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 26-FEB-2020, entry version 156. 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; ORFNames=L2949; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 90840 / EAY235 / FY23; RX 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, tRNA- RT Arg3 and 23 new open reading frames, among which several homologies to RT proteins involved in cell division control and to mammalian growth factors RT and other animal proteins are found."; RL Yeast 13:241-250(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., 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; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). 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 are RT 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 machinery RT 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 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 splicing."; RL EMBO J. 19:1873-1886(2000). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX 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 PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA 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 target RT proteins."; RL Mol. Cell. Proteomics 4:1797-1811(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95; TYR-100 AND RP SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Required for pre-spliceosome formation, which is the first CC step of pre-mRNA splicing. 2 commitment complexes, CC1 and CC2, have CC been defined. CC1 is a basal complex dependent only on the 5'-splice CC site. CC2 is a complex of lower mobility and is dependent on a CC branchpoint as well as a 5'-splice site region. This protein is CC involved in CC2 formation where it binds to the snRNP U1-associated CC protein PRP40, bridging the U1 snRNP-associated 5'-splice site and the CC MSL5-associated branch point 3' intron splice site. Involved in nuclear CC retention of pre-mRNA. {ECO:0000269|PubMed:10376880, CC ECO:0000269|PubMed:10775271, ECO:0000269|PubMed:9150140}. CC -!- SUBUNIT: Interacts with MUD2 and PRP40. The proline-rich sequence of CC this protein interacts with the GYF domains of SMY2 and SYH1. CC {ECO:0000269|PubMed:10376880, ECO:0000269|PubMed:16120600, CC ECO:0000269|PubMed:9150140}. CC -!- INTERACTION: CC P36084:MUD2; NbExp=5; IntAct=EBI-34012, EBI-11612; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC -!- MISCELLANEOUS: Present with 4380 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}. 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 PDB; 4WAL; X-ray; 2.20 A; A=144-271. DR PDB; 4WAN; X-ray; 1.80 A; A/C/E/G=144-271. DR PDBsum; 3FMA; -. DR PDBsum; 4WAL; -. DR PDBsum; 4WAN; -. DR SMR; Q12186; -. DR BioGrid; 31388; 262. DR ComplexPortal; CPX-1417; BBP-MUD2 branchpoint-binding complex. DR DIP; DIP-991N; -. DR IntAct; Q12186; 6. DR MINT; Q12186; -. DR STRING; 4932.YLR116W; -. DR iPTMnet; Q12186; -. DR MaxQB; Q12186; -. DR PaxDb; Q12186; -. DR PRIDE; Q12186; -. DR EnsemblFungi; YLR116W_mRNA; YLR116W; YLR116W. DR GeneID; 850807; -. DR KEGG; sce:YLR116W; -. DR EuPathDB; FungiDB:YLR116W; -. DR SGD; S000004106; MSL5. DR HOGENOM; CLU_016864_1_1_1; -. DR InParanoid; Q12186; -. DR KO; K13095; -. DR OMA; HYNSNTH; -. DR BioCyc; YEAST:G3O-32261-MONOMER; -. DR EvolutionaryTrace; Q12186; -. DR PRO; PR:Q12186; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; Q12186; protein. DR GO; GO:0000243; C:commitment complex; IDA:SGD. DR GO; GO:0005829; C:cytosol; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0045131; F:pre-mRNA branch point binding; IDA:SGD. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD. DR Gene3D; 3.30.1370.10; -; 1. DR InterPro; IPR031150; BBP/SF1. DR InterPro; IPR013041; Clathrin_app_Ig-like_sf. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR032570; SF1-HH. DR InterPro; IPR001878; Znf_CCHC. DR InterPro; IPR036875; Znf_CCHC_sf. DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF16275; SF1-HH; 1. DR Pfam; PF00098; zf-CCHC; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00343; ZnF_C2HC; 2. DR SUPFAM; SSF49348; SSF49348; 1. DR SUPFAM; SSF54791; SSF54791; 1. DR SUPFAM; SSF57756; SSF57756; 1. DR PROSITE; PS50158; ZF_CCHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. FT CHAIN 1..476 FT /note="Branchpoint-bridging protein" FT /id="PRO_0000234564" FT DOMAIN 153..219 FT /note="KH" FT ZN_FING 271..288 FT /note="CCHC-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT ZN_FING 297..314 FT /note="CCHC-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT COMPBIAS 363..474 FT /note="Pro-rich" FT MOD_RES 93 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198" FT MOD_RES 100 FT /note="Phosphotyrosine" FT /evidence="ECO:0000244|PubMed:19779198" FT MOD_RES 382 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:19779198" FT MUTAGEN 60 FT /note="R->G: In MSL5-2; temperature-sensitive; growth FT defect; when associated with N-72 and S-155." FT /evidence="ECO:0000269|PubMed:10775271" FT MUTAGEN 72 FT /note="I->N: In MSL5-2; temperature-sensitive; growth FT defect; when associated with G-60 and S-155." FT /evidence="ECO:0000269|PubMed:10775271" FT MUTAGEN 155 FT /note="P->S: In MSL5-2; temperature-sensitive; growth FT defect; when associated with G-60 and N-72." FT /evidence="ECO:0000269|PubMed:10775271" FT MUTAGEN 195 FT /note="V->D: In MSL5-5; cold-sensitive; growth defect; when FT associated with V-258." FT /evidence="ECO:0000269|PubMed:10775271" FT MUTAGEN 230 FT /note="G->S: In msl-5; loss of function." FT /evidence="ECO:0000269|PubMed:9150140" FT MUTAGEN 258 FT /note="E->V: In MSL5-5; cold-sensitive; growth defect; when FT associated with D-195." FT /evidence="ECO:0000269|PubMed:10775271" FT STRAND 148..153 FT /evidence="ECO:0000244|PDB:4WAN" FT TURN 156..158 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 164..169 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 171..173 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 174..183 FT /evidence="ECO:0000244|PDB:4WAN" FT STRAND 186..192 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 201..203 FT /evidence="ECO:0000244|PDB:4WAN" FT TURN 206..209 FT /evidence="ECO:0000244|PDB:4WAN" FT STRAND 212..223 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 224..242 FT /evidence="ECO:0000244|PDB:4WAN" FT HELIX 250..262 FT /evidence="ECO:0000244|PDB:4WAN" 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 //