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Q9UMS4 (PRP19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-processing factor 19
Alternative name(s):
Nuclear matrix protein 200
PRP19/PSO4 homolog
Short name=hPso4
Senescence evasion factor
Gene names
Name:PRPF19
Synonyms:NMP200, PRP19, SNEV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in DNA double-strand break (DSB) repair. 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. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Ref.1 Ref.2 Ref.9 Ref.10 Ref.11 Ref.12

Subunit structure

Homooligomer. Identified in the spliceosome C complex. Component of the PSO4 complex, composed of PRPF19, CDC5L, PLRG1. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts in the complex directly with CDC5L, PLRG1 and BCAS2. Interacts with APEX1, DNTT and PSMB4. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Ref.2 Ref.8 Ref.9 Ref.10 Ref.11 Ref.15 Ref.17 Ref.20

Subcellular location

Nucleus. Nucleusnucleoplasm. Cytoplasmcytoskeletonspindle. Note: Nucleoplasmic in interphase cells. Irregularly distributed in anaphase cells. In prophase cells, uniformly distributed, but not associated with condensing chromosomes. Found in extrachromosomal regions in metaphase cells. Mainly localized to the mitotic spindle apparatus when chromosomes segregate during anaphase. When nuclei reform during late telophase, uniformly distributed in daughter cells and displays no preferred association with decondensing chromatin. Ref.1 Ref.7 Ref.15 Ref.17

Tissue specificity

Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines. Ref.1 Ref.2 Ref.6 Ref.12

Induction

By gamma irradiation and chemical mutagens but not by UV irradiation. Ref.2

Sequence similarities

Belongs to the WD repeat PRP19 family.

Contains 1 U-box domain.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
mRNA processing
mRNA splicing
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
Spliceosome
   DomainRepeat
WD repeat
   LigandDNA-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

inner cell mass cell proliferation

Inferred from electronic annotation. Source: Ensembl

lipid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

mRNA splicing, via spliceosome

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mRNA splicing, via spliceosome

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Inferred from direct assay PubMed 11435423. Source: MGI

spliceosomal complex assembly

Inferred from mutant phenotype Ref.9. Source: BHF-UCL

   Cellular_componentPrp19 complex

Inferred from direct assay Ref.17. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 11435423. Source: MGI

lipid particle

Inferred from electronic annotation. Source: Ensembl

nuclear speck

Inferred from direct assay Ref.9. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.15. Source: UniProtKB

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

ubiquitin ligase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.15Ref.17Ref.20. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay PubMed 11435423. Source: MGI

ubiquitin-ubiquitin ligase activity

Inferred from direct assay PubMed 11435423. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 504503Pre-mRNA-processing factor 19
PRO_0000051145

Regions

Domain2 – 7372U-box
Repeat219 – 25941WD 1
Repeat262 – 30140WD 2
Repeat304 – 34542WD 3
Repeat348 – 38740WD 4
Repeat390 – 42940WD 5
Repeat433 – 47240WD 6
Repeat473 – 50331WD 7

Amino acid modifications

Modified residue21N-acetylserine Ref.4 Ref.5 Ref.14 Ref.19
Modified residue1221N6-acetyllysine Ref.16
Modified residue1791N6-acetyllysine By similarity
Modified residue2441N6-acetyllysine By similarity
Modified residue2611N6-acetyllysine Ref.16

Secondary structure

.................................................................. 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UMS4 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: B34C37496E8AA032

FASTA50455,181
        10         20         30         40         50         60 
MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE QLIDIKVAHP 

        70         80         90        100        110        120 
IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR QELSHALYQH DAACRVIARL 

       130        140        150        160        170        180 
TKEVTAAREA LATLKPQAGL IVPQAVPSSQ PSVVGAGEPM DLGELVGMTP EIIQKLQDKA 

       190        200        210        220        230        240 
TVLTTERKKR GKTVPEELVK PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG 

       250        260        270        280        290        300 
GADKNVVVFD KSSEQILATL KGHTKKVTSV VFHPSQDLVF SASPDATIRI WSVPNASCVQ 

       310        320        330        340        350        360 
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG CSLTCAQFHP 

       370        380        390        400        410        420 
DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF SENGYYLATA ADDSSVKLWD 

       430        440        450        460        470        480 
LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL ALGGTDVQIY ICKQWTEILH FTEHSGLTTG 

       490        500 
VAFGHHAKFI ASTGMDRSLK FYSL 

« Hide

References

« Hide 'large scale' references
[1]"hNMP 200: a novel human common nuclear matrix protein combining structural and regulatory functions."
Gotzmann J., Gerner C., Meissner M., Holzmann K., Grimm R., Mikulits W., Sauermann G.
Exp. Cell Res. 261:166-179(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-40; 100-115; 179-187; 192-199 AND 334-342, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CHROMOSOMAL LOCATION.
Tissue: Cervix.
[2]"Role of human Pso4 in mammalian DNA repair and association with terminal deoxynucleotidyl transferase."
Mahajan K.N., Mitchell B.S.
Proc. Natl. Acad. Sci. U.S.A. 100:10746-10751(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH DNTT.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[4]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 77-93; 101-115; 193-206; 209-236; 252-261 AND 266-303, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-27; 33-56; 63-93; 101-115; 193-206; 209-261; 266-303; 344-375 AND 429-439, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[6]"Reassembling proteins and chaperones in human nuclear matrix protein fractions."
Gerner C., Holzmann K., Meissner M., Gotzmann J., Grimm R., Sauermann G.
J. Cell. Biochem. 74:145-151(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 32-40, TISSUE SPECIFICITY.
Tissue: Peripheral blood.
[7]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[9]"SNEV is an evolutionarily conserved splicing factor whose oligomerization is necessary for spliceosome assembly."
Grillari J., Ajuh P., Stadler G., Loescher M., Voglauer R., Ernst W., Chusainow J., Eisenhaber F., Pokar M., Fortschegger K., Grey M., Lamond A.I., Katinger H.
Nucleic Acids Res. 33:6868-6883(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[10]"Interaction of U-box E3 ligase SNEV with PSMB4, the beta7 subunit of the 20 S proteasome."
Loescher M., Fortschegger K., Ritter G., Wostry M., Voglauer R., Schmid J.A., Watters S., Rivett A.J., Ajuh P., Lamond A.I., Katinger H., Grillari J.
Biochem. J. 388:593-603(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSMB4, FUNCTION.
[11]"The Pso4 mRNA splicing and DNA repair complex interacts with WRN for processing of DNA interstrand cross-links."
Zhang N., Kaur R., Lu X., Shen X., Li L., Legerski R.J.
J. Biol. Chem. 280:40559-40567(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[12]"SNEV overexpression extends the life span of human endothelial cells."
Voglauer R., Chang M.W.-F., Dampier B., Wieser M., Baumann K., Sterovsky T., Schreiber M., Katinger H., Grillari J.
Exp. Cell Res. 312:746-759(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process."
Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G.
Mol. Cell. Biol. 29:1834-1854(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122 AND LYS-261, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Molecular architecture of the human Prp19/CDC5L complex."
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., Fischle W., Urlaub H., Luhrmann R.
Mol. Cell. Biol. 30:2105-2119(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CDC5L; PLRG1 AND BCAS2.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly."
Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C., Blanchette M., Le Hir H.
Nat. Struct. Mol. Biol. 19:983-990(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CWC22 AND EIF4A3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131186 mRNA. Translation: CAB51857.1.
BC008719 mRNA. Translation: AAH08719.1.
BC018665 mRNA. Translation: AAH18665.1.
BC018698 mRNA. Translation: AAH18698.1.
CCDSCCDS7995.1.
RefSeqNP_055317.1. NM_014502.4.
UniGeneHs.502705.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG8X-ray1.89A169-504[»]
ProteinModelPortalQ9UMS4.
SMRQ9UMS4. Positions 3-55, 195-504.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118151. 104 interactions.
IntActQ9UMS4. 31 interactions.
MINTMINT-1454442.
STRING9606.ENSP00000227524.

PTM databases

PhosphoSiteQ9UMS4.

Polymorphism databases

DMDM55976619.

2D gel databases

REPRODUCTION-2DPAGEIPI00004968.
SWISS-2DPAGEQ9UMS4.

Proteomic databases

MaxQBQ9UMS4.
PaxDbQ9UMS4.
PeptideAtlasQ9UMS4.
PRIDEQ9UMS4.

Protocols and materials databases

DNASU27339.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227524; ENSP00000227524; ENSG00000110107.
GeneID27339.
KEGGhsa:27339.
UCSCuc001nqf.3. human.

Organism-specific databases

CTD27339.
GeneCardsGC11M060658.
HGNCHGNC:17896. PRPF19.
HPACAB012448.
HPA038051.
MIM608330. gene.
neXtProtNX_Q9UMS4.
PharmGKBPA134941355.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000177308.
HOVERGENHBG053697.
InParanoidQ9UMS4.
KOK10599.
OMAQWQELKV.
OrthoDBEOG7K9K2R.
PhylomeDBQ9UMS4.
TreeFamTF105919.

Enzyme and pathway databases

SignaLinkQ9UMS4.

Gene expression databases

ArrayExpressQ9UMS4.
BgeeQ9UMS4.
CleanExHS_PRPF19.
GenevestigatorQ9UMS4.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR013915. Pre-mRNA_splic_Prp19.
IPR000772. Ricin_B_lectin.
IPR003613. Ubox_domain.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF08606. Prp19. 1 hit.
PF04564. U-box. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00504. Ubox. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS51698. U_BOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPRPF19.
GenomeRNAi27339.
NextBio50404.
PROQ9UMS4.
SOURCESearch...

Entry information

Entry namePRP19_HUMAN
AccessionPrimary (citable) accession number: Q9UMS4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM