ID ARRB1_HUMAN Reviewed; 418 AA. AC P49407; O75625; O75630; Q2PP20; Q9BTK8; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 05-MAR-2002, sequence version 2. DT 28-JUL-2009, entry version 81. DE RecName: Full=Beta-arrestin-1; DE AltName: Full=Arrestin beta-1; GN Name=ARRB1; Synonyms=ARR1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B). RC TISSUE=Peripheral blood; RX MEDLINE=93252853; PubMed=8486659; RA Parruti G., Peracchia F., Sallese M., Ambrosini G., Masini M., RA Rotilio D., de Blasi A.; RT "Molecular analysis of human beta-arrestin-1: cloning, tissue RT distribution, and regulation of expression. Identification of two RT isoforms generated by alternative splicing."; RL J. Biol. Chem. 268:9753-9761(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B). RC TISSUE=Brain; RA Yu Q.M., Zhou T.H., Cheng Z.J., Ma L., Pei G.; RT "Molecular cloning of two isoforms of human beta-arrestin 1."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A). RC TISSUE=Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Regulates beta-adrenergic receptor function. Beta- CC arrestins seem to bind phosphorylated beta-adrenergic receptors, CC thereby causing a significant impairment of their capacity to CC activate G(S) proteins. CC -!- INTERACTION: CC O00203:AP3B1; NbExp=1; IntAct=EBI-743313, EBI-1044383; CC P36575:ARR3; NbExp=1; IntAct=EBI-743313, EBI-718116; CC P32121:ARRB2; NbExp=1; IntAct=EBI-743313, EBI-714559; CC Q14137:BOP1; NbExp=1; IntAct=EBI-743313, EBI-1050828; CC P62158:CALM1; NbExp=1; IntAct=EBI-743313, EBI-397435; CC Q16627:CCL14; NbExp=1; IntAct=EBI-743313, EBI-1046947; CC Q96DG6:CMBL; NbExp=1; IntAct=EBI-743313, EBI-1044268; CC P68400:CSNK2A1; NbExp=1; IntAct=EBI-743313, EBI-347804; CC Q96GQ7:DDX27; NbExp=1; IntAct=EBI-743313, EBI-722051; CC P06396:GSN; NbExp=1; IntAct=EBI-743313, EBI-351506; CC Q7Z4V5:HDGFRP2; NbExp=1; IntAct=EBI-743313, EBI-1049136; CC P11142:HSPA8; NbExp=1; IntAct=EBI-743313, EBI-351896; CC P50053:KHK; NbExp=1; IntAct=EBI-743313, EBI-1053974; CC O00505:KPNA3; NbExp=1; IntAct=EBI-743313, EBI-358297; CC P19338:NCL; NbExp=1; IntAct=EBI-743313, EBI-352553; CC Q14978:NOLC1; NbExp=2; IntAct=EBI-743313, EBI-396155; CC O00541:PES1; NbExp=1; IntAct=EBI-743313, EBI-1053271; CC P14618:PKM2; NbExp=1; IntAct=EBI-743313, EBI-353408; CC P35813:PPM1A; NbExp=1; IntAct=EBI-743313, EBI-989143; CC O75688:PPM1B; NbExp=1; IntAct=EBI-743313, EBI-1047039; CC Q13523:PRPF4B; NbExp=1; IntAct=EBI-743313, EBI-395940; CC Q6DKI1:RPL7L1; NbExp=1; IntAct=EBI-743313, EBI-1052408; CC Q92541:RTF1; NbExp=1; IntAct=EBI-743313, EBI-1055239; CC P06702:S100A9; NbExp=1; IntAct=EBI-743313, EBI-1055001; CC Q15208:STK38; NbExp=1; IntAct=EBI-743313, EBI-458376; CC Q13428:TCOF1; NbExp=2; IntAct=EBI-743313, EBI-396105; CC P27348:YWHAQ; NbExp=1; IntAct=EBI-743313, EBI-359854; CC O95218:ZRANB2; NbExp=2; IntAct=EBI-743313, EBI-1051583; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1A; CC IsoId=P49407-1; Sequence=Displayed; CC Name=1B; CC IsoId=P49407-2; Sequence=VSP_000322; CC -!- SIMILARITY: Belongs to the arrestin family. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Arrestin entry; CC URL="http://en.wikipedia.org/wiki/Arrestin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L04685; AAA35559.1; -; mRNA. DR EMBL; L04685; AAA35558.1; -; mRNA. DR EMBL; AF084040; AAC33295.1; -; mRNA. DR EMBL; AF084940; AAC34123.1; -; mRNA. DR EMBL; DQ314865; ABC40724.1; -; Genomic_DNA. DR EMBL; BC003636; AAH03636.1; -; mRNA. DR IPI; IPI00293857; -. DR IPI; IPI00336017; -. DR PIR; B46682; B46682. DR RefSeq; NP_004032.2; -. DR RefSeq; NP_064647.1; -. DR UniGene; Hs.503284; -. DR UniGene; Hs.625320; -. DR PDB; 2IV8; X-ray; 2.80 A; P/Q=383-402. DR PDBsum; 2IV8; -. DR IntAct; P49407; 189. DR PhosphoSite; P49407; -. DR OGP; P49407; -. DR PRIDE; P49407; -. DR Ensembl; ENST00000360025; ENSP00000353124; ENSG00000137486; Homo sapiens. DR Ensembl; ENST00000393505; ENSP00000377141; ENSG00000137486; Homo sapiens. DR GeneID; 408; -. DR KEGG; hsa:408; -. DR UCSC; uc001owe.1; human. DR UCSC; uc001owf.1; human. DR GeneCards; GC11M074654; -. DR H-InvDB; HIX0009944; -. DR HGNC; HGNC:711; ARRB1. DR HPA; CAB003763; -. DR MIM; 107940; gene. DR PharmGKB; PA59; -. DR HOGENOM; P49407; -. DR HOVERGEN; P49407; -. DR Pathway_Interaction_DB; arf6cyclingpathway; Arf6 signaling events. DR Reactome; REACT_11123; Membrane Trafficking. DR NextBio; 1713; -. DR ArrayExpress; P49407; -. DR Bgee; P49407; -. DR CleanEx; HS_ARRB1; -. DR GermOnline; ENSG00000137486; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005624; C:membrane fraction; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0005625; C:soluble fraction; TAS:UniProtKB. DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR000698; Arrestin. DR InterPro; IPR011022; Arrestin-like_C. DR InterPro; IPR011021; Arrestin-like_N. DR InterPro; IPR014752; Arrestin_C. DR InterPro; IPR017864; Arrestin_CS. DR InterPro; IPR014753; Arrestin_N. DR Gene3D; G3DSA:2.60.40.640; Arrestin_C; 1. DR Gene3D; G3DSA:2.60.40.840; Arrestin_N; 1. DR PANTHER; PTHR11792; Arrestin; 1. DR Pfam; PF02752; Arrestin_C; 1. DR Pfam; PF00339; Arrestin_N; 1. DR PRINTS; PR00309; ARRESTIN. DR ProDom; PD002099; Arrestin; 2. DR PROSITE; PS00295; ARRESTINS; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Complete proteome; Phosphoprotein; KW Sensory transduction. FT CHAIN 1 418 Beta-arrestin-1. FT /FTId=PRO_0000205194. FT MOD_RES 47 47 Phosphotyrosine (By similarity). FT MOD_RES 410 410 Phosphothreonine (By similarity). FT MOD_RES 412 412 Phosphoserine (By similarity). FT VAR_SEQ 334 341 Missing (in isoform 1B). FT /FTId=VSP_000322. FT CONFLICT 146 146 V -> A (in Ref. 1; AAA35559/AAA35558). FT CONFLICT 165 165 R -> G (in Ref. 1; AAA35559/AAA35558). FT CONFLICT 229 229 K -> E (in Ref. 1; AAA35559/AAA35558). FT CONFLICT 329 329 V -> E (in Ref. 2; AAC33295/AAC34123). FT CONFLICT 400 400 K -> E (in Ref. 1; AAA35559/AAA35558). FT CONFLICT 414 414 Q -> R (in Ref. 1; AAA35559/AAA35558). FT CONFLICT 417 417 N -> D (in Ref. 1; AAA35559/AAA35558). FT HELIX 384 394 SQ SEQUENCE 418 AA; 47066 MW; 0A3C135092338D10 CRC64; MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HAYPFTFEIP PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD ICLFNTAQYK CPVAMEEADD TVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP PHREVPENET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKEEEEDGT GSPQLNNR //