Gene Symbol: TXNL4A
Description: thioredoxin like 4A
Alias: BMKS, DIB1, DIM1, SNRNP15, TXNL4, U5-15kD, thioredoxin-like protein 4A, DIM1 protein homolog, spliceosomal U5 snRNP-specific 15 kDa protein, thioredoxin-like 4, thioredoxin-like U5 snRNP protein U5-15kD
Species: human
Products:     TXNL4A

Top Publications

  1. Jin T, Guo F, Wang Y, Zhang Y. High-resolution crystal structure of human Dim2/TXNL4B. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013;69:223-7 pubmed publisher
    b>TXNL4A (thioredoxin-like 4A) is an essential protein conserved from yeast to humans and is a component of the pre-mRNA splicing machinery...
  2. Bitterlich M, Krügel U, Boldt Burisch K, Franken P, Kühn C. Interaction of brassinosteroid functions and sucrose transporter SlSUT2 regulate the formation of arbuscular mycorrhiza. Plant Signal Behav. 2014;9:e970426 pubmed publisher
    ..Here, we include a rice mutant defective in DIM1/DWARF1 involved in BR biosynthesis to investigate the effects on mycorrhization...
  3. Gupta K, Gupta A, Habib S. Characterization of a Plasmodium falciparum rRNA methyltransferase. Mol Biochem Parasitol. 2018;223:13-18 pubmed publisher
    The ribosomal RNA adenine dimethyltransferases (rAD) of KsgA/Dim1 family are universally conserved with eukaryotic rADs separated into distinct cytosolic Dim1 and organellar KsgA/TFB homologs...
  4. Schreib C, Bowman E, Hernandez C, Lucas A, Potts C, Maeder C. Functional and Biochemical Characterization of Dib1's Role in Pre-Messenger RNA Splicing. J Mol Biol. 2018;430:1640-1651 pubmed publisher
    ..part of spliceosome assembly and is defined by the departure of several proteins, including essential U5 component Dib1. Recent structural studies suggest that Dib1 has a role in preventing premature spliceosome activation, as it is ..
  5. Wang L, Wang W, Ma N, Tian D, Wang J, Qiu Y. Interlayer charge-transfer in impacting the second hyperpolarizabilities: radical and cation species of hexathiophenalenylium and its nitro dimers. J Mol Graph Model. 2015;55:33-40 pubmed publisher
    ..More importantly, radical dimers [4]dim3 and [5]dim1 exhibit a significant increase in the second hyperpolarizabilities as compared to cation dimers, which is due to ..
  6. Zorbas C, Nicolas E, Wacheul L, Huvelle E, Heurgué Hamard V, Lafontaine D. The human 18S rRNA base methyltransferases DIMT1L and WBSCR22-TRMT112 but not rRNA modification are required for ribosome biogenesis. Mol Biol Cell. 2015;26:2080-95 pubmed publisher
    ..ribosomal subunit of budding yeast, on the 18S rRNA, two adjacent adenosines (A1781/A1782) are N(6)-dimethylated by Dim1 near the decoding site, and one guanosine (G1575) is N(7)-methylated by Bud23-Trm112 at a ridge between the P- and ..
  7. Berry L, Gould K. Fission yeast dim1(+) encodes a functionally conserved polypeptide essential for mitosis. J Cell Biol. 1997;137:1337-54 pubmed
    ..temperature of the fission yeast mutant cdc2-D217N, we have isolated a novel temperature-sensitive mutant, dim1-35...
  8. Mizuguchi M, Obita T, Serita T, Kojima R, Nabeshima Y, Okazawa H. Mutations in the PQBP1 gene prevent its interaction with the spliceosomal protein U5-15 kD. Nat Commun. 2014;5:3822 pubmed publisher
    ..These results suggest a mechanism by which the loss of the YxxPxxVL motif could lead to the functional defects seen in this type of mental retardation. ..
  9. Reuter K, Nottrott S, Fabrizio P, Luhrmann R, Ficner R. Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. J Mol Biol. 1999;294:515-25 pubmed
    ..Our data suggest that the previously reported involvement of its Schizosaccharomyces pombe ortholog Dim1p in cell cycle regulation is a consequence of its essential role in pre-mRNA splicing. ..

More Information


  1. Pessa H, Will C, Meng X, Schneider C, Watkins N, Perälä N, et al. Minor spliceosome components are predominantly localized in the nucleus. Proc Natl Acad Sci U S A. 2008;105:8655-60 pubmed publisher
    ..Thus, our data, combined with several earlier publications, establish that, like the major spliceosome, components of the U12-dependent spliceosome are localized predominantly in the nucleus. ..
  2. Johnson M, Ghalei H, Doxtader K, Karbstein K, Stroupe M. Structural Heterogeneity in Pre-40S Ribosomes. Structure. 2017;25:329-340 pubmed publisher
    ..These models are supported by biochemical analyses using point variants and suggest that maturation of the 18S 3' end is regulated by dissociation of the AF Dim1 from the subunit interface, consistent with previous biochemical analyses.
  3. Mizuguchi M, Obita T, Kajiyama A, Kozakai Y, Nakai T, Nabeshima Y, et al. Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD. FEBS Lett. 2016;590:2221-31 pubmed publisher
    ..Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism. ..
  4. Goos J, Swagemakers S, Twigg S, van Dooren M, Hoogeboom A, Beetz C, et al. Identification of causative variants in TXNL4A in Burn-McKeown syndrome and isolated choanal atresia. Eur J Hum Genet. 2017;25:1126-1133 pubmed publisher
    ..Recently, causative compound heterozygous variants were identified in TXNL4A. We analyzed an individual with clinical features of BMKS and her parents by whole-genome sequencing and ..
  5. Hussain A, Tian M, Wen S. Exploring the Caste-Specific Multi-Layer Defense Mechanism of Formosan Subterranean Termites, Coptotermes formosanus Shiraki. Int J Mol Sci. 2017;18: pubmed publisher
    ..i>CAT, GST, PRXSL, Cu/Zn-SOD2, TXN1, TXN2, TXNL1, TXNL2, TXNL4A and TPx genes among winged imagoes upon infection with the most virulent isolate, M...
  6. Jin T, Guo F, Wang Y, Zhang Y. Identification of human dim1 as a peptidase with autocleavage activity. Chem Biol Drug Des. 2006;68:266-72 pubmed
    b>Dim1 is a highly conserved splicing factor. It is encoded by an essential gene in fission yeast and the Caenorhabditis elegans. It may also be involved in tissue-specific or pathway-specific alternative splicing...
  7. Zhang Y, Cheng H, Gould K, Golemis E, Roder H. Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis. Biochemistry. 2003;42:9609-18 pubmed
    ..Other residues essential for hDim1 function are identified by using mutational and genetic approaches. The residues thus identified are not identical with those previously shown to govern Dim1 interaction with defined protein partners.
  8. Wieczorek D, Newman W, Wieland T, Berulava T, Kaffe M, Falkenstein D, et al. Compound heterozygosity of low-frequency promoter deletions and rare loss-of-function mutations in TXNL4A causes Burn-McKeown syndrome. Am J Hum Genet. 2014;95:698-707 pubmed publisher
    ..We identified biallelic mutations in TXNL4A, a member of this complex, in individuals with Burn-McKeown syndrome (BMKS)...
  9. Liu S, Rauhut R, Vornlocher H, Luhrmann R. The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP. RNA. 2006;12:1418-30 pubmed
    ..Taken together, data presented here provide a detailed picture of the network of protein interactions within the human tri-snRNP. ..
  10. Zhang Y, Gould K, Dunbrack RL J, Cheng H, Roder H, Golemis E. The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily. Physiol Genomics. 1999;1:109-18 pubmed
    b>Dim1 is a small evolutionarily conserved protein essential for G2/M transition that has recently been implicated as a component of the mRNA splicing machinery...
  11. Bertram K, Agafonov D, Dybkov O, Haselbach D, Leelaram M, Will C, et al. Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation. Cell. 2017;170:701-713.e11 pubmed publisher
    ..These include formation of a partially closed Prp8 conformation that creates, together with Dim1, a 5' splice site (ss) binding pocket, displacement of Sad1, and rearrangement of Brr2 such that it contacts its U4/..
  12. Gilmore Hebert M, Ramabhadran R, Stern D. Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways. Mol Cancer Res. 2010;8:1388-98 pubmed publisher
    ..Overall, these findings further substantiate the role of ErbB4 in conjoint regulation of growth factor signaling and DNA damage responses. ..
  13. Takahashi M, Mizuguchi M, Shinoda H, Aizawa T, Demura M, Okazawa H, et al. Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain. Biochim Biophys Acta. 2010;1804:1500-7 pubmed publisher
    ..These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD. ..
  14. Ghalei H, Trepreau J, Collins J, Bhaskaran H, Strunk B, Karbstein K. The ATPase Fap7 Tests the Ability to Carry Out Translocation-like Conformational Changes and Releases Dim1 during 40S Ribosome Maturation. Mol Cell. 2017;67:990-1000.e3 pubmed publisher
    ..of the rotated state, a key intermediate in translocation, thereby releasing the essential assembly factor Dim1 from pre-40S subunits. Bypassing this quality control step produces defects in reading frame maintenance...
  15. Laggerbauer B, Liu S, Makarov E, Vornlocher H, Makarova O, Ingelfinger D, et al. The human U5 snRNP 52K protein (CD2BP2) interacts with U5-102K (hPrp6), a U4/U6.U5 tri-snRNP bridging protein, but dissociates upon tri-snRNP formation. RNA. 2005;11:598-608 pubmed
    ..The interaction of 52K with a tri-snRNP bridging protein, coupled with its absence from the tri-snRNP, suggests it might function in tri-snRNP assembly. ..
  16. Zhang Y, Lindblom T, Chang A, Sudol M, Sluder A, Golemis E. Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Gene. 2000;257:33-43 pubmed
    ..U5 tri-snRNP, required for pre-mRNA splicing. To investigate the mechanism(s) of Dim1 function, reiterative two-hybrid screening was performed to identify interacting proteins...
  17. Waragai M, Junn E, Kajikawa M, Takeuchi S, Kanazawa I, Shibata M, et al. PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain. Biochem Biophys Res Commun. 2000;273:592-5 pubmed
    ..This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases. ..