PRPF19

Protein-coding gene in the species Homo sapiens
PRPF19
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4LG8

Identifiers
AliasesPRPF19, NMP200, PRP19, PSO4, SNEV, UBOX4, hPSO4, pre-mRNA processing factor 19
External IDsOMIM: 608330; MGI: 106247; HomoloGene: 6421; GeneCards: PRPF19; OMA:PRPF19 - orthologs
Gene location (Human)
Chromosome 11 (human)
Chr.Chromosome 11 (human)[1]
Chromosome 11 (human)
Genomic location for PRPF19
Genomic location for PRPF19
Band11q12.2Start60,890,547 bp[1]
End60,906,585 bp[1]
Gene location (Mouse)
Chromosome 19 (mouse)
Chr.Chromosome 19 (mouse)[2]
Chromosome 19 (mouse)
Genomic location for PRPF19
Genomic location for PRPF19
Band19 A|19 7.33 cMStart10,872,595 bp[2]
End10,886,923 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pons

  • right frontal lobe

  • Brodmann area 9

  • ventricular zone

  • ganglionic eminence

  • prefrontal cortex

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • anterior pituitary

  • islet of Langerhans
Top expressed in
  • aortic valve

  • primitive streak

  • motor neuron

  • ascending aorta

  • fossa

  • right ventricle

  • epiblast

  • Paneth cell

  • facial motor nucleus

  • ankle
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
SpeciesHumanMouse
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 MbChr 19: 10.87 – 10.89 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000110107 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b "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.
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