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Reviewed, UniProtKB/Swiss-Prot P33203 (PRP40_YEAST)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pre-mRNA-processing protein PRP40
Gene names
Name: PRP40
Ordered Locus Names: YKL012W
ORF Names: YKL165
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for pre-spliceosome formation, which is the first step of pre-mRNA splicing. This protein is associated with snRNP U1. Two commitment complexes, CC1 and CC2, have been defined in yeast. CC1 is a basal complex dependent only on the 5' splice site. CC2 is a complex of lower mobility and is dependent on a branchpoint as well as a 5' splice site region. This protein is involved in CC2 formation where it binds to the branchpoint binding protein MSL5, bridging the U1 snRNP-associated 5' splice site and the MSL5-associated branch point 3' intron splice site. Ref.5 Ref.6 Ref.7

Subunit structure

Interacts with CRM1, MSL5, PRP8, and the RNA polymerase II largest subunit (RPB1). MSL5, MUD2 and PRP40 interact to form the commitment complex 2 (CC2), a precursor of mature spliceosomes. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus. Ref.7

Domain

The WW and FF domains bind to the phosphorylated carboxy-terminal domain of RPB1.

Sequence similarities

Belongs to the PRPF40 family.

Contains 4 FF domains.

Contains 2 WW domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   DomainRepeat
   Molecular functionRibonucleoprotein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processnuclear mRNA splicing, via spliceosome Ref.4

Inferred from direct assay. Source: SGD

   Cellular componentsnRNP U1

Inferred from direct assay. Source: SGD

   Molecular functionRNA binding Ref.4

Inferred from direct assay. Source: SGD

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

O135501EBI-701,EBI-35936
P103561EBI-701,EBI-22726
P255611EBI-701,EBI-21696
P255761EBI-701,EBI-21752
P256171EBI-701,EBI-375711
P380811EBI-701,EBI-21453
P387161EBI-701,EBI-24682
P387291EBI-701,EBI-24394
P387581EBI-701,EBI-24443
P388871EBI-701,EBI-24252
P404831EBI-701,EBI-25176
P471371EBI-701,EBI-25572
P471481EBI-701,EBI-25619
P532651EBI-701,EBI-23264
P538641EBI-701,EBI-29179
Q043361EBI-701,EBI-27435
Q065221EBI-701,EBI-37313
Q122981EBI-701,EBI-34580
AAT2P235421EBI-701,EBI-2002
ABZ1P372541EBI-701,EBI-12831
ACR2Q065971EBI-701,EBI-2117
ADE12P802101EBI-701,EBI-14267
AIP1P466801EBI-701,EBI-2406
AMD1P152741EBI-701,EBI-2548
ARP2P323811EBI-701,EBI-2927
BNA5Q059791EBI-701,EBI-10016
CMD1P067871EBI-701,EBI-3976
COX17Q122871EBI-701,EBI-5086
CTF4Q014541EBI-701,EBI-5209
DOG2P387731EBI-701,EBI-6028
DPS1P048021EBI-701,EBI-18655
ELP2P429351EBI-701,EBI-23459
EMP24P328031EBI-701,EBI-6431
ENO2P009251EBI-701,EBI-6475
ERG24P324621EBI-701,EBI-6502
FMP40Q089681EBI-701,EBI-29375
FSP2P530511EBI-701,EBI-10464
GND1P387201EBI-701,EBI-1965
GPH1P067381EBI-701,EBI-13389
GSF2Q046971EBI-701,EBI-27807
GUS1P466551EBI-701,EBI-18665
HCR1Q057751EBI-701,EBI-8944
HEM13P113531EBI-701,EBI-8257
HFD1Q044581EBI-701,EBI-27205
HTD2P387901EBI-701,EBI-24577
IDI1P154961EBI-701,EBI-8902
IDP3P539821EBI-701,EBI-8892
INP51P405591EBI-701,EBI-24915
LAH1P333991EBI-701,EBI-10046
LYS1P389981EBI-701,EBI-10264
LYS21Q121221EBI-701,EBI-8508
MAL32P381581EBI-701,EBI-10326
MCR1P360601EBI-701,EBI-10565
MDH3P324191EBI-701,EBI-10598
MDM35O602001EBI-701,EBI-2080774
MEF1P250391EBI-701,EBI-6353
MES1P009581EBI-701,EBI-18762
MET12P461511EBI-701,EBI-11567
MET7Q086451EBI-701,EBI-7058
MGE1P385231EBI-701,EBI-7891
MLS1P309521EBI-701,EBI-10428
MVP1P409591EBI-701,EBI-11636
NGL3Q032101EBI-701,EBI-27960
NPL3Q015601EBI-701,EBI-12114
NPT1P396831EBI-701,EBI-12218
OYE2Q035581EBI-701,EBI-12729
PAI3P010941EBI-701,EBI-9305
PAN5P387871EBI-701,EBI-12913
PCK1P109631EBI-701,EBI-13770
PEX30Q061691EBI-701,EBI-31008
PFK2P168621EBI-701,EBI-9435
PHR1P050661EBI-701,EBI-13385
PRP2P200951EBI-701,EBI-13820
PTP1P250441EBI-701,EBI-14183
PYC1P111541EBI-701,EBI-14358
RNR4P497231EBI-701,EBI-15251
RPB8P204361EBI-701,EBI-15794
RPS14AP063671EBI-701,EBI-14460
RUB1Q039191EBI-701,EBI-37695
SIP2P341641EBI-701,EBI-17187
SLM5P253451EBI-701,EBI-18781
SNU71P532071EBI-701,EBI-736
SSA2P105921EBI-701,EBI-8603
STM1P390151EBI-701,EBI-11238
STR3P531011EBI-701,EBI-24097
TCP1P126121EBI-701,EBI-19045
TES1P419031EBI-701,EBI-14154
TGL4P361651EBI-701,EBI-26531
THI80P352021EBI-701,EBI-19195
THS1P048011EBI-701,EBI-18814
TIF34P402171EBI-701,EBI-8951
TKL1P232541EBI-701,EBI-19291
UBP10P538741EBI-701,EBI-19873
UBP15P501011EBI-701,EBI-19898
VMA13P418071EBI-701,EBI-20281
VPS66Q065081EBI-701,EBI-36961
YDL086WQ075051EBI-701,EBI-5951
YEL047CP326141EBI-701,EBI-22366
YJR149WP471771EBI-701,EBI-25740
YNL045WQ107401EBI-701,EBI-10175
YPT11P485591EBI-701,EBI-29362

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Pre-mRNA-processing protein PRP40
PRO_0000076084

Regions

Domain1 – 3131WW 1
Domain42 – 7231WW 2
Domain134 – 18552FF 1
Domain203 – 25452FF 2
Domain357 – 41054FF 3
Domain494 – 54956FF 4

Amino acid modifications

Modified residue5761Phosphothreonine Ref.8
Modified residue5831Phosphotyrosine Ref.8

Experimental info

Mutagenesis2401S → P in PRP40-1 suppressor; affects SAR1 mRNA accumulation in U1-U4 mutant at 18 degrees Celsius. Ref.4
Mutagenesis2741L → A: Temperature sensitive growth at 36 degrees Celsius. Ref.7
Mutagenesis2771L → A: Temperature sensitive growth at 36 degrees Celsius. Ref.7
Mutagenesis2811L → A: Temperature sensitive growth at 36 degrees Celsius. Ref.7
Mutagenesis3401L → A: Wild-type growth at 36 degrees Celsius. Ref.7
Mutagenesis3441L → A: Wild-type growth at 36 degrees Celsius. Ref.7
Mutagenesis3471L → I: Wild-type growth at 36 degrees Celsius. Ref.7

Secondary structure

....................... 583
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33203-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: BA1C1C91D532524C

FASTA58369,065
        10         20         30         40         50         60 
MSIWKEAKDA SGRIYYYNTL TKKSTWEKPK ELISQEELLL RENGWKAAKT ADGKVYYYNP 

        70         80         90        100        110        120 
TTRETSWTIP AFEKKVEPIA EQKHDTVSHA QVNGNRIALT AGEKQEPGRT INEEESQYAN 

       130        140        150        160        170        180 
NSKLLNVRRR TKEEAEKEFI TMLKENQVDS TWSFSRIISE LGTRDPRYWM VDDDPLWKKE 

       190        200        210        220        230        240 
MFEKYLSNRS ADQLLKEHNE TSKFKEAFQK MLQNNSHIKY YTRWPTAKRL IADEPIYKHS 

       250        260        270        280        290        300 
VVNEKTKRQT FQDYIDTLID TQKESKKKLK TQALKELREY LNGIITTSSS ETFITWQQLL 

       310        320        330        340        350        360 
NHYVFDKSKR YMANRHFKVL THEDVLNEYL KIVNTIENDL QNKLNELRLR NYTRDRIARD 

       370        380        390        400        410        420 
NFKSLLREVP IKIKANTRWS DIYPHIKSDP RFLHMLGRNG SSCLDLFLDF VDEQRMYIFA 

       430        440        450        460        470        480 
QRSIAQQTLI DQNFEWNDAD SDEITKQNIE KVLENDRKFD KVDKEDISLI VDGLIKQRNE 

       490        500        510        520        530        540 
KIQQKLQNER RILEQKKHYF WLLLQRTYTK TGKPKPSTWD LASKELGESL EYKALGDEDN 

       550        560        570        580 
IRRQIFEDFK PESSAPTAES ATANLTLTAS KKRHLTPAVE LDY 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of a 9.3 kb segment located on the left arm of the yeast chromosome XI reveals five open reading frames including the CCE1 gene and putative products related to MYO2 and to the ribosomal protein L10."
Pascolo S., Ghazvini M., Boyer J., Colleaux L., Thierry A., Dujon B.
Yeast 8:987-995(1992) [PubMed: 1481574] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed: 8196765] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry."
Neubauer G., Gottschalk A., Fabrizio P., Seraphin B., Luehrmann R., Mann M.
Proc. Natl. Acad. Sci. U.S.A. 94:385-390(1997) [PubMed: 9012791] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[4]"Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle."
Kao H.-Y., Siliciano P.G.
Mol. Cell. Biol. 16:960-967(1996) [PubMed: 8622699] [Abstract]
Cited for: IDENTIFICATION, MUTAGENESIS OF SER-240.
[5]"Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals."
Abovich N., Rosbash M.
Cell 89:403-412(1997) [PubMed: 9150140] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MSL5; MUD2 AND PRP8.
[6]"The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II."
Morris D.P., Greenleaf A.L.
J. Biol. Chem. 275:39935-39943(2000) [PubMed: 10978320] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RPB1.
[7]"The yeast splicing factor Prp40p contains functional leucine-rich nuclear export signals that are essential for splicing."
Murphy M.W., Olson B.L., Siliciano P.G.
Genetics 166:53-65(2004) [PubMed: 15020406] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CRM1, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-274; LEU-277; LEU-281; LEU-340; LEU-344 AND LEU-347.
[8]"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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-576 AND TYR-583, MASS SPECTROMETRY.
[9]"Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40."
Wiesner S., Stier G., Sattler M., Macias M.J.
J. Mol. Biol. 324:807-822(2002) [PubMed: 12460579] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-75.
+Additional computationally mapped references.

Cross-references

Sequence databases

S53418 Genomic DNA. Translation: AAB24902.1.
Z28012 Genomic DNA. Translation: CAA81847.1.
PIRS30014.
RefSeqNP_012913.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1O6WNMR-A1-75[»]
2B7ENMR-A134-189[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1620N.
IntActP33203. 123 interactions.

Genome annotation databases

EnsemblYKL012W. Saccharomyces cerevisiae. [Contig view]
GeneID853857.
GenomeReviewsGene locus YKL012W in contig Y13137_GR.
KEGGsce:YKL012W.
NMPDRfig|4932.3.peg.3899.

Organism-specific databases

CYGDYKL012w.
SGDS000001495. PRP40.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP33203.
OMAP33203. VDSTWSF.

Gene expression databases

ArrayExpressP33203.
GermOnlineYKL012W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002713. FF_domain.
IPR001202. WW_Rsp5_WWP.
[Graphical view]
Gene3DG3DSA:1.10.10.440. FF. 1 hit.
PfamPF01846. FF. 4 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00441. FF. 4 hits.
SM00456. WW. 2 hits.
[Graphical view]
PROSITEPS01159. WW_DOMAIN_1. 2 hits.
PS50020. WW_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio975100.

Entry information

Entry namePRP40_YEAST
AccessionPrimary (citable) accession number: P33203
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents