true2001-11-162024-03-27188MBNL1_HUMANBorsani G.Barbieri A.1997-06EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro.Ishikawa K.Nagase T.Nakajima D.Seki N.Ohira M.Miyajima N.Tanaka A.Kotani H.Nomura N.Ohara O.doi:10.1093/dnares/4.5.3071997DNA Res.4307-313NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)BrainRecruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy.Miller J.W.Urbinati C.R.Teng-Umnuay P.Stenberg M.G.Byrne B.J.Thornton C.A.Swanson M.S.doi:10.1093/emboj/19.17.44392000EMBO J.194439-4448NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4)FUNCTIONALTERNATIVE SPLICINGSUBCELLULAR LOCATIONRNA-BINDINGTISSUE SPECIFICITYROLE IN MYOTONIC DYSTROPHYIDENTIFICATION BY MASS SPECTROMETRYMuscleblind localizes to nuclear foci of aberrant RNA in myotonic dystrophy types 1 and 2.Mankodi A.Urbinati C.R.Yuan Q.P.Moxley R.T.Sansone V.Krym M.Henderson D.Schalling M.Swanson M.S.Thornton C.A.doi:10.1093/hmg/10.19.21652001Hum. Mol. Genet.102165-2170NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5)SUBCELLULAR LOCATIONStudy of the role of the MBNL gene in the origin myotonic dystrophies in humans.Pascual M.Terol J.Perez-Alonso M.2001-01EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5)BloodDirect evidence that EXP/muscleblind interacts with CCUG tetranucleotide repeats.Kino Y.Ishiura S.2002-04EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7)MuscleThe DNA sequence, annotation and analysis of human chromosome 3.Muzny D.M.Scherer S.E.Kaul R.Wang J.Yu J.Sudbrak R.Buhay C.J.Chen R.Cree A.Ding Y.Dugan-Rocha S.Gill R.Gunaratne P.Harris R.A.Hawes A.C.Hernandez J.Hodgson A.V.Hume J.Jackson A.Khan Z.M.Kovar-Smith C.Lewis L.R.Lozado R.J.Metzker M.L.Milosavljevic A.Miner G.R.Morgan M.B.Nazareth L.V.Scott G.Sodergren E.Song X.-Z.Steffen D.Wei S.Wheeler D.A.Wright M.W.Worley K.C.Yuan Y.Zhang Z.Adams C.Q.Ansari-Lari M.A.Ayele M.Brown M.J.Chen G.Chen Z.Clendenning J.Clerc-Blankenburg K.P.Chen R.'Chen Z.'Davis C.Delgado O.Dinh H.H.Dong W.Draper H.Ernst S.Fu G.Gonzalez-Garay M.L.Garcia D.K.Gillett W.Gu J.Hao B.Haugen E.Havlak P.He X.Hennig S.Hu S.Huang W.Jackson L.R.Jacob L.S.Kelly S.H.Kube M.Levy R.Li Z.Liu B.Liu J.Liu W.Lu J.Maheshwari M.Nguyen B.-V.Okwuonu G.O.Palmeiri A.Pasternak S.Perez L.M.Phelps K.A.Plopper F.J.Qiang B.Raymond C.Rodriguez R.Saenphimmachak C.Santibanez J.Shen H.Shen Y.Subramanian S.Tabor P.E.Verduzco D.Waldron L.Wang J.'Wang J.''Wang Q.Williams G.A.Wong G.K.-S.Yao Z.Zhang J.Zhang X.Zhao G.Zhou J.Zhou Y.Nelson D.Lehrach H.Reinhardt R.Naylor S.L.Yang H.Olson M.Weinstock G.Gibbs R.A.doi:10.1038/nature047282006Nature4401194-1198NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]Mural R.J.Istrail S.Sutton G.Florea L.Halpern A.L.Mobarry C.M.Lippert R.Walenz B.Shatkay H.Dew I.Miller J.R.Flanigan M.J.Edwards N.J.Bolanos R.Fasulo D.Halldorsson B.V.Hannenhalli S.Turner R.Yooseph S.Lu F.Nusskern D.R.Shue B.C.Zheng X.H.Zhong F.Delcher A.L.Huson D.H.Kravitz S.A.Mouchard L.Reinert K.Remington K.A.Clark A.G.Waterman M.S.Eichler E.E.Adams M.D.Hunkapiller M.W.Myers E.W.Venter J.C.2005-09EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5)TestisThree proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci of expanded-repeat transcripts in DM1 and DM2 cells.Fardaei M.Rogers M.T.Thorpe H.M.Larkin K.Hamshere M.G.Harper P.S.Brook J.D.doi:10.1093/hmg/11.7.8052002Hum. Mol. Genet.11805-814SUBCELLULAR LOCATIONTISSUE SPECIFICITYPOSSIBLE INVOLVEMENT IN DM1Muscleblind proteins regulate alternative splicing.Ho T.H.Charlet-B N.Poulos M.G.Singh G.Swanson M.S.Cooper T.A.doi:10.1038/sj.emboj.76003002004EMBO J.233103-3112FUNCTIONRNA-BINDINGInteraction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing.Paul S.Dansithong W.Kim D.Rossi J.Webster N.J.Comai L.Reddy S.doi:10.1038/sj.emboj.76012962006EMBO J.254271-4283FUNCTIONINTERACTION WITH HNRNPH1RNA-BINDINGMBNL1 associates with YB-1 in cytoplasmic stress granules.Onishi H.Kino Y.Morita T.Futai E.Sasagawa N.Ishiura S.doi:10.1002/jnr.216552008J. Neurosci. Res.861994-2002FUNCTIONINTERACTION WITH DDX1 AND YBX1SUBCELLULAR LOCATIONIDENTIFICATION BY MASS SPECTROMETRYThe protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing.Warf M.B.Diegel J.V.von Hippel P.H.Berglund J.A.doi:10.1073/pnas.09003421062009Proc. Natl. Acad. Sci. U.S.A.1069203-9208FUNCTIONRNA-BINDINGInitial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]ErythroleukemiaRNA toxicity and missplicing in the common eye disease fuchs endothelial corneal dystrophy.Du J.Aleff R.A.Soragni E.Kalari K.Nie J.Tang X.Davila J.Kocher J.P.Patel S.V.Gottesfeld J.M.Baratz K.H.Wieben E.D.doi:10.1074/jbc.m114.6216072015J. Biol. Chem.2905979-5990INVOLVEMENT IN FECD3Cell-type specific regulator RBPMS switches alternative splicing via higher-order oligomerization and heterotypic interactions with other splicing regulators.Yang Y.Lee G.C.Nakagaki-Silva E.Huang Y.Peacey M.Partridge R.Gooding C.Smith C.W.J.doi:10.1093/nar/gkad6522023Nucleic Acids Res.FUNCTIONINTERACTION WITH RBPMSStructural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1.Teplova M.Patel D.J.doi:10.1038/nsmb.15192008Nat. Struct. Mol. Biol.151343-1351X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 9-90 IN COMPLEX WITH ZINC IONS AND 178-246 IN COMPLEX WITH ZINC IONS AND RNARNA-BINDINGIdentification of variants in MBNL1 in patients with a myotonic dystrophy-like phenotype.Larsen M.Kress W.Schoser B.Hehr U.Mueller C.R.Rost S.doi:10.1038/ejhg.2016.412016Eur. J. Hum. Genet.241467-1472VARIANTS DM1 MET-32; 171-ALA--ALA-173 DEL AND SER-338Different initiation.2.70A=9-901.50A/B/C/D=178-2461.70A/B/C/D=178-246A=1-92A=173-255A=1-92294341 site, 1 glycan1 site, 1 O-linked glycan (1 site)385 antibodies from 34 providershumanMBNL1Low tissue specificityphenotypegenephenotypeEukaryota91 hits in 1172 CRISPR screenshumanTbioProteinExpressed in calcaneal tendon and 216 other cell types or tissuesbaseline and differentialZnf_CCCHMUSCLEBLIND-LIKE PROTEINMUSCLEBLIND-LIKE PROTEIN 1zf-CCCHzf-CCCH_2ZnF_C3H1ZF_C3H1HSMuscleblind-like protein 1Triplet-expansion RNA-binding proteinMBNL1EXPKIAA0428MBNLMediates pre-mRNA alternative splicing regulation. Acts either as activator or repressor of splicing on specific pre-mRNA targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle. Antagonizes the alternative splicing activity pattern of CELF proteins. Regulates the TNNT2 exon 5 skipping through competition with U2AF2. Inhibits the formation of the spliceosome A complex on intron 4 of TNNT2 pre-mRNA. Binds to the stem-loop structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA. Binds to expanded CUG repeat RNA, which folds into a hairpin structure containing GC base pairs and bulged, unpaired U residues. Together with RNA binding proteins RBPMS and RBFOX2, activates vascular smooth muscle cells alternative splicing events (PubMed:37548402). Regulates NCOR2 alternative splicing (By similarity).Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the interaction in RNA-independent. Interacts with RBPMS; the interaction allows cooperative assembly of RNA-bound stable cell-specific alternative splicing regulatory complexes (PubMed:37548402).Localized with DDX1, TIAL1 and YBX1 in stress granules upon stress (PubMed:18335541). Localized in the cytoplasm of multinucleated myotubes (PubMed:18335541). Colocalizes with nuclear foci of retained expanded-repeat transcripts in myotubes from patients affected by myotonic dystrophy (PubMed:10970838, PubMed:11590133, PubMed:11929853).Highly expressed in cardiac, skeletal muscle and during myoblast differentiation. Weakly expressed in other tissues (at protein level). Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.The protein represented in this entry may be involved in disease pathogenesis. In muscle cells from patients, MBNL1 is sequestered by DMPK RNAs containing pathogenic CUG triplet repeat expansions. MBNL1 binding is proportional to repeat length consistent with the direct correlation between the length of repeat expansion and disease severity.The protein represented in this entry is involved in disease pathogenesis. In corneal endothelial cells from patients, MBNL1 is sequestered by TCF4 RNAs containing pathogenic CUG triplet repeat expansions. This results in missplicing of essential MBNL1-regulated mRNAs.Belongs to the muscleblind family.Extended N-terminus.Muscleblind-like protein 1418171388C3H1-type 11341C3H1-type 24773C3H1-type 3179207C3H1-type 4215241Phosphothreonine6In isoform 3 and isoform 4.116183In isoform 7.FPWCTVLRQPLCPQQQHLPQVFPSLQQPQPTSPILDASTLLGATSCPAAAGKM270370In isoform 2, isoform 3, isoform 4, isoform 5 and isoform 6.287In isoform 4, isoform 5 and isoform 6.PGSILCMTPATSV338In isoform 6.DTHNICRTSD339In DM1; uncertain significance.M32In DM1; uncertain significance.171173In DM1; uncertain significance.S2512141518222431333537495154576769828991176178181184186189197199201203208210213216217220222225235237244252254AA317false4false2false6DAB1HNRNPH1ATXN12001-11-16241817981bb519bccbf95122bd9efaf3611dd11EXP42MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMTQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM2EXP40MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM3EXP35MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM4EXP36MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM5EXP41MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVVPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM6EXP41SMAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQQALANMQLQQHTAFLPPGSILCMTPATSVDTHNICRTSD7MAVSVTPIRDTKWLTLEVCREFQRGTCSRPDTECKFAHPSKSCQVENGRVIACFDSLKGRCSRENCKYLHPPPHLKTQLEINGRNNLIQQKNMAMLAQQMQLANAMMPGAPLQPVPMFSVAPSLATNASAAAFNPYLGPVSPSLVPAEILPTAPMLVTGNPGVPVPAAAAAAAQKLMRTDRLEVCREYQRGNCNRGENDCRFAHPADSTMIDTNDNTVTVCMDYIKGRCSREKCKYFHPPAHLQAKIKAAQYQVNQAAAAQAAATAAAMFPWCTVLRQPLCPQQQHLPQVFPSLQQPQPTSPILDASTLLGATSCPAAAGKMIPIISAEHLTSHKYVTQMtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue