TXNL4A

TXNL4A
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1PQN, 1QGV, 1SYX, 4BWQ, 4BWS, 4CDO, 3JCR
Identifiers
Aliases	TXNL4A , DIB1, DIM1, HsT161, SNRNP15, TXNL4, U5-15kD, BMKS, thioredoxin like 4A
External IDs	OMIM: 611595 MGI: 1351613 HomoloGene: 7150 GeneCards: TXNL4A
Gene location (Human)
Chr.	Chromosome 18 (human)
End	80,033,949 bp
RNA expression pattern
	Top expressed in
	parotid gland; ; amygdala; ; endothelial cell; ; anterior pituitary; ; prefrontal cortex; ; substantia nigra; ; periodontal fiber; ; cingulate gyrus; ; nucleus accumbens; ; putamen;
	n/a
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein binding ;
Cellular component	U5 snRNP ; spliceosomal complex ; nucleoplasm ; nucleus ; cytosol ; nuclear membrane ; U4/U6 x U5 tri-snRNP complex ; U2-type precatalytic spliceosome ;
Biological process	RNA splicing, via transesterification reactions ; mRNA splicing, via spliceosome ; cell cycle ; mRNA processing ; spliceosomal complex assembly ; cell division ; RNA splicing ;
	Sources:Amigo / QuickGO
Orthologs
	10907
	27366
	ENSG00000141759
	ENSMUSG00000057130
	P83876
	P83877
	NM_001303471 ; NM_001305557 ; NM_001305563 ; NM_001305564 ; NM_006701 Contents Interactions ; References ; Further reading ;
	NM_001038608 ; NM_001042408 ; NM_001042409 ; NM_025299 ; NM_178604
	NP_001290400 ; NP_001292486 ; NP_001292492 ; NP_001292493 ; NP_006692
NP_001033697 ; NP_001035867 ; NP_079575 ; NP_848719 ; NP_001371102 ;
	NP_001371103 ; NP_001371104 ; NP_001371105 ; NP_001371106
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 04, 2023

Thioredoxin-like protein 4A is a protein that is encoded by the TXNL4A gene in humans.^[4]^[5]

Interactions

TXNL4A has been shown to interact with PQBP1.^[6]

Related Research Articles

A spliceosome is a large ribonucleoprotein (RNP) complex found primarily within the nucleus of eukaryotic cells. The spliceosome is assembled from small nuclear RNAs (snRNA) and numerous proteins. Small nuclear RNA (snRNA) molecules bind to specific proteins to form a small nuclear ribonucleoprotein complex, which in turn combines with other snRNPs to form a large ribonucleoprotein complex called a spliceosome. The spliceosome removes introns from a transcribed pre-mRNA, a type of primary transcript. This process is generally referred to as splicing. An analogy is a film editor, who selectively cuts out irrelevant or incorrect material from the initial film and sends the cleaned-up version to the director for the final cut.

snRNPs, or small nuclear ribonucleoproteins, are RNA-protein complexes that combine with unmodified pre-mRNA and various other proteins to form a spliceosome, a large RNA-protein molecular complex upon which splicing of pre-mRNA occurs. The action of snRNPs is essential to the removal of introns from pre-mRNA, a critical aspect of post-transcriptional modification of RNA, occurring only in the nucleus of eukaryotic cells. Additionally, U7 snRNP is not involved in splicing at all, as U7 snRNP is responsible for processing the 3′ stem-loop of histone pre-mRNA.

Small nuclear RNA (snRNA) is a class of small RNA molecules that are found within the splicing speckles and Cajal bodies of the cell nucleus in eukaryotic cells. The length of an average snRNA is approximately 150 nucleotides. They are transcribed by either RNA polymerase II or RNA polymerase III. Their primary function is in the processing of pre-messenger RNA (hnRNA) in the nucleus. They have also been shown to aid in the regulation of transcription factors or RNA polymerase II, and maintaining the telomeres.

<span class="mw-page-title-main">U4 spliceosomal RNA</span> Non-coding RNA component of the spliceosome

The U4 small nuclear Ribo-Nucleic Acid is a non-coding RNA component of the major or U2-dependent spliceosome – a eukaryotic molecular machine involved in the splicing of pre-messenger RNA (pre-mRNA). It forms a duplex with U6, and with each splicing round, it is displaced from the U6 snRNA in an ATP-dependent manner, allowing U6 to re-fold and create the active site for splicing catalysis. A recycling process involving protein Brr2 releases U4 from U6, while protein Prp24 re-anneals U4 and U6. The crystal structure of a 5′ stem-loop of U4 in complex with a binding protein has been solved.

Pre-mRNA-processing-splicing factor 8 is a protein that in humans is encoded by the PRPF8 gene.

Small nuclear ribonucleoprotein Sm D1 is a protein that in humans is encoded by the SNRPD1 gene.

PRP31 pre-mRNA processing factor 31 homolog , also known as PRPF31, is a protein which in humans is encoded by the PRPF31 gene.

Heterogeneous nuclear ribonucleoprotein F is a protein that in humans is encoded by the HNRNPF gene.

U4/U6.U5 tri-snRNP-associated protein 1 is a protein that in humans is encoded by the SART1 gene. This gene encodes two proteins, the SART1(800) protein expressed in the nucleus of the majority of proliferating cells, and the SART1(259) protein expressed in the cytosol of epithelial cancers. The SART1(259) protein is translated by the mechanism of -1 frameshifting during posttranscriptional regulation. The two encoded proteins are thought to be involved in the regulation of proliferation. Both proteins have tumor-rejection antigens. The SART1(259) protein possesses tumor epitopes capable of inducing HLA-A2402-restricted cytotoxic T lymphocytes in cancer patients. This SART1(259) antigen may be useful in specific immunotherapy for cancer patients and may serve as a paradigmatic tool for the diagnosis and treatment of patients with atopy. The SART1(259) protein is found to be essential for the recruitment of the tri-snRNP to the pre-spliceosome in the spliceosome assembly pathway.

U5 small nuclear ribonucleoprotein 200 kDa helicase is an enzyme that in humans is encoded by the SNRNP200 gene.

Polyglutamine-binding protein 1 (PQBP1) is a protein that in humans is encoded by the PQBP1 gene.

Small nuclear ribonucleoprotein F is a protein that in humans is encoded by the SNRPF gene.

Pre-mRNA-processing factor 6 is a protein that in humans is encoded by the PRPF6 gene.

116 kDa U5 small nuclear ribonucleoprotein component is a protein that in humans is encoded by the EFTUD2 gene.

Heterogeneous nuclear ribonucleoprotein H2 is a protein that in humans is encoded by the HNRNPH2 gene.

WD repeat domain 57 , also known as WDR57, is a gene found in many organisms, including, but not limited to Homo sapiens, Gallus gallus, Pan troglodytes, Canus familiaris, Bos taurus, Mus musculus, and Rattus norvegicus.

Peptidyl-prolyl cis-trans isomerase H is an enzyme that in humans is encoded by the PPIH gene.

Thioredoxin-like protein 4B is a protein that in humans is encoded by the TXNL4B gene.

Probable ATP-dependent RNA helicase DDX23 is an enzyme that in humans is encoded by the DDX23 gene.

Prp8 refers to both the Prp8 protein and Prp8 gene. Prp8's name originates from its involvement in pre-mRNA processing. The Prp8 protein is a large, highly conserved, and unique protein that resides in the catalytic core of the spliceosome and has been found to have a central role in molecular rearrangements that occur there. Prp8 protein is a major central component of the catalytic core in the spliceosome, and the spliceosome is responsible for splicing of precursor mRNA that contains introns and exons. Unexpressed introns are removed by the spliceosome complex in order to create a more concise mRNA transcript. Splicing is just one of many different post-transcriptional modifications that mRNA must undergo before translation. Prp8 has also been hypothesized to be a cofactor in RNA catalysis.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000141759 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Zhang YZ, Gould KL, Dunbrack RL JR, Cheng H, Roder H, Golemis EA (October 2000). "The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily". Physiol Genomics. 1 (3): 109–18. doi:10.1152/physiolgenomics.1999.1.3.109. PMID 11015569. S2CID 16086223.
↑ "Entrez Gene: TXNL4A thioredoxin-like 4A".
↑ Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (October 2000). "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. 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. PMID 11054566.

Reuter K, Nottrott S, Fabrizio P, Lührmann R, Ficner R (2000). "Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein". J. Mol. Biol. 294 (2): 515–25. doi:10.1006/jmbi.1999.3258. PMID 10610776.
Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (2001). "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. 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. PMID 11054566.
Zhang YZ, Cheng H, Gould KL, Golemis EA, Roder H (2003). "Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis". Biochemistry. 42 (32): 9609–18. doi:10.1021/bi034486i. PMID 12911302.
Laggerbauer B, Liu S, Makarov E, Vornlocher HP, Makarova O, Ingelfinger D, Achsel T, Lührmann R (2005). "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" (PDF). RNA. 11 (5): 598–608. doi:10.1261/rna.2300805. PMC 1370748 . PMID 15840814.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Jin T, Guo F, Wang Y, Zhang YZ (2007). "Identification of human dim1 as a peptidase with autocleavage activity". Chemical Biology & Drug Design. 68 (5): 266–72. doi:10.1111/j.1747-0285.2006.00447.x. PMID 17177886. S2CID 13020526.

This article on a gene on human chromosome 18 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000141759 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11015569-4] Zhang YZ, Gould KL, Dunbrack RL JR, Cheng H, Roder H, Golemis EA (October 2000). "The evolutionarily conserved Dim1 protein defines a novel branch of the thioredoxin fold superfamily". Physiol Genomics. 1 (3): 109–18. doi:10.1152/physiolgenomics.1999.1.3.109. PMID 11015569. S2CID 16086223.

[entrez-5] "Entrez Gene: TXNL4A thioredoxin-like 4A".

[pmid11054566-6] Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (October 2000). "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. 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. PMID 11054566.

[1]

[2]

[3]

[4]

[5]

[6]

TXNL4A

Contents

Interactions

Related Research Articles

References

Further reading