Splicing issue U2AF 65 kDa subunit is a protein that in people is encoded by the U2AF2 gene.[5]


In eukaryotes, the introns within the transcribed pre-mRNA first must be eliminated by spliceosome as a way to kind a mature mRNA. A spliceosome is assembled from small nuclear ribonucleoproteins(snRNP) and small nuclear RNAs(snRNA). And the splicing issue may be divided into snRNP and non snRNP proteins.U2 auxiliary issue (U2AF), composed of a giant and a small subunit, is a non-snRNP protein required for the binding of U2 snRNP to the pre-mRNA department website. This gene encodes the U2AF massive subunit, which accommodates a sequence-specific RNA-binding area with 3 RNA recognition motifs and an Arg/Ser-rich area needed for splicing. The massive subunit binds to the polypyrimidine tract of introns early throughout spliceosome meeting. A number of alternatively spliced transcript variants have been detected for this gene, however the full-length natures of solely two have been decided thus far.[6]

In people and different tetrapods, it has been proven that with out U2AF2, the splicing course of is inhibited. Nevertheless, in zebrafish and different teleosts the RNA splicing course of can nonetheless happen on sure genes within the absence of U2AF2. This can be as a result of 10{ae90547d17d4d74b17007ee836a04674fd006933c139011dc78eb03c100070a7} of genes have alternating TG and AC base pairs on the 3′ splice website (3’ss) and 5′ splice website (5’ss) respectively on every intron, which alters the secondary construction of the RNA and influences splicing.[7]

The splicing issue U2AF65 can particularly acknowledges the polypyrimidine tract (Py tract), that’s as a result of U2AF65 consists of three RNA binding domains (RRMs), all of them have a excessive binding affinity to the Py tract on its adjoining 3’ splice website.[6]The RRM1 and RRM2 are adequate for particular RNA/protein binding, whereas RRM3 is chargeable for protein/protein interactions. For instance, the C-Terminal RRM3 contribute to determine protein–protein contacts with splicing components like UAP56, SAP155, and mBBP/SF1.[8]


U2AF2 has been proven to work together with:

  • PUF60,[9][10]
  • SF1,[9][11][12]
  • SFRS11,[13]
  • SFRS2IP,[14]
  • SRPK2,[9][15]
  • U2 small nuclear RNA auxiliary issue 1[9][16] and
  • WT1.[17]

Additional studying

  • Zhang M, Zamore PD, Carmo-Fonseca M, Lamond AI, Inexperienced MR (September 1992). “Cloning and intracellular localization of the U2 small nuclear ribonucleoprotein auxiliary issue small subunit”. Proceedings of the Nationwide Academy of Sciences of the US of America. 89 (18): 8769–8773. Bibcode:1992PNAS…89.8769Z. doi:10.1073/pnas.89.18.8769. PMC 50002. PMID 1388271.
  • Zamore PD, Inexperienced MR (January 1991). “Biochemical characterization of U2 snRNP auxiliary issue: a necessary pre-mRNA splicing issue with a novel intranuclear distribution”. The EMBO Journal. 10 (1): 207–214. doi:10.1002/j.1460-2075.1991.tb07937.x. PMC 452631. PMID 1824937.
  • Zuo P, Maniatis T (June 1996). “The splicing issue U2AF35 mediates crucial protein-protein interactions in constitutive and enhancer-dependent splicing”. Genes & Improvement. 10 (11): 1356–1368. doi:10.1101/gad.10.11.1356. PMID 8647433.
  • Zhang WJ, Wu JY (October 1996). “Practical properties of p54, a novel SR protein lively in constitutive and various splicing”. Molecular and Mobile Biology. 16 (10): 5400–5408. doi:10.1128/MCB.16.10.5400. PMC 231539. PMID 8816452.
  • Hong W, Bennett M, Xiao Y, Feld Kramer R, Wang C, Reed R (January 1997). “Affiliation of U2 snRNP with the spliceosomal complicated E”. Nucleic Acids Analysis. 25 (2): 354–361. doi:10.1093/nar/25.2.354. PMC 146436. PMID 9016565.
  • Abovich N, Rosbash M (Could 1997). “Cross-intron bridging interactions within the yeast dedication complicated are conserved in mammals”. Cell. 89 (3): 403–412. doi:10.1016/S0092-8674(00)80221-4. PMID 9150140. S2CID 18466775.
  • Tronchère H, Wang J, Fu XD (July 1997). “A protein associated to splicing issue U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA”. Nature. 388 (6640): 397–400. Bibcode:1997Natur.388..397T. doi:10.1038/41137. PMID 9237760. S2CID 4386808.
  • Fleckner J, Zhang M, Valcárcel J, Inexperienced MR (July 1997). “U2AF65 recruits a novel human DEAD field protein required for the U2 snRNP-branchpoint interplay”. Genes & Improvement. 11 (14): 1864–1872. doi:10.1101/gad.11.14.1864. PMID 9242493.
  • Zhang WJ, Wu JY (February 1998). “Sip1, a novel RS domain-containing protein important for pre-mRNA splicing”. Molecular and Mobile Biology. 18 (2): 676–684. doi:10.1128/MCB.18.2.676. PMC 108778. PMID 9447963.
  • Wang HY, Lin W, Dyck JA, Yeakley JM, Songyang Z, Cantley LC, Fu XD (February 1998). “SRPK2: a differentially expressed SR protein-specific kinase concerned in mediating the interplay and localization of pre-mRNA splicing components in mammalian cells”. The Journal of Cell Biology. 140 (4): 737–750. doi:10.1083/jcb.140.4.737. PMC 2141757. PMID 9472028.
  • Berglund JA, Abovich N, Rosbash M (March 1998). “A cooperative interplay between U2AF65 and mBBP/SF1 facilitates branchpoint area recognition”. Genes & Improvement. 12 (6): 858–867. doi:10.1101/gad.12.6.858. PMC 316625. PMID 9512519.
  • Rudner DZ, Kanaar R, Breger KS, Rio DC (April 1998). “Interplay between subunits of heterodimeric splicing issue U2AF is crucial in vivo”. Molecular and Mobile Biology. 18 (4): 1765–1773. doi:10.1128/MCB.18.4.1765. PMC 121406. PMID 9528748.
  • Lallena MJ, Martínez C, Valcárcel J, Correas I (July 1998). “Practical affiliation of nuclear protein 4.1 with pre-mRNA splicing components”. Journal of Cell Science. 111 (14): 1963–1971. doi:10.1242/jcs.111.14.1963. PMID 9645944.
  • Gozani O, Potashkin J, Reed R (August 1998). “A possible function for U2AF-SAP 155 interactions in recruiting U2 snRNP to the department website”. Molecular and Mobile Biology. 18 (8): 4752–4760. doi:10.1128/mcb.18.8.4752. PMC 109061. PMID 9671485.
  • Neubauer G, King A, Rappsilber J, Calvio C, Watson M, Ajuh P, et al. (September 1998). “Mass spectrometry and EST-database looking permits characterization of the multi-protein spliceosome complicated”. Nature Genetics. 20 (1): 46–50. doi:10.1038/1700. PMID 9731529. S2CID 585778.
  • Davies RC, Calvio C, Bratt E, Larsson SH, Lamond AI, Hastie ND (October 1998). “WT1 interacts with the splicing issue U2AF65 in an isoform-dependent method and may be included into spliceosomes”. Genes & Improvement. 12 (20): 3217–3225. doi:10.1101/gad.12.20.3217. PMC 317218. PMID 9784496.
  • Ito T, Muto Y, Inexperienced MR, Yokoyama S (August 1999). “Resolution constructions of the primary and second RNA-binding domains of human U2 small nuclear ribonucleoprotein particle auxiliary issue (U2AF(65))”. The EMBO Journal. 18 (16): 4523–4534. doi:10.1093/emboj/18.16.4523. PMC 1171527. PMID 10449418.
  • Wang X, Bruderer S, Rafi Z, Xue J, Milburn PJ, Krämer A, Robinson PJ (August 1999). “Phosphorylation of splicing issue SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome meeting”. The EMBO Journal. 18 (16): 4549–4559. doi:10.1093/emboj/18.16.4549. PMC 1171529. PMID 10449420.
  • Ladomery MR, Slight J, Mc Ghee S, Hastie ND (December 1999). “Presence of WT1, the Wilm’s tumor suppressor gene product, in nuclear poly(A)(+) ribonucleoprotein”. The Journal of Organic Chemistry. 274 (51): 36520–36526. doi:10.1074/jbc.274.51.36520. PMID 10593950.

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