ID MSL5_YEAST STANDARD; PRT; 476 AA. AC Q12186; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-JUN-2006, entry version 37. DE Branchpoint-bridging protein MSL5 (MUD synthesis lethal 5 protein). GN Name=MSL5; OrderedLocusNames=YLR116W; 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=S288c / 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=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 LEVEL OF PROTEIN EXPRESSION. 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). 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. CC -!- SUBUNIT: Interacts with MUD2 and PRP40. 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 -!- MISCELLANEOUS: Present with 4380 molecules/cell. 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 PIR; S64953; S64953. DR HSSP; Q9BW01; 1K1G. DR IntAct; Q12186; -. 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. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0003723; F:RNA binding; IDA. DR GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IPI. 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 Repeat; RNA-binding; Zinc; Zinc-finger. FT CHAIN 1 476 Branchpoint-bridging protein MSL5. 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 230 230 G->S: In msl-5; loss of function. 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 //