Learn and talk about PRPF19, Human proteins

PRP19/PSO4 pre-mRNA processing factor 19 homolog (S. cerevisiae)

Identifiers

PRPF19; NMP200; PRP19; PSO4; SNEV; UBOX4; hPSO4

External IDs

OMIM: 608330 MGI: 106247 HomoloGene: 6421 GeneCards: PRPF19 Gene

Gene Ontology
Molecular function	• DNA binding • ubiquitin-protein ligase activity • protein binding • ubiquitin-ubiquitin ligase activity • identical protein binding
Cellular component	• ubiquitin ligase complex • Prp19 complex • nucleus • cytoplasm • lipid particle • spindle • nuclear speck • catalytic step 2 spliceosome
Biological process	• protein polyubiquitination • spliceosomal complex assembly • mRNA splicing, via spliceosome • inner cell mass cell proliferation • DNA repair • lipid biosynthetic process • negative regulation of neuron differentiation • positive regulation of mRNA splicing, via spliceosome • positive regulation of astrocyte differentiation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
60.66 – 60.67 Mb

Chr 19:
10.89 – 10.91 Mb

PubMed search

[1]

[2]

Pre-mRNA-processing factor 19 is a protein that in humans is encoded by the PRPF19 gene.^[1]^[2]

In S. cerevisiae, Pso4 has pleiotropic functions in DNA recombination and in error-prone nonhomologous end-joining DNA repair.[supplied by OMIM]^[2]

Interactions [edit]

PRPF19 has been shown to interact with CDC5L.^[3]

References [edit]

^ Mahajan KN, Mitchell BS (September 2003). "Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase". Proc Natl Acad Sci U S A 100 (19): 10746–51. doi:10.1073/pnas.1631060100. PMC 196874. PMID 12960389.
^ ^a ^b "Entrez Gene: PRPF19 PRP19/PSO4 pre-mRNA processing factor 19 homolog (S. cerevisiae)".
^ Ajuh, P; Kuster B, Panov K, Zomerdijk J C, Mann M, Lamond A I (December 2000). "Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry". EMBO J. (ENGLAND) 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. ISSN 0261-4189. PMC 305846. PMID 11101529.

Further reading [edit]

Gerner C, Holzmann K, Meissner M, et al. (1999). "Reassembling proteins and chaperones in human nuclear matrix protein fractions.". J. Cell. Biochem. 74 (2): 145–51. doi:10.1002/(SICI)1097-4644(19990801)74:2<145::AID-JCB1>3.0.CO;2-#. PMID 10404385.
Gotzmann J, Gerner C, Meissner M, et al. (2000). "hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions.". Exp. Cell Res. 261 (1): 166–79. doi:10.1006/excr.2000.5025. PMID 11082287.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
Jurica MS, Licklider LJ, Gygi SR, et al. (2002). "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.". RNA 8 (4): 426–39. doi:10.1017/S1355838202021088. PMC 1370266. PMID 11991638.
Scherl A, Couté Y, Déon C, et al. (2003). "Functional proteomic analysis of human nucleolus.". Mol. Biol. Cell 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC 133617. PMID 12429849.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Makarova OV, Makarov EM, Urlaub H, et al. (2004). "A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing.". EMBO J. 23 (12): 2381–91. doi:10.1038/sj.emboj.7600241. PMC 423283. PMID 15175653.
Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization.". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
Löscher M, Fortschegger K, Ritter G, et al. (2005). "Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome.". Biochem. J. 388 (Pt 2): 593–603. doi:10.1042/BJ20041517. PMC 1138967. PMID 15660529.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Zhang N, Kaur R, Lu X, et al. (2006). "The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links.". J. Biol. Chem. 280 (49): 40559–67. doi:10.1074/jbc.M508453200. PMID 16223718.
Grillari J, Ajuh P, Stadler G, et al. (2005). "SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly.". Nucleic Acids Res. 33 (21): 6868–83. doi:10.1093/nar/gki986. PMC 1310963. PMID 16332694.
Voglauer R, Chang MW, Dampier B, et al. (2006). "SNEV overexpression extends the life span of human endothelial cells.". Exp. Cell Res. 312 (6): 746–59. doi:10.1016/j.yexcr.2005.11.025. PMID 16388800.
Lu X, Legerski RJ (2007). "The Prp19/Pso4 core complex undergoes ubiquitylation and structural alterations in response to DNA damage.". Biochem. Biophys. Res. Commun. 354 (4): 968–74. doi:10.1016/j.bbrc.2007.01.097. PMC 1810354. PMID 17276391.
Fortschegger K, Wagner B, Voglauer R, et al. (2007). "Early embryonic lethality of mice lacking the essential protein SNEV.". Mol. Cell. Biol. 27 (8): 3123–30. doi:10.1128/MCB.01188-06. PMC 1899945. PMID 17283042.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

v t e Post-transcriptional modification

Nuclear	Precursor mRNA 5′ cap formation Polyadenylation CPSF CstF PAP PAB2 CFI CFII Poly(A)-binding protein RNA splicing: intron/exon snRNP spliceosome minor spliceosome U1 alternative splicing pre-mRNA processing factor PLRG1 PRPF3 PRPF4 PRPF4B PRPF6 PRPF8 PRPF18 PRPF19 PRPF31 PRPF38A PRPF38B PRPF39 PRPF40A PRPF40B RNA editing Polyuridylation

Cytosolic	5′ cap methylation Messenger RNA decapping: DCP1A DCP1B DCP2 DCPS EDC3 EDC4

see also: disorders of transcription and post transcriptional modification, Transcription B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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PRPF19

Interactions [edit]

References [edit]

Further reading [edit]

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