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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1002/yea.320081109; PubMed=1481574 [NCBI, ExPASy, EBI, Israel, Japan]
Pascolo S.,
Ghazvini M.,
Boyer J.,
Colleaux L.,
Thierry A.,
Dujon B.;
"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.";
Yeast 8:987-995(1992).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
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.,
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.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
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[3]
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PARTIAL PROTEIN SEQUENCE.
DOI=10.1073/pnas.94.2.385; PubMed=9012791 [NCBI, ExPASy, EBI, Israel, Japan]
Neubauer G.,
Gottschalk A.,
Fabrizio P.,
Seraphin B.,
Luehrmann R.,
Mann M.;
"Identification of the proteins of the yeast U1 small nuclear ribonucleoprotein complex by mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 94:385-390(1997).
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[4]
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IDENTIFICATION, AND MUTAGENESIS OF SER-240.
PubMed=8622699 [NCBI, ExPASy, EBI, Israel, Japan]
Kao H.-Y.,
Siliciano P.G.;
"Identification of Prp40, a novel essential yeast splicing factor associated with the U1 small nuclear ribonucleoprotein particle.";
Mol. Cell. Biol. 16:960-967(1996).
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[5]
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FUNCTION, AND INTERACTION WITH MSL5; MUD2 AND PRP8.
DOI=10.1016/S0092-8674(00)80221-4; PubMed=9150140 [NCBI, ExPASy, EBI, Israel, Japan]
Abovich N.,
Rosbash M.;
"Cross-intron bridging interactions in the yeast commitment complex are conserved in mammals.";
Cell 89:403-412(1997).
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[6]
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FUNCTION, AND INTERACTION WITH RPB1.
DOI=10.1074/jbc.M004118200; PubMed=10978320 [NCBI, ExPASy, EBI, Israel, Japan]
Morris D.P.,
Greenleaf A.L.;
"The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II.";
J. Biol. Chem. 275:39935-39943(2000).
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[7]
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FUNCTION, INTERACTION WITH CRM1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-274; LEU-277; LEU-281; LEU-340; LEU-344 AND LEU-347.
DOI=10.1534/genetics.166.1.53; PubMed=15020406 [NCBI, ExPASy, EBI, Israel, Japan]
Murphy M.W.,
Olson B.L.,
Siliciano P.G.;
"The yeast splicing factor Prp40p contains functional leucine-rich nuclear export signals that are essential for splicing.";
Genetics 166:53-65(2004).
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[8]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-576 AND TYR-583, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P.,
Smolka M.B.,
Payne S.H.,
Bafna V.,
Eng J.,
Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
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[9]
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STRUCTURE BY NMR OF 1-75.
DOI=10.1016/S0022-2836(02)01145-2; PubMed=12460579 [NCBI, ExPASy, EBI, Israel, Japan]
Wiesner S.,
Stier G.,
Sattler M.,
Macias M.J.;
"Solution structure and ligand recognition of the WW domain pair of the yeast splicing factor Prp40.";
J. Mol. Biol. 324:807-822(2002).
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- 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.
- SUBUNIT: 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.
- INTERACTION:
O13550:-; NbExp=1; IntAct=EBI-701, EBI-35936;
P10356:-; NbExp=1; IntAct=EBI-701, EBI-22726;
P25561:-; NbExp=1; IntAct=EBI-701, EBI-21696;
P25576:-; NbExp=1; IntAct=EBI-701, EBI-21752;
P25617:-; NbExp=1; IntAct=EBI-701, EBI-375711;
P38081:-; NbExp=1; IntAct=EBI-701, EBI-21453;
P38716:-; NbExp=1; IntAct=EBI-701, EBI-24682;
P38729:-; NbExp=1; IntAct=EBI-701, EBI-24394;
P38758:-; NbExp=1; IntAct=EBI-701, EBI-24443;
P38887:-; NbExp=1; IntAct=EBI-701, EBI-24252;
P40483:-; NbExp=1; IntAct=EBI-701, EBI-25176;
P47137:-; NbExp=1; IntAct=EBI-701, EBI-25572;
P47148:-; NbExp=1; IntAct=EBI-701, EBI-25619;
P47177:-; NbExp=1; IntAct=EBI-701, EBI-25740;
P53265:-; NbExp=1; IntAct=EBI-701, EBI-23264;
P53864:-; NbExp=1; IntAct=EBI-701, EBI-29179;
Q04336:-; NbExp=1; IntAct=EBI-701, EBI-27435;
Q04458:-; NbExp=1; IntAct=EBI-701, EBI-27205;
Q06522:-; NbExp=1; IntAct=EBI-701, EBI-37313;
Q08968:-; NbExp=1; IntAct=EBI-701, EBI-29375;
Q12298:-; NbExp=1; IntAct=EBI-701, EBI-34580;
P23542:AAT2; NbExp=1; IntAct=EBI-701, EBI-2002;
P37254:ABZ1; NbExp=1; IntAct=EBI-701, EBI-12831;
Q06597:ACR2; NbExp=1; IntAct=EBI-701, EBI-2117;
P80210:ADE12; NbExp=1; IntAct=EBI-701, EBI-14267;
P46680:AIP1; NbExp=1; IntAct=EBI-701, EBI-2406;
P15274:AMD1; NbExp=1; IntAct=EBI-701, EBI-2548;
P32381:ARP2; NbExp=1; IntAct=EBI-701, EBI-2927;
Q05979:BNA5; NbExp=1; IntAct=EBI-701, EBI-10016;
P12612:CCT1; NbExp=1; IntAct=EBI-701, EBI-19045;
P06787:CMD1; NbExp=1; IntAct=EBI-701, EBI-3976;
Q12287:COX17; NbExp=1; IntAct=EBI-701, EBI-5086;
Q01454:CTF4; NbExp=1; IntAct=EBI-701, EBI-5209;
P38773:DOG2; NbExp=1; IntAct=EBI-701, EBI-6028;
P04802:DPS1; NbExp=1; IntAct=EBI-701, EBI-18655;
P42935:ELP2; NbExp=1; IntAct=EBI-701, EBI-23459;
P32803:EMP24; NbExp=1; IntAct=EBI-701, EBI-6431;
P00925:ENO2; NbExp=1; IntAct=EBI-701, EBI-6475;
P32462:ERG24; NbExp=1; IntAct=EBI-701, EBI-6502;
P53051:FSP2; NbExp=1; IntAct=EBI-701, EBI-10464;
P38720:GND1; NbExp=1; IntAct=EBI-701, EBI-1965;
P06738:GPH1; NbExp=1; IntAct=EBI-701, EBI-13389;
Q04697:GSF2; NbExp=1; IntAct=EBI-701, EBI-27807;
P46655:GUS1; NbExp=1; IntAct=EBI-701, EBI-18665;
Q05775:HCR1; NbExp=1; IntAct=EBI-701, EBI-8944;
P11353:HEM13; NbExp=1; IntAct=EBI-701, EBI-8257;
P38790:HTD2; NbExp=1; IntAct=EBI-701, EBI-24577;
P15496:IDI1; NbExp=1; IntAct=EBI-701, EBI-8902;
P53982:IDP3; NbExp=1; IntAct=EBI-701, EBI-8892;
P33399:LAH1; NbExp=1; IntAct=EBI-701, EBI-10046;
P38998:LYS1; NbExp=1; IntAct=EBI-701, EBI-10264;
Q12122:LYS21; NbExp=1; IntAct=EBI-701, EBI-8508;
P38158:MAL32; NbExp=1; IntAct=EBI-701, EBI-10326;
P36060:MCR1; NbExp=1; IntAct=EBI-701, EBI-10565;
P32419:MDH3; NbExp=1; IntAct=EBI-701, EBI-10598;
P25039:MEF1; NbExp=1; IntAct=EBI-701, EBI-6353;
P00958:MES1; NbExp=1; IntAct=EBI-701, EBI-18762;
P46151:MET12; NbExp=1; IntAct=EBI-701, EBI-11567;
Q08645:MET7; NbExp=1; IntAct=EBI-701, EBI-7058;
P38523:MGE1; NbExp=1; IntAct=EBI-701, EBI-7891;
P30952:MLS1; NbExp=1; IntAct=EBI-701, EBI-10428;
P40959:MVP1; NbExp=1; IntAct=EBI-701, EBI-11636;
Q03210:NGL3; NbExp=1; IntAct=EBI-701, EBI-27960;
Q01560:NOP3; NbExp=1; IntAct=EBI-701, EBI-12114;
P39683:NPT1; NbExp=1; IntAct=EBI-701, EBI-12218;
Q03558:OYE2; NbExp=1; IntAct=EBI-701, EBI-12729;
P01094:PAI3; NbExp=1; IntAct=EBI-701, EBI-9305;
P38787:PAN5; NbExp=1; IntAct=EBI-701, EBI-12913;
P10963:PCK1; NbExp=1; IntAct=EBI-701, EBI-13770;
Q06169:PEX30; NbExp=1; IntAct=EBI-701, EBI-31008;
P16862:PFK2; NbExp=1; IntAct=EBI-701, EBI-9435;
P05066:PHR1; NbExp=1; IntAct=EBI-701, EBI-13385;
P20095:PRP2; NbExp=1; IntAct=EBI-701, EBI-13820;
P25044:PTP1; NbExp=1; IntAct=EBI-701, EBI-14183;
P11154:PYC1; NbExp=1; IntAct=EBI-701, EBI-14358;
P49723:RNR4; NbExp=1; IntAct=EBI-701, EBI-15251;
P20436:RPB8; NbExp=1; IntAct=EBI-701, EBI-15794;
P06367:RPS14A; NbExp=1; IntAct=EBI-701, EBI-14460;
Q03919:RUB1; NbExp=1; IntAct=EBI-701, EBI-37695;
P34164:SIP2; NbExp=1; IntAct=EBI-701, EBI-17187;
P25345:SLM5; NbExp=1; IntAct=EBI-701, EBI-18781;
P53207:SNU71; NbExp=1; IntAct=EBI-701, EBI-736;
P10592:SSA2; NbExp=1; IntAct=EBI-701, EBI-8603;
P39015:STM1; NbExp=1; IntAct=EBI-701, EBI-11238;
P53101:STR3; NbExp=1; IntAct=EBI-701, EBI-24097;
P41903:TES1; NbExp=1; IntAct=EBI-701, EBI-14154;
P36165:TGL4; NbExp=1; IntAct=EBI-701, EBI-26531;
P35202:THI80; NbExp=1; IntAct=EBI-701, EBI-19195;
P04801:THS1; NbExp=1; IntAct=EBI-701, EBI-18814;
P40217:TIF34; NbExp=1; IntAct=EBI-701, EBI-8951;
P23254:TKL1; NbExp=1; IntAct=EBI-701, EBI-19291;
P53874:UBP10; NbExp=1; IntAct=EBI-701, EBI-19873;
P50101:UBP15; NbExp=1; IntAct=EBI-701, EBI-19898;
P41807:VMA13; NbExp=1; IntAct=EBI-701, EBI-20281;
Q06508:VPS66; NbExp=1; IntAct=EBI-701, EBI-36961;
Q07505:YDL086W; NbExp=1; IntAct=EBI-701, EBI-5951;
P32614:YEL047C; NbExp=1; IntAct=EBI-701, EBI-22366;
P40559:YIL002C; NbExp=1; IntAct=EBI-701, EBI-24915;
Q10740:YNL045W; NbExp=1; IntAct=EBI-701, EBI-10175;
P48559:YPT11; NbExp=1; IntAct=EBI-701, EBI-29362;
- SUBCELLULAR LOCATION: Nucleus.
- DOMAIN: The WW and FF domains bind to the phosphorylated carboxy-terminal domain of RPB1.
- SIMILARITY: Belongs to the PRPF40 family.
- SIMILARITY: Contains 4 FF domains.
- SIMILARITY: Contains 2 WW domains.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 583 AA [This is the length of the unprocessed precursor] |
Molecular weight: 69065 Da [This is the MW of the unprocessed precursor] |
CRC64: BA1C1C91D532524C [This is a checksum on the sequence] |
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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
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P33203 in FASTA format |
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