SF3A3_HUMAN
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 03-AUG-2022, entry version 211.
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].
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).
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:8022796,
CC PubMed:10882114, PubMed:11533230). Involved in pre-mRNA splicing as a
CC component of pre-catalytic spliceosome 'B' complexes (PubMed:29360106,
CC PubMed:30315277). {ECO:0000269|PubMed:10882114,
CC ECO:0000269|PubMed:11533230, ECO:0000269|PubMed:29360106,
CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:8022796}.
CC -!- SUBUNIT: Component of splicing factor SF3A which is composed of three
CC subunits; SF3A3/SAP61, SF3A2/SAP62 and SF3A1/SAP114 (PubMed:8022796,
CC PubMed:10882114, PubMed:11533230, PubMed:21349847). SF3A1 functions as
CC scaffold that interacts directly with both SF3A2 and SF3A3
CC (PubMed:11533230, PubMed:21349847, PubMed:17098193). SF3A associates
CC with the splicing factor SF3B and a 12S RNA unit to form the mature 17S
CC U2 small nuclear ribonucleoprotein complex (17S U2 snRNP)
CC (PubMed:10882114, PubMed:11533230, PubMed:17098193). Identified in the
CC spliceosome 'E' complex, a precursor of the spliceosome 'A' complex
CC (PubMed:10882114). Identified in the spliceosome 'A' and 'B' complexes
CC (PubMed:8022796, PubMed:10882114, PubMed:29360106, PubMed:30315277).
CC Identified in the 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: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.
CC -!- SIMILARITY: Belongs to the SF3A3 family. {ECO:0000305}.
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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; 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 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; 7ONB; -.
DR PDBsum; 7Q3L; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q12874; -.
DR BMRB; Q12874; -.
DR SMR; Q12874; -.
DR BioGRID; 116146; 248.
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; 65.
DR MINT; Q12874; -.
DR STRING; 9606.ENSP00000362110; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; Q12874; 1 site, 1 O-linked glycan (1 site).
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; Q12874; -.
DR PeptideAtlas; Q12874; -.
DR PRIDE; Q12874; -.
DR ProteomicsDB; 58997; -.
DR Antibodypedia; 31818; 134 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 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; KDAHRRN; -.
DR OrthoDB; 383503at2759; -.
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; 791 hits in 1048 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 206 other tissues.
DR Genevisible; Q12874; 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:0005684; C:U2-type spliceosomal complex; IPI:ComplexPortal.
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; IPR031776; SF3A3.
DR InterPro; IPR031774; SF3A3_dom.
DR InterPro; IPR024598; SF3a60/Prp9_C.
DR InterPro; IPR021966; SF3a60_bindingd.
DR PANTHER; PTHR12786:SF3; PTHR12786:SF3; 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.
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 HELIX 80..96
FT /evidence="ECO:0007829|PDB:2DT7"
FT HELIX 394..400
FT /evidence="ECO:0007829|PDB:7ONB"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:7ONB"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 419..424
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 429..437
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 452..469
FT /evidence="ECO:0007829|PDB:7ONB"
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
