ID BBP_YEAST Reviewed; 476 AA.
AC Q12186;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 12-DEC-2006, entry version 41.
DE Branchpoint bridging protein (Splicing factor 1) (Zinc finger protein
DE BBP) (Mud synthetic-lethal 5 protein).
GN Name=MSL5; Synonyms=BBP, SF1; OrderedLocusNames=YLR116W;
GN ORFNames=L2949;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 90840 / EAY235 / FY23;
RX MEDLINE=97245294; PubMed=9090053;
RX DOI=10.1002/(SICI)1097-0061(19970315)13:3<241::AID-YEA61>3.0.CO;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6,
RT tRNA-Arg3 and 23 new open reading frames, among which several
RT homologies to proteins involved in cell division control and to
RT mammalian growth factors and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX MEDLINE=97313267; PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP FUNCTION, INTERACTION WITH MUD2 AND PRP40, AND MUTAGENESIS OF GLY-230.
RX PubMed=9150140; DOI=10.1016/S0092-8674(00)80221-4;
RA Abovich N., Rosbash M.;
RT "Cross-intron bridging interactions in the yeast commitment complex
RT are conserved in mammals.";
RL Cell 89:403-412(1997).
RN [4]
RP FUNCTION, AND INTERACTION WITH MUD2.
RX PubMed=10376880; DOI=10.1017/S1355838299982286;
RA Rutz B., Seraphin B.;
RT "Transient interaction of BBP/ScSF1 and Mud2 with the splicing
RT machinery affects the kinetics of spliceosome assembly.";
RL RNA 5:819-831(1999).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF ARG-60; ILE-72; PRO-155; VAL-195 AND
RP GLU-258.
RX PubMed=10775271; DOI=10.1093/emboj/19.8.1873;
RA Rutz B., Seraphin B.;
RT "A dual role for BBP/ScSF1 in nuclear pre-mRNA retention and
RT splicing.";
RL EMBO J. 19:1873-1886(2000).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP INTERACTION WITH SMY2.
RX PubMed=16120600; DOI=10.1074/mcp.M500129-MCP200;
RA Kofler M., Motzny K., Freund C.;
RT "GYF domain proteomics reveals interaction sites in known and novel
RT target proteins.";
RL Mol. Cell. Proteomics 4:1797-1811(2005).
CC -!- FUNCTION: Required for pre-spliceosome formation, which is the
CC first step of pre-mRNA splicing. 2 commitment complexes, CC1 and
CC CC2, have been defined. CC1 is a basal complex dependent only on
CC the 5' splice site. CC2 is a complex of lower mobility and is
CC dependent on a branchpoint as well as a 5' splice site region.
CC This protein is involved in CC2 formation where it binds to the
CC snRNP U1-associated protein PRP40, bridging the U1 snRNP-
CC associated 5' splice site and the MSL5-associated branch point 3'
CC intron splice site. Involved in nuclear retention of pre-mRNA.
CC -!- SUBUNIT: Interacts with MUD2 and PRP40. The proline-rich sequence
CC of this protein interacts with the GYF domain of SMY2.
CC -!- INTERACTION:
CC P36084:MUD2; NbExp=1; IntAct=EBI-34012, EBI-11612;
CC P32909:SMY2; NbExp=1; IntAct=EBI-34012, EBI-17503;
CC Q02875:YPL105C; NbExp=1; IntAct=EBI-34012, EBI-33176;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 4380 molecules/cell.
CC -!- SIMILARITY: Contains 2 CCHC-type zinc fingers.
CC -!- SIMILARITY: Contains 1 KH domain.
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DR EMBL; X89514; CAA61695.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82363.1; -; Genomic_DNA.
DR EMBL; Z73288; CAA97683.1; -; Genomic_DNA.
DR PIR; S64953; S64953.
DR HSSP; Q9BW01; 1K1G.
DR DIP; DIP:991N; -.
DR IntAct; Q12186; -.
DR GermOnline; YLR116W; Saccharomyces cerevisiae.
DR Ensembl; YLR116W; Saccharomyces cerevisiae.
DR GenomeReviews; Y13138_GR; YLR116W.
DR SGD; S000004106; MSL5.
DR LinkHub; Q12186; -.
DR GO; GO:0000243; C:commitment complex; IDA:SGD.
DR GO; GO:0005515; F:protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IPI:SGD.
DR InterPro; IPR004087; KH.
DR InterPro; IPR004088; KH_type_1.
DR InterPro; IPR001878; Znf_CCHC.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR PRINTS; PR00939; C2HCZNFINGER.
DR SMART; SM00322; KH; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR PROSITE; PS50084; KH_TYPE_1; FALSE_NEG.
DR PROSITE; PS50158; ZF_CCHC; 1.
KW Complete proteome; Metal-binding; mRNA processing; mRNA splicing;
KW Nuclear protein; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1 476 Branchpoint bridging protein.
FT /FTId=PRO_0000234564.
FT DOMAIN 153 219 KH.
FT ZN_FING 271 288 CCHC-type 1.
FT ZN_FING 297 314 CCHC-type 2.
FT COMPBIAS 363 474 Pro-rich.
FT MUTAGEN 60 60 R->G: In MSL5-2; temperature-sensitive;
FT growth defect; when associated with N-72
FT and S-155.
FT MUTAGEN 72 72 I->N: In MSL5-2; temperature-sensitive;
FT growth defect; when associated with G-60
FT and S-155.
FT MUTAGEN 155 155 P->S: In MSL5-2; temperature-sensitive;
FT growth defect; when associated with G-60
FT and N-72.
FT MUTAGEN 195 195 V->D: In MSL5-5; cold-sensitive; growth
FT defect; when associated with V-258.
FT MUTAGEN 230 230 G->S: In msl-5; loss of function.
FT MUTAGEN 258 258 E->V: In MSL5-5; cold-sensitive; growth
FT defect; when associated with D-195.
SQ SEQUENCE 476 AA; 53034 MW; F94FF7175345C47D CRC64;
MSFRRINSRY FENRKGSSME EKKAKVPPNV NLSLWRKNTV ESDVHRFNSL PSKISGALTR
EQIYSYQVMF RIQEITIKLR TNDFVPPSRK NRSPSPPPVY DAQGKRTNTR EQRYRKKLED
ERIKLVEIAL KTIPYFVPPD DYKRPTKFQD KYYIPVDQYP DVNFVGLLLG PRGRTLRKLQ
EDSNCKIAIR GRGSVKEGKN ASDLPPGAMN FEDPLHCLII ADSEDKIQKG IKVCQNIVIK
AVTSPEGQND LKRGQLRELA ELNGTLREDN RPCPICGLKD HKRYDCPNRK IPNIQGIVCK
ICGQTGHFSR DCNSSSQRMS RFDRNATVNN SAPIQSNDVH YNSNTHPIQA PKRSRYDNNS
TEPPLKFPAS SRYAPSPSPP ASHISRQAQN VTPTPPPGLT SSSFSSGVPG IAPPPLQSPP
ESEQPKFSLP PPPGMTTVQS SIAPPPGLSG PPGFSNNMGN DINKPTPPGL QGPPGL
//