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Protein

Pre-mRNA-processing factor 19

Gene

PRP19

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable ubiquitin-protein ligase involved in pre-mRNA splicing. Acts as a central component of the NTC complex (or PRP19-associated complex) that associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation. It is also probably involved in DNA repair.1 Publication

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: UniProtKB
  • ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  • DNA repair Source: UniProtKB-KW
  • generation of catalytic spliceosome for first transesterification step Source: SGD
  • protein K63-linked ubiquitination Source: UniProtKB
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

BioCyciYEAST:G3O-32139-MONOMER.
BRENDAi2.3.2.B10. 984.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-processing factor 19Curated (EC:6.3.2.-1 Publication)
Gene namesi
Name:PRP19
Synonyms:PSO4
Ordered Locus Names:YLL036C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL036C.
SGDiS000003959. PRP19.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
  • Prp19 complex Source: SGD
  • U2-type catalytic step 1 spliceosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503Pre-mRNA-processing factor 19PRO_0000058587Add
BLAST

Proteomic databases

MaxQBiP32523.
PeptideAtlasiP32523.

PTM databases

iPTMnetiP32523.

Interactioni

Subunit structurei

Homotetramer. Component of the NTC complex (or PRP19-associated complex), composed of at least CEF1, CLF1, ISY1, NTC20, SNT309, SYF1, SYF2, and PRP19. The NTC complex associates with the spliceosome after the release of the U1 and U4 snRNAs and forms the CWC spliceosome subcomplex (or CEF1-associated complex) reminiscent of a late-stage spliceosome composed also of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, LEA1, MSL1, PRP8, PRP9, PRP11, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNU114, SPP2, RSE1 and YJU2. Interacts with CLF1, ISY1, NTC20, PRP19, PRP46, SYF1 and SYF2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC40P409687EBI-493,EBI-13834
CEF1Q036548EBI-493,EBI-476
CLF1Q123099EBI-493,EBI-484
CWC2Q120469EBI-493,EBI-553
ISY1P213746EBI-493,EBI-9382
NTC20P383025EBI-493,EBI-20921
SNT309Q060917EBI-493,EBI-818
SYF1Q040486EBI-493,EBI-540
SYF2P532774EBI-493,EBI-23308
URN1Q065257EBI-493,EBI-35138
USB1Q122083EBI-493,EBI-31589

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31217. 163 interactions.
DIPiDIP-1112N.
IntActiP32523. 58 interactions.
MINTiMINT-632220.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 63Combined sources
Beta strandi11 – 166Combined sources
Turni17 – 204Combined sources
Beta strandi21 – 244Combined sources
Helixi25 – 3511Combined sources
Turni39 – 413Combined sources
Helixi47 – 493Combined sources
Beta strandi179 – 1879Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi197 – 2004Combined sources
Beta strandi202 – 21615Combined sources
Beta strandi219 – 22911Combined sources
Beta strandi231 – 2377Combined sources
Beta strandi247 – 2515Combined sources
Beta strandi256 – 2616Combined sources
Turni262 – 2643Combined sources
Beta strandi265 – 2706Combined sources
Turni271 – 2733Combined sources
Beta strandi276 – 2816Combined sources
Beta strandi288 – 2925Combined sources
Beta strandi301 – 3066Combined sources
Beta strandi311 – 3199Combined sources
Beta strandi321 – 3255Combined sources
Beta strandi335 – 3384Combined sources
Beta strandi344 – 3485Combined sources
Beta strandi354 – 3607Combined sources
Beta strandi377 – 3826Combined sources
Beta strandi386 – 40116Combined sources
Beta strandi409 – 4113Combined sources
Beta strandi424 – 4285Combined sources
Beta strandi432 – 4398Combined sources
Turni440 – 4434Combined sources
Beta strandi444 – 4507Combined sources
Turni452 – 4543Combined sources
Beta strandi456 – 4649Combined sources
Beta strandi476 – 4827Combined sources
Beta strandi485 – 4917Combined sources
Beta strandi493 – 50210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N87NMR-A1-56[»]
2BAYX-ray1.50A/B/C/D/E/F1-58[»]
3LRVX-ray2.60A165-503[»]
ProteinModelPortaliP32523.
SMRiP32523. Positions 1-57, 171-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32523.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7171U-boxAdd
BLAST
Repeati328 – 36740WD 1Add
BLAST
Repeati372 – 41039WD 2Add
BLAST
Repeati418 – 45841WD 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 14488Required for self-associationAdd
BLAST
Regioni76 – 13459Interaction with CEF1Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat PRP19 family.Curated
Contains 1 U-box domain.Curated
Contains 3 WD repeats.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

HOGENOMiHOG000115709.
InParanoidiP32523.
KOiK10599.
OMAiYSHENVK.
OrthoDBiEOG7V76GC.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR013915. Pre-mRNA_splic_Prp19.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR003613. Ubox_domain.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08606. Prp19. 1 hit.
[Graphical view]
SMARTiSM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
PROSITEiPS51698. U_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32523-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLCAISGKVP RRPVLSPKSR TIFEKSLLEQ YVKDTGNDPI TNEPLSIEEI
60 70 80 90 100
VEIVPSAQQA SLTESTNSAT LKANYSIPNL LTSLQNEWDA IMLENFKLRS
110 120 130 140 150
TLDSLTKKLS TVMYERDAAK LVAAQLLMEK NEDSKDLPKS SQQAVAITRE
160 170 180 190 200
EFLQGLLQSS RDFVARGKLK APKWPILKNL ELLQAQNYSR NIKTFPYKEL
210 220 230 240 250
NKSMYYDKWV CMCRCEDGAL HFTQLKDSKT ITTITTPNPR TGGEHPAIIS
260 270 280 290 300
RGPCNRLLLL YPGNQITILD SKTNKVLREI EVDSANEIIY MYGHNEVNTE
310 320 330 340 350
YFIWADNRGT IGFQSYEDDS QYIVHSAKSD VEYSSGVLHK DSLLLALYSP
360 370 380 390 400
DGILDVYNLS SPDQASSRFP VDEEAKIKEV KFADNGYWMV VECDQTVVCF
410 420 430 440 450
DLRKDVGTLA YPTYTIPEFK TGTVTYDIDD SGKNMIAYSN ESNSLTIYKF
460 470 480 490 500
DKKTKNWTKD EESALCLQSD TADFTDMDVV CGDGGIAAIL KTNDSFNIVA

LTP
Length:503
Mass (Da):56,570
Last modified:October 1, 1996 - v2
Checksum:iA44D8C7DD6F64185
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391Missing in AAA34912 (PubMed:8441419).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09721 Genomic DNA. Translation: AAA34912.1.
X99770 Genomic DNA. Translation: CAA68103.1.
Z73142 Genomic DNA. Translation: CAA97487.1.
BK006945 Genomic DNA. Translation: DAA09285.1.
PIRiS64787.
RefSeqiNP_013064.1. NM_001181856.1.

Genome annotation databases

EnsemblFungiiYLL036C; YLL036C; YLL036C.
GeneIDi850623.
KEGGisce:YLL036C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09721 Genomic DNA. Translation: AAA34912.1.
X99770 Genomic DNA. Translation: CAA68103.1.
Z73142 Genomic DNA. Translation: CAA97487.1.
BK006945 Genomic DNA. Translation: DAA09285.1.
PIRiS64787.
RefSeqiNP_013064.1. NM_001181856.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N87NMR-A1-56[»]
2BAYX-ray1.50A/B/C/D/E/F1-58[»]
3LRVX-ray2.60A165-503[»]
ProteinModelPortaliP32523.
SMRiP32523. Positions 1-57, 171-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31217. 163 interactions.
DIPiDIP-1112N.
IntActiP32523. 58 interactions.
MINTiMINT-632220.

PTM databases

iPTMnetiP32523.

Proteomic databases

MaxQBiP32523.
PeptideAtlasiP32523.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL036C; YLL036C; YLL036C.
GeneIDi850623.
KEGGisce:YLL036C.

Organism-specific databases

EuPathDBiFungiDB:YLL036C.
SGDiS000003959. PRP19.

Phylogenomic databases

HOGENOMiHOG000115709.
InParanoidiP32523.
KOiK10599.
OMAiYSHENVK.
OrthoDBiEOG7V76GC.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciYEAST:G3O-32139-MONOMER.
BRENDAi2.3.2.B10. 984.

Miscellaneous databases

EvolutionaryTraceiP32523.
NextBioi966526.
PROiP32523.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR013915. Pre-mRNA_splic_Prp19.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR003613. Ubox_domain.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF08606. Prp19. 1 hit.
[Graphical view]
SMARTiSM00504. Ubox. 1 hit.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
PROSITEiPS51698. U_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PRP19: a novel spliceosomal component."
    Cheng S.C., Tarn W.Y., Tsao T.Y., Abelson J.
    Mol. Cell. Biol. 13:1876-1882(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Allelism of PSO4 and PRP19 links pre-mRNA processing with recombination and error-prone DNA repair in Saccharomyces cerevisiae."
    Grey M., Duesterhoeft A., Henriques J.A.P., Brendel M.
    Nucleic Acids Res. 24:4009-4014(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The yeast PRP19 protein is not tightly associated with small nuclear RNAs, but appears to associate with the spliceosome after binding of U2 to the pre-mRNA and prior to formation of the functional spliceosome."
    Tarn W.Y., Lee K.R., Cheng S.C.
    Mol. Cell. Biol. 13:1883-1891(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Functional association of essential splicing factor(s) with PRP19 in a protein complex."
    Tarn W.Y., Hsu C.H., Huang K.T., Chen H.R., Kao H.Y., Lee K.R., Cheng S.C.
    EMBO J. 13:2421-2431(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, IDENTIFICATION IN THE PRP19-ASSOCIATED COMPLEX.
  7. "Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs."
    Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.
    Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Structural and functional analysis of essential pre-mRNA splicing factor Prp19p."
    Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Ren L., Hirsch J.P., Chazin W.J., Walz T., Gould K.L.
    Mol. Cell. Biol. 25:451-460(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TETRAMERIZATION, ELECTRON MICROSCOPY OF THE TETRAMER, INTERACTION WITH CEF1.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structural insights into the U-box, a domain associated with multi-ubiquitination."
    Ohi M.D., Vander Kooi C.W., Rosenberg J.A., Chazin W.J., Gould K.L.
    Nat. Struct. Biol. 10:250-255(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-56, FUNCTION, CATALYTIC ACTIVITY, PATHWAY.

Entry informationi

Entry nameiPRP19_YEAST
AccessioniPrimary (citable) accession number: P32523
Secondary accession number(s): D6VXW9, Q07870
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 11700 molecules/cell in log phase SD medium.1 Publication
The tetramer is an elongated particle consisting of four globular WD40 domains held together by a central stalk.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.