ID BBP_YEAST Reviewed; 476 AA. AC Q12186; D6VYB4; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 05-APR-2011, entry version 82. DE RecName: Full=Branchpoint-bridging protein; DE AltName: Full=Mud synthetic-lethal 5 protein; DE AltName: Full=Splicing factor 1; DE AltName: Full=Zinc finger protein BBP; GN Name=MSL5; Synonyms=BBP, SF1; OrderedLocusNames=YLR116W; GN ORFNames=L2949; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; 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 GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RG Saccharomyces Genome Database; RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 [9] RP INTERACTION WITH SMY2 AND SYH1. 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). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; SER-376 AND RP SER-378, AND MASS SPECTROMETRY. RX PubMed=17563356; DOI=10.1073/pnas.0701622104; RA Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; RT "Proteome-wide identification of in vivo targets of DNA damage RT checkpoint kinases."; RL Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; SER-376 AND RP SER-378, AND MASS SPECTROMETRY. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). 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 domains of SMY2 and SYH1. CC -!- INTERACTION: CC Q02875:-; NbExp=1; IntAct=EBI-34012, EBI-33176; CC P36084:MUD2; NbExp=1; IntAct=EBI-34012, EBI-11612; CC P32909:SMY2; NbExp=1; IntAct=EBI-34012, EBI-17503; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 4380 molecules/cell in log phase SD CC medium. CC -!- SIMILARITY: Belongs to the BBP/SF1 family. CC -!- SIMILARITY: Contains 2 CCHC-type zinc fingers. CC -!- SIMILARITY: Contains 1 KH domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X89514; CAA61695.1; -; Genomic_DNA. DR EMBL; U53877; AAB82363.1; -; Genomic_DNA. DR EMBL; Z73288; CAA97683.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09430.1; -; Genomic_DNA. DR PIR; S64953; S64953. DR RefSeq; NP_013217.1; NM_001182003.1. DR PDB; 3FMA; X-ray; 2.50 A; L/M/N/O/P=440-450. DR PDBsum; 3FMA; -. DR ProteinModelPortal; Q12186; -. DR SMR; Q12186; 146-267, 270-316. DR DIP; DIP-991N; -. DR IntAct; Q12186; 26. DR MINT; MINT-489287; -. DR STRING; Q12186; -. DR EnsemblFungi; YLR116W; YLR116W; YLR116W. DR GeneID; 850807; -. DR NMPDR; fig|4932.3.peg.4209; -. DR CYGD; YLR116w; -. DR SGD; S000004106; MSL5. DR eggNOG; fuNOG06293; -. DR GeneTree; EFGT00050000001048; -. DR HOGENOM; HBG605582; -. DR OMA; PPASHIS; -. DR OrthoDB; EOG4HQHTF; -. DR PhylomeDB; Q12186; -. DR NextBio; 967037; -. DR ArrayExpress; Q12186; -. DR Genevestigator; Q12186; -. DR GermOnline; YLR116W; Saccharomyces cerevisiae. DR GO; GO:0000243; C:commitment complex; IDA:SGD. DR GO; GO:0030117; C:membrane coat; IEA:InterPro. DR GO; GO:0045131; F:pre-mRNA branch point binding; IDA:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IPI:SGD. DR GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro. DR InterPro; IPR013041; Clathrin/coatomer_app_Ig-like. DR InterPro; IPR004087; KH. DR InterPro; IPR018111; KH_type_1_subgr. DR InterPro; IPR013084; Znf_CCH_retrovir. DR InterPro; IPR001878; Znf_CCHC. DR Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF00098; zf-CCHC; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00343; ZnF_C2HC; 2. DR SUPFAM; SSF49348; Clath_adapt; 1. DR PROSITE; PS50084; KH_TYPE_1; FALSE_NEG. DR PROSITE; PS50158; ZF_CCHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc; KW 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 MOD_RES 93 93 Phosphoserine. FT MOD_RES 95 95 Phosphoserine. FT MOD_RES 376 376 Phosphoserine. FT MOD_RES 378 378 Phosphoserine. 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 //