ID SF3A2_HUMAN Reviewed; 464 AA. AC Q15428; B2RBU1; D6W605; O75245; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2002, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=Splicing factor 3A subunit 2; DE AltName: Full=SF3a66 {ECO:0000303|PubMed:11533230, ECO:0000303|PubMed:21349847}; DE AltName: Full=Spliceosome-associated protein 62; DE Short=SAP 62; GN Name=SF3A2; Synonyms=SAP62; 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 [GENOMIC DNA]. RX PubMed=8211113; DOI=10.1126/science.8211113; RA Bennett M., Reed R.; RT "Correspondence between a mammalian spliceosome component and an essential RT yeast splicing factor."; RL Science 262:105-108(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). 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=Lung, 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 [6] RP PROTEIN SEQUENCE OF 1-10; 151-158 AND 205-213, ACETYLATION AT MET-1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [7] RP INTERACTION WITH HTATSF1. RX PubMed=9710584; DOI=10.1128/mcb.18.9.5000; RA Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.; RT "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 RT through an unusual RNA recognition motif."; RL Mol. Cell. Biol. 18:5000-5009(1998). RN [8] 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 [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL RP C COMPLEX. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [11] RP IDENTIFICATION 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 [12] RP SUBCELLULAR LOCATION, AND SUBUNIT. 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] {ECO:0007744|PDB:6FF4} RP STRUCTURE BY ELECTRON MICROSCOPY (16.00 ANGSTROMS), FUNCTION, RP IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010; RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O., RA Urlaub H., Kastner B., Luhrmann R., Stark H.; RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact RT Complex."; RL Cell 172:454-464(2018). RN [15] {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 [16] 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 [17] {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 [18] {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 [19] {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, CC PubMed:34822310). The 17S U2 SnRNP complex (1) directly participates in CC early spliceosome assembly and (2) mediates recognition of the intron CC branch site during pre-mRNA splicing by promoting the selection of the CC pre-mRNA branch-site adenosine, the nucleophile for the first step of CC splicing (PubMed:10882114, PubMed:11533230, PubMed:32494006, CC PubMed:34822310). Within the 17S U2 SnRNP complex, SF3A2 is part of the CC SF3A subcomplex that contributes to the assembly of the 17S U2 snRNP, CC and the subsequent assembly of the pre-spliceosome 'E' complex and the CC 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, including the Bact complex CC (PubMed:29360106, PubMed:29361316, PubMed:30315277). Interacts directly CC with the duplex formed by U2 snRNA and the intron (PubMed:29360106). CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:11533230, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:32494006, CC ECO:0000269|PubMed:34822310}. 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:10882114, PubMed:11533230, PubMed:21349847). CC SF3A associates with the splicing factor SF3B and a 12S RNA unit to CC form the mature 17S U2 small nuclear ribonucleoprotein complex (17S U2 CC snRNP) (PubMed:10882114, PubMed:11533230). 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:10882114, PubMed:29361316, PubMed:29360106, PubMed:30315277). CC Identified in the spliceosome 'C' complex (PubMed:11991638). Interacts CC with HTATSF1 (PubMed:9710584). {ECO:0000269|PubMed:10882114, CC ECO:0000269|PubMed:11533230, ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:21349847, ECO:0000269|PubMed:29360106, CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277, CC ECO:0000269|PubMed:32494006, ECO:0000269|PubMed:34822310, CC ECO:0000269|PubMed:36797247, ECO:0000269|PubMed:9710584}. CC -!- INTERACTION: CC Q15428; Q12797-6: ASPH; NbExp=3; IntAct=EBI-2462271, EBI-12092171; CC Q15428; Q9UQB8-6: BAIAP2; NbExp=3; IntAct=EBI-2462271, EBI-9092016; CC Q15428; Q8NDZ0: BEND2; NbExp=3; IntAct=EBI-2462271, EBI-954079; CC Q15428; Q99459: CDC5L; NbExp=2; IntAct=EBI-2462271, EBI-374880; CC Q15428; O43143: DHX15; NbExp=2; IntAct=EBI-2462271, EBI-1237044; CC Q15428; P62993: GRB2; NbExp=3; IntAct=EBI-2462271, EBI-401755; CC Q15428; P11142: HSPA8; NbExp=2; IntAct=EBI-2462271, EBI-351896; CC Q15428; Q6MZP7: LIN54; NbExp=3; IntAct=EBI-2462271, EBI-1389411; CC Q15428; Q8IVT2: MISP; NbExp=3; IntAct=EBI-2462271, EBI-2555085; CC Q15428; O43639: NCK2; NbExp=3; IntAct=EBI-2462271, EBI-713635; CC Q15428; Q7RTV0: PHF5A; NbExp=2; IntAct=EBI-2462271, EBI-2555365; CC Q15428; Q96I25: RBM17; NbExp=2; IntAct=EBI-2462271, EBI-740272; CC Q15428; Q15637: SF1; NbExp=2; IntAct=EBI-2462271, EBI-744603; CC Q15428; Q15459: SF3A1; NbExp=4; IntAct=EBI-2462271, EBI-1054743; CC Q15428; P09661: SNRPA1; NbExp=2; IntAct=EBI-2462271, EBI-876439; CC Q15428; P62304: SNRPE; NbExp=2; IntAct=EBI-2462271, EBI-348082; CC Q15428; P62306: SNRPF; NbExp=2; IntAct=EBI-2462271, EBI-356900; CC Q15428; Q92734: TFG; NbExp=3; IntAct=EBI-2462271, EBI-357061; CC Q15428; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-2462271, EBI-6550597; CC Q15428; Q14119: VEZF1; NbExp=3; IntAct=EBI-2462271, EBI-11980193; CC Q15428; P07947: YES1; NbExp=3; IntAct=EBI-2462271, EBI-515331; CC Q15428; P25490: YY1; NbExp=5; IntAct=EBI-2462271, EBI-765538; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, CC ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:21349847, CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316, CC ECO:0000269|PubMed:30315277}. CC -!- SIMILARITY: Belongs to the SF3A2 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; L21990; AAA60301.1; -; Genomic_DNA. DR EMBL; AK314815; BAG37338.1; -; mRNA. DR EMBL; AC005263; AAC25613.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69398.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69400.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69401.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69402.1; -; Genomic_DNA. DR EMBL; BC004434; AAH04434.1; -; mRNA. DR EMBL; BC009903; AAH09903.1; -; mRNA. DR CCDS; CCDS12084.1; -. DR PIR; A47655; A47655. DR RefSeq; NP_009096.2; NM_007165.4. DR PDB; 5Z56; EM; 5.10 A; v=1-464. DR PDB; 5Z57; EM; 6.50 A; u=88-369. DR PDB; 5Z58; EM; 4.90 A; u=88-369. DR PDB; 6AH0; EM; 5.70 A; v=1-464. DR PDB; 6AHD; EM; 3.80 A; v=1-464. DR PDB; 6FF4; EM; 16.00 A; 7=1-464. DR PDB; 6FF7; EM; 4.50 A; 7=1-464. DR PDB; 6QX9; EM; 3.28 A; A2=1-209. DR PDB; 6Y53; EM; 7.10 A; 7=1-464. DR PDB; 6Y5Q; EM; 7.10 A; 7=1-464. DR PDB; 7ABG; EM; 7.80 A; F=1-464. DR PDB; 7ABH; EM; 4.50 A; F=1-464. DR PDB; 7ABI; EM; 8.00 A; F=1-464. DR PDB; 7EVO; EM; 2.50 A; B=1-464. DR PDB; 7ONB; EM; 3.10 A; M=1-464. DR PDB; 7Q4O; EM; 2.20 A; 1=1-464. DR PDB; 7Q4P; EM; 2.20 A; 1=1-464. DR PDB; 7QTT; EM; 3.10 A; I=1-464. DR PDB; 7VPX; EM; 3.00 A; B=1-464. DR PDB; 8CH6; EM; 5.90 A; I=1-464. DR PDB; 8HK1; EM; 2.70 A; B=1-464. DR PDBsum; 5Z56; -. DR PDBsum; 5Z57; -. DR PDBsum; 5Z58; -. DR PDBsum; 6AH0; -. DR PDBsum; 6AHD; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6QX9; -. DR PDBsum; 6Y53; -. DR PDBsum; 6Y5Q; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABH; -. DR PDBsum; 7ABI; -. DR PDBsum; 7EVO; -. DR PDBsum; 7ONB; -. DR PDBsum; 7Q4O; -. DR PDBsum; 7Q4P; -. DR PDBsum; 7QTT; -. DR PDBsum; 7VPX; -. DR PDBsum; 8CH6; -. DR PDBsum; 8HK1; -. DR AlphaFoldDB; Q15428; -. DR EMDB; EMD-10689; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11696; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-12994; -. 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-4255; -. 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; Q15428; -. DR BioGRID; 113826; 410. DR ComplexPortal; CPX-2539; U2 small nuclear ribonucleoprotein complex. DR ComplexPortal; CPX-2565; SF3A complex. DR CORUM; Q15428; -. DR DIP; DIP-42521N; -. DR IntAct; Q15428; 145. DR MINT; Q15428; -. DR STRING; 9606.ENSP00000221494; -. DR DrugBank; DB09130; Copper. DR MoonProt; Q15428; -. DR GlyGen; Q15428; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q15428; -. DR PhosphoSitePlus; Q15428; -. DR SwissPalm; Q15428; -. DR BioMuta; SF3A2; -. DR DMDM; 20141793; -. DR EPD; Q15428; -. DR jPOST; Q15428; -. DR MassIVE; Q15428; -. DR MaxQB; Q15428; -. DR PaxDb; 9606-ENSP00000221494; -. DR PeptideAtlas; Q15428; -. DR ProteomicsDB; 60588; -. DR Pumba; Q15428; -. DR Antibodypedia; 22956; 182 antibodies from 24 providers. DR DNASU; 8175; -. DR Ensembl; ENST00000221494.10; ENSP00000221494.3; ENSG00000104897.10. DR GeneID; 8175; -. DR KEGG; hsa:8175; -. DR MANE-Select; ENST00000221494.10; ENSP00000221494.3; NM_007165.5; NP_009096.2. DR UCSC; uc002lvg.4; human. DR AGR; HGNC:10766; -. DR CTD; 8175; -. DR DisGeNET; 8175; -. DR GeneCards; SF3A2; -. DR HGNC; HGNC:10766; SF3A2. DR HPA; ENSG00000104897; Low tissue specificity. DR MIM; 600796; gene. DR neXtProt; NX_Q15428; -. DR OpenTargets; ENSG00000104897; -. DR PharmGKB; PA35684; -. DR VEuPathDB; HostDB:ENSG00000104897; -. DR eggNOG; KOG0227; Eukaryota. DR GeneTree; ENSGT00720000108823; -. DR HOGENOM; CLU_050757_1_1_1; -. DR InParanoid; Q15428; -. DR OMA; SREGMPH; -. DR OrthoDB; 5475496at2759; -. DR PhylomeDB; Q15428; -. DR TreeFam; TF314370; -. DR PathwayCommons; Q15428; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q15428; -. DR SIGNOR; Q15428; -. DR BioGRID-ORCS; 8175; 831 hits in 1158 CRISPR screens. DR ChiTaRS; SF3A2; human. DR GeneWiki; SF3A2; -. DR GenomeRNAi; 8175; -. DR Pharos; Q15428; Tbio. DR PRO; PR:Q15428; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q15428; Protein. DR Bgee; ENSG00000104897; Expressed in left testis and 166 other cell types or tissues. DR ExpressionAtlas; Q15428; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. 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; IBA:GO_Central. 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:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central. DR GO; GO:1903241; P:U2-type prespliceosome assembly; IDA:UniProtKB. DR Gene3D; 2.60.40.2690; -; 1. DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2. DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2. DR InterPro; IPR031781; SF3A2_dom. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23205; SPLICING FACTOR 3A SUBUNIT 2; 1. DR PANTHER; PTHR23205:SF0; SPLICING FACTOR 3A SUBUNIT 2; 1. DR Pfam; PF16835; SF3A2; 1. DR Pfam; PF12874; zf-met; 1. DR SMART; SM01050; CactinC_cactus; 1. DR SMART; SM00451; ZnF_U1; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS50171; ZF_MATRIN; 1. DR Genevisible; Q15428; 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; Repeat; Spliceosome; Zinc; Zinc-finger. FT CHAIN 1..464 FT /note="Splicing factor 3A subunit 2" FT /id="PRO_0000174315" FT ZN_FING 54..84 FT /note="Matrin-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 217..464 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 217..374 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 388..464 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000269|Ref.6" FT MOD_RES 10 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q62203" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CONFLICT 29 FT /note="R -> P (in Ref. 1; AAA60301)" FT /evidence="ECO:0000305" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:6FF4" FT HELIX 19..41 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 45..48 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:7Q4O" FT TURN 57..60 FT /evidence="ECO:0007829|PDB:7Q4O" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 66..73 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 76..82 FT /evidence="ECO:0007829|PDB:7Q4O" FT HELIX 105..108 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 134..137 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 167..172 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 196..200 FT /evidence="ECO:0007829|PDB:7EVO" FT TURN 201..204 FT /evidence="ECO:0007829|PDB:7EVO" FT STRAND 205..208 FT /evidence="ECO:0007829|PDB:7EVO" SQ SEQUENCE 464 AA; 49256 MW; FA46F064A55EA2CE CRC64; MDFQHRPGGK TGSGGVASSS ESNRDRRERL RQLALETIDI NKDPYFMKNH LGSYECKLCL TLHNNEGSYL AHTQGKKHQT NLARRAAKEA KEAPAQPAPE KVKVEVKKFV KIGRPGYKVT KQRDSEMGQQ SLLFQIDYPE IAEGIMPRHR FMSAYEQRIE PPDRRWQYLL MAAEPYETIA FKVPSREIDK AEGKFWTHWN RETKQFFLQF HFKMEKPPAP PSLPAGPPGV KRPPPPLMNG LPPRPPLPES LPPPPPGGLP LPPMPPTGPA PSGPPGPPQL PPPAPGVHPP APVVHPPASG VHPPAPGVHP PAPGVHPPAP GVHPPTSGVH PPAPGVHPPA PGVHPPAPGV HPPAPGVHPP APGVHPPPSA GVHPQAPGVH PAAPAVHPQA PGVHPPAPGM HPQAPGVHPQ PPGVHPSAPG VHPQPPGVHP SNPGVHPPTP MPPMLRPPLP SEGPGNIPPP PPTN //