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Showing Protein Pre-mRNA-processing factor 19 (HMDBP09278)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 4 metabolites
Identification
HMDB Protein ID HMDBP09278
Secondary Accession Numbers
  • 15106
Name Pre-mRNA-processing factor 19
Synonyms
  1. Nuclear matrix protein 200
  2. PRP19/PSO4 homolog
  3. Senescence evasion factor
  4. hPso4
Gene Name PRPF19
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin-protein ligase activity
Specific Function Plays a role in DNA double-strand break (DSB) repair and pre-mRNA splicing reaction. Binds double-stranded DNA in a sequence-nonspecific manner. Acts as a structural component of the nuclear framework. May also serve as a support for spliceosome binding and activity. Essential for spliceosome assembly in a oligomerization-dependent manner and might also be important for spliceosome stability. May have E3 ubiquitin ligase activity. The PSO4 complex is required in the DNA interstrand cross-links (ICLs) repair process. Overexpression of PRPF19 might extend the cellular life span by increasing the resistance to stress or by improving the DNA repair capacity of the cells
Pathways Not Available
Reactions Not Available
GO Classification
Component
macromolecular complex
protein complex
ubiquitin ligase complex
Function
catalytic activity
small conjugating protein ligase activity
ligase activity
ligase activity, forming carbon-nitrogen bonds
acid-amino acid ligase activity
ubiquitin-protein ligase activity
Process
metabolic process
macromolecule metabolic process
protein modification by small protein conjugation or removal
protein modification by small protein conjugation
protein ubiquitination
macromolecule modification
protein modification process
Cellular Location
  1. Nucleus
  2. Nucleus
  3. Cytoplasm
  4. cytoskeleton
  5. spindle
  6. nucleoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 11q12.2
SNPs PRPF19
Gene Sequence 
>1515 bp
ATGTCCCTAATCTGCTCCATCTCTAACGAAGTGCCGGAGCACCCATGTGTATCCCCTGTC
TCTAATCATGTTTATGAGCGGCGGCTCATCGAGAAGTACATTGCGGAGAATGGTACCGAC
CCCATCAACAACCAGCCTCTCTCCGAGGAGCAGCTCATCGACATCAAAGTTGCTCACCCA
ATCCGGCCCAAGCCTCCCTCAGCCACCAGCATCCCGGCCATTCTGAAAGCTTTGCAGGAT
GAGTGGGATGCAGTCATGCTGCACAGCTTCACTCTGCGCCAGCAGCTGCAGACAACCCGC
CAAGAGCTGTCACACGCTCTGTACCAGCACGATGCCGCCTGCCGTGTCATTGCCCGTCTC
ACCAAGGAAGTCACTGCTGCCCGAGAAGCTCTGGCTACCCTGAAACCACAGGCTGGCCTC
ATTGTGCCCCAGGCTGTGCCAAGTTCCCAACCAAGTGTTGTGGGTGCGGGTGAGCCAATG
GATTTGGGTGAGCTGGTGGGAATGACCCCAGAGATTATTCAGAAGCTTCAAGACAAAGCC
ACTGTGCTAACCACGGAGCGCAAGAAGAGAGGGAAGACTGTGCCTGAGGAGCTGGTGAAG
CCAGAAGAGCTCAGCAAATACCGGCAGGTGGCATCCCACGTGGGGTTGCACAGTGCCAGC
ATTCCTGGGATCCTGGCCCTGGACCTCTGCCCGTCCGACACCAACAAGATCCTCACTGGT
GGGGCGGATAAAAATGTCGTTGTGTTTGACAAAAGTTCTGAACAAATCCTGGCTACCCTC
AAAGGCCATACCAAGAAGGTCACCAGCGTGGTGTTTCACCCTTCCCAGGACCTGGTGTTT
TCTGCTTCCCCCGATGCCACTATCAGGATTTGGTCGGTCCCCAATGCCTCTTGTGTACAG
GTGGTTCGGGCCCATGAGAGTGCTGTGACAGGCCTCAGCCTTCATGCCACTGGCGACTAT
CTCCTGAGCTCCTCCGATGATCAGTACTGGGCTTTCTCTGACATCCAGACAGGGCGTGTG
CTCACCAAGGTGACAGATGAGACCTCCGGCTGCTCTCTCACCTGTGCACAGTTCCACCCT
GACGGACTCATCTTTGGAACAGGAACCATGGACTCTCAGATCAAGATCTGGGACTTGAAG
GAACGTACTAATGTGGCCAACTTCCCTGGCCACTCGGGCCCCATCACTAGCATCGCCTTC
TCTGAGAATGGTTACTACCTGGCTACAGCGGCTGATGACTCCTCTGTCAAGCTCTGGGAT
CTGCGCAAGCTTAAGAACTTTAAGACTTTGCAGCTGGATAACAACTTTGAGGTAAAGTCA
CTGATCTTTGACCAGAGTGGTACCTACCTGGCTCTTGGGGGCACGGATGTCCAGATCTAC
ATCTGCAAACAATGGACGGAGATTCTTCACTTTACAGAGCACAGTGGCCTGACCACAGGG
GTGGCCTTCGGGCATCACGCCAAGTTCATCGCTTCAACAGGCATGGACAGAAGCCTCAAG
TTCTACAGCCTGTAG
Protein Properties
Number of Residues 504
Molecular Weight 55180.3
Theoretical pI 6.6
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Pre-mRNA-processing factor 19
MSLICSISNEVPEHPCVSPVSNHVYERRLIEKYIAENGTDPINNQPLSEEQLIDIKVAHP
IRPKPPSATSIPAILKALQDEWDAVMLHSFTLRQQLQTTRQELSHALYQHDAACRVIARL
TKEVTAAREALATLKPQAGLIVPQAVPSSQPSVVGAGEPMDLGELVGMTPEIIQKLQDKA
TVLTTERKKRGKTVPEELVKPEELSKYRQVASHVGLHSASIPGILALDLCPSDTNKILTG
GADKNVVVFDKSSEQILATLKGHTKKVTSVVFHPSQDLVFSASPDATIRIWSVPNASCVQ
VVRAHESAVTGLSLHATGDYLLSSSDDQYWAFSDIQTGRVLTKVTDETSGCSLTCAQFHP
DGLIFGTGTMDSQIKIWDLKERTNVANFPGHSGPITSIAFSENGYYLATAADDSSVKLWD
LRKLKNFKTLQLDNNFEVKSLIFDQSGTYLALGGTDVQIYICKQWTEILHFTEHSGLTTG
VAFGHHAKFIASTGMDRSLKFYSL
GenBank ID Protein 5689738
UniProtKB/Swiss-Prot ID Q9UMS4
UniProtKB/Swiss-Prot Entry Name PRP19_HUMAN
PDB IDs Not Available
GenBank Gene ID AJ131186
GeneCard ID PRPF19
GenAtlas ID PRPF19
HGNC ID HGNC:17896
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. Scherl A, Coute Y, Deon C, Calle A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ: Functional proteomic analysis of human nucleolus. Mol Biol Cell. 2002 Nov;13(11):4100-9. [PubMed:12429849 ]
  6. Mahajan KN, Mitchell BS: Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase. Proc Natl Acad Sci U S A. 2003 Sep 16;100(19):10746-51. Epub 2003 Sep 5. [PubMed:12960389 ]
  7. Jurica MS, Licklider LJ, Gygi SR, Grigorieff N, Moore MJ: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. RNA. 2002 Apr;8(4):426-39. [PubMed:11991638 ]
  8. Gotzmann J, Gerner C, Meissner M, Holzmann K, Grimm R, Mikulits W, Sauermann G: hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions. Exp Cell Res. 2000 Nov 25;261(1):166-79. [PubMed:11082287 ]
  9. Gerner C, Holzmann K, Meissner M, Gotzmann J, Grimm R, Sauermann G: Reassembling proteins and chaperones in human nuclear matrix protein fractions. J Cell Biochem. 1999 Aug 1;74(2):145-51. [PubMed:10404385 ]
  10. Grillari J, Ajuh P, Stadler G, Loscher M, Voglauer R, Ernst W, Chusainow J, Eisenhaber F, Pokar M, Fortschegger K, Grey M, Lamond AI, Katinger H: SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly. Nucleic Acids Res. 2005 Dec 6;33(21):6868-83. Print 2005. [PubMed:16332694 ]
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  12. Zhang N, Kaur R, Lu X, Shen X, Li L, Legerski RJ: The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links. J Biol Chem. 2005 Dec 9;280(49):40559-67. Epub 2005 Oct 12. [PubMed:16223718 ]
  13. Voglauer R, Chang MW, Dampier B, Wieser M, Baumann K, Sterovsky T, Schreiber M, Katinger H, Grillari J: SNEV overexpression extends the life span of human endothelial cells. Exp Cell Res. 2006 Apr 1;312(6):746-59. Epub 2006 Jan 4. [PubMed:16388800 ]