MBNL1
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Official Full Name
muscleblind-like splicing regulator 1
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Overview
Mediates 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. -
Synonyms
MBNL1; muscleblind-like splicing regulator 1; EXP; MBNL; EXP35; EXP40; EXP42; muscleblind-like protein 1; triplet-expansion RNA-binding protein;
- Recombinant Proteins
- Cell & Tissue Lysates
- Chicken
- Human
- Mouse
- Zebrafish
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mamanlian cells
- Mammalian Cell
- Wheat Germ
- C
- Myc
- DDK
- Flag
- His
- His|SUMO
- Myc|DDK
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- MBNL1 Related Articles
MBNL1 involved in several pathways and played different roles in them. We selected most pathways MBNL1 participated on our site, such as Adipogenesis, which may be useful for your reference. Also, other proteins which involved in the same pathway with MBNL1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Adipogenesis | NR1H3;MBNL1;E2F1;PLIN2;EBF1;KLF7;GDF10;KLF7A;SMAD3B |
MBNL1 has several biochemical functions, for example, RNA binding, double-stranded RNA binding, metal ion binding. Some of the functions are cooperated with other proteins, some of the functions could acted by MBNL1 itself. We selected most functions MBNL1 had, and list some proteins which have the same functions with MBNL1. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| RNA binding | ATXN1A;RBMS1;DKC1;DNAJC17;RPL8;HSP90B1;EIF4E3;LSM5;RBM6 |
| double-stranded RNA binding | PRKRIP1;DROSHA;ILF3;HSPD1;STRBP;AGO3;OAS2;RFTN1;DGCR8 |
| metal ion binding | G2E3;GALNTL1;FTR43;SMYD1A;ZNF12;ACACA;MYLIPB;ZBTB7C;BLF |
| poly(A) RNA binding | ZYX;TRIM56;RBM12;HIST1H1B;STAU1;PPP1R2P9;FUBP3;HNRNPU;ZCCHC11 |
| protein binding | KLC3;CWC15;PRDM7;PLXNB2;LRP5;FSTL3;SSH1;DDX58;RAB3A |
MBNL1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with MBNL1 here. Most of them are supplied by our site. Hope this information will be useful for your research of MBNL1.
DAB1; HNRNPH1; CELF1; IDH3A; ZNHIT3; glmU; ugpC; mhpC2; proP24; pstC; ABI3BP; q81l89_bacan; q8clr7_yerpe; uvrC; maeA; fimD2; VCAM1
- Q&As
- Reviews
Q&As (7)
Ask a questionIt contributes to tissue-specific splicing patterns, essential for proper development and function of various tissues.
MBNL1 regulates alternative splicing, polyadenylation, and localization of mRNAs, impacting gene expression.
MBNL1 plays a key role in muscle development and differentiation, influencing muscle-specific gene expression.
In myotonic dystrophy, MBNL1 becomes sequestered by toxic RNA repeats, leading to mis-splicing and muscular dysfunction.
Therapeutic modulation of MBNL1 is being explored, focusing on releasing MBNL1 from sequestration and correcting mis-splicing in conditions like myotonic dystrophy.
Sequestration of MBNL1 results in altered splicing patterns of numerous genes, contributing to cellular dysfunction.
There is limited information on post-translational modifications regulating MBNL1, necessitating further research.
Customer Reviews (3)
Write a reviewExcellent product, fast delivery.
Reliable for my research.
Worked perfectly, highly recommend.
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