ID SF3A1_HUMAN Reviewed; 793 AA. AC Q15459; E9PAW1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 227. DE RecName: Full=Splicing factor 3A subunit 1; DE AltName: Full=SF3a120 {ECO:0000303|PubMed:11533230, ECO:0000303|PubMed:21349847, ECO:0000303|PubMed:7489498}; DE AltName: Full=Spliceosome-associated protein 114; DE Short=SAP 114; GN Name=SF3A1; Synonyms=SAP114; 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], AND TISSUE SPECIFICITY. RX PubMed=7489498; RA Kraemer A., Mulhauser F., Wersig C., Groning K., Bilbe G.; RT "Mammalian splicing factor SF3a120 represents a new member of the SURP RT family of proteins and is homologous to the essential splicing factor RT PRP21p of Saccharomyces cerevisiae."; RL RNA 1:260-272(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix, and Lymph; 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 SUBUNIT, IDENTIFICATION IN A COMPLEX WITH SF3A2 AND SF3A3 AND IN THE 17S U2 RP SNRNP, AND SUBCELLULAR LOCATION. 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 FUNCTION, AND SUBUNIT. RX PubMed=11533230; DOI=10.1128/mcb.21.19.6406-6417.2001; RA Nesic D., Kraemer A.; RT "Domains in human splicing factors SF3a60 and SF3a66 required for binding RT to SF3a120, assembly of the 17S U2 snRNP, and prespliceosome formation."; RL Mol. Cell. Biol. 21:6406-6417(2001). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C RP COMPLEX, AND SUBUNIT. 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-456 AND TYR-759, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-359, AND RP 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-413 AND SER-451, AND RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329; SER-359 AND RP SER-451, 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-359; SER-413 AND RP SER-451, AND IDENTIFICATION 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 [17] 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 [18] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=21349847; DOI=10.1074/jbc.m110.201491; RA Huang C.J., Ferfoglia F., Raleff F., Kraemer A.; RT "Interaction domains and nuclear targeting signals in subunits of the U2 RT small nuclear ribonucleoprotein particle-associated splicing factor SF3a."; RL J. Biol. Chem. 286:13106-13114(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320; SER-329 AND SER-359, AND RP IDENTIFICATION BY MASS SPECTROMETRY [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 [20] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-359; SER-413; RP SER-451 AND SER-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND IDENTIFICATION BY RP 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-542 AND LYS-686, AND RP IDENTIFICATION BY MASS 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 [24] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-686, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [25] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-20; LYS-131; LYS-424; LYS-499; RP LYS-542 AND LYS-686, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [26] RP STRUCTURE BY NMR OF 704-789. RG Structural genomics consortium (SGC); RT "Solution structure of a human ubiquitin-like domain in SF3A1."; RL Submitted (JUN-2005) to the PDB data bank. RN [27] RP STRUCTURE BY NMR OF 48-110 AND 134-217 IN COMPLEX WITH SF3A3, SUBUNIT, SURP RP MOTIFS, AND MUTAGENESIS OF GLU-48; LYS-55; PHE-162 AND LEU-169. RX PubMed=17098193; DOI=10.1016/j.str.2006.09.009; RA Kuwasako K., He F., Inoue M., Tanaka A., Sugano S., Guntert P., Muto Y., RA Yokoyama S.; RT "Solution structures of the SURP domains and the subunit-assembly mechanism RT within the splicing factor SF3a complex in 17S U2 snRNP."; RL Structure 14:1677-1689(2006). RN [28] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58} RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=29360106; DOI=10.1038/cr.2018.14; RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.; RT "Structure of the human activated spliceosome in three conformational RT states."; RL Cell Res. 28:307-322(2018). RN [29] RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=30315277; DOI=10.1038/s41422-018-0094-7; RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.; RT "Structures of the human pre-catalytic spliceosome and its precursor RT spliceosome."; RL Cell Res. 28:1129-1140(2018). RN [30] RP VARIANT [LARGE SCALE ANALYSIS] TRP-511. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [31] {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 [32] {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:10882114, PubMed:11533230, PubMed:32494006). The 17S CC U2 SnRNP complex (1) directly participates in early spliceosome CC assembly and (2) mediates recognition of the intron branch site during CC pre-mRNA splicing by promoting the selection of the pre-mRNA branch- CC site adenosine, the nucleophile for the first step of splicing CC (PubMed:10882114, PubMed:11533230, PubMed:32494006). Within the 17S U2 CC SnRNP complex, SF3A1 is part of the SF3A subcomplex that contributes to CC the assembly of the 17S U2 snRNP, and the subsequent assembly of the CC pre-spliceosome 'E' complex and the pre-catalytic spliceosome 'A' CC complex (PubMed:10882114, PubMed:11533230). Involved in pre-mRNA CC splicing as a component of pre-catalytic spliceosome 'B' complexes CC (PubMed:29360106, PubMed:30315277). {ECO:0000269|PubMed:10882114, CC ECO:0000269|PubMed:11533230, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:32494006}. 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:32494006, PubMed:36797247). Part of the SF3A CC subcomplex of the 17S U2 SnRNP complex which is composed of three CC subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114, CC PubMed:11533230, PubMed:21349847). SF3A associates with the splicing CC factor SF3B and a 12S RNA unit to form the mature 17S U2 small nuclear CC ribonucleoprotein complex (17S U2 snRNP) (PubMed:10882114, CC PubMed:11533230). SF3A1 functions as a scaffold that interacts directly CC with both SF3A2 and SF3A3 (PubMed:11533230, PubMed:21349847, CC PubMed:17098193). Identified in the spliceosome 'E' complex, a CC precursor of the spliceosome 'A' complex (PubMed:10882114). Identified CC in the spliceosome 'A' and 'B' complexes (PubMed:29360106, CC PubMed:30315277). Identified in the spliceosome 'C' complex CC (PubMed:11991638). {ECO:0000269|PubMed:10882114, CC ECO:0000269|PubMed:11533230, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:17098193, ECO:0000269|PubMed:21349847, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:36797247}. CC -!- INTERACTION: CC Q15459; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-1054743, EBI-2603996; CC Q15459; O75400: PRPF40A; NbExp=2; IntAct=EBI-1054743, EBI-473291; CC Q15459; P98175: RBM10; NbExp=2; IntAct=EBI-1054743, EBI-721525; CC Q15459; Q15637: SF1; NbExp=8; IntAct=EBI-1054743, EBI-744603; CC Q15459; Q15428: SF3A2; NbExp=4; IntAct=EBI-1054743, EBI-2462271; CC Q15459; Q12874: SF3A3; NbExp=7; IntAct=EBI-1054743, EBI-1051880; CC Q15459; P08047: SP1; NbExp=2; IntAct=EBI-1054743, EBI-298336; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882114, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277}. Nucleus CC speckle {ECO:0000269|PubMed:21349847}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q15459-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15459-2; Sequence=VSP_054090; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:7489498}. CC -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3. 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; X85237; CAA59494.1; -; mRNA. DR EMBL; CR456575; CAG30461.1; -; mRNA. DR EMBL; AC004997; AAC23435.1; -; Genomic_DNA. DR EMBL; BC001976; AAH01976.1; -; mRNA. DR EMBL; BC007684; AAH07684.1; -; mRNA. DR CCDS; CCDS13875.1; -. [Q15459-1] DR PIR; S60735; S60735. DR RefSeq; NP_005868.1; NM_005877.5. [Q15459-1] DR PDB; 1ZKH; NMR; -; A=704-789. DR PDB; 2DT6; NMR; -; A=48-110. DR PDB; 2DT7; NMR; -; B=134-217. DR PDB; 5Z56; EM; 5.10 A; u=1-793. DR PDB; 5Z57; EM; 6.50 A; w=310-384. DR PDB; 5Z58; EM; 4.90 A; w=310-384. DR PDB; 6AH0; EM; 5.70 A; u=1-793. DR PDB; 6AHD; EM; 3.80 A; u=1-793. DR PDB; 6FF7; EM; 4.50 A; p=1-793. DR PDB; 6QX9; EM; 3.28 A; A1=1-793. DR PDB; 6Y53; EM; 7.10 A; 6=1-793. DR PDB; 6Y5Q; EM; 7.10 A; 6=1-793. DR PDB; 7ABG; EM; 7.80 A; p=1-793. DR PDB; 7ABI; EM; 8.00 A; p=1-793. DR PDB; 7EVO; EM; 2.50 A; A=1-793. DR PDB; 7P08; NMR; -; A=704-793. DR PDB; 7P0V; X-ray; 1.56 A; A=704-793. DR PDB; 7VH9; NMR; -; A=48-110. DR PDB; 7VPX; EM; 3.00 A; A=1-793. DR PDB; 8CH6; EM; 5.90 A; H=1-793. DR PDB; 8HK1; EM; 2.70 A; A=1-793. DR PDB; 8ID2; X-ray; 1.80 A; A/B=703-793. DR PDBsum; 1ZKH; -. DR PDBsum; 2DT6; -. DR PDBsum; 2DT7; -. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6FF7; -. DR PDBsum; 6QX9; -. DR PDBsum; 6Y53; -. DR PDBsum; 6Y5Q; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7EVO; -. DR PDBsum; 7P08; -. DR PDBsum; 7P0V; -. DR PDBsum; 7VH9; -. DR PDBsum; 7VPX; -. DR PDBsum; 8CH6; -. DR PDBsum; 8HK1; -. DR PDBsum; 8ID2; -. DR AlphaFoldDB; Q15459; -. DR BMRB; Q15459; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-31334; -. DR EMDB; EMD-32074; -. DR EMDB; EMD-34841; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-6889; -. DR EMDB; EMD-6890; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9621; -. DR EMDB; EMD-9624; -. DR SMR; Q15459; -. DR BioGRID; 115580; 456. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2565; SF3A complex. DR CORUM; Q15459; -. DR DIP; DIP-29164N; -. DR IntAct; Q15459; 86. DR MINT; Q15459; -. DR STRING; 9606.ENSP00000215793; -. DR GlyGen; Q15459; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15459; -. DR MetOSite; Q15459; -. DR PhosphoSitePlus; Q15459; -. DR SwissPalm; Q15459; -. DR BioMuta; SF3A1; -. DR DMDM; 2498882; -. DR EPD; Q15459; -. DR jPOST; Q15459; -. DR MassIVE; Q15459; -. DR MaxQB; Q15459; -. DR PaxDb; 9606-ENSP00000215793; -. DR PeptideAtlas; Q15459; -. DR ProteomicsDB; 19091; -. DR ProteomicsDB; 60599; -. [Q15459-1] DR Pumba; Q15459; -. DR Antibodypedia; 254; 354 antibodies from 27 providers. DR DNASU; 10291; -. DR Ensembl; ENST00000215793.13; ENSP00000215793.7; ENSG00000099995.19. [Q15459-1] DR GeneID; 10291; -. DR KEGG; hsa:10291; -. DR MANE-Select; ENST00000215793.13; ENSP00000215793.7; NM_005877.6; NP_005868.1. DR UCSC; uc003ahl.4; human. [Q15459-1] DR AGR; HGNC:10765; -. DR CTD; 10291; -. DR DisGeNET; 10291; -. DR GeneCards; SF3A1; -. DR HGNC; HGNC:10765; SF3A1. DR HPA; ENSG00000099995; Low tissue specificity. DR MIM; 605595; gene. DR neXtProt; NX_Q15459; -. DR OpenTargets; ENSG00000099995; -. DR PharmGKB; PA35683; -. DR VEuPathDB; HostDB:ENSG00000099995; -. DR eggNOG; KOG0007; Eukaryota. DR GeneTree; ENSGT00730000111077; -. DR HOGENOM; CLU_013259_1_0_1; -. DR InParanoid; Q15459; -. DR OMA; HAYYRHR; -. DR OrthoDB; 168687at2759; -. DR PhylomeDB; Q15459; -. DR TreeFam; TF105705; -. DR PathwayCommons; Q15459; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q15459; -. DR SIGNOR; Q15459; -. DR BioGRID-ORCS; 10291; 792 hits in 1165 CRISPR screens. DR ChiTaRS; SF3A1; human. DR EvolutionaryTrace; Q15459; -. DR GeneWiki; SF3A1; -. DR GenomeRNAi; 10291; -. DR Pharos; Q15459; Tbio. DR PRO; PR:Q15459; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; Q15459; Protein. DR Bgee; ENSG00000099995; Expressed in sperm and 218 other cell types or tissues. DR ExpressionAtlas; Q15459; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL. DR GO; GO:0005686; C:U2 snRNP; IDA:UniProtKB. DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB. DR GO; GO:0071004; C:U2-type prespliceosome; IDA:UniProtKB. DR GO; GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC-UCL. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro. DR GO; GO:0006397; P:mRNA processing; IMP:HGNC-UCL. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:1903241; P:U2-type prespliceosome assembly; IDA:UniProtKB. DR CDD; cd01800; Ubl_SF3a120; 1. DR Gene3D; 1.10.10.790; Surp module; 2. DR InterPro; IPR045146; SF3A1. DR InterPro; IPR022030; SF3A1_dom. DR InterPro; IPR035563; SF3As1_ubi. DR InterPro; IPR000061; Surp. DR InterPro; IPR035967; SWAP/Surp_sf. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR15316; SPLICEOSOME ASSOCIATED PROTEIN 114/SWAP SPLICING FACTOR-RELATED; 1. DR PANTHER; PTHR15316:SF1; SPLICING FACTOR 3A SUBUNIT 1; 1. DR Pfam; PF12230; PRP21_like_P; 1. DR Pfam; PF01805; Surp; 2. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00648; SWAP; 2. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF109905; Surp module (SWAP domain); 2. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50128; SURP; 2. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR Genevisible; Q15459; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Spliceosome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..793 FT /note="Splicing factor 3A subunit 1" FT /id="PRO_0000114917" FT REPEAT 52..94 FT /note="SURP motif 1" FT REPEAT 166..208 FT /note="SURP motif 2" FT DOMAIN 707..793 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..428 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 488..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 530..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 665..688 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 680..702 FT /note="Required and sufficient for nuclear import" FT /evidence="ECO:0000269|PubMed:21349847" FT COMPBIAS 1..20 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 321..337 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 369..385 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..504 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..547 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..584 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 169 FT /note="Critical for binding to SF3A3" FT MOD_RES 55 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 359 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 413 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 451 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 456 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 508 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 759 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT CROSSLNK 20 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 131 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 424 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 499 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 542 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 686 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT VAR_SEQ 106..170 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_054090" FT VARIANT 511 FT /note="R -> W (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs765594577)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036290" FT MUTAGEN 48 FT /note="E->F: SLURP 1 motif acquires binding to SF3A3; when FT associated with Leu-55." FT /evidence="ECO:0000269|PubMed:17098193" FT MUTAGEN 55 FT /note="K->L: SLURP 1 motif acquires binding to SF3A3; when FT associated with Phe-48." FT /evidence="ECO:0000269|PubMed:17098193" FT MUTAGEN 162 FT /note="F->E: No effect on binding to SF3A3." FT /evidence="ECO:0000269|PubMed:17098193" FT MUTAGEN 169 FT /note="L->K: Abolishes binding to SF3A3." FT /evidence="ECO:0000269|PubMed:17098193" FT HELIX 48..63 FT /evidence="ECO:0007829|PDB:2DT6" FT HELIX 66..74 FT /evidence="ECO:0007829|PDB:2DT6" FT HELIX 79..84 FT /evidence="ECO:0007829|PDB:2DT6" FT HELIX 91..103 FT /evidence="ECO:0007829|PDB:2DT6" FT HELIX 161..174 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 186..189 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 193..198 FT /evidence="ECO:0007829|PDB:2DT7" FT HELIX 205..217 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 221..225 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 231..233 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 236..271 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 704..710 FT /evidence="ECO:0007829|PDB:7P0V" FT STRAND 715..721 FT /evidence="ECO:0007829|PDB:1ZKH" FT STRAND 726..732 FT /evidence="ECO:0007829|PDB:7P0V" FT HELIX 737..748 FT /evidence="ECO:0007829|PDB:7P0V" FT HELIX 752..754 FT /evidence="ECO:0007829|PDB:7P0V" FT STRAND 755..759 FT /evidence="ECO:0007829|PDB:7P0V" FT STRAND 762..764 FT /evidence="ECO:0007829|PDB:1ZKH" FT STRAND 766..769 FT /evidence="ECO:0007829|PDB:7P08" FT HELIX 771..773 FT /evidence="ECO:0007829|PDB:7P0V" FT STRAND 779..785 FT /evidence="ECO:0007829|PDB:7P0V" SQ SEQUENCE 793 AA; 88886 MW; 7259F1EC4577305C CRC64; MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR NIVDKTASFV ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT QVQDMDEGSD DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV IHLALKERGG RKK //