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Q9UMS4

- PRP19_HUMAN

UniProt

Q9UMS4 - PRP19_HUMAN

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Protein

Pre-mRNA-processing factor 19

Gene

PRPF19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity).By similarity11 Publications2 Publications

Pathwayi

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. identical protein binding Source: BHF-UCL
  3. ubiquitin-protein transferase activity Source: MGI
  4. ubiquitin-ubiquitin ligase activity Source: MGI

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. protein polyubiquitination Source: MGI
  4. spliceosomal complex assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, mRNA processing, mRNA splicing, Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.
SignaLinkiQ9UMS4.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing factor 19Curated (EC:6.3.2.-1 Publication)
Alternative name(s):
Nuclear matrix protein 2001 Publication
PRP19/PSO4 homolog1 Publication
Short name:
hPso41 Publication
Senescence evasion factor1 Publication
Gene namesi
Name:PRPF19Imported
Synonyms:NMP2001 Publication, PRP191 Publication, SNEV1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:17896. PRPF19.

Subcellular locationi

Nucleus 4 Publications. Nucleusnucleoplasm 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Cytoplasm 1 Publication. Lipid droplet By similarity
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. Recruited on damaged DNA at sites of double-strand break.2 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: MGI
  3. cytoskeleton Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nuclear speck Source: BHF-UCL
  6. nucleus Source: UniProtKB
  7. Prp19 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Lipid droplet, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi405 – 4051Y → A: Loss of interaction with the RPA complex and loss of recruitment to sites of DNA damage. 1 Publication

Organism-specific databases

PharmGKBiPA134941355.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 504503Pre-mRNA-processing factor 19PRO_0000051145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine4 Publications
Modified residuei122 – 1221N6-acetyllysine1 Publication
Modified residuei179 – 1791N6-acetyllysineBy similarity
Modified residuei244 – 2441N6-acetyllysineBy similarity
Modified residuei261 – 2611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UMS4.
PaxDbiQ9UMS4.
PeptideAtlasiQ9UMS4.
PRIDEiQ9UMS4.

2D gel databases

REPRODUCTION-2DPAGEIPI00004968.
SWISS-2DPAGEQ9UMS4.

PTM databases

PhosphoSiteiQ9UMS4.

Expressioni

Tissue specificityi

Ubiquitous. Weakly expressed in senescent cells of different tissue origins. Highly expressed in tumor cell lines.5 Publications

Inductioni

By gamma irradiation and chemical mutagens but not by UV irradiation.1 Publication

Gene expression databases

BgeeiQ9UMS4.
CleanExiHS_PRPF19.
ExpressionAtlasiQ9UMS4. baseline and differential.
GenevestigatoriQ9UMS4.

Organism-specific databases

HPAiCAB012448.
HPA038051.

Interactioni

Subunit structurei

Homotetramer. Component of the Prp19 complex/PRP19C/Nineteen complex/NTC and related complexes described as PRP19-CDC5L splicing complex and PSO4 complex. A homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2 constitute the core of those complexes. The interaction with CDC5L, PLRG1 and BCAS2 is direct within this core complex. At least three less stably associated proteins CTNNBL1, CWC15 and HSPA8 are found in the Prp19 complex. The Prp19 complex associates with the spliceosome during its assembly and remodeling recruiting additional proteins. Component of the XAB2 complex, a multimeric protein complex composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE. Interacts with CWC22 and EIF4A3 in an RNA-independent manner. Interacts with RPA1 and RPA2; the PRP19-CDC5L complex is recruited to the sites of DNA repair where it interacts with the replication protein A complex (RPA). Interacts with SETMAR; required for SETMAR recruitment to site of DNA damage. Interacts with U2AF2; the interaction is direct and recruits the Prp19 complex to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA. Interacts with PRPF3. Interacts with APEX1, DNTT and PSMB4. Interacts with PSMC5 (By similarity). Interacts with KNSTRN (PubMed:24718257). Interacts (via N-terminus) with CDC5L (By similarity).By similarity14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAS2O759342EBI-395746,EBI-1050106
CDC40O605082EBI-395746,EBI-2557812
CDC5LQ994592EBI-395746,EBI-374880
PRPF8Q6P2Q92EBI-395746,EBI-538479
RBM10P981752EBI-395746,EBI-721525
RBM5P527568EBI-395746,EBI-714003

Protein-protein interaction databases

BioGridi118151. 111 interactions.
IntActiQ9UMS4. 32 interactions.
MINTiMINT-1454442.
STRINGi9606.ENSP00000227524.

Structurei

Secondary structure

1
504
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi201 – 2044Combined sources
Beta strandi208 – 2136Combined sources
Beta strandi219 – 2213Combined sources
Beta strandi224 – 2307Combined sources
Beta strandi233 – 2419Combined sources
Beta strandi246 – 2505Combined sources
Turni251 – 2544Combined sources
Beta strandi255 – 2606Combined sources
Beta strandi269 – 2724Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi288 – 2925Combined sources
Turni293 – 2964Combined sources
Beta strandi297 – 3026Combined sources
Beta strandi309 – 3146Combined sources
Beta strandi318 – 3258Combined sources
Beta strandi328 – 3347Combined sources
Turni335 – 3373Combined sources
Beta strandi340 – 3456Combined sources
Turni347 – 3493Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi362 – 3698Combined sources
Beta strandi374 – 3785Combined sources
Turni379 – 3824Combined sources
Beta strandi383 – 3886Combined sources
Beta strandi395 – 4006Combined sources
Beta strandi404 – 4118Combined sources
Beta strandi414 – 4207Combined sources
Turni421 – 4244Combined sources
Beta strandi425 – 4317Combined sources
Beta strandi438 – 4436Combined sources
Beta strandi447 – 46115Combined sources
Turni462 – 4654Combined sources
Beta strandi466 – 4716Combined sources
Beta strandi474 – 4763Combined sources
Beta strandi478 – 4836Combined sources
Helixi485 – 4873Combined sources
Beta strandi490 – 4945Combined sources
Beta strandi499 – 5035Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LG8X-ray1.89A169-504[»]
ProteinModelPortaliQ9UMS4.
SMRiQ9UMS4. Positions 3-55, 195-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 7372U-boxAdd
BLAST
Repeati219 – 25941WD 1Add
BLAST
Repeati262 – 30140WD 2Add
BLAST
Repeati304 – 34542WD 3Add
BLAST
Repeati348 – 38740WD 4Add
BLAST
Repeati390 – 42940WD 5Add
BLAST
Repeati433 – 47240WD 6Add
BLAST
Repeati473 – 50331WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 223156May mediate interaction with PSMC5By similarityAdd
BLAST

Domaini

The 7 WD repeats are necessary and sufficient to support interaction with the RPA complex.1 Publication

Sequence similaritiesi

Belongs to the WD repeat PRP19 family.Curated
Contains 1 U-box domain.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00770000120537.
HOGENOMiHOG000177308.
HOVERGENiHBG053697.
InParanoidiQ9UMS4.
KOiK10599.
OMAiQWQELKV.
OrthoDBiEOG7K9K2R.
PhylomeDBiQ9UMS4.
TreeFamiTF105919.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR020472. 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]
PfamiPF08606. Prp19. 1 hit.
PF04564. U-box. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00504. Ubox. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS51698. U_BOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UMS4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLICSISNE VPEHPCVSPV SNHVYERRLI EKYIAENGTD PINNQPLSEE
60 70 80 90 100
QLIDIKVAHP IRPKPPSATS IPAILKALQD EWDAVMLHSF TLRQQLQTTR
110 120 130 140 150
QELSHALYQH DAACRVIARL TKEVTAAREA LATLKPQAGL IVPQAVPSSQ
160 170 180 190 200
PSVVGAGEPM DLGELVGMTP EIIQKLQDKA TVLTTERKKR GKTVPEELVK
210 220 230 240 250
PEELSKYRQV ASHVGLHSAS IPGILALDLC PSDTNKILTG GADKNVVVFD
260 270 280 290 300
KSSEQILATL KGHTKKVTSV VFHPSQDLVF SASPDATIRI WSVPNASCVQ
310 320 330 340 350
VVRAHESAVT GLSLHATGDY LLSSSDDQYW AFSDIQTGRV LTKVTDETSG
360 370 380 390 400
CSLTCAQFHP DGLIFGTGTM DSQIKIWDLK ERTNVANFPG HSGPITSIAF
410 420 430 440 450
SENGYYLATA ADDSSVKLWD LRKLKNFKTL QLDNNFEVKS LIFDQSGTYL
460 470 480 490 500
ALGGTDVQIY ICKQWTEILH FTEHSGLTTG VAFGHHAKFI ASTGMDRSLK

FYSL
Length:504
Mass (Da):55,181
Last modified:May 1, 2000 - v1
Checksum:iB34C37496E8AA032
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131186 mRNA. Translation: CAB51857.1.
BC008719 mRNA. Translation: AAH08719.1.
BC018665 mRNA. Translation: AAH18665.1.
BC018698 mRNA. Translation: AAH18698.1.
CCDSiCCDS7995.1.
RefSeqiNP_055317.1. NM_014502.4.
UniGeneiHs.502705.

Genome annotation databases

EnsembliENST00000227524; ENSP00000227524; ENSG00000110107.
GeneIDi27339.
KEGGihsa:27339.
UCSCiuc001nqf.3. human.

Polymorphism databases

DMDMi55976619.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ131186 mRNA. Translation: CAB51857.1 .
BC008719 mRNA. Translation: AAH08719.1 .
BC018665 mRNA. Translation: AAH18665.1 .
BC018698 mRNA. Translation: AAH18698.1 .
CCDSi CCDS7995.1.
RefSeqi NP_055317.1. NM_014502.4.
UniGenei Hs.502705.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LG8 X-ray 1.89 A 169-504 [» ]
ProteinModelPortali Q9UMS4.
SMRi Q9UMS4. Positions 3-55, 195-504.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118151. 111 interactions.
IntActi Q9UMS4. 32 interactions.
MINTi MINT-1454442.
STRINGi 9606.ENSP00000227524.

PTM databases

PhosphoSitei Q9UMS4.

Polymorphism databases

DMDMi 55976619.

2D gel databases

REPRODUCTION-2DPAGE IPI00004968.
SWISS-2DPAGE Q9UMS4.

Proteomic databases

MaxQBi Q9UMS4.
PaxDbi Q9UMS4.
PeptideAtlasi Q9UMS4.
PRIDEi Q9UMS4.

Protocols and materials databases

DNASUi 27339.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227524 ; ENSP00000227524 ; ENSG00000110107 .
GeneIDi 27339.
KEGGi hsa:27339.
UCSCi uc001nqf.3. human.

Organism-specific databases

CTDi 27339.
GeneCardsi GC11M060658.
HGNCi HGNC:17896. PRPF19.
HPAi CAB012448.
HPA038051.
MIMi 608330. gene.
neXtProti NX_Q9UMS4.
PharmGKBi PA134941355.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00770000120537.
HOGENOMi HOG000177308.
HOVERGENi HBG053697.
InParanoidi Q9UMS4.
KOi K10599.
OMAi QWQELKV.
OrthoDBi EOG7K9K2R.
PhylomeDBi Q9UMS4.
TreeFami TF105919.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_467. mRNA Splicing - Major Pathway.
SignaLinki Q9UMS4.

Miscellaneous databases

ChiTaRSi PRPF19. human.
GeneWikii PRPF19.
GenomeRNAii 27339.
NextBioi 50404.
PROi Q9UMS4.
SOURCEi Search...

Gene expression databases

Bgeei Q9UMS4.
CleanExi HS_PRPF19.
ExpressionAtlasi Q9UMS4. baseline and differential.
Genevestigatori Q9UMS4.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProi IPR020472. 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 ]
Pfami PF08606. Prp19. 1 hit.
PF04564. U-box. 1 hit.
PF00400. WD40. 5 hits.
[Graphical view ]
PRINTSi PR00320. GPROTEINBRPT.
SMARTi SM00504. Ubox. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS51698. U_BOX. 1 hit.
PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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.
  10. "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.
  11. "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.
  12. "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, IDENTIFICATION AS A COMPONENT OF THE PSO4 COMPLEX.
  13. Cited for: FUNCTION, TISSUE SPECIFICITY.
  14. "Mouse homologue of yeast Prp19 interacts with mouse SUG1, the regulatory subunit of 26S proteasome."
    Sihn C.R., Cho S.Y., Lee J.H., Lee T.R., Kim S.H.
    Biochem. Biophys. Res. Commun. 356:175-180(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription, and transcription-coupled repair."
    Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y., Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.
    J. Biol. Chem. 283:940-950(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION AS PART OF THE XAB2 COMPLEX.
  16. "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair."
    Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.
    J. Biol. Chem. 283:9023-9030(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SETMAR, SUBCELLULAR LOCATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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].
  19. "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.
  20. "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].
  21. "The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome."
    Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D., Harper J.W., Elledge S.J., Kirschner M.W., Rape M.
    Genes Dev. 24:1434-1447(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRPF3.
  22. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CDC5L; PLRG1 AND BCAS2.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "The RNA polymerase II C-terminal domain promotes splicing activation through recruitment of a U2AF65-Prp19 complex."
    David C.J., Boyne A.R., Millhouse S.R., Manley J.L.
    Genes Dev. 25:972-983(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH U2AF2.
  25. "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].
  26. "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.
  27. "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry."
    Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., Jimenez A.E., Jin J., Zou L.
    Mol. Cell 53:235-246(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPA1 AND RPA2, DOMAIN, MUTAGENESIS OF TYR-405.
  28. "Crystal structure of PRPF19 WD40 repeats."
    Structural genomics consortium (SGC)
    Submitted (JUN-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 169-504.
  29. "Small kinetochore associated protein (SKAP) promotes UV-induced cell apoptosis through negatively regulating pre-mRNA processing factor 19 (Prp19)."
    Lu S., Wang R., Cai C., Liang J., Xu L., Miao S., Wang L., Song W.
    PLoS ONE 9:E92712-E92712(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KNSTRN.

Entry informationi

Entry nameiPRP19_HUMAN
AccessioniPrimary (citable) accession number: Q9UMS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 2000
Last modified: November 26, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3