BBP_YEAST
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 03-AUG-2022, entry version 167.
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 Q12186; 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}.
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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 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 AlphaFoldDB; Q12186; -.
DR SMR; Q12186; -.
DR BioGRID; 31388; 284.
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 SGD; S000004106; MSL5.
DR VEuPathDB; FungiDB:YLR116W; -.
DR eggNOG; KOG0119; Eukaryota.
DR GeneTree; ENSGT00940000157258; -.
DR HOGENOM; CLU_016864_1_1_1; -.
DR InParanoid; Q12186; -.
DR OMA; HYNSNTH; -.
DR BioCyc; YEAST:G3O-32261-MON; -.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:SGD.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000245; P:spliceosomal complex assembly; IC:ComplexPortal.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
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; PTHR11208; 1.
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 REGION 83..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|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:0007829|PDB:4WAN"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 164..169
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4WAN"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:4WAN"
FT TURN 206..209
FT /evidence="ECO:0007829|PDB:4WAN"
FT STRAND 212..223
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 224..242
FT /evidence="ECO:0007829|PDB:4WAN"
FT HELIX 250..262
FT /evidence="ECO:0007829|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
