SF3B1_HUMAN
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 03-AUG-2022, entry version 208.
DE RecName: Full=Splicing factor 3B subunit 1;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 155 kDa subunit;
DE Short=SF3b155;
DE AltName: Full=Spliceosome-associated protein 155;
DE Short=SAP 155;
GN Name=SF3B1; Synonyms=SAP155;
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 INTERACTION WITH PPP1R8, PHOSPHORYLATION AT THR-244; THR-248 AND THR-313,
RP AND MUTAGENESIS OF THR-223; THR-227; THR-235; THR-244; THR-248; THR-257;
RP THR-261; THR-267; THR-273; THR-278; THR-296; THR-303 AND 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 U11/U12 SPLICEOSOME, 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 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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex (PubMed:27720643). SF3B complex is required for 'A'
CC complex assembly formed by the stable binding of U2 snRNP to the
CC branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of
CC SF3A/SF3B complex upstream of the branch site is essential, it may
CC anchor U2 snRNP to the pre-mRNA (PubMed:12234937). Together with other
CC U2 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). May also be involved in the
CC assembly of the 'E' complex (PubMed:10882114). Belongs also to the
CC minor U12-dependent spliceosome, which is involved in the splicing of
CC rare class of nuclear pre-mRNA intron (PubMed:15146077).
CC {ECO:0000250|UniProtKB:Q99NB9, ECO:0000269|PubMed:10882114,
CC ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:27720643}.
CC -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21
CC (PubMed:16603771). Identified in the spliceosome C complex
CC (PubMed:11991638). Component of the U11/U12 snRNPs that are part of the
CC U12-type spliceosome (PubMed:15146077). Component of splicing factor
CC SF3B complex which is composed of at least eight subunits; SF3B1,
CC SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and DDX42 (PubMed:12234937,
CC PubMed:12738865, PubMed:28541300, PubMed:27720643). SF3B associates
CC with the splicing factor SF3A and a 12S RNA unit to form the U2 small
CC nuclear ribonucleoproteins complex (U2 snRNP). Interacts directly with
CC the splicing factor U2AF (PubMed:12234937). Within the SF3B complex
CC interacts directly (via HEAT domain) with SF3B3, SF3B5 and (via HEAT
CC domain) with PHF5A (PubMed:27720643). Interacts directly with SF3B6
CC (PubMed:16432215, Ref.37, PubMed:21062891). The SF3B complex composed
CC of SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with
CC U2AF2 (PubMed:27720643). 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).
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12105215,
CC ECO:0000269|PubMed:12234937, ECO:0000269|PubMed:12738865,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:16432215,
CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:17589525,
CC ECO:0000269|PubMed:21062891, ECO:0000269|PubMed:21700224,
CC ECO:0000269|PubMed:23512658, ECO:0000269|PubMed:24795046,
CC ECO:0000269|PubMed:26575292, ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:34023904,
CC ECO:0000269|Ref.37}.
CC -!- INTERACTION:
CC O75533; Q96I25: RBM17; NbExp=3; 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. Note=During mitosis, transiently dispersed from the nuclear
CC speckles to the cytoplasm.
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}.
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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; 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 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; 7OMF; -.
DR PDBsum; 7ONB; -.
DR PDBsum; 7OPI; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; O75533; -.
DR BMRB; O75533; -.
DR SMR; O75533; -.
DR BioGRID; 117017; 423.
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; 110.
DR MINT; O75533; -.
DR STRING; 9606.ENSP00000335321; -.
DR ChEMBL; CHEMBL1229013; -.
DR DrugBank; DB14017; H3B-8800.
DR GlyGen; O75533; 1 site, 1 O-linked glycan (1 site).
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; O75533; -.
DR PeptideAtlas; O75533; -.
DR PRIDE; O75533; -.
DR ProteomicsDB; 19445; -.
DR ProteomicsDB; 50072; -. [O75533-1]
DR Antibodypedia; 19893; 282 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 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 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; 681 hits in 1084 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 198 other tissues.
DR ExpressionAtlas; O75533; baseline and differential.
DR Genevisible; O75533; HS.
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; IC: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; IPI:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC: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; IC:ComplexPortal.
DR DisProt; DP01863; -.
DR Gene3D; 1.25.10.10; -; 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; PTHR12097; 2.
DR Pfam; PF08920; SF3b1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 A-
FT 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 380..394
FT /evidence="ECO:0007829|PDB:3LQV"
FT HELIX 401..406
FT /evidence="ECO:0007829|PDB:3LQV"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:3LQV"
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 489..506
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 509..521
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 528..539
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 546..563
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 564..570
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 571..578
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 579..583
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 587..604
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 606..613
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 622..639
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 641..652
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 658..675
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 676..682
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 683..690
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 691..695
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 699..716
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 722..727
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 728..734
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 735..737
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 740..753
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 754..756
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 759..776
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 782..796
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 798..801
FT /evidence="ECO:0007829|PDB:7B91"
FT HELIX 803..809
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 811..817
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:6FF4"
FT HELIX 823..825
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 827..844
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 846..850
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 851..853
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 854..858
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 862..879
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 886..901
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 908..921
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 922..928
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 929..940
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 942..944
FT /evidence="ECO:0007829|PDB:6FF4"
FT HELIX 945..964
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 968..980
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 981..983
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 987..1004
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1006..1008
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1013..1020
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1021..1025
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1029..1045
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1047..1049
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1052..1063
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1064..1067
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1071..1088
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1091..1103
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1106..1108
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1109..1122
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1125..1127
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1129..1134
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1135..1137
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1142..1158
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1159..1164
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1166..1177
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1178..1180
FT /evidence="ECO:0007829|PDB:7B0I"
FT HELIX 1182..1198
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1200..1203
FT /evidence="ECO:0007829|PDB:7B91"
FT HELIX 1205..1215
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1216..1220
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1224..1241
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1243..1250
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1251..1255
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1259..1275
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1276..1278
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 1279..1282
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1298..1301
FT /evidence="ECO:0007829|PDB:7B9C"
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
