SF3B3_HUMAN
ID SF3B3_HUMAN Reviewed; 1217 AA.
AC Q15393; Q6NTI8; Q96GC0; Q9BPY2; Q9UFX7; Q9UJ29;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Splicing factor 3B subunit 3;
DE AltName: Full=Pre-mRNA-splicing factor SF3b 130 kDa subunit;
DE Short=SF3b130;
DE AltName: Full=STAF130;
DE AltName: Full=Spliceosome-associated protein 130;
DE Short=SAP 130 {ECO:0000303|PubMed:10490618};
GN Name=SF3B3; Synonyms=KIAA0017, SAP130 {ECO:0000303|PubMed:10490618};
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), PROTEIN SEQUENCE OF 1192-1217,
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=10490618; DOI=10.1128/mcb.19.10.6796;
RA Das B.K., Xia L., Palandjian L., Gozani O., Chyung Y., Reed R.;
RT "Characterization of a protein complex containing spliceosomal proteins
RT saps 49,130,145 and 155.";
RL Mol. Cell. Biol. 19:6796-6802(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [3]
RP SEQUENCE REVISION.
RA Nomura N.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Lung, Skeletal muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1003-1217 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP CHARACTERIZATION OF THE SPLICEOSOME, FUNCTION, AND SUBUNIT.
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 [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH SUPT3H, INTERACTION WITH THE STAGA
RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11564863; DOI=10.1128/mcb.21.20.6782-6795.2001;
RA Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA Kundu T.K., Chait B.T., Roeder R.G.;
RT "Human STAGA complex is a chromatin-acetylating transcription coactivator
RT that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT vivo.";
RL Mol. Cell. Biol. 21:6782-6795(2001).
RN [8]
RP INTERACTION WITH TAF3.
RX PubMed=11438666; DOI=10.1128/mcb.21.15.5109-5121.2001;
RA Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are
RT novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT PHD finger.";
RL Mol. Cell. Biol. 21:5109-5121(2001).
RN [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND THR-1200, 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 [17]
RP 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 [18]
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 [19]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH SF3B1; SF3B5 AND
RP PHF5A, FUNCTION, INTERACTION WITH SF3B1; SF3B5 AND PHF5A, IDENTIFICATION IN
RP THE SF3B COMPLEX, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
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 [20] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3B complex, a constituent of the spliceosome (PubMed:10490618,
CC PubMed:10882114, PubMed:27720643, PubMed:28781166). SF3B complex is
CC required for 'A' complex assembly formed by the stable binding of U2
CC snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence
CC independent binding of SF3A/SF3B complex upstream of the branch site is
CC essential, it may anchor U2 snRNP to the pre-mRNA (PubMed:12234937).
CC May also be involved in the assembly of the 'E' complex
CC (PubMed:10882114). Belongs also to the minor U12-dependent spliceosome,
CC which is involved in the splicing of rare class of nuclear pre-mRNA
CC intron (PubMed:15146077). {ECO:0000269|PubMed:10490618,
CC ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:15146077, ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28781166}.
CC -!- SUBUNIT: Identified in the spliceosome A complex; remains associated
CC with the spliceosome throughout the splicing process (PubMed:10490618).
CC Component of the spliceosome B complex (PubMed:28781166). Identified in
CC the spliceosome C complex (PubMed:11991638). Identified in the
CC spliceosome E complex (PubMed:10882114). Component of the U11/U12
CC snRNPs that are part of the U12-type spliceosome (PubMed:15146077).
CC Component of splicing factor SF3B complex which is composed of at least
CC eight subunits; SF3B1, SF3B2, SF3B3, SF3B4, SF3B5, SF3B6, PHF5A and
CC DDX42 (PubMed:12234937, PubMed:12738865, PubMed:28541300,
CC PubMed:27720643). SF3B associates with the splicing factor SF3A and a
CC 12S RNA unit to form the U2 small nuclear ribonucleoproteins complex
CC (U2 snRNP). Interaction between SF3B3 and SF3B1 is tighter than the
CC interaction between SF3B3 and SF3B2 (PubMed:12234937). Within the SF3B
CC complex interacts directly with SF3B1 (via HEAT domain), SF3B5 and
CC PHF5A (PubMed:27720643). The SF3B complex composed of SF3B1, SF3B2,
CC SF3B3, SF3B4, SF3B5, SF3B6 and PHF5A interacts with U2AF2
CC (PubMed:27720643). Associates with the STAGA transcription coactivator-
CC HAT complex. Interacts with SUPT3H (PubMed:11564863). Interacts with
CC TAF3 (PubMed:11438666). {ECO:0000269|PubMed:10490618,
CC ECO:0000269|PubMed:11438666, ECO:0000269|PubMed:11564863,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12234937,
CC ECO:0000269|PubMed:12738865, ECO:0000269|PubMed:15146077,
CC ECO:0000269|PubMed:27720643, ECO:0000269|PubMed:28541300,
CC ECO:0000269|PubMed:28781166}.
CC -!- INTERACTION:
CC Q15393; P54253: ATXN1; NbExp=3; IntAct=EBI-346977, EBI-930964;
CC Q15393; P55212: CASP6; NbExp=3; IntAct=EBI-346977, EBI-718729;
CC Q15393; O00291: HIP1; NbExp=3; IntAct=EBI-346977, EBI-473886;
CC Q15393; P42858: HTT; NbExp=3; IntAct=EBI-346977, EBI-466029;
CC Q15393; Q8IVD9: NUDCD3; NbExp=2; IntAct=EBI-346977, EBI-744342;
CC Q15393; O60260-5: PRKN; NbExp=3; IntAct=EBI-346977, EBI-21251460;
CC Q15393; P00441: SOD1; NbExp=3; IntAct=EBI-346977, EBI-990792;
CC Q15393; Q13148: TARDBP; NbExp=6; IntAct=EBI-346977, EBI-372899;
CC Q15393; P40337-2: VHL; NbExp=3; IntAct=EBI-346977, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10490618,
CC ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:27720643,
CC ECO:0000269|PubMed:28541300, ECO:0000269|PubMed:28781166}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15393-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15393-2; Sequence=VSP_022978, VSP_022979;
CC Name=3;
CC IsoId=Q15393-3; Sequence=VSP_022977;
CC -!- DOMAIN: The core of the protein consists of three beta-propeller
CC domains. {ECO:0000269|PubMed:27720643}.
CC -!- SIMILARITY: Belongs to the RSE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA02805.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA32662.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ001443; CAB56791.1; -; mRNA.
DR EMBL; D87686; BAA32662.2; ALT_INIT; mRNA.
DR EMBL; D13642; BAA02805.1; ALT_INIT; mRNA.
DR EMBL; BC000463; AAH00463.1; -; mRNA.
DR EMBL; BC003146; AAH03146.1; -; mRNA.
DR EMBL; BC009780; AAH09780.1; -; mRNA.
DR EMBL; BC068974; AAH68974.1; -; mRNA.
DR EMBL; AL110251; CAB53699.1; -; mRNA.
DR CCDS; CCDS10894.1; -. [Q15393-1]
DR PIR; T14779; T14779.
DR RefSeq; NP_036558.3; NM_012426.4. [Q15393-1]
DR PDB; 5IFE; X-ray; 3.10 A; A=1-1217.
DR PDB; 5O9Z; EM; 4.50 A; w=1-1217.
DR PDB; 5Z56; EM; 5.10 A; 3=1-1217.
DR PDB; 5Z57; EM; 6.50 A; 3=1-1217.
DR PDB; 5Z58; EM; 4.90 A; 3=1-1217.
DR PDB; 5ZYA; EM; 3.95 A; A=1-1217.
DR PDB; 6AH0; EM; 5.70 A; 3=1-1217.
DR PDB; 6AHD; EM; 3.80 A; 3=1-1217.
DR PDB; 6EN4; X-ray; 3.08 A; A=1-1217.
DR PDB; 6FF4; EM; 16.00 A; v=1-1217.
DR PDB; 6FF7; EM; 4.50 A; v=1-1217.
DR PDB; 6QX9; EM; 3.28 A; B3=1-1217.
DR PDB; 6Y50; EM; 4.10 A; v=1-1217.
DR PDB; 6Y5Q; EM; 7.10 A; v=1-1217.
DR PDB; 7ABG; EM; 7.80 A; E=1-1217.
DR PDB; 7ABH; EM; 4.50 A; E=1-1217.
DR PDB; 7ABI; EM; 8.00 A; E=1-1217.
DR PDB; 7B0I; X-ray; 3.00 A; A=1-442, A=768-1217.
DR PDB; 7B91; X-ray; 3.00 A; A=1-442, A=768-1216.
DR PDB; 7B92; X-ray; 3.00 A; A=1-442, A=768-1216.
DR PDB; 7B9C; X-ray; 2.40 A; A=916-1216.
DR PDB; 7DVQ; EM; 2.89 A; 3=1-1217.
DR PDB; 7KTS; EM; 19.09 A; S=1-1217.
DR PDB; 7OMF; X-ray; 3.00 A; A=1-442, A=768-1217.
DR PDB; 7ONB; EM; 3.10 A; A=1-1217.
DR PDB; 7OPI; X-ray; 3.10 A; A=916-1217.
DR PDB; 7Q3L; EM; 2.30 A; C=1-1217.
DR PDB; 7Q4O; EM; 2.20 A; C=1-1217.
DR PDB; 7Q4P; EM; 2.20 A; C=1-1217.
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; 6QX9; -.
DR PDBsum; 6Y50; -.
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; 7KTS; -.
DR PDBsum; 7OMF; -.
DR PDBsum; 7ONB; -.
DR PDBsum; 7OPI; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q15393; -.
DR SMR; Q15393; -.
DR BioGRID; 117016; 461.
DR ComplexPortal; CPX-2227; SF3B complex.
DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR CORUM; Q15393; -.
DR DIP; DIP-28152N; -.
DR IntAct; Q15393; 105.
DR MINT; Q15393; -.
DR STRING; 9606.ENSP00000305790; -.
DR BindingDB; Q15393; -.
DR ChEMBL; CHEMBL1250378; -.
DR DrugBank; DB04216; Quercetin.
DR DrugCentral; Q15393; -.
DR GlyGen; Q15393; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15393; -.
DR MetOSite; Q15393; -.
DR PhosphoSitePlus; Q15393; -.
DR SwissPalm; Q15393; -.
DR BioMuta; SF3B3; -.
DR DMDM; 116242787; -.
DR EPD; Q15393; -.
DR jPOST; Q15393; -.
DR MassIVE; Q15393; -.
DR MaxQB; Q15393; -.
DR PaxDb; Q15393; -.
DR PeptideAtlas; Q15393; -.
DR PRIDE; Q15393; -.
DR ProteomicsDB; 60563; -. [Q15393-1]
DR ProteomicsDB; 60564; -. [Q15393-2]
DR ProteomicsDB; 60565; -. [Q15393-3]
DR Antibodypedia; 30001; 325 antibodies from 38 providers.
DR DNASU; 23450; -.
DR Ensembl; ENST00000302516.10; ENSP00000305790.5; ENSG00000189091.13. [Q15393-1]
DR GeneID; 23450; -.
DR KEGG; hsa:23450; -.
DR MANE-Select; ENST00000302516.10; ENSP00000305790.5; NM_012426.5; NP_036558.3.
DR UCSC; uc002ezf.3; human. [Q15393-1]
DR CTD; 23450; -.
DR DisGeNET; 23450; -.
DR GeneCards; SF3B3; -.
DR HGNC; HGNC:10770; SF3B3.
DR HPA; ENSG00000189091; Low tissue specificity.
DR MIM; 605592; gene.
DR neXtProt; NX_Q15393; -.
DR OpenTargets; ENSG00000189091; -.
DR PharmGKB; PA35688; -.
DR VEuPathDB; HostDB:ENSG00000189091; -.
DR eggNOG; KOG1898; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_003246_0_0_1; -.
DR InParanoid; Q15393; -.
DR OMA; FFLVQTE; -.
DR PhylomeDB; Q15393; -.
DR TreeFam; TF105685; -.
DR PathwayCommons; Q15393; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q15393; -.
DR SIGNOR; Q15393; -.
DR BioGRID-ORCS; 23450; 799 hits in 1061 CRISPR screens.
DR ChiTaRS; SF3B3; human.
DR GeneWiki; SF3B3; -.
DR GenomeRNAi; 23450; -.
DR Pharos; Q15393; Tchem.
DR PRO; PR:Q15393; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15393; protein.
DR Bgee; ENSG00000189091; Expressed in ventricular zone and 209 other tissues.
DR ExpressionAtlas; Q15393; baseline and differential.
DR Genevisible; Q15393; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IC:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IC:ComplexPortal.
DR GO; GO:0005689; C:U12-type spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0030620; F:U2 snRNA binding; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IC:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:CACAO.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0008380; P:RNA splicing; IC:UniProtKB.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR GO; GO:1903241; P:U2-type prespliceosome assembly; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 3.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..1217
FT /note="Splicing factor 3B subunit 3"
FT /id="PRO_0000218639"
FT REGION 105..119
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT REGION 145..168
FT /note="Interaction with PHF5A, SF3B1 and SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT REGION 193..231
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT REGION 786..804
FT /note="Interaction with SF3B1 and SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT REGION 1028..1049
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000269|PubMed:27720643"
FT REGION 1100..1123
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 284
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 306
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 352
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 429
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 916
FT /note="Interaction with SF3B5"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 988
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000269|PubMed:27720643"
FT SITE 1171
FT /note="Interaction with SF3B1"
FT /evidence="ECO:0000269|PubMed:27720643"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1200
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..818
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022977"
FT VAR_SEQ 250..275
FT /note="ICSENYITYKNFGDQPDIRCPIPRRR -> NLSPPFPKAIPALICLDSPVYF
FT CTHP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022978"
FT VAR_SEQ 276..1217
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022979"
FT VARIANT 908
FT /note="G -> R (in dbSNP:rs11551673)"
FT /id="VAR_053647"
FT CONFLICT 193
FT /note="D -> G (in Ref. 1; CAB56791)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="F -> S (in Ref. 4; AAH68974)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="L -> W (in Ref. 1; CAB56791)"
FT /evidence="ECO:0000305"
FT CONFLICT 899
FT /note="T -> I (in Ref. 4; AAH00463/AAH03146)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 83..93
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 165..173
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 181..188
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7B91"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 248..259
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 308..318
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 321..332
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 336..342
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:7B91"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 393..401
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 422..427
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 488..493
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 496..500
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 501..503
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:6EN4"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 544..549
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 562..568
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 572..576
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 587..592
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 604..609
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 612..619
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:5IFE"
FT STRAND 624..632
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 637..646
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 662..678
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 681..683
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 689..693
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 712..725
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 740..745
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 751..757
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 762..766
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 774..780
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 782..790
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 792..794
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 797..805
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 809..825
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 832..844
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 849..852
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 858..860
FT /evidence="ECO:0007829|PDB:6FF4"
FT STRAND 862..869
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 871..873
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 876..881
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 886..894
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 897..899
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 903..912
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 915..918
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 922..931
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 932..935
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 936..947
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 949..955
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 958..963
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 966..972
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 974..983
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 990..996
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 999..1007
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1009..1015
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1016..1019
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1020..1026
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1028..1030
FT /evidence="ECO:0007829|PDB:7OPI"
FT STRAND 1033..1038
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1040..1048
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1051..1057
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1064..1067
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 1081..1084
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 1086..1088
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 1090..1096
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1101..1107
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1109..1113
FT /evidence="ECO:0007829|PDB:7OPI"
FT STRAND 1116..1121
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1126..1131
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1135..1151
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1160..1164
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1166..1168
FT /evidence="ECO:0007829|PDB:7B9C"
FT STRAND 1171..1175
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1176..1179
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1180..1184
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1187..1195
FT /evidence="ECO:0007829|PDB:7B9C"
FT TURN 1196..1198
FT /evidence="ECO:0007829|PDB:7B9C"
FT HELIX 1201..1214
FT /evidence="ECO:0007829|PDB:7B9C"
SQ SEQUENCE 1217 AA; 135577 MW; 35CACAF5ACC32512 CRC64;
MFLYNLTLQR ATGISFAIHG NFSGTKQQEI VVSRGKILEL LRPDPNTGKV HTLLTVEVFG
VIRSLMAFRL TGGTKDYIVV GSDSGRIVIL EYQPSKNMFE KIHQETFGKS GCRRIVPGQF
LAVDPKGRAV MISAIEKQKL VYILNRDAAA RLTISSPLEA HKANTLVYHV VGVDVGFENP
MFACLEMDYE EADNDPTGEA AANTQQTLTF YELDLGLNHV VRKYSEPLEE HGNFLITVPG
GSDGPSGVLI CSENYITYKN FGDQPDIRCP IPRRRNDLDD PERGMIFVCS ATHKTKSMFF
FLAQTEQGDI FKITLETDED MVTEIRLKYF DTVPVAAAMC VLKTGFLFVA SEFGNHYLYQ
IAHLGDDDEE PEFSSAMPLE EGDTFFFQPR PLKNLVLVDE LDSLSPILFC QIADLANEDT
PQLYVACGRG PRSSLRVLRH GLEVSEMAVS ELPGNPNAVW TVRRHIEDEF DAYIIVSFVN
ATLVLSIGET VEEVTDSGFL GTTPTLSCSL LGDDALVQVY PDGIRHIRAD KRVNEWKTPG
KKTIVKCAVN QRQVVIALTG GELVYFEMDP SGQLNEYTER KEMSADVVCM SLANVPPGEQ
RSRFLAVGLV DNTVRIISLD PSDCLQPLSM QALPAQPESL CIVEMGGTEK QDELGERGSI
GFLYLNIGLQ NGVLLRTVLD PVTGDLSDTR TRYLGSRPVK LFRVRMQGQE AVLAMSSRSW
LSYSYQSRFH LTPLSYETLE FASGFASEQC PEGIVAISTN TLRILALEKL GAVFNQVAFP
LQYTPRKFVI HPESNNLIII ETDHNAYTEA TKAQRKQQMA EEMVEAAGED ERELAAEMAA
AFLNENLPES IFGAPKAGNG QWASVIRVMN PIQGNTLDLV QLEQNEAAFS VAVCRFSNTG
EDWYVLVGVA KDLILNPRSV AGGFVYTYKL VNNGEKLEFL HKTPVEEVPA AIAPFQGRVL
IGVGKLLRVY DLGKKKLLRK CENKHIANYI SGIQTIGHRV IVSDVQESFI WVRYKRNENQ
LIIFADDTYP RWVTTASLLD YDTVAGADKF GNICVVRLPP NTNDEVDEDP TGNKALWDRG
LLNGASQKAE VIMNYHVGET VLSLQKTTLI PGGSESLVYT TLSGGIGILV PFTSHEDHDF
FQHVEMHLRS EHPPLCGRDH LSFRSYYFPV KNVIDGDLCE QFNSMEPNKQ KNVSEELDRT
PPEVSKKLED IRTRYAF
