ID REN3B_HUMAN Reviewed; 483 AA. AC Q9BZI7; D3DWI3; D3DWI4; Q0VAK8; Q9H1J0; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 24-JAN-2024, entry version 188. DE RecName: Full=Regulator of nonsense transcripts 3B {ECO:0000312|HGNC:HGNC:20439}; DE AltName: Full=Nonsense mRNA reducing factor 3B {ECO:0000312|HGNC:HGNC:20439}; DE AltName: Full=Up-frameshift suppressor 3 homolog B {ECO:0000250|UniProtKB:P48412}; DE Short=hUpf3B; DE AltName: Full=Up-frameshift suppressor 3 homolog on chromosome X; DE Short=hUpf3p-X; GN Name=UPF3B {ECO:0000312|HGNC:HGNC:20439}; GN Synonyms=RENT3B {ECO:0000312|HGNC:HGNC:20439}, UPF3X; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION IN NONSENSE-MEDIATED MRNA RP DECAY, INTERACTION WITH UPF1 AND UPF2, AND SUBCELLULAR LOCATION. RX PubMed=11163187; DOI=10.1016/s0092-8674(00)00214-2; RA Lykke-Andersen J., Shu M.-D., Steitz J.A.; RT "Human Upf proteins target an mRNA for nonsense-mediated decay when bound RT downstream of a termination codon."; RL Cell 103:1121-1131(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH UPF2, MUTAGENESIS RP OF 53-VAL--LEU-58 AND 117-TYR--PHE-119, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Cervix carcinoma; RX PubMed=11113196; DOI=10.1128/mcb.21.1.209-223.2001; RA Serin G., Gersappe A., Black J.D., Aronoff R., Maquat L.E.; RT "Identification and characterization of human orthologues to Saccharomyces RT cerevisiae Upf2 protein and Upf3 protein (Caenorhabditis elegans SMG-4)."; RL Mol. Cell. Biol. 21:209-223(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH RBM8A, IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, RP ASSOCIATION WITH THE EJC COMPLEX, AND RNA-BINDING. RX PubMed=11546873; DOI=10.1126/science.1062829; RA Kim V.N., Kataoka N., Dreyfuss G.; RT "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent RT exon-exon junction complex."; RL Science 293:1832-1836(2001). RN [6] RP IDENTIFICATION IN A POST-SPLICING MRNP COMPLEX, AND ASSOCIATION WITH THE RP EJC COMPLEX. RX PubMed=11546874; DOI=10.1126/science.1062786; RA Lykke-Andersen J., Shu M.-D., Steitz J.A.; RT "Communication of the position of exon-exon junctions to the mRNA RT surveillance machinery by the protein RNPS1."; RL Science 293:1836-1839(2001). RN [7] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH RBM8A, AND RP MUTAGENESIS OF ARG-430; ARG-432; 434-LYS--ARG-447; LYS-434; ASP-435; RP ARG-436 AND LEU-441. RX PubMed=12718880; DOI=10.1016/s1097-2765(03)00142-4; RA Gehring N.H., Neu-Yilik G., Schell T., Hentze M.W., Kulozik A.E.; RT "Y14 and hUpf3b form an NMD-activating complex."; RL Mol. Cell 11:939-949(2003). RN [8] RP INTERACTION WITH EST1A. RX PubMed=12554878; DOI=10.1261/rna.2137903; RA Chiu S.-Y., Serin G., Ohara O., Maquat L.E.; RT "Characterization of human Smg5/7a: a protein with similarities to RT Caenorhabditis elegans SMG5 and SMG7 that functions in the RT dephosphorylation of Upf1."; RL RNA 9:77-87(2003). RN [9] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, ASSOCIATION WITH THE EJC COMPLEX, RP AND IDENTIFICATION IN A COMPLEX WITH UPF2 AND RNPS1. RX PubMed=16209946; DOI=10.1016/j.molcel.2005.08.012; RA Gehring N.H., Kunz J.B., Neu-Yilik G., Breit S., Viegas M.H., Hentze M.W., RA Kulozik A.E.; RT "Exon-junction complex components specify distinct routes of nonsense- RT mediated mRNA decay with differential cofactor requirements."; RL Mol. Cell 20:65-75(2005). RN [10] RP FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, FUNCTION IN TRANSLATION RP STIMULATION, ASSOCIATION WITH THE EJC COMPLEX, AND MUTAGENESIS OF ARG-432. RX PubMed=16601204; DOI=10.1261/rna.12506; RA Kunz J.B., Neu-Yilik G., Hentze M.W., Kulozik A.E., Gehring N.H.; RT "Functions of hUpf3a and hUpf3b in nonsense-mediated mRNA decay and RT translation."; RL RNA 12:1015-1022(2006). RN [11] RP FUNCTION, AND RECONSTITUTION OF THE EJC CORE-UPF COMPLEX. RX PubMed=18066079; DOI=10.1038/nsmb1330; RA Chamieh H., Ballut L., Bonneau F., Le Hir H.; RT "NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and RT stimulate its RNA helicase activity."; RL Nat. Struct. Mol. Biol. 15:85-93(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP INTERACTION WITH CPSF6. RX PubMed=19864460; DOI=10.1091/mbc.e09-05-0389; RA Ruepp M.D., Aringhieri C., Vivarelli S., Cardinale S., Paro S., RA Schuemperli D., Barabino S.M.; RT "Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA RT export."; RL Mol. Biol. Cell 20:5211-5223(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169 AND SER-310, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169 AND SER-310, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [19] RP IDENTIFICATION IN THE EXON JUNCTION COMPLEX. RX PubMed=23917022; DOI=10.4161/rna.25827; RA Singh K.K., Wachsmuth L., Kulozik A.E., Gehring N.H.; RT "Two mammalian MAGOH genes contribute to exon junction complex composition RT and nonsense-mediated decay."; RL RNA Biol. 10:1291-1298(2013). RN [20] RP INTERACTION WITH DHX34. RX PubMed=25220460; DOI=10.1016/j.celrep.2014.08.020; RA Hug N., Caceres J.F.; RT "The RNA helicase DHX34 activates NMD by promoting a transition from the RT surveillance to the decay-inducing complex."; RL Cell Rep. 8:1845-1856(2014). RN [21] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-447, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 50-140 IN COMPLEX WITH UPF2, RP RNA-BINDING, AND MUTAGENESIS OF LYS-52 AND ARG-56. RX PubMed=15004547; DOI=10.1038/nsmb741; RA Kadlec J., Izaurralde E., Cusack S.; RT "The structural basis for the interaction between nonsense-mediated mRNA RT decay factors UPF2 and UPF3."; RL Nat. Struct. Mol. Biol. 11:330-337(2004). RN [23] RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 424-483 IN COMPLEX WITH EIF4A3; RP MAGOH; RBM8A AND CASC3, AND MUTAGENESIS OF ARG-436; TYR-442; ARG-447; RP ARG-449 AND ARG-451. RX PubMed=20479275; DOI=10.1073/pnas.1000993107; RA Buchwald G., Ebert J., Basquin C., Sauliere J., Jayachandran U., Bono F., RA Le Hir H., Conti E.; RT "Insights into the recruitment of the NMD machinery from the crystal RT structure of a core EJC-UPF3b complex."; RL Proc. Natl. Acad. Sci. U.S.A. 107:10050-10055(2010). RN [24] RP VARIANT MRXS14 ASP-160. RX PubMed=17704778; DOI=10.1038/ng2100; RA Tarpey P.S., Raymond F.L., Nguyen L.S., Rodriguez J., Hackett A., RA Vandeleur L., Smith R., Shoubridge C., Edkins S., Stevens C., O'Meara S., RA Tofts C., Barthorpe S., Buck G., Cole J., Halliday K., Hills K., Jones D., RA Mironenko T., Perry J., Varian J., West S., Widaa S., Teague J., Dicks E., RA Butler A., Menzies A., Richardson D., Jenkinson A., Shepherd R., Raine K., RA Moon J., Luo Y., Parnau J., Bhat S.S., Gardner A., Corbett M., Brooks D., RA Thomas P., Parkinson-Lawrence E., Porteous M.E., Warner J.P., Sanderson T., RA Pearson P., Simensen R.J., Skinner C., Hoganson G., Superneau D., RA Wooster R., Bobrow M., Turner G., Stevenson R.E., Schwartz C.E., RA Futreal P.A., Srivastava A.K., Stratton M.R., Gecz J.; RT "Mutations in UPF3B, a member of the nonsense-mediated mRNA decay complex, RT cause syndromic and nonsyndromic mental retardation."; RL Nat. Genet. 39:1127-1133(2007). CC -!- FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing CC premature stop codons by associating with the nuclear exon junction CC complex (EJC) and serving as link between the EJC core and NMD CC machinery. Recruits UPF2 at the cytoplasmic side of the nuclear CC envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance CC complex (including UPF1 bound to release factors at the stalled CC ribosome) is believed to activate NMD. In cooperation with UPF2 CC stimulates both ATPase and RNA helicase activities of UPF1. Binds CC spliced mRNA upstream of exon-exon junctions. In vitro, stimulates CC translation; the function is independent of association with UPF2 and CC components of the EJC core. {ECO:0000269|PubMed:11163187, CC ECO:0000269|PubMed:12718880, ECO:0000269|PubMed:16209946, CC ECO:0000269|PubMed:16601204, ECO:0000269|PubMed:18066079}. CC -!- SUBUNIT: Found in a post-splicing messenger ribonucleoprotein (mRNP) CC complex. Core component of the mRNA splicing-dependent exon junction CC complex (EJC); the core complex contains CASC3, EIF4A3, MAGOH or CC MAGOHB, and RBM8A. The EJC core components EIF4A3 and the MAGOH-RBM8A CC dimer form a composite binding site for UPF3B which overlaps with the CC EJC binding site for WIBG (PubMed:16601204, PubMed:18066079, CC PubMed:23917022, PubMed:20479275). Interacts with EST1A, UPF2 and RBM8A CC (PubMed:12554878, PubMed:18066079, PubMed:15004547). Interacts with CC CPSF6 (PubMed:19864460). Interacts with DHX34; the interaction is RNA- CC independent. {ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187, CC ECO:0000269|PubMed:11546873, ECO:0000269|PubMed:11546874, CC ECO:0000269|PubMed:12554878, ECO:0000269|PubMed:12718880, CC ECO:0000269|PubMed:15004547, ECO:0000269|PubMed:16209946, CC ECO:0000269|PubMed:16601204, ECO:0000269|PubMed:18066079, CC ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20479275, CC ECO:0000269|PubMed:23917022}. CC -!- INTERACTION: CC Q9BZI7; P38919: EIF4A3; NbExp=9; IntAct=EBI-372780, EBI-299104; CC Q9BZI7; P61326: MAGOH; NbExp=7; IntAct=EBI-372780, EBI-299134; CC Q9BZI7; Q9Y5S9: RBM8A; NbExp=9; IntAct=EBI-372780, EBI-447231; CC Q9BZI7; Q92900: UPF1; NbExp=10; IntAct=EBI-372780, EBI-373471; CC Q9BZI7; Q9HAU5: UPF2; NbExp=8; IntAct=EBI-372780, EBI-372073; CC Q9BZI7-2; P61326: MAGOH; NbExp=2; IntAct=EBI-15674130, EBI-299134; CC Q9BZI7-2; Q9HAU5: UPF2; NbExp=7; IntAct=EBI-15674130, EBI-372073; CC Q9BZI7-2; Q9H1J1: UPF3A; NbExp=2; IntAct=EBI-15674130, EBI-521530; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11113196, CC ECO:0000269|PubMed:11163187}. Cytoplasm {ECO:0000269|PubMed:11163187}. CC Note=Shuttling between the nucleus and the cytoplasm. CC {ECO:0000269|PubMed:11163187}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BZI7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZI7-2; Sequence=VSP_012963; CC -!- TISSUE SPECIFICITY: Expressed in testis, uterus, prostate, heart, CC muscle, brain, spinal cord and placenta. {ECO:0000269|PubMed:11113196}. CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic 14 CC (MRXS14) [MIM:300676]: A disorder characterized by significantly below CC average general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC MRXS14 patients manifest intellectual disability associated with other CC variable signs such as autistic features, slender build, poor CC musculature, long, thin face, high-arched palate, high nasal bridge, CC and pectus deformities. {ECO:0000269|PubMed:17704778}. Note=The disease CC is caused by variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RENT3 family. {ECO:0000305}. 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; AY013251; AAG48511.1; -; mRNA. DR EMBL; AF318576; AAG60691.1; -; mRNA. DR EMBL; CH471161; EAW89842.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89844.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89845.1; -; Genomic_DNA. DR EMBL; CH471161; EAW89846.1; -; Genomic_DNA. DR EMBL; BC121017; AAI21018.1; -; mRNA. DR CCDS; CCDS14587.1; -. [Q9BZI7-2] DR CCDS; CCDS14588.1; -. [Q9BZI7-1] DR RefSeq; NP_075386.1; NM_023010.3. [Q9BZI7-2] DR RefSeq; NP_542199.1; NM_080632.2. [Q9BZI7-1] DR PDB; 1UW4; X-ray; 1.95 A; A/C=50-140. DR PDB; 2XB2; X-ray; 3.40 A; G/U=424-483. DR PDB; 7NWU; X-ray; 2.60 A; A/C/E/G=49-170. DR PDBsum; 1UW4; -. DR PDBsum; 2XB2; -. DR PDBsum; 7NWU; -. DR AlphaFoldDB; Q9BZI7; -. DR SMR; Q9BZI7; -. DR BioGRID; 122396; 145. DR CORUM; Q9BZI7; -. DR DIP; DIP-31143N; -. DR IntAct; Q9BZI7; 37. DR MINT; Q9BZI7; -. DR STRING; 9606.ENSP00000276201; -. DR GlyGen; Q9BZI7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BZI7; -. DR PhosphoSitePlus; Q9BZI7; -. DR BioMuta; UPF3B; -. DR DMDM; 60390643; -. DR EPD; Q9BZI7; -. DR jPOST; Q9BZI7; -. DR MassIVE; Q9BZI7; -. DR MaxQB; Q9BZI7; -. DR PaxDb; 9606-ENSP00000276201; -. DR PeptideAtlas; Q9BZI7; -. DR ProteomicsDB; 79849; -. [Q9BZI7-1] DR ProteomicsDB; 79850; -. [Q9BZI7-2] DR Pumba; Q9BZI7; -. DR Antibodypedia; 464; 121 antibodies from 24 providers. DR DNASU; 65109; -. DR Ensembl; ENST00000276201.7; ENSP00000276201.3; ENSG00000125351.14. [Q9BZI7-1] DR Ensembl; ENST00000345865.6; ENSP00000245418.2; ENSG00000125351.14. [Q9BZI7-2] DR GeneID; 65109; -. DR KEGG; hsa:65109; -. DR MANE-Select; ENST00000276201.7; ENSP00000276201.3; NM_080632.3; NP_542199.1. DR UCSC; uc004erz.3; human. [Q9BZI7-1] DR AGR; HGNC:20439; -. DR CTD; 65109; -. DR DisGeNET; 65109; -. DR GeneCards; UPF3B; -. DR HGNC; HGNC:20439; UPF3B. DR HPA; ENSG00000125351; Low tissue specificity. DR MalaCards; UPF3B; -. DR MIM; 300298; gene. DR MIM; 300676; phenotype. DR neXtProt; NX_Q9BZI7; -. DR OpenTargets; ENSG00000125351; -. DR Orphanet; 776; Lujan-Fryns syndrome. DR Orphanet; 323; NON RARE IN EUROPE: FG syndrome phenotypic spectrum. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA128394708; -. DR VEuPathDB; HostDB:ENSG00000125351; -. DR eggNOG; KOG1295; Eukaryota. DR GeneTree; ENSGT00390000017146; -. DR HOGENOM; CLU_041202_1_0_1; -. DR InParanoid; Q9BZI7; -. DR OMA; DWFQYKP; -. DR OrthoDB; 3037106at2759; -. DR PhylomeDB; Q9BZI7; -. DR TreeFam; TF316034; -. DR PathwayCommons; Q9BZI7; -. DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72187; mRNA 3'-end processing. DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC). DR SignaLink; Q9BZI7; -. DR SIGNOR; Q9BZI7; -. DR BioGRID-ORCS; 65109; 29 hits in 798 CRISPR screens. DR EvolutionaryTrace; Q9BZI7; -. DR GeneWiki; UPF3B; -. DR GenomeRNAi; 65109; -. DR Pharos; Q9BZI7; Tbio. DR PRO; PR:Q9BZI7; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9BZI7; Protein. DR Bgee; ENSG00000125351; Expressed in sural nerve and 188 other cell types or tissues. DR ExpressionAtlas; Q9BZI7; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0035145; C:exon-exon junction complex; IDA:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW. DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:UniProtKB. DR GO; GO:1905746; P:positive regulation of mRNA cis splicing, via spliceosome; IEA:Ensembl. DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl. DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB. DR CDD; cd12728; RRM_like_Smg4_UPF3B; 1. DR Gene3D; 3.30.70.330; -; 1. DR IDEAL; IID00251; -. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR039722; Upf3. DR InterPro; IPR005120; UPF3_dom. DR InterPro; IPR034979; UPF3B_RRM-like. DR PANTHER; PTHR13112:SF1; REGULATOR OF NONSENSE TRANSCRIPTS 3B; 1. DR PANTHER; PTHR13112; UPF3 REGULATOR OF NONSENSE TRANSCRIPTS-LIKE PROTEIN; 1. DR Pfam; PF03467; Smg4_UPF3; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR Genevisible; Q9BZI7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; KW Intellectual disability; Methylation; mRNA transport; KW Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; Transport. FT CHAIN 1..483 FT /note="Regulator of nonsense transcripts 3B" FT /id="PRO_0000215297" FT REGION 1..51 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 30..255 FT /note="Necessary for interaction with UPF2" FT REGION 52..57 FT /note="Binds to UPF2" FT REGION 206..483 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 424..483 FT /note="Sufficient for association with EJC core" FT /evidence="ECO:0000269|PubMed:20479275" FT REGION 430..447 FT /note="Necessary for interaction with RBM8A and for FT activating NMD" FT COMPBIAS 34..51 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 206..271 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 284..312 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..436 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 453..483 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 169 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 198 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 310 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 447 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 270..282 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11163187, FT ECO:0000303|PubMed:15489334" FT /id="VSP_012963" FT VARIANT 160 FT /note="Y -> D (in MRXS14; dbSNP:rs122468182)" FT /evidence="ECO:0000269|PubMed:17704778" FT /id="VAR_037666" FT MUTAGEN 52 FT /note="K->E: Abolishes interaction with UPF2." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 53..58 FT /note="VVIRRL->AVARRA: Abolishes interaction with UPF2." FT /evidence="ECO:0000269|PubMed:11113196" FT MUTAGEN 56 FT /note="R->E: Does not abolish interaction with UPF2." FT /evidence="ECO:0000269|PubMed:15004547" FT MUTAGEN 117..119 FT /note="YVF->DVD: Abolishes interaction with UPF2." FT /evidence="ECO:0000269|PubMed:11113196" FT MUTAGEN 430 FT /note="R->A: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880" FT MUTAGEN 432 FT /note="R->A: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880, FT ECO:0000269|PubMed:16601204" FT MUTAGEN 434..447 FT /note="Missing: Abolishes NMD." FT /evidence="ECO:0000269|PubMed:12718880" FT MUTAGEN 434 FT /note="K->A: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880" FT MUTAGEN 435 FT /note="D->A: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880" FT MUTAGEN 436 FT /note="R->A: Impairs association with EJC." FT /evidence="ECO:0000269|PubMed:12718880, FT ECO:0000269|PubMed:20479275" FT MUTAGEN 436 FT /note="R->A: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880, FT ECO:0000269|PubMed:20479275" FT MUTAGEN 441 FT /note="L->F: Reduces NMD." FT /evidence="ECO:0000269|PubMed:12718880" FT MUTAGEN 442 FT /note="Y->A: Impairs association with EJC." FT /evidence="ECO:0000269|PubMed:20479275" FT MUTAGEN 447 FT /note="R->E: Abolishes NMD; when associated with E-449 and FT E-451." FT /evidence="ECO:0000269|PubMed:20479275" FT MUTAGEN 449 FT /note="R->E: Abolishes NMD; when associated with E-447 and FT E-451." FT /evidence="ECO:0000269|PubMed:20479275" FT MUTAGEN 451 FT /note="R->E: Abolishes NMD; when associated with E-447 and FT E-449." FT /evidence="ECO:0000269|PubMed:20479275" FT CONFLICT 358 FT /note="R -> H (in Ref. 4; AAI21018)" FT /evidence="ECO:0000305" FT STRAND 52..58 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 77..85 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 95..104 FT /evidence="ECO:0007829|PDB:1UW4" FT HELIX 105..114 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 118..120 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:1UW4" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:1UW4" FT TURN 149..152 FT /evidence="ECO:0007829|PDB:7NWU" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:7NWU" FT HELIX 158..166 FT /evidence="ECO:0007829|PDB:7NWU" FT TURN 433..435 FT /evidence="ECO:0007829|PDB:2XB2" SQ SEQUENCE 483 AA; 57762 MW; F5A8A395783D1A69 CRC64; MKEEKEHRPK EKRVTLLTPA GATGSGGGTS GDSSKGEDKQ DRNKEKKEAL SKVVIRRLPP TLTKEQLQEH LQPMPEHDYF EFFSNDTSLY PHMYARAYIN FKNQEDIILF RDRFDGYVFL DNKGQEYPAI VEFAPFQKAA KKKTKKRDTK VGTIDDDPEY RKFLESYATD NEKMTSTPET LLEEIEAKNR ELIAKKTTPL LSFLKNKQRM REEKREERRR REIERKRQRE EERRKWKEEE KRKRKDIEKL KKIDRIPERD KLKDEPKIKV HRFLLQAVNQ KNLLKKPEKG DEKELDKREK AKKLDKENLS DERASGQSCT LPKRSDSELK DEKPKRPEDE SGRDYRERER EYERDQERIL RERERLKRQE EERRRQKERY EKEKTFKRKE EEMKKEKDTL RDKGKKAEST ESIGSSEKTE KKEEVVKRDR IRNKDRPAMQ LYQPGARSRN RLCPPDDSTK SGDSAAERKQ ESGISHRKEG GEE //