YHR165C
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| Systematic name | YHR165C |
| Gene name | PRP8 |
| Aliases | DBF3, DNA39, RNA8, SLT21, USA2 |
| Feature type | ORF, Verified |
| Coordinates | Chr VIII:436950..429709 |
| Primary SGDID | S000001208 |
Description of YHR165C: Component of the U4/U6-U5 snRNP complex, involved in the second catalytic step of splicing; mutations of human Prp8 cause retinitis pigmentosa[1][2][3]
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Community Commentary
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Interactions
Two Hybrid
Two Hybrid interaction with Prp40
Prp8 interacts with the U1snRNP protein Prp40 [4] [5]
Two Hybrid interaction with Snp1
Prp8 interacts with the U1snRNP protein Snp1 [6] [5]
Two Hybrid interaction with Exo84
Prp8 binds to C-terminus of Exo84 [7] [5]
Two Hybrid interaction with Prp39
N-terminal region of Prp8 interacts with Prp39 [8] [5]
Two Hybrid interaction with Brr2
C-terminus of Prp8 binds to full length Brr2. N-terminus of Prp8 binds to Prp39 [8] [5]
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References
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- ↑ Stevens SW and Abelson J (1999) Purification of the yeast U4/U6.U5 small nuclear ribonucleoprotein particle and identification of its proteins. Proc Natl Acad Sci U S A 96(13):7226-31 SGD PMID 10377396
- ↑ Umen JG and Guthrie C (1995) The second catalytic step of pre-mRNA splicing. RNA 1(9):869-85 SGD PMID 8548652
- ↑ Boon KL, et al. (2007) prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast. Nat Struct Mol Biol 14(11):1077-83 SGD PMID 17934474
- ↑ Abovich N and Rosbash M (1997) Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals. Cell 89(3):403-12 SGD PMID 9150140
- ↑ 5.0 5.1 5.2 5.3 5.4 submitted by Richard Grainger on 2003-04-11
- ↑ Awasthi S, et al. (2001) New roles for the Snp1 and Exo84 proteins in yeast pre-mRNA splicing. J Biol Chem 276(33):31004-15 SGD PMID 11425851
- ↑ Kuhn AN and Brow DA (2000) Suppressors of a cold-sensitive mutation in yeast U4 RNA define five domains in the splicing factor Prp8 that influence spliceosome activation. Genetics 155(4):1667-82 SGD PMID 10924465
- ↑ 8.0 8.1 van Nues RW and Beggs JD (2001) Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae. Genetics 157(4):1451-67 SGD PMID 11290703
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