Q8BWG8 (ARRB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-arrestin-1

Alternative name(s):
Arrestin beta-1

Gene names

Name:

Arrb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	418 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Involved in internalization of P2RY4 and UTP-stimulated internalization of P2RY2. Involved in phosphorylation-dependent internalization of OPRD1 ands subsequent recycling. Involved in the degradation of cAMP by recruiting cAMP phosphodiesterases to ligand-activated receptors. Beta-arrestins function as multivalent adapter proteins that can switch the GPCR from a G-protein signaling mode that transmits short-lived signals from the plasma membrane via small molecule second messengers and ion channels to a beta-arrestin signaling mode that transmits a distinct set of signals that are initiated as the receptor internalizes and transits the intracellular compartment. Acts as signaling scaffold for MAPK pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-arrestin scaffold is largely excluded from the nucleus and confined to cytoplasmic locations such as endocytic vesicles, also called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2 resulting in ERK activation. GPCRs for which the beta-arrestin-mediated signaling relies on both ARRB1 and ARRB2 (codependent regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2 and is inhibited by the other respective beta-arrestin form (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and AVPR2-mediated activation (reciprocal regulation). Is required for SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to internalized NK1R resulting in ERK1/2 activation, which is required for the antiapoptotic effects of SP. Is involved in proteinase-activated F2RL1-mediated ERK activity. Acts as signaling scaffold for the AKT1 pathway. Is involved in alpha-thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated AKT1 signaling leading to increased protection from apoptosis. Involved in activation of the p38 MAPK signaling pathway and in actin bundle formation. Involved in F2RL1-mediated cytoskeletal rearrangement and chemotaxis. Involved in AGTR1-mediated stress fiber formation by acting together with GNAQ to activate RHOA. Appears to function as signaling scaffold involved in regulation of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in attenuation of NF-kappa-B-dependent transcription in response to GPCR or cytokine stimulation by interacting with and stabilizing CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-stimulated transcriptional regulation by translocating to CDKN1B and FOS promoter regions and recruiting EP300 resulting in acetylation of histone H4. Involved in regulation of LEF1 transcriptional activity via interaction with DVL1 and/or DVL2 Also involved in regulation of receptors other than GPCRs. Involved in Toll-like receptor and IL-1 receptor signaling through the interaction with TRAF6 which prevents TRAF6 autoubiquitination and oligomerization required for activation of NF-kappa-B and JUN. Involved in IL8-mediated granule release in neutrophils. Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6) By similarity. Required for atypical chemokine receptor ACKR2-induced RAC1-LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. Involved in the internalization of the atypical chemokine receptor ACKR3 By similarity. Ref.3 Ref.5
Subunit structure	Monomer. Homodimer. Homooligomer; the self-association is mediated by InsP6-binding. Heterooligomer with ARRB2; the association is mediated by InsP6-binding. Interacts with ADRB2 (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1 (dephosphorylated); phosphorylation of AP2B1 disrupts the interaction. Interacts (dephosphorylated at Ser-412) with CLTC. Interacts with CCR2 and ADRBK1. Interacts with CRR5. Interacts with PTAFR (phosphorylated on serine residues). Interacts with CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6. Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts with PDE4D. Interacts with SRC (via the SH3 domain and the protein kinase domain); the interaction is independent of the phosphorylation state of SRC C-terminus. Interacts with TACR1. Interacts with RAF1. Interacts with DVL1; the interaction is enhanced by phosphorylation of DVL1. Interacts with DVL2; the interaction is enhanced by phosphorylation of DVL2. Interacts with IGF1R. Interacts with CHUK, IKBKB and MAP3K14. Associates with MAP kinase p38. Part of a MAPK signaling complex consisting of TACR1, ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1 (activated) and MAPK3 (activated). Interacts with GPR143 By similarity. Interacts with MAP2K4/MKK4. Interacts with HCK and CXCR1 (phosphorylated) By similarity. Interacts with ACKR3 and ACKR4 By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. Membrane › clathrin-coated pit Probable. Cell projection › pseudopodium By similarity. Cytoplasmic vesicle By similarity. Note: Translocates to the plasma membrane and colocalizes with antagonist-stimulated GPCRs. The monomeric form is predominantly located in the nucleus. The oligomeric form is located in the cytoplasm. Translocates to the nucleus upon stimulation of OPRD1 By similarity.
Domain	The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. Binding to phosphorylated GPCRs induces a conformationanl change that exposes the motif to the surface By similarity. The N-terminus binds InsP6 with low affinity By similarity. The C-terminus binds InsP6 with high affinity By similarity.
Post-translational modification	Constitutively phosphorylated at in the cytoplasm. At the plasma membrane, is rapidly dephosphorylated, a process that is required for clathrin binding and ADRB2 endocytosis but not for ADRB2 binding and desensitization. Once internalized, is rephosphorylated 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 By similarity.
Sequence similarities	Belongs to the arrestin family.

Ontologies

Keywords
Biological process	Protein transport Transcription Transcription regulation Transport
Cellular component	Cell membrane Cell projection Coated pit Cytoplasm Cytoplasmic vesicle Membrane Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Signal transduction inhibitor
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G-protein coupled receptor internalization Inferred from electronic annotation. Source: Ensembl negative regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Ensembl negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB negative regulation of interleukin-6 production Inferred from electronic annotation. Source: Ensembl negative regulation of interleukin-8 production Inferred from electronic annotation. Source: Ensembl negative regulation of protein ubiquitination Inferred from electronic annotation. Source: Ensembl phototransduction Inferred from mutant phenotype PubMed 11853756. Source: MGI positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB positive regulation of Rho protein signal transduction Inferred from electronic annotation. Source: Ensembl positive regulation of histone H4 acetylation Inferred from electronic annotation. Source: Ensembl positive regulation of insulin secretion involved in cellular response to glucose stimulus Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB positive regulation of peptidyl-serine phosphorylation Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB positive regulation of protein binding Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB positive regulation of protein phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of receptor internalization Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl proteasome-mediated ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Ensembl protein transport Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Inferred from electronic annotation. Source: Ensembl regulation of G-protein coupled receptor protein signaling pathway Inferred from mutant phenotype PubMed 11171997PubMed 9400383. Source: MGI stress fiber assembly Inferred from electronic annotation. Source: Ensembl transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Ensembl
Cellular_component	chromatin Inferred from electronic annotation. Source: Ensembl coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 19915011. Source: UniProtKB intracellular Inferred from direct assay PubMed 11171997. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell pseudopodium Inferred from direct assay PubMed 12821670. Source: UniProtKB
Molecular_function	GTPase activator activity Inferred from electronic annotation. Source: Ensembl cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from mutant phenotype PubMed 19915011. Source: UniProtKB mitogen-activated protein kinase kinase binding Inferred from direct assay PubMed 19915011. Source: UniProtKB transcription regulatory region DNA binding Inferred from electronic annotation. Source: Ensembl
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dnajb6	O54946	6	EBI-641778,EBI-642500
Hax1	O35387	6	EBI-641778,EBI-642449
Mdm2	P23804	4	EBI-641778,EBI-641788
Nfe2l2	Q60795	4	EBI-641778,EBI-642563

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1A (identifier: Q8BWG8-1)

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 1B (identifier: Q8BWG8-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 418	418	Beta-arrestin-1		PRO_0000205195
Regions
	Region	1 – 163	163	Interaction with SRC By similarity
	Region	45 – 86	42	Interaction with CHRM2 By similarity
	Region	318 – 418	101	Interaction with TRAF6 By similarity
Sites
	Binding site	250	1	Inositol hexakisphosphate By similarity
	Binding site	255	1	Inositol hexakisphosphate By similarity
	Binding site	324	1	Inositol hexakisphosphate By similarity
	Binding site	326	1	Inositol hexakisphosphate By similarity
Amino acid modifications
	Modified residue	47	1	Phosphotyrosine Ref.4
	Modified residue	412	1	Phosphoserine; by GRK5 By similarity
Natural variations
	Alternative sequence	334 – 341	8	Missing in isoform 1B.		VSP_019545

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1A [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 389C24F8CDA06E64	FASTA	418	46,973
	10 20 30 40 50 60 MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA 70 80 90 100 110 120 FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HACPFTFEIP 130 140 150 160 170 180 PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP 190 200 210 220 230 240 QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD 250 260 270 280 290 300 ICLFNTAQYK CPVAMEEADD NVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL 310 320 330 340 350 360 ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP 370 380 390 400 410 PHREVPESET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKDEEDDGT GSPHLNNR
	Isoform 1B [UniParc]. Checksum: 087D1966062C7291	FASTA	410	46,216
	10 20 30 40 50 60 MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA 70 80 90 100 110 120 FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HACPFTFEIP 130 140 150 160 170 180 PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP 190 200 210 220 230 240 QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD 250 260 270 280 290 300 ICLFNTAQYK CPVAMEEADD NVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL 310 320 330 340 350 360 ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGDVAVELP FTLMHPKPKE EPPHREVPES 370 380 390 400 410 ETPVDTNLIE LDTNDDDIVF EDFARQRLKG MKDDKDEEDD GTGSPHLNNR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B). Strain: C57BL/6J. Tissue: Colon and Kidney.
[2]	"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 1B).
[3]	"Beta-arrestin1 mediates insulin-like growth factor 1 (IGF-1) activation of phosphatidylinositol 3-kinase (PI3K) and anti-apoptosis." Povsic T.J., Kohout T.A., Lefkowitz R.J. J. Biol. Chem. 278:51334-51339(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN AKT1 SIGNALING.
[4]	"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling." Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R. J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Mast cell.
[5]	"Beta-arrestins specifically constrain beta2-adrenergic receptor signaling and function in airway smooth muscle." Deshpande D.A., Theriot B.S., Penn R.B., Walker J.K. FASEB J. 22:2134-2141(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK052588 mRNA. Translation: BAC35050.1. AK090090 mRNA. Translation: BAC41087.1. AK144054 mRNA. Translation: BAE25673.1. AK147508 mRNA. Translation: BAE27962.1. AK165514 mRNA. Translation: BAE38230.1. BC108969 mRNA. Translation: AAI08970.1. BC108970 mRNA. Translation: AAI08971.1.
RefSeq	NP_796205.1. NM_177231.2. NP_835738.1. NM_178220.3.
UniGene	Mm.260193.
3D structure databases
ProteinModelPortal	Q8BWG8.
SMR	Q8BWG8. Positions 5-393.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	224960. 5 interactions.
IntAct	Q8BWG8. 15 interactions.
MINT	MINT-4088374.
PTM databases
PhosphoSite	Q8BWG8.
Proteomic databases
PaxDb	Q8BWG8.
PRIDE	Q8BWG8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000032995; ENSMUSP00000032995; ENSMUSG00000018909. [Q8BWG8-2] ENSMUST00000098266; ENSMUSP00000095866; ENSMUSG00000018909. [Q8BWG8-1]
GeneID	109689.
KEGG	mmu:109689.
UCSC	uc009ilu.1. mouse. [Q8BWG8-1] uc009ilv.1. mouse. [Q8BWG8-2]
Organism-specific databases
CTD	408.
MGI	MGI:99473. Arrb1.
Phylogenomic databases
eggNOG	NOG302111.
GeneTree	ENSGT00390000013152.
HOGENOM	HOG000231319.
HOVERGEN	HBG002399.
InParanoid	Q8BWG8.
KO	K04439.
OrthoDB	EOG79W954.
PhylomeDB	Q8BWG8.
TreeFam	TF314260.
Gene expression databases
ArrayExpress	Q8BWG8.
Bgee	Q8BWG8.
CleanEx	MM_ARRB1.
Genevestigator	Q8BWG8.
Family and domain databases
Gene3D	2.60.40.640. 1 hit. 2.60.40.840. 1 hit.
InterPro	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]
PANTHER	PTHR11792. PTHR11792. 1 hit.
Pfam	PF02752. Arrestin_C. 1 hit. PF00339. Arrestin_N. 1 hit. [Graphical view]
PRINTS	PR00309. ARRESTIN.
SMART	SM01017. Arrestin_C. 1 hit. [Graphical view]
SUPFAM	SSF81296. SSF81296. 2 hits.
PROSITE	PS00295. ARRESTINS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	362583.
PRO	Q8BWG8.
SOURCE	Search...

Entry information

Entry name

ARRB1_MOUSE

Accession

Primary (citable) accession number: Q8BWG8
Secondary accession number(s): Q3UH95, Q8BTJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
Last sequence update:	March 1, 2003
Last modified:	April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program