ID SF3B1_HUMAN Reviewed; 1304 AA. AC O75533; E9PCH3; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 3. DT 27-MAR-2024, entry version 217. DE RecName: Full=Splicing factor 3B subunit 1; DE AltName: Full=Pre-mRNA-splicing factor SF3b 155 kDa subunit; DE Short=SF3b155 {ECO:0000303|Ref.39}; DE AltName: Full=Spliceosome-associated protein 155 {ECO:0000303|PubMed:9585501}; DE Short=SAP 155 {ECO:0000303|PubMed:9585501}; GN Name=SF3B1 {ECO:0000303|PubMed:30567737, ECO:0000312|HGNC:HGNC:10768}; GN Synonyms=SAP155 {ECO:0000303|PubMed:9585501}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION. RX PubMed=9585501; DOI=10.1101/gad.12.10.1409; RA Wang C., Chua K., Seghezzi W., Lees E., Gozani O., Reed R.; RT "Phosphorylation of spliceosomal protein SAP 155 coupled with splicing RT catalysis."; RL Genes Dev. 12:1409-1414(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Woessner J., Tan F., Marra M., Kucaba T., Yandell M., Martin J., Marth G., RA Bowles L., Wylie T., Bowers Y., Steptoe M., Theising B., Geisel S., RA Allen M., Underwood K., Chappell J., Person B., Gibbons M., Harvey N., RA Pape D., Chamberlain A., Morales R., Schurk R., Ritter E., Kohn S., RA Swaller T., Behymer K., Hillier L., Wilson R., Waterston R.; RT "Full clone sequencing of the longest available member from each UniGene RT cluster."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1011-1304 (ISOFORM 1). RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP CHARACTERIZATION OF THE SPLICEOSOME. RX PubMed=10882114; DOI=10.1016/s1097-2765(00)80318-4; RA Das R., Zhou Z., Reed R.; RT "Functional association of U2 snRNP with the ATP-independent spliceosomal RT complex E."; RL Mol. Cell 5:779-787(2000). RN [6] RP IDENTIFICATION IN THE SF3B COMPLEX. RX PubMed=12234937; DOI=10.1093/emboj/cdf480; RA Will C.L., Urlaub H., Achsel T., Gentzel M., Wilm M., Luehrmann R.; RT "Characterization of novel SF3b and 17S U2 snRNP proteins, including a RT human Prp5p homologue and an SF3b DEAD-box protein."; RL EMBO J. 21:4978-4988(2002). RN [7] RP SUBCELLULAR LOCATION, INTERACTION WITH PPP1R8, PHOSPHORYLATION AT THR-244; RP THR-248 AND THR-313, AND MUTAGENESIS OF THR-223; THR-227; THR-235; THR-244; RP THR-248; THR-257; THR-261; THR-267; THR-273; THR-278; THR-296; THR-303 AND RP THR-313. RX PubMed=12105215; DOI=10.1074/jbc.m204427200; RA Boudrez A., Beullens M., Waelkens E., Stalmans W., Bollen M.; RT "Phosphorylation-dependent interaction between the splicing factors SAP155 RT and NIPP1."; RL J. Biol. Chem. 277:31834-31841(2002). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [9] RP IDENTIFICATION IN THE SF3B COMPLEX, AND ELECTRON MICROSCOPY OF THE SF3B RP COMPLEX. RX PubMed=12738865; DOI=10.1126/science.1084155; RA Golas M.M., Sander B., Will C.L., Luhrmann R., Stark H.; RT "Molecular architecture of the multiprotein splicing factor SF3b."; RL Science 300:980-984(2003). RN [10] RP IDENTIFICATION IN A COMPLEX WITH THE MINOR SPLICEOSOME, FUNCTION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15146077; DOI=10.1261/rna.7320604; RA Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., RA Tuschl T., Luehrmann R.; RT "The human 18S U11/U12 snRNP contains a set of novel proteins not found in RT the U2-dependent spliceosome."; RL RNA 10:929-941(2004). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-211; THR-223; THR-296 AND RP THR-299, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [12] RP IDENTIFICATION IN THE B-WICH COMPLEX. RX PubMed=16603771; DOI=10.1074/jbc.m600233200; RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.; RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear RT proteins in transcription."; RL J. Biol. Chem. 281:16264-16271(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211 AND THR-328, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142 AND THR-223, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-223 AND THR-267, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-142; SER-194; RP THR-207; THR-211; THR-223; THR-227; THR-326; THR-328; SER-332 AND SER-488, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; THR-211; THR-223; RP THR-227; THR-326; THR-341; SER-349; THR-350; SER-400; THR-434 AND THR-436, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-554 AND LYS-562, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-194; THR-203; RP THR-207; THR-211; THR-223; THR-326; THR-328 AND SER-488, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [23] RP INTERACTION WITH SETX. RX PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026; RA Skourti-Stathaki K., Proudfoot N.J., Gromak N.; RT "Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause RT sites to promote Xrn2-dependent termination."; RL Mol. Cell 42:794-805(2011). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-211; THR-341; RP SER-344; SER-349 AND THR-354, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [25] RP INTERACTION WITH PQBP1. RX PubMed=23512658; DOI=10.1101/gad.212308.112; RA Wang Q., Moore M.J., Adelmant G., Marto J.A., Silver P.A.; RT "PQBP1, a factor linked to intellectual disability, affects alternative RT splicing associated with neurite outgrowth."; RL Genes Dev. 27:615-626(2013). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-129; THR-142; RP SER-194; THR-207; THR-211; THR-223; THR-227; THR-235; THR-257; THR-261; RP THR-267; THR-278; THR-296; THR-303; THR-313; SER-322; THR-326; SER-332; RP THR-350; THR-354; SER-400; THR-426; THR-434; THR-436 AND SER-488, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-211; THR-257; RP THR-261; THR-267; THR-273; THR-278; SER-287; THR-303; THR-313 AND SER-488, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [28] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [29] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [30] RP INTERACTION WITH RBM15. RX PubMed=26575292; DOI=10.7554/elife.07938; RA Zhang L., Tran N.T., Su H., Wang R., Lu Y., Tang H., Aoyagi S., Guo A., RA Khodadadi-Jamayran A., Zhou D., Qian K., Hricik T., Cote J., Han X., RA Zhou W., Laha S., Abdel-Wahab O., Levine R.L., Raffel G., Liu Y., Chen D., RA Li H., Townes T., Wang H., Deng H., Zheng Y.G., Leslie C., Luo M., Zhao X.; RT "Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 RT controls RNA splicing."; RL Elife 4:0-0(2015). RN [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SF3B COMPLEX, RP AND SUBCELLULAR LOCATION. RX PubMed=28541300; DOI=10.1038/ncomms15522; RA Teng T., Tsai J.H., Puyang X., Seiler M., Peng S., Prajapati S., Aird D., RA Buonamici S., Caleb B., Chan B., Corson L., Feala J., Fekkes P., Gerard B., RA Karr C., Korpal M., Liu X., Lowe J.T., Mizui Y., Palacino J., Park E., RA Smith P.G., Subramanian V., Wu Z.J., Zou J., Yu L., Chicas A., Warmuth M., RA Larsen N., Zhu P.; RT "Splicing modulators act at the branch point adenosine binding pocket RT defined by the PHF5A-SF3b complex."; RL Nat. Commun. 8:15522-15522(2017). RN [33] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-214; LYS-413 AND LYS-430, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [34] RP INTERACTION WITH USH1G, AND SUBCELLULAR LOCATION. RX PubMed=34023904; DOI=10.1093/nar/gkab386; RA Yildirim A., Mozaffari-Jovin S., Wallisch A.K., Schaefer J., Ludwig S.E.J., RA Urlaub H., Luehrmann R., Wolfrum U.; RT "SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear RT transfer of tri-snRNP complexes."; RL Nucleic Acids Res. 49:5845-5866(2021). RN [35] RP INTERACTION WITH SDE2; CACTIN AND U2AF1. RX PubMed=34365507; DOI=10.1093/nar/gkab647; RA Floro J., Dai A., Metzger A., Mora-Martin A., Ganem N.J., Cifuentes D., RA Wu C.S., Dalal J., Lyons S.M., Labadorf A., Flynn R.L.; RT "SDE2 is an essential gene required for ribosome biogenesis and the RT regulation of alternative splicing."; RL Nucleic Acids Res. 49:9424-9443(2021). RN [36] RP INTERACTION WITH CYREN. RX PubMed=37813856; DOI=10.1021/acs.biochem.3c00397; RA Xie L., Bowman M.E., Louie G.V., Zhang C., Ardejani M.S., Huang X., Chu Q., RA Donaldson C.J., Vaughan J.M., Shan H., Powers E.T., Kelly J.W., Lyumkis D., RA Noel J.P., Saghatelian A.; RT "Biochemistry and Protein Interactions of the CYREN Microprotein."; RL Biochemistry 0:0-0(2023). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 373-415 IN COMPLEX WITH SF3B6, RP AND INTERACTION WITH SF3B6. RX PubMed=16432215; DOI=10.1073/pnas.0508048103; RA Schellenberg M.J., Edwards R.A., Ritchie D.B., Kent O.A., Golas M.M., RA Stark H., Luhrmann R., Glover J.N., MacMillan A.M.; RT "Crystal structure of a core spliceosomal protein interface."; RL Proc. Natl. Acad. Sci. U.S.A. 103:1266-1271(2006). RN [38] RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 333-342 IN COMPLEX WITH RBM17, RP AND INTERACTION WITH RBM17. RX PubMed=17589525; DOI=10.1038/nsmb1260; RA Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., RA Sattler M.; RT "U2AF-homology motif interactions are required for alternative splicing RT regulation by SPF45."; RL Nat. Struct. Mol. Biol. 14:620-629(2007). RN [39] RP STRUCTURE BY NMR OF 379-424 IN COMPLEX WITH SF3B6. RG RIKEN structural genomics initiative (RSGI); RT "NMR solution structure of the human spliceosomal protein complex p14- RT SF3B155."; RL Submitted (JAN-2007) to the PDB data bank. RN [40] RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 377-415 IN COMPLEX WITH SF3B6, RP AND INTERACTION WITH SF3B6. RX PubMed=21062891; DOI=10.1261/rna.2224411; RA Schellenberg M.J., Dul E.L., MacMillan A.M.; RT "Structural model of the p14/SF3b155 - branch duplex complex."; RL RNA 17:155-165(2011). RN [41] RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 333-342 IN COMPLEX WITH RBM39, RP INTERACTION WITH RBM39, AND MUTAGENESIS OF TRP-200; TRP-218; TRP-232; RP TRP-254; TRP-293; TRP-310 AND TRP-338. RX PubMed=24795046; DOI=10.1074/jbc.m114.558825; RA Loerch S., Maucuer A., Manceau V., Green M.R., Kielkopf C.L.; RT "Cancer-relevant splicing factor CAPERalpha engages the essential splicing RT factor SF3b155 in a specific ternary complex."; RL J. Biol. Chem. 289:17325-17337(2014). RN [42] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SF3B3; SF3B5 AND RP PHF5A, FUNCTION, INTERACTION WITH SF3B3; SF3B5 AND PHF5A, IDENTIFICATION IN RP THE SF3B COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, RNA-BINDING, AND RP MUTAGENESIS OF LYS-700. RX PubMed=27720643; DOI=10.1016/j.molcel.2016.08.036; RA Cretu C., Schmitzova J., Ponce-Salvatierra A., Dybkov O., RA De Laurentiis E.I., Sharma K., Will C.L., Urlaub H., Luehrmann R., Pena V.; RT "Molecular architecture of SF3b and structural consequences of its cancer- RT related mutations."; RL Mol. Cell 64:307-319(2016). RN [43] {ECO:0007744|PDB:6N3E} RP X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) OF 291-297 IN COMPLEX WITH HTATSF1. RX PubMed=30567737; DOI=10.1074/jbc.ra118.006764; RA Loerch S., Leach J.R., Horner S.W., Maji D., Jenkins J.L., Pulvino M.J., RA Kielkopf C.L.; RT "The pre-mRNA splicing and transcription factor Tat-SF1 is a functional RT partner of the spliceosome SF3b1 subunit via a U2AF homology motif RT interface."; RL J. Biol. Chem. 294:2892-2902(2019). RN [44] {ECO:0007744|PDB:6Y50, ECO:0007744|PDB:6Y53, ECO:0007744|PDB:6Y5Q} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=32494006; DOI=10.1038/s41586-020-2344-3; RA Zhang Z., Will C.L., Bertram K., Dybkov O., Hartmuth K., Agafonov D.E., RA Hofele R., Urlaub H., Kastner B., Luehrmann R., Stark H.; RT "Molecular architecture of the human 17S U2 snRNP."; RL Nature 583:310-313(2020). RN [45] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), FUNCTION, AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). RN [46] {ECO:0007744|PDB:7Q3L} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=34822310; DOI=10.1126/science.abm4245; RA Tholen J., Razew M., Weis F., Galej W.P.; RT "Structural basis of branch site recognition by the human spliceosome."; RL Science 375:50-57(2022). RN [47] {ECO:0007744|PDB:8HK1} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=36797247; DOI=10.1038/s41467-023-36489-x; RA Yang F., Bian T., Zhan X., Chen Z., Xing Z., Larsen N.A., Zhang X., Shi Y.; RT "Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP RT assembly."; RL Nat. Commun. 14:897-897(2023). CC -!- FUNCTION: Component of the 17S U2 SnRNP complex of the spliceosome, a CC large ribonucleoprotein complex that removes introns from transcribed CC pre-mRNAs (PubMed:12234937, PubMed:27720643, PubMed:32494006, CC PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in CC early spliceosome assembly and (2) mediates recognition of the intron CC branch site during pre-mRNA splicing by promoting the selection of the CC pre-mRNA branch-site adenosine, the nucleophile for the first step of CC splicing (PubMed:32494006, PubMed:34822310). Within the 17S U2 SnRNP CC complex, SF3B1 is part of the SF3B subcomplex, which is required for CC 'A' complex assembly formed by the stable binding of U2 snRNP to the CC branchpoint sequence in pre-mRNA (PubMed:12234937). Sequence CC independent binding of SF3A and SF3B subcomplexes upstream of the CC branch site is essential, it may anchor U2 snRNP to the pre-mRNA CC (PubMed:12234937). May also be involved in the assembly of the 'E' CC complex (PubMed:10882114). Also acts as a component of the minor CC spliceosome, which is involved in the splicing of U12-type introns in CC pre-mRNAs (PubMed:15146077, PubMed:33509932). Together with other U2 CC snRNP complex components may also play a role in the selective CC processing of microRNAs (miRNAs) from the long primary miRNA CC transcript, pri-miR-17-92 (By similarity). CC {ECO:0000250|UniProtKB:Q99NB9, ECO:0000269|PubMed:10882114, CC ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:32494006, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34822310}. CC -!- SUBUNIT: Component of the 17S U2 SnRNP complex, a ribonucleoprotein CC complex that contains small nuclear RNA (snRNA) U2 and a number of CC specific proteins (PubMed:30567737, PubMed:32494006, PubMed:34822310, CC PubMed:36797247). Part of the SF3B subcomplex of the 17S U2 SnRNP CC complex (PubMed:12234937, PubMed:12738865, PubMed:28541300, CC PubMed:27720643). SF3B associates with the splicing subcomplex SF3A and CC a 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex CC (U2 snRNP) (PubMed:12234937). Within the SF3B complex, interacts CC directly (via HEAT domain) with SF3B3, SF3B5, SF3B6 and (via HEAT CC domain) with PHF5A (PubMed:16432215, Ref.39, PubMed:21062891, CC PubMed:27720643). The SF3B subcomplex interacts with U2AF2 CC (PubMed:27720643). Identified in the spliceosome C complex CC (PubMed:11991638). Component of the minor (U12-type spliceosome) CC spliceosome (PubMed:15146077, PubMed:33509932). Within the minor CC spliceosome complex, interacts with SCNM1 and CRIPT (PubMed:33509932). CC Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, CC BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21 CC (PubMed:16603771). Phosphorylated form interacts with PPP1R8 CC (PubMed:12105215). Interacts with PQBP1 (PubMed:23512658). Interacts CC with RBM17 (PubMed:17589525). Interacts with RBM39 (PubMed:24795046). CC Interacts with SETX (PubMed:21700224). Interacts with RBM15 CC (PubMed:26575292). Interacts with USH1G (PubMed:34023904). Interacts CC with SDE2 (PubMed:34365507). Interacts with U2AF1 (PubMed:34365507). CC Interacts with CACTIN (PubMed:34365507). Interacts with ZRSR1 (By CC similarity). Interacts with CYREN (PubMed:37813856). CC {ECO:0000250|UniProtKB:Q99NB9, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:12234937, CC ECO:0000269|PubMed:12738865, ECO:0000269|PubMed:15146077, CC ECO:0000269|PubMed:16432215, ECO:0000269|PubMed:16603771, CC ECO:0000269|PubMed:17589525, ECO:0000269|PubMed:21062891, CC ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:23512658, CC ECO:0000269|PubMed:24795046, ECO:0000269|PubMed:26575292, CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300, CC ECO:0000269|PubMed:30567737, ECO:0000269|PubMed:32494006, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:34023904, CC ECO:0000269|PubMed:34365507, ECO:0000269|PubMed:34822310, CC ECO:0000269|PubMed:36797247, ECO:0000269|PubMed:37813856, CC ECO:0000269|Ref.39}. CC -!- INTERACTION: CC O75533; Q96I25: RBM17; NbExp=4; IntAct=EBI-876542, EBI-740272; CC O75533-1; O43719: HTATSF1; NbExp=6; IntAct=EBI-15565798, EBI-720468; CC O75533-1; Q96I25: RBM17; NbExp=3; IntAct=EBI-15565798, EBI-740272; CC O75533-1; Q9Y3B4: SF3B6; NbExp=3; IntAct=EBI-15565798, EBI-1046261; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27720643, CC ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904}. Nucleus CC speckle {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:28541300, CC ECO:0000269|PubMed:34023904}. Note=During mitosis, transiently CC dispersed from the nuclear speckles to the cytoplasm. CC {ECO:0000269|PubMed:12105215}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75533-1; Sequence=Displayed; CC Name=2; CC IsoId=O75533-2; Sequence=VSP_046182, VSP_046183; CC -!- PTM: Phosphorylated. Phosphorylation occurs concomitantly with the CC splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and Thr- CC 313 by cyclin-dependent kinases promotes interaction with PPP1R8 during CC mitosis. {ECO:0000269|PubMed:12105215, ECO:0000269|PubMed:9585501}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q99NB9}. CC -!- SIMILARITY: Belongs to the SF3B1 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; AF054284; AAC97189.1; -; mRNA. DR EMBL; AF086296; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC010746; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF070540; AAC28633.1; -; mRNA. DR CCDS; CCDS33356.1; -. [O75533-1] DR CCDS; CCDS46479.1; -. [O75533-2] DR RefSeq; NP_036565.2; NM_012433.3. [O75533-1] DR PDB; 2F9D; X-ray; 2.50 A; P/Q=373-415. DR PDB; 2F9J; X-ray; 3.00 A; P/Q=380-415. DR PDB; 2FHO; NMR; -; A=379-424. DR PDB; 2PEH; X-ray; 2.11 A; C/D=333-342. DR PDB; 3LQV; X-ray; 2.38 A; P/Q=377-415. DR PDB; 4OZ1; X-ray; 1.74 A; C=333-342. DR PDB; 5IFE; X-ray; 3.10 A; C=1-1304. DR PDB; 5O9Z; EM; 4.50 A; v=1-1304. DR PDB; 5Z56; EM; 5.10 A; 1=1-1304. DR PDB; 5Z57; EM; 6.50 A; 1=1-1304. DR PDB; 5Z58; EM; 4.90 A; 1=1-1304. DR PDB; 5ZYA; EM; 3.95 A; C=1-1304. DR PDB; 6AH0; EM; 5.70 A; 1=1-1304. DR PDB; 6AHD; EM; 3.80 A; 1=1-1304. DR PDB; 6EN4; X-ray; 3.08 A; C=453-1304. DR PDB; 6FF4; EM; 16.00 A; u=1-1304. DR PDB; 6FF7; EM; 4.50 A; u=1-1304. DR PDB; 6N3E; X-ray; 1.89 A; B=291-297. DR PDB; 6QX9; EM; 3.28 A; B1=1-1304. DR PDB; 6Y50; EM; 4.10 A; u=1-1304. DR PDB; 6Y53; EM; 7.10 A; u=1-1304. DR PDB; 6Y5Q; EM; 7.10 A; u=1-1304. DR PDB; 7ABG; EM; 7.80 A; u=1-1304. DR PDB; 7ABH; EM; 4.50 A; u=1-1304. DR PDB; 7ABI; EM; 8.00 A; u=1-1304. DR PDB; 7B0I; X-ray; 3.00 A; C=453-1304. DR PDB; 7B91; X-ray; 3.00 A; C=453-1304. DR PDB; 7B92; X-ray; 3.00 A; C=453-1304. DR PDB; 7B9C; X-ray; 2.40 A; C=453-1304. DR PDB; 7DVQ; EM; 2.89 A; 1=1-1304. DR PDB; 7EVN; EM; 2.60 A; C=452-1304. DR PDB; 7EVO; EM; 2.50 A; 1=1-1304. DR PDB; 7OMF; X-ray; 3.00 A; C=453-1304. DR PDB; 7ONB; EM; 3.10 A; C=1-1304. DR PDB; 7OPI; X-ray; 3.10 A; C=453-1304. DR PDB; 7Q3L; EM; 2.30 A; A=1-1304. DR PDB; 7Q4O; EM; 2.20 A; A=1-1304. DR PDB; 7Q4P; EM; 2.20 A; A=1-1304. DR PDB; 7QTT; EM; 3.10 A; C=1-1304. DR PDB; 7SN6; X-ray; 1.80 A; C/D=333-351. DR PDB; 7VPX; EM; 3.00 A; 1=1-1304. DR PDB; 8CH6; EM; 5.90 A; C=1-1304. DR PDB; 8HK1; EM; 2.70 A; 1=1-1304. DR PDBsum; 2F9D; -. DR PDBsum; 2F9J; -. DR PDBsum; 2FHO; -. DR PDBsum; 2PEH; -. DR PDBsum; 3LQV; -. DR PDBsum; 4OZ1; -. DR PDBsum; 5IFE; -. DR PDBsum; 5O9Z; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 5ZYA; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6EN4; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6N3E; -. DR PDBsum; 6QX9; -. DR PDBsum; 6Y50; -. DR PDBsum; 6Y53; -. DR PDBsum; 6Y5Q; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABH; -. DR PDBsum; 7ABI; -. DR PDBsum; 7B0I; -. DR PDBsum; 7B91; -. DR PDBsum; 7B92; -. DR PDBsum; 7B9C; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7EVN; -. DR PDBsum; 7EVO; -. DR PDBsum; 7OMF; -. DR PDBsum; 7ONB; -. DR PDBsum; 7OPI; -. DR PDBsum; 7Q3L; -. DR PDBsum; 7Q4O; -. DR PDBsum; 7Q4P; -. DR PDBsum; 7QTT; -. DR PDBsum; 7SN6; -. DR PDBsum; 7VPX; -. DR PDBsum; 8CH6; -. DR PDBsum; 8HK1; -. DR AlphaFoldDB; O75533; -. DR BMRB; O75533; -. DR EMDB; EMD-10688; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11696; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-12994; -. DR EMDB; EMD-13793; -. DR EMDB; EMD-13811; -. DR EMDB; EMD-13812; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-31330; -. DR EMDB; EMD-31334; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-34841; -. DR EMDB; EMD-3766; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-6915; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR SMR; O75533; -. DR BioGRID; 117017; 549. DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. DR ComplexPortal; CPX-2227; SF3B complex. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR CORUM; O75533; -. DR DIP; DIP-29411N; -. DR ELM; O75533; -. DR IntAct; O75533; 113. DR MINT; O75533; -. DR STRING; 9606.ENSP00000335321; -. DR ChEMBL; CHEMBL1229013; -. DR DrugBank; DB14017; H3B-8800. DR GlyGen; O75533; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O75533; -. DR MetOSite; O75533; -. DR PhosphoSitePlus; O75533; -. DR SwissPalm; O75533; -. DR BioMuta; SF3B1; -. DR EPD; O75533; -. DR jPOST; O75533; -. DR MassIVE; O75533; -. DR MaxQB; O75533; -. DR PaxDb; 9606-ENSP00000335321; -. DR PeptideAtlas; O75533; -. DR ProteomicsDB; 19445; -. DR ProteomicsDB; 50072; -. [O75533-1] DR Pumba; O75533; -. DR Antibodypedia; 19893; 326 antibodies from 34 providers. DR DNASU; 23451; -. DR Ensembl; ENST00000335508.11; ENSP00000335321.6; ENSG00000115524.17. [O75533-1] DR Ensembl; ENST00000409915.8; ENSP00000428820.1; ENSG00000115524.17. [O75533-2] DR Ensembl; ENST00000414963.2; ENSP00000402997.2; ENSG00000115524.17. [O75533-2] DR GeneID; 23451; -. DR KEGG; hsa:23451; -. DR MANE-Select; ENST00000335508.11; ENSP00000335321.6; NM_012433.4; NP_036565.2. DR UCSC; uc002uue.4; human. [O75533-1] DR AGR; HGNC:10768; -. DR CTD; 23451; -. DR DisGeNET; 23451; -. DR GeneCards; SF3B1; -. DR HGNC; HGNC:10768; SF3B1. DR HPA; ENSG00000115524; Low tissue specificity. DR MalaCards; SF3B1; -. DR MIM; 605590; gene. DR neXtProt; NX_O75533; -. DR OpenTargets; ENSG00000115524; -. DR Orphanet; 75564; Acquired idiopathic sideroblastic anemia. DR Orphanet; 39044; Uveal melanoma. DR PharmGKB; PA35686; -. DR VEuPathDB; HostDB:ENSG00000115524; -. DR eggNOG; KOG0213; Eukaryota. DR GeneTree; ENSGT00390000018393; -. DR HOGENOM; CLU_002242_0_0_1; -. DR InParanoid; O75533; -. DR OMA; LWHPARK; -. DR OrthoDB; 226540at2759; -. DR PhylomeDB; O75533; -. DR TreeFam; TF105680; -. DR PathwayCommons; O75533; -. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway. DR SignaLink; O75533; -. DR SIGNOR; O75533; -. DR BioGRID-ORCS; 23451; 716 hits in 1171 CRISPR screens. DR ChiTaRS; SF3B1; human. DR EvolutionaryTrace; O75533; -. DR GeneWiki; SF3B1; -. DR GenomeRNAi; 23451; -. DR Pharos; O75533; Tbio. DR PRO; PR:O75533; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O75533; Protein. DR Bgee; ENSG00000115524; Expressed in tibia and 200 other cell types or tissues. DR ExpressionAtlas; O75533; baseline and differential. DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005730; C:nucleolus; NAS:ComplexPortal. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; NAS:UniProtKB. DR GO; GO:0034693; C:U11/U12 snRNP; IDA:MGI. DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0005686; C:U2 snRNP; IDA:MGI. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central. DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:1990935; F:splicing factor binding; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; NAS:ComplexPortal. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0035066; P:positive regulation of histone acetylation; NAS:ComplexPortal. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal. DR GO; GO:0008380; P:RNA splicing; IC:UniProtKB. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; NAS:UniProtKB. DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central. DR GO; GO:1903241; P:U2-type prespliceosome assembly; NAS:ComplexPortal. DR DisProt; DP01863; -. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2. DR IDEAL; IID00190; -. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015016; SF3b_su1. DR InterPro; IPR038737; SF3b_su1-like. DR PANTHER; PTHR12097:SF0; SPLICING FACTOR 3B SUBUNIT 1; 1. DR PANTHER; PTHR12097; SPLICING FACTOR 3B, SUBUNIT 1-RELATED; 1. DR Pfam; PF08920; SF3b1; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; O75533; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Citrullination; KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Spliceosome; Ubl conjugation. FT CHAIN 1..1304 FT /note="Splicing factor 3B subunit 1" FT /id="PRO_0000174323" FT REPEAT 529..568 FT /note="HEAT 1" FT REPEAT 569..603 FT /note="HEAT 2" FT REPEAT 604..641 FT /note="HEAT 3" FT REPEAT 643..677 FT /note="HEAT 4" FT REPEAT 680..718 FT /note="HEAT 5" FT REPEAT 763..801 FT /note="HEAT 6" FT REPEAT 843..881 FT /note="HEAT 7" FT REPEAT 1010..1048 FT /note="HEAT 8" FT REPEAT 1052..1090 FT /note="HEAT 9" FT REPEAT 1122..1160 FT /note="HEAT 10" FT REPEAT 1163..1201 FT /note="HEAT 11" FT REGION 100..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 124..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 173..360 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 190..342 FT /note="U2AF homology region; mediates interaction with FT RBM39" FT /evidence="ECO:0000269|PubMed:24795046" FT REGION 223..491 FT /note="Interaction with PPP1R8" FT /evidence="ECO:0000269|PubMed:12105215" FT REGION 529..568 FT /note="Interaction with SF3B14" FT REGION 547..550 FT /note="Interaction with PHF5A" FT /evidence="ECO:0000269|PubMed:27720643" FT REGION 1156..1157 FT /note="Interaction with PHF5A" FT /evidence="ECO:0000269|PubMed:27720643" FT REGION 1248..1304 FT /note="Interaction with SF3B3 and SF3B5" FT /evidence="ECO:0000269|PubMed:27720643" FT COMPBIAS 104..119 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 204..224 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..356 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 469 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 587 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 592 FT /note="Interaction with PHF5A" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 602 FT /note="Interaction with SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 677 FT /note="Interaction with SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 1035 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 1049 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 1141 FT /note="Interaction with RNA" FT /evidence="ECO:0000269|PubMed:27720643" FT SITE 1205 FT /note="Interaction with SF3B3" FT /evidence="ECO:0000269|PubMed:27720643" FT MOD_RES 125 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 141 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 142 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 157 FT /note="Citrulline" FT /evidence="ECO:0000250" FT MOD_RES 194 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 203 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 207 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 211 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 214 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q99NB9" FT MOD_RES 223 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 227 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163" FT MOD_RES 229 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99NB9" FT MOD_RES 235 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 244 FT /note="Phosphothreonine" FT /evidence="ECO:0000269|PubMed:12105215" FT MOD_RES 248 FT /note="Phosphothreonine" FT /evidence="ECO:0000305|PubMed:12105215" FT MOD_RES 257 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 261 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 267 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 273 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 278 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 296 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163" FT MOD_RES 299 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 303 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 313 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 322 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 326 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 328 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 341 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 349 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 350 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 354 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 400 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 426 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 434 FT /note="Phosphothreonine; by DYRK1A" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 436 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 554 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 562 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 214 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 413 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 430 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 140..144 FT /note="GKTPD -> FYSAA (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046182" FT VAR_SEQ 145..1304 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_046183" FT MUTAGEN 200 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-218; A-232; A-254; A-293; A-310 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 218 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-232; A-254; A-293; A-310 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 223 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 227 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 232 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-218; A-254; A-293; A-310 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 235 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 244 FT /note="T->A: Slight inhibition of interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 248 FT /note="T->A: Slight inhibition of interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 254 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-218; A-232; A-293; A-310 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 257 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 261 FT /note="T->A: Slight inhibition of interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 267 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 273 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 278 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 293 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-218; A-232; A-254; A-310 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 296 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 303 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 310 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-218; A-232; A-254; A-293 and FT A-338." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 313 FT /note="T->A: No effect on interaction with PPP1R8." FT /evidence="ECO:0000269|PubMed:12105215" FT MUTAGEN 338 FT /note="W->A: Abolishes interaction with RBM39; when FT associated with A-200; A-218; A-232; A-254; A-293 and FT A-310." FT /evidence="ECO:0000269|PubMed:24795046" FT MUTAGEN 700 FT /note="K->E: Does not affect the stability of the SF3B FT complex interaction with U2AF65. Does not decrease the FT affinity to RNA." FT /evidence="ECO:0000269|PubMed:27720643" FT CONFLICT 149 FT /note="A -> V (in Ref. 1; AAC97189)" FT /evidence="ECO:0000305" FT CONFLICT 594 FT /note="R -> L (in Ref. 1; AAC97189)" FT /evidence="ECO:0000305" FT HELIX 88..92 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 103..106 FT /evidence="ECO:0007829|PDB:7DVQ" FT TURN 112..114 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 120..124 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 137..140 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 152..175 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:7SN6" FT HELIX 380..394 FT /evidence="ECO:0007829|PDB:3LQV" FT HELIX 401..405 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 410..414 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 452..455 FT /evidence="ECO:0007829|PDB:7DVQ" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 469..471 FT /evidence="ECO:0007829|PDB:7B9C" FT HELIX 472..475 FT /evidence="ECO:0007829|PDB:7B9C" FT HELIX 476..478 FT /evidence="ECO:0007829|PDB:7B9C" FT STRAND 484..487 FT /evidence="ECO:0007829|PDB:7B9C" FT HELIX 492..505 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 509..526 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 528..539 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 546..563 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 564..570 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 571..578 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 579..582 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 587..603 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 606..613 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 616..618 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 622..636 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 641..651 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 658..675 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 676..682 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 683..690 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 691..694 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 699..716 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 721..723 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 725..737 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 740..753 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 754..756 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 759..776 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 782..797 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 798..801 FT /evidence="ECO:0007829|PDB:7Q3L" FT HELIX 803..809 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 811..818 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 821..825 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 827..844 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 846..853 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 854..858 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 862..879 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 886..901 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 908..921 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 922..925 FT /evidence="ECO:0007829|PDB:7Q4O" FT TURN 926..928 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 929..940 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 942..944 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 945..958 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 959..963 FT /evidence="ECO:0007829|PDB:7Q4O" FT TURN 964..966 FT /evidence="ECO:0007829|PDB:6EN4" FT HELIX 967..980 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 981..983 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 987..1003 FT /evidence="ECO:0007829|PDB:7Q4O" FT TURN 1006..1008 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 1009..1011 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1013..1025 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1029..1045 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1047..1049 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1052..1065 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1071..1088 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1090..1099 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1100..1102 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1106..1122 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1125..1137 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 1138..1140 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 1141..1158 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1159..1161 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1162..1177 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 1178..1180 FT /evidence="ECO:0007829|PDB:7B0I" FT HELIX 1182..1198 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 1199..1203 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 1205..1215 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1216..1220 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1224..1241 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1243..1250 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1251..1253 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 1259..1283 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 1291..1293 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 1299..1301 FT /evidence="ECO:0007829|PDB:7Q4O" SQ SEQUENCE 1304 AA; 145830 MW; 12F051757D2B9DEE CRC64; MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGG KTPDPKMNAR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL DYIL //