SF3A2_HUMAN
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 03-AUG-2022, entry version 192.
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).
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, including the Bact complex
CC (PubMed:29361316, PubMed:29360106, 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}.
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). SF3A associates with the splicing factor SF3B and a
CC 12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein
CC complex (17S U2 snRNP) (PubMed:10882114, PubMed:11533230). Identified
CC in the spliceosome 'E' complex, a precursor of the spliceosome 'A'
CC complex (PubMed:10882114). Identified in the spliceosome 'A' and 'B'
CC complexes (PubMed:10882114, PubMed:29361316, PubMed:29360106,
CC PubMed:30315277). Identified in the spliceosome 'C' complex
CC (PubMed:11991638). Interacts with HTATSF1 (PubMed:9710584).
CC {ECO:0000269|PubMed:10882114, ECO:0000269|PubMed:11533230,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:21349847,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000269|PubMed:30315277, 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}.
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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; 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 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; 7ONB; -.
DR PDBsum; 7Q4O; -.
DR PDBsum; 7Q4P; -.
DR AlphaFoldDB; Q15428; -.
DR SMR; Q15428; -.
DR BioGRID; 113826; 365.
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; 143.
DR MINT; Q15428; -.
DR STRING; 9606.ENSP00000221494; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; Q15428; 1 site, 1 O-linked glycan (1 site).
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; Q15428; -.
DR PeptideAtlas; Q15428; -.
DR PRIDE; Q15428; -.
DR ProteomicsDB; 60588; -.
DR Antibodypedia; 22956; 173 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 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; PGVHPPN; -.
DR OrthoDB; 1320891at2759; -.
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; 797 hits in 1079 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 164 other tissues.
DR ExpressionAtlas; Q15428; baseline and differential.
DR Genevisible; Q15428; HS.
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; 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: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 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 Pfam; PF16835; SF3A2; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 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; 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:6FF4"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:7ONB"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:7ONB"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:7ONB"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:7ONB"
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
