PRPF19

PRPF19
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4LG8
Identifiers
Aliases	PRPF19 , NMP200, PRP19, PSO4, SNEV, UBOX4, hPSO4, pre-mRNA processing factor 19
External IDs	OMIM: 608330 MGI: 106247 HomoloGene: 6421 GeneCards: PRPF19
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11q12.2 Start 60,890,547 bp [1] End 60,906,585 bp [1]
Gene location (Mouse) Chr. Chromosome 19 (mouse) [2] Band 19 A|19 7.33 cM Start 10,872,595 bp [2] End 10,886,923 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pons Brodmann area 9 ganglionic eminence prefrontal cortex cerebellar hemisphere anterior pituitary islet of Langerhans superior vestibular nucleus skin of abdomen cingulate gyrus Top expressed in aortic valve primitive streak motor neuron ascending aorta fossa right ventricle Paneth cell facial motor nucleus ankle abdominal wall More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ubiquitin protein ligase activity ubiquitin-protein transferase activity ubiquitin-ubiquitin ligase activity protein binding identical protein binding transferase activity Cellular component site of double-strand break nuclear speck catalytic step 2 spliceosome membrane lipid droplet spindle Prp19 complex DNA replication factor A complex spliceosomal complex cytoskeleton nucleus cytoplasm nucleoplasm U2-type catalytic step 1 spliceosome U2-type catalytic step 2 spliceosome Biological process mRNA splicing, via spliceosome spliceosomal tri-snRNP complex assembly lipid biosynthetic process negative regulation of neuron differentiation positive regulation of astrocyte differentiation positive regulation of mRNA splicing, via spliceosome protein K63-linked ubiquitination mRNA processing protein polyubiquitination inner cell mass cell proliferation cellular response to DNA damage stimulus spliceosomal complex assembly protein ubiquitination proteasomal protein catabolic process transcription-coupled nucleotide-excision repair double-strand break repair via nonhomologous end joining DNA repair RNA splicing generation of catalytic spliceosome for first transesterification step positive regulation of neuron differentiation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27339 28000 Ensembl ENSG00000110107 ENSMUSG00000024735 UniProt Q9UMS4 Q99KP6 RefSeq (mRNA) NM_014502 NM_001253843 NM_001253844 NM_134129 RefSeq (protein) NP_055317 NP_001240772 NP_001240773 NP_598890 Location (UCSC) Chr 11: 60.89 – 60.91 Mb Chr 19: 10.87 – 10.89 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Pre-mRNA-processing factor 19 is a protein that in humans is encoded by the PRPF19 gene. ^{[5] [6]}

In S. cerevisiae, Pso4 has pleiotropic functions in DNA recombination and in error-prone nonhomologous end-joining DNA repair.[supplied by OMIM] ^[6]

Interactions

PRPF19 has been shown to interact with CDC5L. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000110107 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024735 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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. Bibcode:2003PNAS..10010746M. doi: 10.1073/pnas.1631060100 . PMC   196874 . PMID   12960389.
6. "Entrez Gene: PRPF19 PRP19/PSO4 pre-mRNA processing factor 19 homolog (S. cerevisiae)".
7. 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. 19 (23): 6569–81. doi:10.1093/emboj/19.23.6569. ISSN   0261-4189. PMC   305846 . PMID   11101529.

Further reading

• 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. S2CID   196598497.
• 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. Bibcode:2002CBio...12....1A. doi: 10.1016/S0960-9822(01)00650-9 . PMID   11790298. S2CID   14132033.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004CBio...14.1436J. doi: 10.1016/j.cub.2004.07.051 . PMID   15324660. S2CID   2371325.
• 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. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID   16189514. S2CID   4427026.
• 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.