MBNL1_HUMAN
ID MBNL1_HUMAN Reviewed; 388 AA.
AC Q9NR56; E9PBW7; O43311; O43797; Q86UV8; Q86UV9; Q96P92; Q96RE3;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Muscleblind-like protein 1;
DE AltName: Full=Triplet-expansion RNA-binding protein;
GN Name=MBNL1; Synonyms=EXP, KIAA0428, MBNL;
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 1).
RA Borsani G., Barbieri A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, ALTERNATIVE
RP SPLICING, SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, ROLE IN
RP MYOTONIC DYSTROPHY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10970838; DOI=10.1093/emboj/19.17.4439;
RA Miller J.W., Urbinati C.R., Teng-Umnuay P., Stenberg M.G., Byrne B.J.,
RA Thornton C.A., Swanson M.S.;
RT "Recruitment of human muscleblind proteins to (CUG)(n) expansions
RT associated with myotonic dystrophy.";
RL EMBO J. 19:4439-4448(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND SUBCELLULAR LOCATION.
RX PubMed=11590133; DOI=10.1093/hmg/10.19.2165;
RA Mankodi A., Urbinati C.R., Yuan Q.P., Moxley R.T., Sansone V., Krym M.,
RA Henderson D., Schalling M., Swanson M.S., Thornton C.A.;
RT "Muscleblind localizes to nuclear foci of aberrant RNA in myotonic
RT dystrophy types 1 and 2.";
RL Hum. Mol. Genet. 10:2165-2170(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC TISSUE=Blood;
RA Pascual M., Terol J., Perez-Alonso M.;
RT "Study of the role of the MBNL gene in the origin myotonic dystrophies in
RT humans.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7).
RC TISSUE=Muscle;
RA Kino Y., Ishiura S.;
RT "Direct evidence that EXP/muscleblind interacts with CCUG tetranucleotide
RT repeats.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Testis;
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 [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND POSSIBLE INVOLVEMENT IN DM1.
RX PubMed=11929853; DOI=10.1093/hmg/11.7.805;
RA Fardaei M., Rogers M.T., Thorpe H.M., Larkin K., Hamshere M.G.,
RA Harper P.S., Brook J.D.;
RT "Three proteins, MBNL, MBLL and MBXL, co-localize in vivo with nuclear foci
RT of expanded-repeat transcripts in DM1 and DM2 cells.";
RL Hum. Mol. Genet. 11:805-814(2002).
RN [11]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15257297; DOI=10.1038/sj.emboj.7600300;
RA Ho T.H., Charlet-B N., Poulos M.G., Singh G., Swanson M.S., Cooper T.A.;
RT "Muscleblind proteins regulate alternative splicing.";
RL EMBO J. 23:3103-3112(2004).
RN [12]
RP FUNCTION, INTERACTION WITH HNRNPH1, AND RNA-BINDING.
RX PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
RA Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.;
RT "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated
RT aberrant IR splicing.";
RL EMBO J. 25:4271-4283(2006).
RN [13]
RP FUNCTION, INTERACTION WITH DDX1 AND YBX1, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18335541; DOI=10.1002/jnr.21655;
RA Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.;
RT "MBNL1 associates with YB-1 in cytoplasmic stress granules.";
RL J. Neurosci. Res. 86:1994-2002(2008).
RN [14]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=19470458; DOI=10.1073/pnas.0900342106;
RA Warf M.B., Diegel J.V., von Hippel P.H., Berglund J.A.;
RT "The protein factors MBNL1 and U2AF65 bind alternative RNA structures to
RT regulate splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9203-9208(2009).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [17]
RP INVOLVEMENT IN FECD3.
RX PubMed=25593321; DOI=10.1074/jbc.m114.621607;
RA Du J., Aleff R.A., Soragni E., Kalari K., Nie J., Tang X., Davila J.,
RA Kocher J.P., Patel S.V., Gottesfeld J.M., Baratz K.H., Wieben E.D.;
RT "RNA toxicity and missplicing in the common eye disease fuchs endothelial
RT corneal dystrophy.";
RL J. Biol. Chem. 290:5979-5990(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 9-90 IN COMPLEX WITH ZINC IONS
RP AND 178-246 IN COMPLEX WITH ZINC IONS AND RNA, AND RNA-BINDING.
RX PubMed=19043415; DOI=10.1038/nsmb.1519;
RA Teplova M., Patel D.J.;
RT "Structural insights into RNA recognition by the alternative-splicing
RT regulator muscleblind-like MBNL1.";
RL Nat. Struct. Mol. Biol. 15:1343-1351(2008).
RN [19]
RP VARIANTS DM1 MET-32; 171-ALA--ALA-173 DEL AND SER-338.
RX PubMed=27222292; DOI=10.1038/ejhg.2016.41;
RA Larsen M., Kress W., Schoser B., Hehr U., Mueller C.R., Rost S.;
RT "Identification of variants in MBNL1 in patients with a myotonic dystrophy-
RT like phenotype.";
RL Eur. J. Hum. Genet. 24:1467-1472(2016).
CC -!- FUNCTION: Mediates pre-mRNA alternative splicing regulation. Acts
CC either as activator or repressor of splicing on specific pre-mRNA
CC targets. Inhibits cardiac troponin-T (TNNT2) pre-mRNA exon inclusion
CC but induces insulin receptor (IR) pre-mRNA exon inclusion in muscle.
CC Antagonizes the alternative splicing activity pattern of CELF proteins.
CC Regulates the TNNT2 exon 5 skipping through competition with U2AF2.
CC Inhibits the formation of the spliceosome A complex on intron 4 of
CC TNNT2 pre-mRNA. Binds to the stem-loop structure within the
CC polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly.
CC Binds to the 5'-YGCU(U/G)Y-3'consensus sequence. Binds to the IR RNA.
CC Binds to expanded CUG repeat RNA, which folds into a hairpin structure
CC containing GC base pairs and bulged, unpaired U residues.
CC {ECO:0000269|PubMed:10970838, ECO:0000269|PubMed:15257297,
CC ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:18335541,
CC ECO:0000269|PubMed:19470458}.
CC -!- SUBUNIT: Interacts with DDX1 and YBX1. Interacts with HNRNPH1; the
CC interaction in RNA-independent. {ECO:0000269|PubMed:16946708,
CC ECO:0000269|PubMed:18335541, ECO:0000269|PubMed:19043415}.
CC -!- INTERACTION:
CC Q9NR56; O75553: DAB1; NbExp=4; IntAct=EBI-2805004, EBI-7875264;
CC Q9NR56; P31943: HNRNPH1; NbExp=2; IntAct=EBI-2805004, EBI-351590;
CC Q9NR56-5; P54253: ATXN1; NbExp=6; IntAct=EBI-25978262, EBI-930964;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10970838,
CC ECO:0000269|PubMed:11590133, ECO:0000269|PubMed:11929853}. Cytoplasm
CC {ECO:0000269|PubMed:18335541}. Cytoplasmic granule
CC {ECO:0000269|PubMed:18335541}. Note=Localized with DDX1, TIAL1 and YBX1
CC in stress granules upon stress (PubMed:18335541). Localized in the
CC cytoplasm of multinucleated myotubes (PubMed:18335541). Colocalizes
CC with nuclear foci of retained expanded-repeat transcripts in myotubes
CC from patients affected by myotonic dystrophy (PubMed:10970838,
CC PubMed:11590133, PubMed:11929853).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=EXP42;
CC IsoId=Q9NR56-1; Sequence=Displayed;
CC Name=2; Synonyms=EXP40;
CC IsoId=Q9NR56-2; Sequence=VSP_006430;
CC Name=3; Synonyms=EXP35;
CC IsoId=Q9NR56-3; Sequence=VSP_006429, VSP_006430;
CC Name=4; Synonyms=EXP36;
CC IsoId=Q9NR56-4; Sequence=VSP_006429, VSP_006430, VSP_043799;
CC Name=5; Synonyms=EXP41;
CC IsoId=Q9NR56-5; Sequence=VSP_006430, VSP_043799;
CC Name=6; Synonyms=EXP41S;
CC IsoId=Q9NR56-6; Sequence=VSP_006430, VSP_043799, VSP_043800;
CC Name=7;
CC IsoId=Q9NR56-7; Sequence=VSP_044903;
CC -!- TISSUE SPECIFICITY: Highly expressed in cardiac, skeletal muscle and
CC during myoblast differentiation. Weakly expressed in other tissues (at
CC protein level). Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. {ECO:0000269|PubMed:10970838,
CC ECO:0000269|PubMed:11929853}.
CC -!- DISEASE: Dystrophia myotonica 1 (DM1) [MIM:160900]: A muscular disorder
CC characterized by myotonia, muscle wasting in the distal extremities,
CC cataract, hypogonadism, defective endocrine functions, male baldness
CC and cardiac arrhythmias. {ECO:0000269|PubMed:11929853,
CC ECO:0000269|PubMed:27222292}. Note=The protein represented in this
CC entry may be involved in disease pathogenesis. In muscle cells from
CC patients, MBNL1 is sequestered by DMPK RNAs containing pathogenic CUG
CC triplet repeat expansions. MBNL1 binding is proportional to repeat
CC length consistent with the direct correlation between the length of
CC repeat expansion and disease severity.
CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 3 (FECD3) [MIM:613267]:
CC A late-onset form of Fuchs endothelial corneal dystrophy, a disease
CC caused by loss of endothelium of the central cornea. It is
CC characterized by focal wart-like guttata that arise from Descemet
CC membrane and develop in the central cornea, epithelial blisters,
CC reduced vision and pain. Descemet membrane is thickened by abnormal
CC collagenous deposition. {ECO:0000269|PubMed:25593321}. Note=The protein
CC represented in this entry is involved in disease pathogenesis. In
CC corneal endothelial cells from patients, MBNL1 is sequestered by TCF4
CC RNAs containing pathogenic CUG triplet repeat expansions. This results
CC in missplicing of essential MBNL1-regulated mRNAs.
CC {ECO:0000269|PubMed:25593321}.
CC -!- SIMILARITY: Belongs to the muscleblind family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA24858.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y13829; CAA74155.1; -; mRNA.
DR EMBL; AB007888; BAA24858.2; ALT_INIT; mRNA.
DR EMBL; AF255334; AAF76138.1; -; mRNA.
DR EMBL; AF395876; AAK82889.1; -; mRNA.
DR EMBL; AF401998; AAK94915.1; -; mRNA.
DR EMBL; AJ308400; CAC83727.1; -; mRNA.
DR EMBL; AF497718; AAP30726.1; -; mRNA.
DR EMBL; AF497719; AAP30727.1; -; mRNA.
DR EMBL; AC026347; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78775.1; -; Genomic_DNA.
DR EMBL; BC043493; AAH43493.1; -; mRNA.
DR CCDS; CCDS3163.1; -. [Q9NR56-5]
DR CCDS; CCDS3164.1; -. [Q9NR56-2]
DR CCDS; CCDS3165.1; -. [Q9NR56-1]
DR CCDS; CCDS3166.1; -. [Q9NR56-4]
DR CCDS; CCDS3167.1; -. [Q9NR56-7]
DR CCDS; CCDS3168.1; -. [Q9NR56-6]
DR CCDS; CCDS54656.1; -. [Q9NR56-3]
DR RefSeq; NP_001300986.1; NM_001314057.1.
DR RefSeq; NP_066368.2; NM_021038.4. [Q9NR56-5]
DR RefSeq; NP_997175.1; NM_207292.2. [Q9NR56-2]
DR RefSeq; NP_997176.1; NM_207293.1. [Q9NR56-1]
DR RefSeq; NP_997177.1; NM_207294.1. [Q9NR56-3]
DR RefSeq; NP_997178.1; NM_207295.1. [Q9NR56-4]
DR RefSeq; NP_997179.1; NM_207296.1. [Q9NR56-7]
DR RefSeq; NP_997180.1; NM_207297.1. [Q9NR56-6]
DR RefSeq; XP_005247523.1; XM_005247466.4.
DR RefSeq; XP_005247528.1; XM_005247471.4.
DR RefSeq; XP_011511149.1; XM_011512847.2.
DR RefSeq; XP_011511151.1; XM_011512849.2.
DR RefSeq; XP_016861914.1; XM_017006425.1.
DR RefSeq; XP_016861915.1; XM_017006426.1.
DR RefSeq; XP_016861916.1; XM_017006427.1.
DR RefSeq; XP_016861917.1; XM_017006428.1.
DR RefSeq; XP_016861918.1; XM_017006429.1.
DR RefSeq; XP_016861919.1; XM_017006430.1.
DR RefSeq; XP_016861920.1; XM_017006431.1.
DR RefSeq; XP_016861925.1; XM_017006436.1.
DR PDB; 3D2N; X-ray; 2.70 A; A=9-90.
DR PDB; 3D2Q; X-ray; 1.50 A; A/B/C/D=178-246.
DR PDB; 3D2S; X-ray; 1.70 A; A/B/C/D=178-246.
DR PDB; 5U6H; NMR; -; A=1-92.
DR PDB; 5U6L; NMR; -; A=173-255.
DR PDB; 5U9B; NMR; -; A=1-92.
DR PDBsum; 3D2N; -.
DR PDBsum; 3D2Q; -.
DR PDBsum; 3D2S; -.
DR PDBsum; 5U6H; -.
DR PDBsum; 5U6L; -.
DR PDBsum; 5U9B; -.
DR AlphaFoldDB; Q9NR56; -.
DR SMR; Q9NR56; -.
DR BioGRID; 110324; 274.
DR IntAct; Q9NR56; 35.
DR MINT; Q9NR56; -.
DR STRING; 9606.ENSP00000282486; -.
DR ChEMBL; CHEMBL1293317; -.
DR GlyGen; Q9NR56; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NR56; -.
DR PhosphoSitePlus; Q9NR56; -.
DR SwissPalm; Q9NR56; -.
DR BioMuta; MBNL1; -.
DR DMDM; 17369313; -.
DR EPD; Q9NR56; -.
DR jPOST; Q9NR56; -.
DR MassIVE; Q9NR56; -.
DR MaxQB; Q9NR56; -.
DR PaxDb; Q9NR56; -.
DR PeptideAtlas; Q9NR56; -.
DR PRIDE; Q9NR56; -.
DR ProteomicsDB; 19310; -.
DR ProteomicsDB; 82279; -. [Q9NR56-1]
DR ProteomicsDB; 82280; -. [Q9NR56-2]
DR ProteomicsDB; 82281; -. [Q9NR56-3]
DR ProteomicsDB; 82282; -. [Q9NR56-4]
DR ProteomicsDB; 82283; -. [Q9NR56-5]
DR ProteomicsDB; 82284; -. [Q9NR56-6]
DR Antibodypedia; 4292; 355 antibodies from 34 providers.
DR DNASU; 4154; -.
DR Ensembl; ENST00000282486.10; ENSP00000282486.6; ENSG00000152601.18. [Q9NR56-1]
DR Ensembl; ENST00000324196.9; ENSP00000319374.5; ENSG00000152601.18. [Q9NR56-7]
DR Ensembl; ENST00000324210.10; ENSP00000319429.5; ENSG00000152601.18. [Q9NR56-5]
DR Ensembl; ENST00000355460.6; ENSP00000347637.2; ENSG00000152601.18. [Q9NR56-2]
DR Ensembl; ENST00000357472.7; ENSP00000350064.3; ENSG00000152601.18. [Q9NR56-6]
DR Ensembl; ENST00000463374.5; ENSP00000418108.1; ENSG00000152601.18. [Q9NR56-1]
DR Ensembl; ENST00000465907.6; ENSP00000417630.2; ENSG00000152601.18. [Q9NR56-4]
DR Ensembl; ENST00000485509.5; ENSP00000418876.1; ENSG00000152601.18. [Q9NR56-7]
DR Ensembl; ENST00000485910.5; ENSP00000418427.1; ENSG00000152601.18. [Q9NR56-3]
DR Ensembl; ENST00000492948.5; ENSP00000420103.1; ENSG00000152601.18. [Q9NR56-6]
DR Ensembl; ENST00000545754.5; ENSP00000437491.1; ENSG00000152601.18. [Q9NR56-4]
DR GeneID; 4154; -.
DR KEGG; hsa:4154; -.
DR MANE-Select; ENST00000324210.10; ENSP00000319429.5; NM_021038.5; NP_066368.2. [Q9NR56-5]
DR UCSC; uc003ezh.4; human. [Q9NR56-1]
DR CTD; 4154; -.
DR DisGeNET; 4154; -.
DR GeneCards; MBNL1; -.
DR HGNC; HGNC:6923; MBNL1.
DR HPA; ENSG00000152601; Low tissue specificity.
DR MIM; 160900; phenotype.
DR MIM; 606516; gene.
DR MIM; 613267; phenotype.
DR neXtProt; NX_Q9NR56; -.
DR OpenTargets; ENSG00000152601; -.
DR PharmGKB; PA30666; -.
DR VEuPathDB; HostDB:ENSG00000152601; -.
DR eggNOG; KOG2494; Eukaryota.
DR GeneTree; ENSGT00950000182897; -.
DR HOGENOM; CLU_053536_0_0_1; -.
DR InParanoid; Q9NR56; -.
DR OMA; KVPMVHG; -.
DR OrthoDB; 1543798at2759; -.
DR PhylomeDB; Q9NR56; -.
DR TreeFam; TF321931; -.
DR PathwayCommons; Q9NR56; -.
DR SignaLink; Q9NR56; -.
DR BioGRID-ORCS; 4154; 86 hits in 1092 CRISPR screens.
DR ChiTaRS; MBNL1; human.
DR EvolutionaryTrace; Q9NR56; -.
DR GeneWiki; MBNL1; -.
DR GenomeRNAi; 4154; -.
DR Pharos; Q9NR56; Tbio.
DR PRO; PR:Q9NR56; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NR56; protein.
DR Bgee; ENSG00000152601; Expressed in calcaneal tendon and 214 other tissues.
DR ExpressionAtlas; Q9NR56; baseline and differential.
DR Genevisible; Q9NR56; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001069; F:regulatory region RNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF00642; zf-CCCH; 1.
DR SMART; SM00356; ZnF_C3H1; 4.
DR PROSITE; PS50103; ZF_C3H1; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Corneal dystrophy; Cytoplasm;
KW Disease variant; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..388
FT /note="Muscleblind-like protein 1"
FT /id="PRO_0000089178"
FT ZN_FING 13..41
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 47..73
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 179..207
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 215..241
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT MOD_RES 6
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 116..183
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10970838"
FT /id="VSP_006429"
FT VAR_SEQ 270..370
FT /note="TQSAVKSLKRPLEATFDLGIPQAVLPPLPKRPALEKTNGATAVFNTGIFQYQ
FT QALANMQLQQHTAFLPPVPMVHGATPATVSAATTSATSVPFAATATANQ -> FPWCTV
FT LRQPLCPQQQHLPQVFPSLQQPQPTSPILDASTLLGATSCPAAAGKM (in isoform
FT 7)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_044903"
FT VAR_SEQ 270..287
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10970838,
FT ECO:0000303|PubMed:11590133, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455477, ECO:0000303|Ref.5,
FT ECO:0000303|Ref.6"
FT /id="VSP_006430"
FT VAR_SEQ 338
FT /note="P -> PGSILCMTPATSV (in isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:10970838,
FT ECO:0000303|PubMed:11590133, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_043799"
FT VAR_SEQ 339..388
FT /note="VPMVHGATPATVSAATTSATSVPFAATATANQIPIISAEHLTSHKYVTQM
FT -> DTHNICRTSD (in isoform 6)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_043800"
FT VARIANT 32
FT /note="T -> M (in DM1; unknown pathological significance;
FT dbSNP:rs185894411)"
FT /evidence="ECO:0000269|PubMed:27222292"
FT /id="VAR_076508"
FT VARIANT 171..173
FT /note="Missing (in DM1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27222292"
FT /id="VAR_076509"
FT VARIANT 338
FT /note="P -> S (in DM1; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:27222292"
FT /id="VAR_076510"
FT TURN 2..5
FT /evidence="ECO:0007829|PDB:5U6H"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3D2N"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:3D2N"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3D2N"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:3D2N"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:3D2N"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3D2N"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:3D2N"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5U6H"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:3D2N"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:5U9B"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:5U6L"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:3D2Q"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:3D2Q"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3D2Q"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3D2Q"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5U6L"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:3D2Q"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3D2Q"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:3D2Q"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3D2S"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:3D2Q"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:5U6L"
FT CONFLICT Q9NR56-7:317
FT /note="A -> AA (in Ref. 6; AAP30726)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 41817 MW; 118D256A81A86695 CRC64;
MAVSVTPIRD TKWLTLEVCR EFQRGTCSRP DTECKFAHPS KSCQVENGRV IACFDSLKGR
CSRENCKYLH PPPHLKTQLE INGRNNLIQQ KNMAMLAQQM QLANAMMPGA PLQPVPMFSV
APSLATNASA AAFNPYLGPV SPSLVPAEIL PTAPMLVTGN PGVPVPAAAA AAAQKLMRTD
RLEVCREYQR GNCNRGENDC RFAHPADSTM IDTNDNTVTV CMDYIKGRCS REKCKYFHPP
AHLQAKIKAA QYQVNQAAAA QAAATAAAMT QSAVKSLKRP LEATFDLGIP QAVLPPLPKR
PALEKTNGAT AVFNTGIFQY QQALANMQLQ QHTAFLPPVP MVHGATPATV SAATTSATSV
PFAATATANQ IPIISAEHLT SHKYVTQM
