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Entry version 156 (18 Sep 2019)
Sequence version 1 (01 Dec 2001)
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Protein

Beta-arrestin-2

Gene

Arrb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Functions in regulating agonist-mediated G-protein coupled receptor (GPCR) signaling by mediating both receptor desensitization and resensitization processes. During homologous desensitization, beta-arrestins bind to the GPRK-phosphorylated receptor and sterically preclude its coupling to the cognate G-protein; the binding appears to require additional receptor determinants exposed only in the active receptor conformation. The beta-arrestins target many receptors for internalization by acting as endocytic adapters (CLASPs, clathrin-associated sorting proteins) and recruiting the GPRCs to the adapter protein 2 complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the extent of beta-arrestin involvement appears to vary significantly depending on the receptor, agonist and cell type. Internalized arrestin-receptor complexes traffic to intracellular endosomes, where they remain uncoupled from G-proteins. Two different modes of arrestin-mediated internalization occur. Class A receptors, like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-arrestin at or near the plasma membrane and undergo rapid recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and TACR1 internalize as a complex with arrestin and traffic with it to endosomal vesicles, presumably as desensitized receptors, for extended periods of time. Receptor resensitization then requires that receptor-bound arrestin is removed so that the receptor can be dephosphorylated and returned to the plasma membrane. Mediates endocytosis of CCR7 following ligation of CCL19 but not CCL21. Involved in internalization of P2RY1, P2RY4, P2RY6 and P2RY11 and ATP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 and subsequent recycling or degradation. Involved in ubiquitination of IGF1R. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2) and MAPK10 (JNK3). ERK1/2 and JNK3 activated by the beta-arrestin scaffold are largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Acts as signaling scaffold for the AKT1 pathway. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Increases ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Involved in CCR7-mediated ERK1/2 signaling involving ligand CCL19. Is involved in type-1A angiotensin II receptor/AGTR1-mediated ERK activity. Is involved in type-1A angiotensin II receptor/AGTR1-mediated MAPK10 activity. Is involved in dopamine-stimulated AKT1 activity in the striatum by disrupting the association of AKT1 with its negative regulator PP2A. Involved in AGTR1-mediated chemotaxis. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. Suppresses UV-induced NF-kappa-B-dependent activation by interacting with CHUK. The function is promoted by stimulation of ADRB2 and dephosphorylation of ARRB2. Involved in IL8-mediated granule release in neutrophils (By similarity). Involved in p53/TP53-mediated apoptosis by regulating MDM2 and reducing the MDM2-mediated degradation of p53/TP53. May serve as nuclear messenger for GPCRs. Upon stimulation of OR1D2, may be involved in regulation of gene expression during the early processes of fertilization. Also involved in regulation of receptors other than GPCRs. Involved in endocytosis of TGFBR2 and TGFBR3 and down-regulates TGF-beta signaling such as NF-kappa-B activation. Involved in endocytosis of low-density lipoprotein receptor/LDLR. Involved in endocytosis of smoothened homolog/Smo, which also requires GRK2. Involved in endocytosis of SLC9A5. Involved in endocytosis of ENG and subsequent TGF-beta-mediated ERK activation and migration of epithelial cells. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in insulin resistance by acting as insulin-induced signaling scaffold for SRC, AKT1 and INSR. Involved in regulation of inhibitory signaling of natural killer cells by recruiting PTPN6 and PTPN11 to KIR2DL1. Involved in the internalization of the atypical chemokine receptor ACKR3 (By similarity).By similarity6 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionSignal transduction inhibitor
Biological processProtein transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-418555 G alpha (s) signalling events
R-MMU-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5635838 Activation of SMO
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5689880 Ub-specific processing proteases
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Beta-arrestin-2
Alternative name(s):
Arrestin beta-2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Arrb2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

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MGIi
MGI:99474 Arrb2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of beta-2 adrenergic receptor/ADRB2 ubiquitination. Reduction of dopamine-dependent behaviors, loss of Akt1 regulation by dopamine in the striatum and disruption of the dopamine-dependent interaction of Akt1 with its negative regulator, protein phosphatase 2A. Increased serum LDL-cholesterol levels upon high fat diet. Exacerbates insulin resistance. Elevated cytotoxicity of natural killer cells and lowered susceptibility to mouse cytomegalovirus infection.5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi395L → A: Nuclear localization. Causes nuclear relocalization of MAPK10. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002052001 – 410Beta-arrestin-2Add BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei48PhosphotyrosineCombined sources1
Modified residuei176Hydroxyproline; by PHD2By similarity1
Modified residuei181Hydroxyproline; by PHD2By similarity1
Modified residuei361PhosphoserineBy similarity1
Modified residuei383PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Thr-383 in the cytoplasm; probably dephosphorylated at the plasma membrane. The phosphorylation does not regulate internalization and recycling of ADRB2, interaction with clathrin or AP2B1 (By similarity).By similarity
The ubiquitination status appears to regulate the formation and trafficking of beta-arrestin-GPCR complexes and signaling. Ubiquitination appears to 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. Stimulation of a class B GPCR promotes a sustained ubiquitination (By similarity).By similarity
Hydroxylation by PHD2 modulates the rate of internalization by slowing down recruitment to the plasma membrane and inhibiting subsequent co-internalization with class A receptors.By similarity

Keywords - PTMi

Hydroxylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q91YI4

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q91YI4

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q91YI4

PeptideAtlas

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PeptideAtlasi
Q91YI4

PRoteomics IDEntifications database

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PRIDEi
Q91YI4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q91YI4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q91YI4

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q91YI4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Predominantly localized in neuronal tissues and in the spleen.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000060216 Expressed in 257 organ(s), highest expression level in bone marrow macrophage

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q91YI4 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q91YI4 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooligomer; the self-association is mediated by InsP6-binding (Probable). Heterooligomer with ARRB1; the association is mediated by InsP6-binding.

Interacts with ADRB2 AND CHRM2.

Interacts with PDE4A.

Interacts with PDE4D.

Interacts with MAPK10, MAPK1 and MAPK3.

Interacts with DRD2.

Interacts with FSHR.

Interacts with CLTC.

Interacts with HTR2C.

Interacts with CCR5.

Interacts with CXCR4.

Interacts with SRC.

Interacts with DUSP16; the interaction is interrupted by stimulation of AGTR1 and activation of MAPK10.

Interacts with CHUK; the interaction is enhanced stimulation of ADRB2.

Interacts with RELA.

Interacts with MDM2; the interaction is enhanced by activation of GPCRs.

Interacts with SLC9A5.

Interacts with TRAF6.

Interacts with IGF1R.

Interacts with ENG.

Interacts with ARRB2.

Interacts with KIR2DL1, KIR2DL3 and KIR2DL4.

Interacts with LDLR.

Interacts with AP2B1.

Interacts with C5AR1.

Interacts with RAF1.

Interacts with MAP2K1.

Interacts with MAPK1.

Interacts with MAPK10; the interaction enhances MAPK10 activation by MAP3K5.

Interacts with MAP2K4; the interaction is enhanced by presence of MAP3K5 and MAPK10.

Interacts with MAP3K5.

Interacts with AKT1.

Interacts with IKBKB and MAP3K14.

Interacts with SMO (activated).

Interacts with GSK3A and GSK3B.

Interacts with CXCR4; the interaction is dependent on C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3.

Interacts with GPR143.

Interacts with HCK and CXCR1 (phosphorylated) (By similarity). Associates with protein phosphatase 2A (PP2A).

Interacts with ACKR3 and ACKR4 (By similarity).

Interacts with ARRDC1; the interaction is direct (By similarity).

Interacts with GPR61, GPR62 and GPR135 (By similarity).

By similarityCurated

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
229812, 35 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q91YI4

Database of interacting proteins

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DIPi
DIP-36064N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q91YI4

Protein interaction database and analysis system

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IntActi
Q91YI4, 34 interactors

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000104208

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q91YI4

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni241 – 410Interaction with TRAF6By similarityAdd BLAST170
Regioni364 – 410Interaction with AP2B1By similarityAdd BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi386 – 396[DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motifBy similarityAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3865 Eukaryota
ENOG410XR0F LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182887

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231319

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q91YI4

KEGG Orthology (KO)

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KOi
K04439

Identification of Orthologs from Complete Genome Data

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OMAi
YQAFPPT

Database of Orthologous Groups

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OrthoDBi
783081at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q91YI4

TreeFam database of animal gene trees

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TreeFami
TF314260

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.640, 1 hit
2.60.40.840, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000698 Arrestin
IPR011021 Arrestin-like_N
IPR014752 Arrestin_C
IPR011022 Arrestin_C-like
IPR017864 Arrestin_CS
IPR014753 Arrestin_N
IPR014756 Ig_E-set

The PANTHER Classification System

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PANTHERi
PTHR11792 PTHR11792, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02752 Arrestin_C, 1 hit
PF00339 Arrestin_N, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00309 ARRESTIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01017 Arrestin_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF81296 SSF81296, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00295 ARRESTINS, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGEKPGTRVF KKSSPNCKLT VYLGKRDFVD HLDKVDPVDG VVLVDPDYLK
60 70 80 90 100
DRKVFVTLTC AFRYGREDLD VLGLSFRKDL FIATYQAFPP MPNPPRPPTR
110 120 130 140 150
LQDRLLKKLG QHAHPFFFTI PQNLPCSVTL QPGPEDTGKA CGVDFEIRAF
160 170 180 190 200
CAKSIEEKSH KRNSVRLIIR KVQFAPETPG PQPSAETTRH FLMSDRRSLH
210 220 230 240 250
LEASLDKELY YHGEPLNVNV HVTNNSAKTV KKIRVSVRQY ADICLFSTAQ
260 270 280 290 300
YKCPVAQLEQ DDQVSPSSTF CKVYTITPLL SDNREKRGLA LDGQLKHEDT
310 320 330 340 350
NLASSTIVKE GANKEVLGIL VSYRVKVKLV VSRGGDVSVE LPFVLMHPKP
360 370 380 390 400
HDHITLPRPQ SAPRETDVPV DTNLIEFDTN YATDDDIVFE DFARLRLKGM
410
KDDDCDDQFC
Length:410
Mass (Da):46,314
Last modified:December 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0DFA73A1C532AE03
GO
Isoform 2 (identifier: Q91YI4-2) [UniParc]FASTAAdd to basket

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

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QN53J3QN53_MOUSE
Beta-arrestin-2
Arrb2
27Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QNV6J3QNV6_MOUSE
Beta-arrestin-2
Arrb2
83Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5F2D9Q5F2D9_MOUSE
Arrestin, beta 2
Arrb2 DN-491F10.4-006
406Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3UZ54G3UZ54_MOUSE
Beta-arrestin-2
Arrb2
37Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti11K → R in BAE41934 (PubMed:16141072).Curated1
Sequence conflicti59T → N in BAE41934 (PubMed:16141072).Curated1
Sequence conflicti75S → Y in BAE41934 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_020652360Q → QSAPIHPPLLCP in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AK154874 mRNA Translation: BAE32894.1
AK159317 mRNA Translation: BAE34984.1
AK170647 mRNA Translation: BAE41934.1
AK170889 mRNA Translation: BAE42096.1
AL596096 Genomic DNA No translation available.
BC016642 mRNA Translation: AAH16642.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS24946.1 [Q91YI4-1]
CCDS70226.1 [Q91YI4-2]

NCBI Reference Sequences

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RefSeqi
NP_001258287.1, NM_001271358.1 [Q91YI4-2]
NP_001258288.1, NM_001271359.1 [Q91YI4-2]
NP_001258289.1, NM_001271360.1 [Q91YI4-1]
NP_663404.1, NM_145429.5 [Q91YI4-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000079056; ENSMUSP00000078065; ENSMUSG00000060216 [Q91YI4-2]
ENSMUST00000102563; ENSMUSP00000099623; ENSMUSG00000060216 [Q91YI4-1]
ENSMUST00000102564; ENSMUSP00000099624; ENSMUSG00000060216 [Q91YI4-1]
ENSMUST00000108568; ENSMUSP00000104208; ENSMUSG00000060216 [Q91YI4-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
216869

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:216869

UCSC genome browser

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UCSCi
uc007jur.2 mouse [Q91YI4-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK154874 mRNA Translation: BAE32894.1
AK159317 mRNA Translation: BAE34984.1
AK170647 mRNA Translation: BAE41934.1
AK170889 mRNA Translation: BAE42096.1
AL596096 Genomic DNA No translation available.
BC016642 mRNA Translation: AAH16642.1
CCDSiCCDS24946.1 [Q91YI4-1]
CCDS70226.1 [Q91YI4-2]
RefSeqiNP_001258287.1, NM_001271358.1 [Q91YI4-2]
NP_001258288.1, NM_001271359.1 [Q91YI4-2]
NP_001258289.1, NM_001271360.1 [Q91YI4-1]
NP_663404.1, NM_145429.5 [Q91YI4-1]

3D structure databases

SMRiQ91YI4
ModBaseiSearch...

Protein-protein interaction databases

BioGridi229812, 35 interactors
CORUMiQ91YI4
DIPiDIP-36064N
ELMiQ91YI4
IntActiQ91YI4, 34 interactors
STRINGi10090.ENSMUSP00000104208

PTM databases

iPTMnetiQ91YI4
PhosphoSitePlusiQ91YI4
SwissPalmiQ91YI4

Proteomic databases

EPDiQ91YI4
jPOSTiQ91YI4
PaxDbiQ91YI4
PeptideAtlasiQ91YI4
PRIDEiQ91YI4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
409
MGIiMGI:99474 Arrb2

Phylogenomic databases

eggNOGiKOG3865 Eukaryota
ENOG410XR0F LUCA
GeneTreeiENSGT00950000182887
HOGENOMiHOG000231319
InParanoidiQ91YI4
KOiK04439
OMAiYQAFPPT
OrthoDBi783081at2759
PhylomeDBiQ91YI4
TreeFamiTF314260

Enzyme and pathway databases

ReactomeiR-MMU-418555 G alpha (s) signalling events
R-MMU-456926 Thrombin signalling through proteinase activated receptors (PARs)
R-MMU-5099900 WNT5A-dependent internalization of FZD4
R-MMU-5635838 Activation of SMO
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5689880 Ub-specific processing proteases
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Arrb2 mouse

Protein Ontology

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PROi
PR:Q91YI4

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000060216 Expressed in 257 organ(s), highest expression level in bone marrow macrophage
ExpressionAtlasiQ91YI4 baseline and differential
GenevisibleiQ91YI4 MM

Family and domain databases

Gene3Di2.60.40.640, 1 hit
2.60.40.840, 1 hit
InterProiView protein in InterPro
IPR000698 Arrestin
IPR011021 Arrestin-like_N
IPR014752 Arrestin_C
IPR011022 Arrestin_C-like
IPR017864 Arrestin_CS
IPR014753 Arrestin_N
IPR014756 Ig_E-set
PANTHERiPTHR11792 PTHR11792, 1 hit
PfamiView protein in Pfam
PF02752 Arrestin_C, 1 hit
PF00339 Arrestin_N, 1 hit
PRINTSiPR00309 ARRESTIN
SMARTiView protein in SMART
SM01017 Arrestin_C, 1 hit
SUPFAMiSSF81296 SSF81296, 2 hits
PROSITEiView protein in PROSITE
PS00295 ARRESTINS, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARRB2_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q91YI4
Secondary accession number(s): Q3TCM2, Q5F2D8, Q5F2E0
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: December 1, 2001
Last modified: September 18, 2019
This is version 156 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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