SF3A1_HUMAN
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 03-AUG-2022, entry version 218.
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].
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as a component of the splicing
CC factor SF3A complex that contributes to the assembly of the 17S U2
CC snRNP, and the subsequent assembly of the pre-spliceosome 'E' complex
CC and the pre-catalytic spliceosome 'A' complex (PubMed:10882114,
CC PubMed:11533230). Involved in pre-mRNA splicing as a component of pre-
CC catalytic spliceosome 'B' complexes (PubMed:29360106, PubMed:30315277).
CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:11533230,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:30315277}.
CC -!- SUBUNIT: Component of splicing factor SF3A which is composed of three
CC subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:10882114,
CC PubMed:11533230, PubMed:21349847). SF3A1 functions as scaffold that
CC interacts directly with both SF3A2 and SF3A3 (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:29360106, PubMed:30315277). Identified in the spliceosome 'C'
CC complex (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 -!- 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 -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3.
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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; 7P08; NMR; -; A=704-793.
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; 7P08; -.
DR AlphaFoldDB; Q15459; -.
DR BMRB; Q15459; -.
DR SMR; Q15459; -.
DR BioGRID; 115580; 335.
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; 83.
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; Q15459; -.
DR PeptideAtlas; Q15459; -.
DR PRIDE; Q15459; -.
DR ProteomicsDB; 19091; -.
DR ProteomicsDB; 60599; -. [Q15459-1]
DR Antibodypedia; 254; 296 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 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; HFSARMP; -.
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; 757 hits in 1086 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 216 other tissues.
DR ExpressionAtlas; Q15459; baseline and differential.
DR Genevisible; Q15459; HS.
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: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; -; 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; PTHR15316; 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; SSF109905; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50128; SURP; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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..177
FT /evidence="ECO:0007829|PDB:2DT7"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2DT7"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2DT7"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2DT7"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:2DT7"
FT STRAND 705..710
FT /evidence="ECO:0007829|PDB:1ZKH"
FT STRAND 715..721
FT /evidence="ECO:0007829|PDB:1ZKH"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:1ZKH"
FT HELIX 737..747
FT /evidence="ECO:0007829|PDB:1ZKH"
FT TURN 752..754
FT /evidence="ECO:0007829|PDB:1ZKH"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:1ZKH"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:1ZKH"
FT HELIX 770..773
FT /evidence="ECO:0007829|PDB:1ZKH"
FT STRAND 779..786
FT /evidence="ECO:0007829|PDB:1ZKH"
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
