ID SF3A3_HUMAN Reviewed; 501 AA. AC Q12874; D3DPT5; Q15460; Q5VT87; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 220. DE RecName: Full=Splicing factor 3A subunit 3; DE AltName: Full=SF3a60 {ECO:0000303|PubMed:11533230, ECO:0000303|PubMed:21349847}; DE AltName: Full=Spliceosome-associated protein 61; DE Short=SAP 61 {ECO:0000303|PubMed:8022796}; GN Name=SF3A3; Synonyms=SAP61; 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], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH RP SF3A1, IDENTIFICATION IN THE PRE-SPLICEOSOME, AND SUBCELLULAR LOCATION. RC TISSUE=Cervix adenocarcinoma; RX PubMed=8022796; DOI=10.1073/pnas.91.14.6403; RA Chiara M.D., Champion-Arnaud P., Buvoli M., Nadal-Ginard B., Reed R.; RT "Specific protein-protein interactions between the essential mammalian RT spliceosome-associated proteins SAP 61 and SAP 114."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6403-6407(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Cervix adenocarcinoma; RX PubMed=7816610; DOI=10.1093/nar/22.24.5223; RA Kraemer A., Legrain P., Mulhauser F., Groening K., Brosi R., Bilbe G.; RT "Splicing factor SF3a60 is the mammalian homologue of PRP9 of S.cerevisiae: RT the conserved zinc finger-like motif is functionally exchangeable in RT vivo."; RL Nucleic Acids Res. 22:5223-5228(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye, and Lung; 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 [6] RP PROTEIN SEQUENCE OF 1-9; 265-273 AND 292-303, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [7] RP FUNCTION, SUBCELLULAR LOCATION, 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 [8] 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 [9] 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 [10] 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-365; SER-367 AND RP SER-369, 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 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 [16] 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 [17] RP SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 174-PRO--ALA-180. 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367 AND SER-369, 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54; SER-121; SER-295; SER-299 RP AND THR-475, 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 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 [23] RP STRUCTURE BY NMR OF 71-107 IN COMPLEX WITH SF3A1, AND SUBUNIT. 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 [24] {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 [25] 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 [26] {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 [27] {ECO:0007744|PDB:7Q4O, ECO:0007744|PDB:7Q4P} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) IN COMPLEX WITH THE 17S RP U2 SNRNP COMPLEX, FUNCTION, AND IDENTIFICATION IN THE 17S U2 SNRNP COMPLEX. RX PubMed=34822310; DOI=10.1126/science.abm4245; RA Tholen J., Razew M., Weis F., Galej W.P.; RT "Structural basis of branch site recognition by the human spliceosome."; RL Science 375:50-57(2022). RN [28] {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:8022796, PubMed:10882114, PubMed:11533230, CC PubMed:32494006, PubMed:34822310). The 17S U2 SnRNP complex (1) CC directly participates in early spliceosome assembly and (2) mediates CC recognition of the intron branch site during pre-mRNA splicing by CC promoting the selection of the pre-mRNA branch-site adenosine, the CC nucleophile for the first step of splicing (PubMed:10882114, CC PubMed:11533230, PubMed:32494006, PubMed:34822310). Within the 17S U2 CC SnRNP complex, SF3A3 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 ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:8022796}. 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:21349847, PubMed:34822310, CC PubMed:36797247). Part of the SF3A subcomplex of the 17S U2 SnRNP CC complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62 CC and SF3A1/SAP114 (PubMed:8022796, PubMed:10882114, PubMed:11533230, CC PubMed:21349847, PubMed:17098193). 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). 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:10882114, CC PubMed:8022796, PubMed:29360106, PubMed:30315277). Identified in the CC spliceosome 'C' complex (PubMed:11991638). CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:11533230, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:17098193, CC ECO:0000269|PubMed:21349847, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:32494006, CC ECO:0000269|PubMed:34822310, ECO:0000269|PubMed:36797247, CC ECO:0000269|PubMed:8022796}. CC -!- INTERACTION: CC Q12874; P54253: ATXN1; NbExp=6; IntAct=EBI-1051880, EBI-930964; CC Q12874; P04792: HSPB1; NbExp=2; IntAct=EBI-1051880, EBI-352682; CC Q12874; P42858: HTT; NbExp=3; IntAct=EBI-1051880, EBI-466029; CC Q12874; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1051880, EBI-1055254; CC Q12874; Q15459: SF3A1; NbExp=7; IntAct=EBI-1051880, EBI-1054743; CC Q12874; O75478: TADA2A; NbExp=3; IntAct=EBI-1051880, EBI-742268; CC Q12874; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-1051880, EBI-749955; CC Q12874; Q9UDV6: ZNF212; NbExp=4; IntAct=EBI-1051880, EBI-1640204; CC Q12874; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-1051880, EBI-6248094; CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:8022796}. CC Nucleus {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:21349847, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277}. CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7816610}. CC -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U08815; AAA19625.1; -; mRNA. DR EMBL; X81789; CAA57388.1; -; mRNA. DR EMBL; AL603790; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07304.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07305.1; -; Genomic_DNA. DR EMBL; BC002395; AAH02395.1; -; mRNA. DR EMBL; BC011523; AAH11523.1; -; mRNA. DR CCDS; CCDS428.1; -. DR PIR; A55749; A55749. DR RefSeq; NP_006793.1; NM_006802.3. DR PDB; 2DT7; NMR; -; A=71-107. DR PDB; 5Z56; EM; 5.10 A; w=1-501. DR PDB; 5Z57; EM; 6.50 A; v=317-376. DR PDB; 5Z58; EM; 4.90 A; v=317-376. DR PDB; 6AH0; EM; 5.70 A; w=1-501. DR PDB; 6AHD; EM; 3.80 A; w=1-501. DR PDB; 6FF7; EM; 4.50 A; 9=1-501. DR PDB; 6QX9; EM; 3.28 A; A3=1-501. DR PDB; 6Y50; EM; 4.10 A; 9=1-501. DR PDB; 6Y53; EM; 7.10 A; 9=1-501. DR PDB; 6Y5Q; EM; 7.10 A; 9=1-501. DR PDB; 7ABG; EM; 7.80 A; 4=1-501. DR PDB; 7ABH; EM; 4.50 A; 4=1-501. DR PDB; 7ABI; EM; 8.00 A; 4=1-501. DR PDB; 7EVO; EM; 2.50 A; C=1-501. DR PDB; 7ONB; EM; 3.10 A; N=1-501. DR PDB; 7Q3L; EM; 2.30 A; 9=1-501. DR PDB; 7Q4O; EM; 2.20 A; 9=1-501. DR PDB; 7Q4P; EM; 2.20 A; 9=1-501. DR PDB; 7QTT; EM; 3.10 A; J=1-501. DR PDB; 7VPX; EM; 3.00 A; C=1-501. DR PDB; 8CH6; EM; 5.90 A; J=1-501. DR PDB; 8HK1; EM; 2.70 A; C=1-501. 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; 6Y50; -. DR PDBsum; 6Y53; -. DR PDBsum; 6Y5Q; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABH; -. DR PDBsum; 7ABI; -. DR PDBsum; 7EVO; -. DR PDBsum; 7ONB; -. DR PDBsum; 7Q3L; -. DR PDBsum; 7Q4O; -. DR PDBsum; 7Q4P; -. DR PDBsum; 7QTT; -. DR PDBsum; 7VPX; -. DR PDBsum; 8CH6; -. DR PDBsum; 8HK1; -. DR AlphaFoldDB; Q12874; -. DR BMRB; Q12874; -. DR EMDB; EMD-10688; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11696; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-12994; -. DR EMDB; EMD-13793; -. DR EMDB; EMD-13811; -. DR EMDB; EMD-13812; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-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; Q12874; -. DR BioGRID; 116146; 302. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2565; SF3A complex. DR CORUM; Q12874; -. DR DIP; DIP-882N; -. DR IntAct; Q12874; 71. DR MINT; Q12874; -. DR STRING; 9606.ENSP00000362110; -. DR DrugBank; DB12695; Phenethyl Isothiocyanate. DR GlyGen; Q12874; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q12874; -. DR MetOSite; Q12874; -. DR PhosphoSitePlus; Q12874; -. DR SwissPalm; Q12874; -. DR BioMuta; SF3A3; -. DR DMDM; 17380310; -. DR EPD; Q12874; -. DR jPOST; Q12874; -. DR MassIVE; Q12874; -. DR MaxQB; Q12874; -. DR PaxDb; 9606-ENSP00000362110; -. DR PeptideAtlas; Q12874; -. DR ProteomicsDB; 58997; -. DR Pumba; Q12874; -. DR Antibodypedia; 31818; 176 antibodies from 29 providers. DR DNASU; 10946; -. DR Ensembl; ENST00000373019.5; ENSP00000362110.4; ENSG00000183431.12. DR GeneID; 10946; -. DR KEGG; hsa:10946; -. DR MANE-Select; ENST00000373019.5; ENSP00000362110.4; NM_006802.4; NP_006793.1. DR UCSC; uc001cci.4; human. DR AGR; HGNC:10767; -. DR CTD; 10946; -. DR DisGeNET; 10946; -. DR GeneCards; SF3A3; -. DR HGNC; HGNC:10767; SF3A3. DR HPA; ENSG00000183431; Low tissue specificity. DR MIM; 605596; gene. DR neXtProt; NX_Q12874; -. DR OpenTargets; ENSG00000183431; -. DR PharmGKB; PA35685; -. DR VEuPathDB; HostDB:ENSG00000183431; -. DR eggNOG; KOG2636; Eukaryota. DR GeneTree; ENSGT00530000063402; -. DR HOGENOM; CLU_027160_2_0_1; -. DR InParanoid; Q12874; -. DR OMA; GPKAFQK; -. DR OrthoDB; 5483967at2759; -. DR PhylomeDB; Q12874; -. DR TreeFam; TF315227; -. DR PathwayCommons; Q12874; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q12874; -. DR SIGNOR; Q12874; -. DR BioGRID-ORCS; 10946; 822 hits in 1125 CRISPR screens. DR ChiTaRS; SF3A3; human. DR EvolutionaryTrace; Q12874; -. DR GeneWiki; SF3A3; -. DR GenomeRNAi; 10946; -. DR Pharos; Q12874; Tbio. DR PRO; PR:Q12874; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q12874; Protein. DR Bgee; ENSG00000183431; Expressed in sural nerve and 208 other cell types or tissues. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. 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:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC-UCL. DR GO; GO:0006397; P:mRNA processing; IMP:HGNC-UCL. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB. DR GO; GO:1903241; P:U2-type prespliceosome assembly; IDA:UniProtKB. DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2. DR InterPro; IPR025086; SDE2-like_C_dom. DR InterPro; IPR031774; SF3A3_dom. DR InterPro; IPR024598; SF3a60/Prp9_C. DR InterPro; IPR021966; SF3a60_bindingd. DR PANTHER; PTHR12786:SF1; REPLICATION STRESS RESPONSE REGULATOR SDE2; 1. DR PANTHER; PTHR12786; SPLICING FACTOR SF3A-RELATED; 1. DR Pfam; PF13297; SDE2_2C; 1. DR Pfam; PF16837; SF3A3; 1. DR Pfam; PF12108; SF3a60_bindingd; 1. DR Pfam; PF11931; SF3a60_Prp9_C; 1. DR PROSITE; PS50171; ZF_MATRIN; 1. DR Genevisible; Q12874; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Metal-binding; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Spliceosome; Zinc; Zinc-finger. FT CHAIN 1..501 FT /note="Splicing factor 3A subunit 3" FT /id="PRO_0000174318" FT ZN_FING 406..437 FT /note="Matrin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130" FT REGION 343..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 175..179 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:21349847" FT COMPBIAS 356..373 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 54 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 121 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 295 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 367 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 369 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 475 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MUTAGEN 174..180 FT /note="Missing: Loss of nuclear location." FT /evidence="ECO:0000269|PubMed:21349847" FT CONFLICT 176 FT /note="E -> G (in Ref. 2; CAA57388)" FT /evidence="ECO:0000305" FT TURN 3..5 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 6..27 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 33..58 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 59..63 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 64..71 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 78..87 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 100..102 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 103..108 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 126..128 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 132..138 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 143..153 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 182..200 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 206..219 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 221..223 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 285..287 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 294..301 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 304..307 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 309..313 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 314..316 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 318..333 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 335..350 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 353..361 FT /evidence="ECO:0007829|PDB:7EVO" FT HELIX 396..399 FT /evidence="ECO:0007829|PDB:7Q4O" FT TURN 400..403 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 404..408 FT /evidence="ECO:0007829|PDB:7Q4P" FT TURN 409..412 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 413..415 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 419..425 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 429..438 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 444..446 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 452..469 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 473..476 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 482..484 FT /evidence="ECO:0007829|PDB:7Q4P" FT STRAND 485..487 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 489..491 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 495..500 FT /evidence="ECO:0007829|PDB:7EVO" SQ SEQUENCE 501 AA; 58849 MW; 6E6F6EA17777E1E2 CRC64; METILEQQRR YHEEKERLMD VMAKEMLTKK STLRDQINSD HRTRAMQDRY MEVSGNLRDL YDDKDGLRKE ELNAISGPNE FAEFYNRLKQ IKEFHRKHPN EICVPMSVEF EELLKARENP SEEAQNLVEF TDEEGYGRYL DLHDCYLKYI NLKASEKLDY ITYLSIFDQL FDIPKERKNA EYKRYLEMLL EYLQDYTDRV KPLQDQNELF GKIQAEFEKK WENGTFPGWP KETSSALTHA GAHLDLSAFS SWEELASLGL DRLKSALLAL GLKCGGTLEE RAQRLFSTKG KSLESLDTSL FAKNPKSKGT KRDTERNKDI AFLEAQIYEY VEILGEQRHL THENVQRKQA RTGEEREEEE EEQISESESE DEENEIIYNP KNLPLGWDGK PIPYWLYKLH GLNINYNCEI CGNYTYRGPK AFQRHFAEWR HAHGMRCLGI PNTAHFANVT QIEDAVSLWA KLKLQKASER WQPDTEEEYE DSSGNVVNKK TYEDLKRQGL L //