediated granule release in neutrophils. Involved in the internalization of the atypical chemokine receptor ACKR3.29 Publications

GO - Molecular functioni

  1. angiotensin receptor binding Source: UniProtKB
  2. enzyme binding Source: UniProt
  3. G-protein coupled receptor binding Source: UniProtKB
  4. protein complex scaffold Source: BHF-UCL
  5. receptor binding Source: UniProtKB
  6. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Signal transduction inhibitor

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinkiP32121.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-arrestin-2
Alternative name(s):
Arrestin beta-2
Gene namesi
Name:ARRB2
Synonyms:ARB2, ARR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:712. ARRB2.

Subcellular locationi

Cytoplasm. Nucleus. Cell membrane. Membraneclathrin-coated pit By similarity. Cytoplasmic vesicle
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. cytoplasmic vesicle Source: UniProtKB
  5. cytosol Source: Reactome
  6. dendritic spine Source: Ensembl
  7. endocytic vesicle Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. postsynaptic density Source: Ensembl
  11. postsynaptic membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi11 – 111K → A: Abolishes interaction with CHUK; when associated with A-12; A-230 and A-231.
Mutagenesisi12 – 121K → A: Abolishes interaction with CHUK; when associated with A-11; A-230 and A-231.
Mutagenesisi54 – 541V → A: Inhibits internalization of CXCR4; no effect on interaction with CXCR4. 1 Publication
Mutagenesisi230 – 2301K → A: Abolishes interaction with CHUK; when associated with A-11; A-12 and A-231.
Mutagenesisi231 – 2311K → A: Abolishes interaction with CHUK; when associated with A-11; A-12 and A-230.
Mutagenesisi360 – 3601S → A or D: Reduces interaction with CHUK; when associated with A-382.
Mutagenesisi382 – 3821T → A or D: Reduces interaction with CHUK; when associated with A-360. 1 Publication
Mutagenesisi382 – 3821T → A: Loss of phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA60.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Beta-arrestin-2PRO_0000205199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphotyrosineBy similarity
Modified residuei176 – 1761Hydroxyproline; by PHD21 Publication
Modified residuei181 – 1811Hydroxyproline; by PHD21 Publication
Modified residuei360 – 3601PhosphoserineBy similarity
Modified residuei382 – 3821Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated at Thr-382 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1.1 Publication
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.1 Publication
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.1 Publication

Keywords - PTMi

Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP32121.
PaxDbiP32121.
PRIDEiP32121.

PTM databases

PhosphoSiteiP32121.

Expressioni

Gene expression databases

BgeeiP32121.
CleanExiHS_ARRB2.
ExpressionAtlasiP32121. baseline and differential.
GenevestigatoriP32121.

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 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. Associates with protein phosphatase 2A (PP2A) By similarity. Interacts with DHX8; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with GAPDHS; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with H2AFX; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with KIF14; the interaction is detected in the nucleus upon OR1D2 stimulation. Interacts with RCC1; the interaction is detected in the nucleus upon OR1D2 stimulation. 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). Interacts with ACKR3 and ACKR4.By similarity22 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
Akt1P317503EBI-714559,EBI-298707From a different organism.
CALM3P621583EBI-714559,EBI-397435
CHUKO151113EBI-714559,EBI-81249
CTNNA1P352213EBI-714559,EBI-701918
CTTNQ142472EBI-714559,EBI-351886
GSNP063963EBI-714559,EBI-351506
HSPA8P111424EBI-714559,EBI-351896
MAP3K1Q132332EBI-714559,EBI-49776
MAP3K5Q996832EBI-714559,EBI-476263
MAPK1P284823EBI-714559,EBI-959949
NCLP193383EBI-714559,EBI-346967
NOLC1Q149783EBI-714559,EBI-396155
ORFQ9Q2G43EBI-714559,EBI-6248094From a different organism.
PKMP146184EBI-714559,EBI-353408
PPM1AP358133EBI-714559,EBI-989143
PPM1BO756884EBI-714559,EBI-1047039
PRPF4BQ135233EBI-714559,EBI-395940
rlP404174EBI-714559,EBI-867790From a different organism.
S100A9P067022EBI-714559,EBI-1055001
STK38Q152083EBI-714559,EBI-458376
TAB1Q157503EBI-714559,EBI-358643
TCOF1Q134283EBI-714559,EBI-396105
YWHAQP273483EBI-714559,EBI-359854
ZRANB2O952184EBI-714559,EBI-1051583

Protein-protein interaction databases

BioGridi106902. 326 interactions.
DIPiDIP-40089N.
IntActiP32121. 288 interactions.
MINTiMINT-216692.
STRINGi9606.ENSP00000269260.

Structurei

3D structure databases

ProteinModelPortaliP32121.
SMRiP32121. Positions 6-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni240 – 409170Interaction with TRAF6Add
BLAST
Regioni363 – 40947Interaction with AP2B1Add
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.By similarity

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiNOG302111.
GeneTreeiENSGT00390000013152.
HOVERGENiHBG002399.
InParanoidiP32121.
KOiK04439.
OMAiKPHDHIT.
OrthoDBiEOG79W954.
PhylomeDBiP32121.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P32121-1) [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 VPNPPRPPTR
110 120 130 140 150
LQDRLLRKLG QHAHPFFFTI PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF
160 170 180 190 200
CAKSLEEKSH KRNSVRLVIR KVQFAPEKPG PQPSAETTRH FLMSDRSLHL
210 220 230 240 250
EASLDKELYY HGEPLNVNVH VTNNSTKTVK KIKVSVRQYA DICLFSTAQY
260 270 280 290 300
KCPVAQLEQD DQVSPSSTFC KVYTITPLLS DNREKRGLAL DGKLKHEDTN
310 320 330 340 350
LASSTIVKEG ANKEVLGILV SYRVKVKLVV SRGGDVSVEL PFVLMHPKPH
360 370 380 390 400
DHIPLPRPQS AAPETDVPVD TNLIEFDTNY ATDDDIVFED FARLRLKGMK

DDDYDDQLC
Length:409
Mass (Da):46,106
Last modified:March 5, 2002 - v2
Checksum:iDEEC507D4A7B84FF
GO
Isoform 2 (identifier: P32121-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-360: S → SAPTPTPPLPVPP

Show »
Length:421
Mass (Da):47,271
Checksum:i1D5F728967E2BF5D
GO
Isoform 3 (identifier: P32121-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-53: Missing.
     360-360: S → SAPTPTPPLPVPP

Note: No experimental confirmation available.

Show »
Length:406
Mass (Da):45,557
Checksum:i2020CE75484DF687
GO
Isoform 4 (identifier: P32121-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: T → TVRMPLPSEGQGAGAGTVSGVG

Note: No experimental confirmation available.

Show »
Length:430
Mass (Da):48,015
Checksum:iD41C217D16CFD41D
GO
Isoform 5 (identifier: P32121-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-53: Missing.

Show »
Length:394
Mass (Da):44,392
Checksum:iEE3C2EC61639E8D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131S → P in BAG59672. (PubMed:14702039)Curated
Sequence conflicti189 – 1891R → P in CAA77577. (PubMed:1587386)Curated
Sequence conflicti190 – 1901H → R in ABG47460. 1 PublicationCurated
Sequence conflicti192 – 1921L → P in CAG29306. 1 PublicationCurated
Sequence conflicti366 – 3661D → G in BAG59672. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 5315Missing in isoform 3 and isoform 5. 1 PublicationVSP_008194Add
BLAST
Alternative sequencei119 – 1191T → TVRMPLPSEGQGAGAGTVSG VG in isoform 4. 1 PublicationVSP_044697
Alternative sequencei360 – 3601S → SAPTPTPPLPVPP in isoform 2 and isoform 3. 2 PublicationsVSP_008195

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11501 mRNA. Translation: CAA77577.1.
AF106941 mRNA. Translation: AAC99468.1.
DQ664180 mRNA. Translation: ABG47460.1.
EU883572 mRNA. Translation: ACG60646.1.
AK097542 mRNA. Translation: BAC05094.1.
AK297181 mRNA. Translation: BAG59672.1.
CR450310 mRNA. Translation: CAG29306.1.
DQ314866 Genomic DNA. Translation: ABC40725.1.
AC091153 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90421.1.
CH471108 Genomic DNA. Translation: EAW90422.1.
BC007427 mRNA. Translation: AAH07427.1.
BC067368 mRNA. Translation: AAH67368.1.
CCDSiCCDS11050.1. [P32121-1]
CCDS11051.1. [P32121-5]
CCDS58504.1. [P32121-4]
CCDS58505.1. [P32121-2]
PIRiS18984.
RefSeqiNP_001244257.1. NM_001257328.1. [P32121-4]
NP_001244258.1. NM_001257329.1.
NP_001244259.1. NM_001257330.1. [P32121-3]
NP_001244260.1. NM_001257331.1. [P32121-2]
NP_004304.1. NM_004313.3. [P32121-1]
NP_945355.1. NM_199004.1. [P32121-5]
UniGeneiHs.435811.

Genome annotation databases

EnsembliENST00000269260; ENSP00000269260; ENSG00000141480. [P32121-1]
ENST00000346341; ENSP00000341895; ENSG00000141480. [P32121-2]
ENST00000381488; ENSP00000370898; ENSG00000141480. [P32121-5]
ENST00000412477; ENSP00000403701; ENSG00000141480. [P32121-4]
GeneIDi409.
KEGGihsa:409.
UCSCiuc002fyj.3. human. [P32121-1]
uc002fyl.3. human. [P32121-3]
uc002fym.3. human. [P32121-2]

Polymorphism databases

DMDMi20141230.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

Arrestin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z11501 mRNA. Translation: CAA77577.1 .
AF106941 mRNA. Translation: AAC99468.1 .
DQ664180 mRNA. Translation: ABG47460.1 .
EU883572 mRNA. Translation: ACG60646.1 .
AK097542 mRNA. Translation: BAC05094.1 .
AK297181 mRNA. Translation: BAG59672.1 .
CR450310 mRNA. Translation: CAG29306.1 .
DQ314866 Genomic DNA. Translation: ABC40725.1 .
AC091153 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90421.1 .
CH471108 Genomic DNA. Translation: EAW90422.1 .
BC007427 mRNA. Translation: AAH07427.1 .
BC067368 mRNA. Translation: AAH67368.1 .
CCDSi CCDS11050.1. [P32121-1 ]
CCDS11051.1. [P32121-5 ]
CCDS58504.1. [P32121-4 ]
CCDS58505.1. [P32121-2 ]
PIRi S18984.
RefSeqi NP_001244257.1. NM_001257328.1. [P32121-4 ]
NP_001244258.1. NM_001257329.1.
NP_001244259.1. NM_001257330.1. [P32121-3 ]
NP_001244260.1. NM_001257331.1. [P32121-2 ]
NP_004304.1. NM_004313.3. [P32121-1 ]
NP_945355.1. NM_199004.1. [P32121-5 ]
UniGenei Hs.435811.

3D structure databases

ProteinModelPortali P32121.
SMRi P32121. Positions 6-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106902. 326 interactions.
DIPi DIP-40089N.
IntActi P32121. 288 interactions.
MINTi MINT-216692.
STRINGi 9606.ENSP00000269260.

PTM databases

PhosphoSitei P32121.

Polymorphism databases

DMDMi 20141230.

Proteomic databases

MaxQBi P32121.
PaxDbi P32121.
PRIDEi P32121.

Protocols and materials databases

DNASUi 409.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269260 ; ENSP00000269260 ; ENSG00000141480 . [P32121-1 ]
ENST00000346341 ; ENSP00000341895 ; ENSG00000141480 . [P32121-2 ]
ENST00000381488 ; ENSP00000370898 ; ENSG00000141480 . [P32121-5 ]
ENST00000412477 ; ENSP00000403701 ; ENSG00000141480 . [P32121-4 ]
GeneIDi 409.
KEGGi hsa:409.
UCSCi uc002fyj.3. human. [P32121-1 ]
uc002fyl.3. human. [P32121-3 ]
uc002fym.3. human. [P32121-2 ]

Organism-specific databases

CTDi 409.
GeneCardsi GC17P004613.
HGNCi HGNC:712. ARRB2.
MIMi 107941. gene.
neXtProti NX_P32121.
PharmGKBi PA60.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG302111.
GeneTreei ENSGT00390000013152.
HOVERGENi HBG002399.
InParanoidi P32121.
KOi K04439.
OMAi KPHDHIT.
OrthoDBi EOG79W954.
PhylomeDBi P32121.
TreeFami TF314260.

Enzyme and pathway databases

Reactomei REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_21384. Thrombin signalling through proteinase activated receptors (PARs).
SignaLinki P32121.

Miscellaneous databases

ChiTaRSi ARRB2. human.
GeneWikii Arrestin_beta_2.
GenomeRNAii 409.
NextBioi 1719.
PROi P32121.
SOURCEi Search...

Gene expression databases

Bgeei P32121.
CleanExi HS_ARRB2.
ExpressionAtlasi P32121. baseline and differential.
Genevestigatori P32121.

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. "Cloning of a member of the arrestin family from a human thyroid cDNA library."
    Rapoport B., Kaufman K.D., Chamenbalk G.D.
    Mol. Cell. Endocrinol. 84:R39-R43(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Thyroid.
  2. "G-protein coupled receptor interaction with beta-arrestin 2 through specific agonist stimulation."
    Yu Q.M., Zhou T.H., Wu Y.L., Cheng Z.J., Ma L., Pei G.
    Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. "A new splice-variant of beta-arrestin 2 is involved in agonist-induced MC1R endocytosis."
    Sanchez-Laorden B.L., Jimenez-Cervantes C., Garcia-Borron J.C.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Isolation of cDNA coding for human arrestin, beta 2 (ARRB2), transcript variant 1."
    Kaighin V.A., Martin A.L., Aronstam R.S.
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
    Tissue: Brain and Testis.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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).
    Tissue: Muscle and Pancreas.
  11. "A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation."
    Barak L.S., Ferguson S.S.G., Zhang J., Caron M.G.
    J. Biol. Chem. 272:27497-27500(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH GPCRS.
  12. "beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4."
    Cheng Z.J., Zhao J., Sun Y., Hu W., Wu Y.L., Cen B., Wu G.-X., Pei G.
    J. Biol. Chem. 275:2479-2485(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IN INTERNALIZATION OF CXCR4, INTERACTION WITH CXCR4, MUTAGENESIS OF VAL-54.
  13. "Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors."
    Oakley R.H., Laporte S.A., Holt J.A., Caron M.G., Barak L.S.
    J. Biol. Chem. 275:17201-17210(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH ANTAGONIST-STIMULATED GPCRS.
  14. "Regulation of tyrosine kinase activation and granule release through beta-arrestin by CXCRI."
    Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L., Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.
    Nat. Immunol. 1:227-233(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCK AND CXCR1.
  15. "Molecular determinants underlying the formation of stable intracellular G protein-coupled receptor-beta-arrestin complexes after receptor endocytosis*."
    Oakley R.H., Laporte S.A., Holt J.A., Barak L.S., Caron M.G.
    J. Biol. Chem. 276:19452-19460(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH ANTAGONIST-STIMULATED GPCRS.
  16. "Regulation of arrestin-3 phosphorylation by casein kinase II."
    Kim Y.-M., Barak L.S., Caron M.G., Benovic J.L.
    J. Biol. Chem. 277:16837-16846(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF ADBR2, PHOSPHORYLATION AT THR-382, INTERACTION WITH AP2B1; CLATHRIN AND SRC, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-382.
  17. "Beta-arrestin 2 functions as a G-protein-coupled receptor-activated regulator of oncoprotein Mdm2."
    Wang P., Gao H., Ni Y., Wang B., Wu Y., Ji L., Qin L., Ma L., Pei G.
    J. Biol. Chem. 278:6363-6370(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TP53-MEDIATED APOPTOSIS, INTERACTION WITH MDM2.
  18. "Desensitization, internalization, and signaling functions of beta-arrestins demonstrated by RNA interference."
    Ahn S., Nelson C.D., Garrison T.R., Miller W.E., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 100:1740-1744(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DESENSITIZATION OF ADRB2, FUNCTION IN INTERNALIZATION OF ADRB2, FUNCTION IN INTERNALIZATION OF AGTR1, FUNCTION IN AGTR1-MEDIATED ERK SIGNALING.
  19. "Independent beta-arrestin 2 and G protein-mediated pathways for angiotensin II activation of extracellular signal-regulated kinases 1 and 2."
    Wei H., Ahn S., Shenoy S.K., Karnik S.S., Hunyady L., Luttrell L.M., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 100:10782-10787(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AGTR1-MEDIATED ERK SIGNALING.
  20. "Beta-arrestin 2 mediates endocytosis of type III TGF-beta receptor and down-regulation of its signaling."
    Chen W., Kirkbride K.C., How T., Nelson C.D., Mo J., Frederick J.P., Wang X.-F., Lefkowitz R.J., Blobe G.C.
    Science 301:1394-1397(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOCYTOSIS OF TGFBR2 AND TGFBR3, FUNCTION IN TGF-BETA SIGNALING, SUBCELLULAR LOCATION.
  21. "Reciprocal regulation of angiotensin receptor-activated extracellular signal-regulated kinases by beta-arrestins 1 and 2."
    Ahn S., Wei H., Garrison T.R., Lefkowitz R.J.
    J. Biol. Chem. 279:7807-7811(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AGTR1-MEDIATED ERK SIGNALING.
  22. "Differential desensitization, receptor phosphorylation, beta-arrestin recruitment, and ERK1/2 activation by the two endogenous ligands for the CC chemokine receptor 7."
    Kohout T.A., Nicholas S.L., Perry S.J., Reinhart G., Junger S., Struthers R.S.
    J. Biol. Chem. 279:23214-23222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CCR7-MEDIATED ERK SIGNALING.
  23. "Differential kinetic and spatial patterns of beta-arrestin and G protein-mediated ERK activation by the angiotensin II receptor."
    Ahn S., Shenoy S.K., Wei H., Lefkowitz R.J.
    J. Biol. Chem. 279:35518-35525(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AGTR1-MEDIATED ERK SIGNALING.
  24. "Identification of beta-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-kappaB pathways."
    Gao H., Sun Y., Wu Y., Luan B., Wang Y., Qu B., Pei G.
    Mol. Cell 14:303-317(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF NF-KAPPA-B, SUBCELLULAR LOCATION, INTERACTION WITH CHUK AND RELA.
  25. "Activity-dependent internalization of smoothened mediated by beta-arrestin 2 and GRK2."
    Chen W., Ren X.R., Nelson C.D., Barak L.S., Chen J.K., Beachy P.A., de Sauvage F., Lefkowitz R.J.
    Science 306:2257-2260(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF SMO.
  26. "{beta}-Arrestin is crucial for ubiquitination and down-regulation of the insulin-like growth factor-1 receptor by acting as adaptor for the MDM2 E3 ligase."
    Girnita L., Shenoy S.K., Sehat B., Vasilcanu R., Girnita A., Lefkowitz R.J., Larsson O.
    J. Biol. Chem. 280:24412-24419(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF IGF1R, INTERACTION WITH IGF1R AND MDM2.
  27. "Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2."
    Willoughby E.A., Collins M.K.
    J. Biol. Chem. 280:25651-25658(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP16, SUBCELLULAR LOCATION.
  28. "G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers."
    Huettenrauch F., Pollok-Kopp B., Oppermann M.
    J. Biol. Chem. 280:37503-37515(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IN INTERNALIZATION OF CCR5, INTERACTION WITH CCR5.
  29. "Multiple independent functions of arrestins in the regulation of protease-activated receptor-2 signaling and trafficking."
    Stalheim L., Ding Y., Gullapalli A., Paing M.M., Wolfe B.L., Morris D.R., Trejo J.
    Mol. Pharmacol. 67:78-87(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN F2LR1-MEDIATED ERK SIGNALING.
  30. "Beta-arrestin 2-dependent angiotensin II type 1A receptor-mediated pathway of chemotaxis."
    Hunton D.L., Barnes W.G., Kim J., Ren X.-R., Violin J.D., Reiter E., Milligan G., Patel D.D., Lefkowitz R.J.
    Mol. Pharmacol. 67:1229-1236(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AGTR1-MEDIATED CHEMOTAXIS.
  31. "Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptor."
    Ren X.-R., Reiter E., Ahn S., Kim J., Chen W., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 102:1448-1453(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AVPR2-MEDIATED ERK SIGNALING.
  32. "beta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoform."
    Szabo E.Z., Numata M., Lukashova V., Iannuzzi P., Orlowski J.
    Proc. Natl. Acad. Sci. U.S.A. 102:2790-2795(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOCYTOSIS OF SLC9A5, INTERACTION WITH SLC9A5.
  33. "Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
    Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
    Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AP2B1.
  34. "beta-arrestin-dependent, G protein-independent ERK1/2 activation by the beta2 adrenergic receptor."
    Shenoy S.K., Drake M.T., Nelson C.D., Houtz D.A., Xiao K., Madabushi S., Reiter E., Premont R.T., Lichtarge O., Lefkowitz R.J.
    J. Biol. Chem. 281:1261-1273(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ADRB2-MEDIATED ERK SIGNALING.
  35. "A beta-arrestin binding determinant common to the second intracellular loops of rhodopsin family G protein-coupled receptors."
    Marion S., Oakley R.H., Kim K.-M., Caron M.G., Barak L.S.
    J. Biol. Chem. 281:2932-2938(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HTR2C.
  36. "Distinct beta-arrestin- and G protein-dependent pathways for parathyroid hormone receptor-stimulated ERK1/2 activation."
    Gesty-Palmer D., Chen M., Reiter E., Ahn S., Nelson C.D., Wang S., Eckhardt A.E., Cowan C.L., Spurney R.F., Luttrell L.M., Lefkowitz R.J.
    J. Biol. Chem. 281:10856-10864(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PTH1R-MEDIATED ERK SIGNALING.
  37. "Novel function of beta-arrestin2 in the nucleus of mature spermatozoa."
    Neuhaus E.M., Mashukova A., Barbour J., Wolters D., Hatt H.
    J. Cell Sci. 119:3047-3056(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE NUCLEUS OF SPERMATOZOA, SUBCELLULAR LOCATION, INTERACTION WITH DHX8; GAPDHS; H2AFX; KIF14 AND RCC1.
  38. "Association of beta-arrestin and TRAF6 negatively regulates Toll-like receptor-interleukin 1 receptor signaling."
    Wang Y., Tang Y., Teng L., Wu Y., Zhao X., Pei G.
    Nat. Immunol. 7:139-147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TLR/IL-1 RECEPTOR SIGNALING, INTERACTION WITH TRAF6.
  39. "The melanosomal/lysosomal protein OA1 has properties of a G protein-coupled receptor."
    Innamorati G., Piccirillo R., Bagnato P., Palmisano I., Schiaffino M.V.
    Pigment Cell Res. 19:125-135(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPR143.
  40. "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, SUBCELLULAR LOCATION, INTERACTION WITH ENG.
  41. "Post-endocytic fates of delta-opioid receptor are regulated by GRK2-mediated receptor phosphorylation and distinct beta-arrestin isoforms."
    Zhang X., Wang F., Chen X., Chen Y., Ma L.
    J. Neurochem. 106:781-792(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF OPRD1, FUNCTION IN DEGRADATION OF OPRD1.
  42. "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, INTERACTION WITH KIR2DL1; KIR2DL3 AND KIR2DL4.
  43. "The type III transforming growth factor-beta receptor negatively regulates nuclear factor kappa B signaling through its interaction with beta-arrestin2."
    You H.J., How T., Blobe G.C.
    Carcinogenesis 30:1281-1287(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TGFBR3-MEDIATED NF-KAPPA-B REGULATION.
  44. "Inhibition of dynamin prevents CCL2-mediated endocytosis of CCR2 and activation of ERK1/2."
    Garcia Lopez M.A., Aguado Martinez A., Lamaze C., Martinez-Alonso C., Fischer T.
    Cell. Signal. 21:1748-1757(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INTERNALIZATION OF CCR2.
  45. "A scanning peptide array approach uncovers association sites within the JNK/beta arrestin signalling complex."
    Li X., MacLeod R., Dunlop A.J., Edwards H.V., Advant N., Gibson L.C., Devine N.M., Brown K.M., Adams D.R., Houslay M.D., Baillie G.S.
    FEBS Lett. 583:3310-3316(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP2K4/MKK4.
  46. "An arrestin-dependent multi-kinase signaling complex mediates MIP-1beta/CCL4 signaling and chemotaxis of primary human macrophages."
    Cheung R., Malik M., Ravyn V., Tomkowicz B., Ptasznik A., Collman R.G.
    J. Leukoc. Biol. 86:833-845(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MIP-1-BETA-STIMULATED CHEMOTAXIS.
  47. "Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2."
    Shenoy S.K., Modi A.S., Shukla A.K., Xiao K., Berthouze M., Ahn S., Wilkinson K.D., Miller W.E., Lefkowitz R.J.
    Proc. Natl. Acad. Sci. U.S.A. 106:6650-6655(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, DEUBIQUITINATION BY USP33, INTERACTION WITH USP33.
  48. "Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling."
    Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M., Benovic J.L.
    J. Biol. Chem. 285:7805-7817(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CXCR4, FUNCTION.
  49. "Prolyl hydroxylase 2: a novel regulator of beta2 -adrenoceptor internalization."
    Yan B., Huo Z., Liu Y., Lin X., Li J., Peng L., Zhao H., Zhou Z.N., Liang X., Liu Y., Zhu W., Liang D., Li L., Sun Y., Cui J., Chen Y.H.
    J. Cell. Mol. Med. 15:2712-2722(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: HYDROXYLATION AT PRO-176 AND PRO-181.
  50. "Carboxy-terminus of CXCR7 regulates receptor localization and function."
    Ray P., Mihalko L.A., Coggins N.L., Moudgil P., Ehrlich A., Luker K.E., Luker G.D.
    Int. J. Biochem. Cell Biol. 44:669-678(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACKR3.
  51. Cited for: FUNCTION, INTERACTION WITH ACKR3.
  52. "Beta-arrestin recruitment and G protein signaling by the atypical human chemokine decoy receptor CCX-CKR."
    Watts A.O., Verkaar F., van der Lee M.M., Timmerman C.A., Kuijer M., van Offenbeek J., van Lith L.H., Smit M.J., Leurs R., Zaman G.J., Vischer H.F.
    J. Biol. Chem. 288:7169-7181(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ACKR4.

Entry informationi

Entry nameiARRB2_HUMAN
AccessioniPrimary (citable) accession number: P32121
Secondary accession number(s): B4DLW0
, B5B0C0, B7WPL3, D3DTK2, H0Y688, Q0Z8D3, Q2PP19, Q6ICT3, Q8N7Y2, Q9UEQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 5, 2002
Last modified: October 29, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3