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P32121 (ARRB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-arrestin-2
Alternative name(s):
Arrestin beta-2
Gene names
Name:ARRB2
Synonyms:ARB2, ARR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in 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. Ref.12 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.48 Ref.51

Subunit structure

Homooligomer; the self-association is mediated by InsP6-binding Probable. Heterooligomer with ARRB1; the association is mediated by InsP6-binding. Interacts with ADRB2 AND CHRM2. Interacts with PDE4A. Interacts with PDE4D. Interacts with MAPK10, MAPK1 and MAPK3. Interacts with DRD2. Interacts with FSHR. Interacts with CLTC. Interacts with HTR2C. Interacts with CCR5. Interacts with CXCR4. Interacts with SRC. Interacts with DUSP16; the interaction is interrupted by stimulation of AGTR1 and activation of MAPK10. Interacts with CHUK; the interaction is enhanced stimulation of ADRB2. Interacts with RELA. Interacts with MDM2; the interaction is enhanced by activation of GPCRs. Interacts with SLC9A5. Interacts with TRAF6. Interacts with IGF1R. Interacts with ENG. Interacts with 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. Ref.12 Ref.14 Ref.16 Ref.17 Ref.24 Ref.26 Ref.27 Ref.28 Ref.32 Ref.33 Ref.35 Ref.37 Ref.38 Ref.39 Ref.40 Ref.42 Ref.45 Ref.47 Ref.48 Ref.50 Ref.51 Ref.52

Subcellular location

Cytoplasm. Nucleus. Cell membrane. Membraneclathrin-coated pit By similarity. Cytoplasmic vesicle. Note: Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. Ref.11 Ref.13 Ref.15 Ref.16 Ref.20 Ref.24 Ref.27 Ref.37 Ref.40 Ref.52

Domain

The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1 By similarity.

Post-translational modification

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. Ref.16

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. Ref.47

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.

Sequence similarities

Belongs to the arrestin family.

Ontologies

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

Inferred from direct assay Ref.12. Source: UniProtKB

Notch signaling pathway

Traceable author statement. Source: Reactome

adult walking behavior

Inferred from electronic annotation. Source: Ensembl

apoptotic DNA fragmentation

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cell chemotaxis

Inferred from mutant phenotype Ref.30. Source: UniProtKB

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

Inferred from mutant phenotype Ref.18. Source: UniProtKB

detection of temperature stimulus involved in sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

follicle-stimulating hormone signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of GTPase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.24Ref.38. Source: UniProtKB

negative regulation of interleukin-1 beta production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-12 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of natural killer cell mediated cytotoxicity

Inferred from mutant phenotype Ref.42. Source: UniProtKB

negative regulation of protein ubiquitination

Inferred from direct assay Ref.38. Source: UniProtKB

negative regulation of smooth muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of toll-like receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of tumor necrosis factor production

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

positive regulation of DNA biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein ubiquitination

Inferred from genetic interaction PubMed 19372219. Source: BHF-UCL

positive regulation of receptor internalization

Inferred from mutant phenotype Ref.51. Source: UniProtKB

positive regulation of release of cytochrome c from mitochondria

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, dopaminergic

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.26. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

protein ubiquitination

Inferred from mutant phenotype Ref.26. Source: UniProtKB

receptor internalization

Inferred from direct assay Ref.20. Source: BHF-UCL

regulation of androgen receptor signaling pathway

Inferred from direct assay PubMed 19372219. Source: BHF-UCL

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.37. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.20. Source: BHF-UCL

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 15611106PubMed 16325578Ref.37Ref.52. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 15611106. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from direct assay Ref.52. Source: UniProtKB

nucleus

Inferred from direct assay Ref.37. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.42. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionG-protein coupled receptor binding

Inferred from physical interaction Ref.12. Source: UniProtKB

angiotensin receptor binding

Inferred from physical interaction PubMed 15611106. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 23382074. Source: UniProt

protein binding

Inferred from physical interaction Ref.24Ref.38Ref.39Ref.37Ref.47Ref.50Ref.51Ref.52. Source: UniProtKB

protein complex scaffold

Inferred from direct assay PubMed 19372219. Source: BHF-UCL

receptor binding

Inferred from physical interaction Ref.42. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.26. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P32121-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P32121-3)

The sequence of this isoform differs from the canonical sequence as follows:
     360-360: S → SAPTPTPPLPVPP
Isoform 3 (identifier: P32121-2)

The sequence of this isoform differs from the canonical sequence as follows:
     39-53: Missing.
     360-360: S → SAPTPTPPLPVPP
Note: No experimental confirmation available.
Isoform 4 (identifier: P32121-4)

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: T → TVRMPLPSEGQGAGAGTVSGVG
Note: No experimental confirmation available.
Isoform 5 (identifier: P32121-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Beta-arrestin-2
PRO_0000205199

Regions

Region240 – 409170Interaction with TRAF6
Region363 – 40947Interaction with AP2B1
Motif385 – 39511[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif

Amino acid modifications

Modified residue481Phosphotyrosine By similarity
Modified residue1761Hydroxyproline; by PHD2
Modified residue1811Hydroxyproline; by PHD2
Modified residue3601Phosphoserine By similarity
Modified residue3821Phosphothreonine Ref.16

Natural variations

Alternative sequence39 – 5315Missing in isoform 3 and isoform 5.
VSP_008194
Alternative sequence1191T → TVRMPLPSEGQGAGAGTVSG VG in isoform 4.
VSP_044697
Alternative sequence3601S → SAPTPTPPLPVPP in isoform 2 and isoform 3.
VSP_008195

Experimental info

Mutagenesis111K → A: Abolishes interaction with CHUK; when associated with A-12; A-230 and A-231.
Mutagenesis121K → A: Abolishes interaction with CHUK; when associated with A-11; A-230 and A-231.
Mutagenesis541V → A: Inhibits internalization of CXCR4; no effect on interaction with CXCR4. Ref.12
Mutagenesis2301K → A: Abolishes interaction with CHUK; when associated with A-11; A-12 and A-231.
Mutagenesis2311K → A: Abolishes interaction with CHUK; when associated with A-11; A-12 and A-230.
Mutagenesis3601S → A or D: Reduces interaction with CHUK; when associated with A-382.
Mutagenesis3821T → A or D: Reduces interaction with CHUK; when associated with A-360. Ref.16
Mutagenesis3821T → A: Loss of phosphorylation. Ref.16
Sequence conflict131S → P in BAG59672. Ref.5
Sequence conflict1891R → P in CAA77577. Ref.1
Sequence conflict1901H → R in ABG47460. Ref.3
Sequence conflict1921L → P in CAG29306. Ref.6
Sequence conflict3661D → G in BAG59672. Ref.5

Sequences

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

Last modified March 5, 2002. Version 2.
Checksum: DEEC507D4A7B84FF

FASTA40946,106
        10         20         30         40         50         60 
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK DRKVFVTLTC 

        70         80         90        100        110        120 
AFRYGREDLD VLGLSFRKDL FIATYQAFPP VPNPPRPPTR LQDRLLRKLG QHAHPFFFTI 

       130        140        150        160        170        180 
PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF CAKSLEEKSH KRNSVRLVIR KVQFAPEKPG 

       190        200        210        220        230        240 
PQPSAETTRH FLMSDRSLHL EASLDKELYY HGEPLNVNVH VTNNSTKTVK KIKVSVRQYA 

       250        260        270        280        290        300 
DICLFSTAQY KCPVAQLEQD DQVSPSSTFC KVYTITPLLS DNREKRGLAL DGKLKHEDTN 

       310        320        330        340        350        360 
LASSTIVKEG ANKEVLGILV SYRVKVKLVV SRGGDVSVEL PFVLMHPKPH DHIPLPRPQS 

       370        380        390        400 
AAPETDVPVD TNLIEFDTNY ATDDDIVFED FARLRLKGMK DDDYDDQLC 

« Hide

Isoform 2 [UniParc].

Checksum: 1D5F728967E2BF5D
Show »

FASTA42147,271
Isoform 3 [UniParc].

Checksum: 2020CE75484DF687
Show »

FASTA40645,557
Isoform 4 [UniParc].

Checksum: D41C217D16CFD41D
Show »

FASTA43048,015
Isoform 5 [UniParc].

Checksum: EE3C2EC61639E8D5
Show »

FASTA39444,392

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Ubiquitination of CXCR7 controls receptor trafficking."
Canals M., Scholten D.J., de Munnik S., Han M.K., Smit M.J., Leurs R.
PLoS ONE 7:E34192-E34192(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Arrestin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS11050.1. [P32121-1]
CCDS11051.1. [P32121-5]
CCDS58504.1. [P32121-4]
CCDS58505.1. [P32121-2]
PIRS18984.
RefSeqNP_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]
UniGeneHs.435811.

3D structure databases

ProteinModelPortalP32121.
SMRP32121. Positions 6-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106902. 321 interactions.
DIPDIP-40089N.
IntActP32121. 286 interactions.
MINTMINT-216692.
STRING9606.ENSP00000269260.

PTM databases

PhosphoSiteP32121.

Polymorphism databases

DMDM20141230.

Proteomic databases

MaxQBP32121.
PaxDbP32121.
PRIDEP32121.

Protocols and materials databases

DNASU409.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269260; ENSP00000269260; ENSG00000141480. [P32121-1]
ENST00000346341; ENSP00000341895; ENSG00000141480. [P32121-2]
ENST00000381488; ENSP00000370898; ENSG00000141480. [P32121-5]
ENST00000412477; ENSP00000403701; ENSG00000141480. [P32121-4]
GeneID409.
KEGGhsa:409.
UCSCuc002fyj.3. human. [P32121-1]
uc002fyl.3. human. [P32121-3]
uc002fym.3. human. [P32121-2]

Organism-specific databases

CTD409.
GeneCardsGC17P004613.
HGNCHGNC:712. ARRB2.
MIM107941. gene.
neXtProtNX_P32121.
PharmGKBPA60.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302111.
HOVERGENHBG002399.
KOK04439.
OMAKPHDHIT.
OrthoDBEOG79W954.
PhylomeDBP32121.
TreeFamTF314260.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
SignaLinkP32121.

Gene expression databases

ArrayExpressP32121.
BgeeP32121.
CleanExHS_ARRB2.
GenevestigatorP32121.

Family and domain databases

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

Other

ChiTaRSARRB2. human.
GeneWikiArrestin_beta_2.
GenomeRNAi409.
NextBio1719.
PROP32121.
SOURCESearch...

Entry information

Entry nameARRB2_HUMAN
AccessionPrimary (citable) accession number: P32121
Secondary accession number(s): B4DLW0 expand/collapse secondary AC list , B5B0C0, B7WPL3, D3DTK2, H0Y688, Q0Z8D3, Q2PP19, Q6ICT3, Q8N7Y2, Q9UEQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: March 5, 2002
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM