ID SON_HUMAN Reviewed; 2426 AA. AC P18583; D3DSF5; D3DSF6; E7ETE8; E7EU67; E7EVW3; E9PFQ2; O14487; O95981; AC Q14120; Q6PKE0; Q9H7B1; Q9P070; Q9P072; Q9UKP9; Q9UPY0; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 27-MAR-2024, entry version 223. DE RecName: Full=Protein SON; DE AltName: Full=Bax antagonist selected in saccharomyces 1; DE Short=BASS1; DE AltName: Full=Negative regulatory element-binding protein; DE Short=NRE-binding protein; DE AltName: Full=Protein DBP-5; DE AltName: Full=SON3; GN Name=SON; Synonyms=C21orf50, DBP5, KIAA1019, NREBP; GN ORFNames=HSPC310, HSPC312; 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] (ISOFORMS A; B; C; D; E AND F), AND VARIANTS RP SER-473; SER-473 AND LEU-1202. RX PubMed=11707072; DOI=10.1006/geno.2001.6640; RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.; RT "From PREDs and open reading frames to cDNA isolation: revisiting the human RT chromosome 21 transcription map."; RL Genomics 78:46-54(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM G), AND VARIANTS SER-473 AND LEU-1202; RP CYS-1575. RC TISSUE=Liver; RX PubMed=11306577; DOI=10.1074/jbc.m101330200; RA Sun C.-T., Lo W.-Y., Wang I.-H., Lo Y.-H., Shiou S.-R., Lai C.-K., RA Ting L.-P.; RT "Transcription repression of human hepatitis B virus genes by negative RT regulatory element-binding protein/SON."; RL J. Biol. Chem. 276:24059-24067(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), AND VARIANTS SER-473 RP AND LEU-1202; CYS-1575. RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-473. 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-689 (ISOFORM H). RC TISSUE=Placenta; RX PubMed=14637006; DOI=10.1016/s0378-1119(03)00835-7; RA Casadei R., Strippoli P., D'Addabbo P., Canaider S., Lenzi L., Vitale L., RA Giannone S., Frabetti F., Facchin F., Carinci P., Zannotti M.; RT "mRNA 5' region sequence incompleteness: a potential source of systematic RT errors in translation initiation codon assignment in human mRNAs."; RL Gene 321:185-193(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-130. RC TISSUE=Smooth muscle; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-114, AND VARIANT CYS-1575. RC TISSUE=Umbilical cord blood; RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.; RT "Human partial CDS from CD34+ stem cells."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 544-1903. RC TISSUE=Brain; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 554-2426 (ISOFORM A). RX PubMed=1944255; RA Chumakov I.M., Berdichevskii F.B., Sokolova N.V., Reznikov M.V., RA Prasolov V.S.; RT "Identification of a protein product of a novel human gene SON and the RT biological effect upon administering a changed form of this gene into RT mammalian cells."; RL Mol. Biol. (Mosk.) 25:731-740(1991). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 709-1079 (ISOFORM I). RC TISSUE=Placenta; RX PubMed=1435774; RA Bliskovskii V.V., Kirillov A.V., Zakhariev V.M., Chumakov I.M.; RT "The human SON gene: the large and small transcripts contains various 5'- RT terminal sequences."; RL Mol. Biol. (Mosk.) 26:807-812(1992). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1009-2426 (ISOFORMS A/D), AND VARIANTS RP SER-473 AND LEU-1202. RC TISSUE=Placenta; RX PubMed=1435773; RA Bliskovskii V.V., Berdichevskii F.B., Tkachenko A.V., Belova M.E., RA Chumakov I.M.; RT "Coding part of the son gene small transcript contains four areas of RT complete tandem repeats."; RL Mol. Biol. (Mosk.) 26:793-806(1992). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1145-2426 (ISOFORM F), SUBCELLULAR LOCATION, RP AND VARIANTS SER-473 AND LEU-1202. RX PubMed=1424986; DOI=10.1007/bf00360539; RA Mattioni T., Hume C.R., Konigorski S., Hayes P., Osterweil Z., Lee J.S.; RT "A cDNA clone for a novel nuclear protein with DNA binding activity."; RL Chromosoma 101:618-624(1992). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2175 (ISOFORM A). RX PubMed=3054499; RA Berdichevskii F.B., Chumakov I.M., Kiselev L.L.; RT "Decoding of the primary structure of the son3 region in human genome: RT identification of a new protein with unusual structure and homology with RT DNA-binding proteins."; RL Mol. Biol. (Mosk.) 22:794-801(1988). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1939-2426 (ISOFORM J). RC TISSUE=Cerebellum; RX PubMed=10509013; RX DOI=10.1002/(sici)1097-0061(19990930)15:13<1307::aid-yea455>3.0.co;2-3; RA Greenhalf W., Lee J., Chaudhuri B.; RT "A selection system for human apoptosis inhibitors using yeast."; RL Yeast 15:1307-1321(1999). RN [16] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1697, AND IDENTIFICATION BY RP 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-1556; SER-1697; RP SER-1783; SER-1948 AND SER-1950, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [19] RP INTERACTION WITH AML1-MTG8 FUSION PROTEIN. RX PubMed=18952841; DOI=10.1073/pnas.0802696105; RA Ahn E.Y., Yan M., Malakhova O.A., Lo M.C., Boyapati A., Ommen H.B., RA Hines R., Hokland P., Zhang D.E.; RT "Disruption of the NHR4 domain structure in AML1-ETO abrogates SON binding RT and promotes leukemogenesis."; RL Proc. Natl. Acad. Sci. U.S.A. 105:17103-17108(2008). RN [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-283 AND RP SER-1556, 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 [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16; LYS-288 AND LYS-2055, AND 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 [23] RP FUNCTION, AND INTERACTION WITH THE SPLICEOSOME. RX PubMed=20581448; DOI=10.4161/cc.9.13.12151; RA Huen M.S., Sy S.M., Leung K.M., Ching Y.P., Tipoe G.L., Man C., Dong S., RA Chen J.; RT "SON is a spliceosome-associated factor required for mitotic progression."; RL Cell Cycle 9:2679-2685(2010). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-142; SER-152; RP SER-154; SER-283; SER-1697; SER-1769; SER-2009; SER-2011; SER-2013 AND RP THR-2163, 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 [25] 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 [26] RP FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION WITH SRSF2. RX PubMed=21504830; DOI=10.1016/j.molcel.2011.03.014; RA Ahn E.Y., Dekelver R.C., Lo M.C., Nguyen T.A., Matsuura S., Boyapati A., RA Pandit S., Fu X.D., Zhang D.E.; RT "SON controls cell-cycle progression by coordinated regulation of RNA RT splicing."; RL Mol. Cell 42:185-198(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-154; SER-160; RP SER-283; SER-1556; SER-1697; SER-1769; SER-2011 AND SER-2013, 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 [28] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94; SER-142; SER-152; RP SER-154; SER-160; THR-959; SER-998; SER-1035; SER-1043; SER-1060; SER-1068; RP SER-1082; SER-1697; SER-1701; SER-1747; SER-1759; SER-1769; SER-1782; RP SER-1783; SER-1948; SER-1950; SER-1952; SER-2009; SER-2011; SER-2013; RP SER-2029; SER-2031; SER-2129 AND SER-2238, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-283; THR-400; RP SER-1556; SER-1651; SER-1697; SER-1766; SER-1769 AND SER-2238, AND 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 [31] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-950, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [32] RP INVOLVEMENT IN ZTTKS. RX PubMed=25590979; DOI=10.1038/gim.2014.191; RA Zhu X., Petrovski S., Xie P., Ruzzo E.K., Lu Y.F., McSweeney K.M., RA Ben-Zeev B., Nissenkorn A., Anikster Y., Oz-Levi D., Dhindsa R.S., RA Hitomi Y., Schoch K., Spillmann R.C., Heimer G., Marek-Yagel D., Tzadok M., RA Han Y., Worley G., Goldstein J., Jiang Y.H., Lancet D., Pras E., Shashi V., RA McHale D., Need A.C., Goldstein D.B.; RT "Whole-exome sequencing in undiagnosed genetic diseases: interpreting 119 RT trios."; RL Genet. Med. 17:774-781(2015). RN [33] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2149, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [34] RP FUNCTION, AND INVOLVEMENT IN ZTTKS. RX PubMed=27545680; DOI=10.1016/j.ajhg.2016.06.029; RG University of Washington Center for Mendelian Genomics; RG Deciphering Developmental Disorders Study; RA Kim J.H., Shinde D.N., Reijnders M.R., Hauser N.S., Belmonte R.L., RA Wilson G.R., Bosch D.G., Bubulya P.A., Shashi V., Petrovski S., Stone J.K., RA Park E.Y., Veltman J.A., Sinnema M., Stumpel C.T., Draaisma J.M., RA Nicolai J., Yntema H.G., Lindstrom K., de Vries B.B., Jewett T., RA Santoro S.L., Vogt J., Bachman K.K., Seeley A.H., Krokosky A., Turner C., RA Rohena L., Hempel M., Kortuem F., Lessel D., Neu A., Strom T.M., RA Wieczorek D., Bramswig N., Laccone F.A., Behunova J., Rehder H., RA Gordon C.T., Rio M., Romana S., Tang S., El-Khechen D., Cho M.T., RA McWalter K., Douglas G., Baskin B., Begtrup A., Funari T., Schoch K., RA Stegmann A.P., Stevens S.J., Zhang D.E., Traver D., Yao X., MacArthur D.G., RA Brunner H.G., Mancini G.M., Myers R.M., Owen L.B., Lim S.T., Stachura D.L., RA Vissers L.E., Ahn E.Y.; RT "De novo mutations in SON disrupt RNA splicing of genes essential for brain RT development and metabolism, causing an intellectual-disability syndrome."; RL Am. J. Hum. Genet. 99:711-719(2016). RN [35] RP INVOLVEMENT IN ZTTKS, AND VARIANTS ZTTKS SER-1637 AND TYR-1843. RX PubMed=27545676; DOI=10.1016/j.ajhg.2016.06.035; RA Tokita M.J., Braxton A.A., Shao Y., Lewis A.M., Vincent M., Kuery S., RA Besnard T., Isidor B., Latypova X., Bezieau S., Liu P., Motter C.S., RA Melver C.W., Robin N.H., Infante E.M., McGuire M., El-Gharbawy A., RA Littlejohn R.O., McLean S.D., Bi W., Bacino C.A., Lalani S.R., Scott D.A., RA Eng C.M., Yang Y., Schaaf C.P., Walkiewicz M.A.; RT "De novo truncating variants in SON cause intellectual disability, RT congenital malformations, and failure to thrive."; RL Am. J. Hum. Genet. 99:720-727(2016). RN [36] RP INVOLVEMENT IN ZTTKS. RX PubMed=27256762; DOI=10.1002/ajmg.a.37761; RA Takenouchi T., Miura K., Uehara T., Mizuno S., Kosaki K.; RT "Establishing SON in 21q22.11 as a cause a new syndromic form of RT intellectual disability: Possible contribution to Braddock-Carey syndrome RT phenotype."; RL Am. J. Med. Genet. A 170:2587-2590(2016). RN [37] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-64; LYS-2055; LYS-2092 AND RP LYS-2149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [38] RP INTERACTION WITH USH1G, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=34023904; DOI=10.1093/nar/gkab386; RA Yildirim A., Mozaffari-Jovin S., Wallisch A.K., Schaefer J., Ludwig S.E.J., RA Urlaub H., Luehrmann R., Wolfrum U.; RT "SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear RT transfer of tri-snRNP complexes."; RL Nucleic Acids Res. 49:5845-5866(2021). CC -!- FUNCTION: RNA-binding protein that acts as a mRNA splicing cofactor by CC promoting efficient splicing of transcripts that possess weak splice CC sites. Specifically promotes splicing of many cell-cycle and DNA-repair CC transcripts that possess weak splice sites, such as TUBG1, KATNB1, CC TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by CC facilitating the interaction between Serine/arginine-rich proteins such CC as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the CC consensus DNA sequence: 5'-GA[GT]AN[CG][AG]CC-3'. May indirectly CC repress hepatitis B virus (HBV) core promoter activity and CC transcription of HBV genes and production of HBV virions. Essential for CC correct RNA splicing of multiple genes critical for brain development, CC neuronal migration and metabolism, including TUBG1, FLNA, PNKP, WDR62, CC PSMD3, PCK2, PFKL, IDH2, and ACY1 (PubMed:27545680). CC {ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830, CC ECO:0000269|PubMed:27545680}. CC -!- SUBUNIT: Interacts with SRSF2. Associates with the spliceosome. CC Interacts with the AML1-MTG8 (AML1-ETO) fusion protein, possibly CC leading to trigger signals inhibiting leukemogenesis. Interacts with CC USH1G (PubMed:34023904). {ECO:0000269|PubMed:18952841, CC ECO:0000269|PubMed:20581448, ECO:0000269|PubMed:21504830, CC ECO:0000269|PubMed:34023904}. CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:1424986, CC ECO:0000269|PubMed:21504830, ECO:0000269|PubMed:34023904}. CC Note=Colocalizes with the pre-mRNA splicing factor SRSF2. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=10; CC Comment=Experimental confirmation may be lacking for some isoforms.; CC Name=F; CC IsoId=P18583-1; Sequence=Displayed; CC Name=A; CC IsoId=P18583-2; Sequence=VSP_004401, VSP_004402, VSP_004403; CC Name=B; CC IsoId=P18583-3; Sequence=VSP_004404, VSP_004405; CC Name=C; CC IsoId=P18583-4; Sequence=VSP_004406, VSP_004407; CC Name=D; CC IsoId=P18583-5; Sequence=VSP_004403; CC Name=E; CC IsoId=P18583-6; Sequence=VSP_004408, VSP_004409; CC Name=G; CC IsoId=P18583-7; Sequence=VSP_004410; CC Name=H; CC IsoId=P18583-8; Sequence=VSP_004411, VSP_004412; CC Name=I; CC IsoId=P18583-9; Sequence=VSP_004413; CC Name=J; CC IsoId=P18583-10; Sequence=VSP_004414, VSP_004415; CC -!- TISSUE SPECIFICITY: Widely expressed, with the higher expression seen CC in leukocyte and heart. CC -!- DOMAIN: Contains 8 types of repeats which are distributed in 3 regions. CC -!- DISEASE: ZTTK syndrome (ZTTKS) [MIM:617140]: An autosomal dominant CC syndrome characterized by intellectual disability, developmental delay, CC malformations of the cerebral cortex, epilepsy, vision problems, CC musculo-skeletal abnormalities, and congenital malformations. CC {ECO:0000269|PubMed:25590979, ECO:0000269|PubMed:27256762, CC ECO:0000269|PubMed:27545676, ECO:0000269|PubMed:27545680}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform C]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform E]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH02422.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=BAA82971.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=CAA44793.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAC69885.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={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; AF380179; AAL34497.1; -; mRNA. DR EMBL; AF380180; AAL34498.1; -; mRNA. DR EMBL; AF380181; AAL34499.1; -; mRNA. DR EMBL; AF380182; AAL34500.1; -; mRNA. DR EMBL; AF380183; AAL34501.1; -; mRNA. DR EMBL; AF380184; AAL34502.1; -; mRNA. DR EMBL; AY026895; AAK07692.1; -; mRNA. DR EMBL; AB028942; BAA82971.2; ALT_INIT; mRNA. DR EMBL; AP000303; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000304; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09814.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09818.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09821.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09823.1; -; Genomic_DNA. DR EMBL; AF435977; AAL30810.1; -; mRNA. DR EMBL; AK024752; BAB14985.1; -; mRNA. DR EMBL; AF161428; AAF28988.1; -; mRNA. DR EMBL; AF161430; AAF28990.1; -; mRNA. DR EMBL; BC002422; AAH02422.1; ALT_SEQ; mRNA. DR EMBL; X63751; CAC69885.1; ALT_SEQ; mRNA. DR EMBL; X63753; CAA45282.1; -; mRNA. DR EMBL; X63071; CAA44793.1; ALT_FRAME; mRNA. DR EMBL; M36428; AAA36624.1; -; Genomic_DNA. DR EMBL; AF139897; AAD50078.1; -; mRNA. DR CCDS; CCDS13629.1; -. [P18583-1] DR CCDS; CCDS13631.1; -. [P18583-3] DR CCDS; CCDS74784.1; -. [P18583-6] DR PIR; S26650; S26650. DR RefSeq; NP_001278340.1; NM_001291411.1. [P18583-6] DR RefSeq; NP_001278341.1; NM_001291412.1. DR RefSeq; NP_115571.2; NM_032195.2. [P18583-3] DR RefSeq; NP_620305.2; NM_138927.2. [P18583-1] DR PDB; 7CIQ; X-ray; 1.59 A; C=2026-2035. DR PDB; 7CIR; X-ray; 1.81 A; C=2026-2035. DR PDB; 7CIS; X-ray; 2.10 A; C=2026-2034. DR PDB; 7DYN; X-ray; 2.00 A; C=2026-2035. DR PDBsum; 7CIQ; -. DR PDBsum; 7CIR; -. DR PDBsum; 7CIS; -. DR PDBsum; 7DYN; -. DR AlphaFoldDB; P18583; -. DR SMR; P18583; -. DR BioGRID; 112534; 199. DR DIP; DIP-42289N; -. DR IntAct; P18583; 58. DR MINT; P18583; -. DR STRING; 9606.ENSP00000348984; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR GlyConnect; 2861; 1 O-GlcNAc glycan (2 sites). [P18583-1] DR GlyCosmos; P18583; 10 sites, 2 glycans. DR GlyGen; P18583; 18 sites, 2 O-linked glycans (18 sites). DR iPTMnet; P18583; -. DR PhosphoSitePlus; P18583; -. DR SwissPalm; P18583; -. DR BioMuta; SON; -. DR DMDM; 296453022; -. DR EPD; P18583; -. DR jPOST; P18583; -. DR MassIVE; P18583; -. DR MaxQB; P18583; -. DR PaxDb; 9606-ENSP00000348984; -. DR PeptideAtlas; P18583; -. DR ProteomicsDB; 53592; -. [P18583-1] DR ProteomicsDB; 53593; -. [P18583-10] DR ProteomicsDB; 53594; -. [P18583-2] DR ProteomicsDB; 53595; -. [P18583-3] DR ProteomicsDB; 53596; -. [P18583-4] DR ProteomicsDB; 53597; -. [P18583-5] DR ProteomicsDB; 53598; -. [P18583-6] DR ProteomicsDB; 53599; -. [P18583-7] DR ProteomicsDB; 53600; -. [P18583-8] DR ProteomicsDB; 53601; -. [P18583-9] DR Pumba; P18583; -. DR Antibodypedia; 7410; 70 antibodies from 20 providers. DR DNASU; 6651; -. DR Ensembl; ENST00000300278.8; ENSP00000300278.2; ENSG00000159140.23. [P18583-3] DR Ensembl; ENST00000356577.10; ENSP00000348984.4; ENSG00000159140.23. [P18583-1] DR Ensembl; ENST00000381679.8; ENSP00000371095.4; ENSG00000159140.23. [P18583-6] DR Ensembl; ENST00000455528.5; ENSP00000399783.1; ENSG00000159140.23. [P18583-4] DR GeneID; 6651; -. DR KEGG; hsa:6651; -. DR MANE-Select; ENST00000356577.10; ENSP00000348984.4; NM_138927.4; NP_620305.3. DR UCSC; uc002ysc.5; human. [P18583-1] DR AGR; HGNC:11183; -. DR CTD; 6651; -. DR DisGeNET; 6651; -. DR GeneCards; SON; -. DR HGNC; HGNC:11183; SON. DR HPA; ENSG00000159140; Low tissue specificity. DR MalaCards; SON; -. DR MIM; 182465; gene. DR MIM; 617140; phenotype. DR neXtProt; NX_P18583; -. DR OpenTargets; ENSG00000159140; -. DR Orphanet; 500150; Brain malformations-musculoskeletal abnormalities-facial dysmorphism-intellectual disability syndrome. DR PharmGKB; PA36020; -. DR VEuPathDB; HostDB:ENSG00000159140; -. DR eggNOG; ENOG502QPQ7; Eukaryota. DR GeneTree; ENSGT00730000111141; -. DR HOGENOM; CLU_230016_0_0_1; -. DR InParanoid; P18583; -. DR OMA; NETEQCT; -. DR OrthoDB; 2882949at2759; -. DR PhylomeDB; P18583; -. DR TreeFam; TF330344; -. DR PathwayCommons; P18583; -. DR SignaLink; P18583; -. DR SIGNOR; P18583; -. DR BioGRID-ORCS; 6651; 700 hits in 1169 CRISPR screens. DR ChiTaRS; SON; human. DR GeneWiki; SON; -. DR GenomeRNAi; 6651; -. DR Pharos; P18583; Tbio. DR PRO; PR:P18583; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P18583; Protein. DR Bgee; ENSG00000159140; Expressed in pylorus and 211 other cell types or tissues. DR ExpressionAtlas; P18583; baseline and differential. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR Gene3D; 3.30.160.20; -; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR032922; SON. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR PANTHER; PTHR46528; PROTEIN SON; 1. DR PANTHER; PTHR46528:SF1; PROTEIN SON; 1. DR Pfam; PF14709; DND1_DSRM; 1. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17069; RSRP; 1. DR SMART; SM00443; G_patch; 1. DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50137; DS_RBD; 1. DR PROSITE; PS50174; G_PATCH; 1. DR Genevisible; P18583; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; KW Disease variant; DNA-binding; Intellectual disability; Isopeptide bond; KW Methylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..2426 FT /note="Protein SON" FT /id="PRO_0000072037" FT REPEAT 1006..1011 FT /note="1-1" FT REPEAT 1014..1019 FT /note="1-2" FT REPEAT 1021..1026 FT /note="1-3" FT REPEAT 1030..1035 FT /note="1-4" FT REPEAT 1038..1043 FT /note="1-5" FT REPEAT 1046..1051 FT /note="1-6" FT REPEAT 1055..1060 FT /note="1-7" FT REPEAT 1063..1068 FT /note="1-8" FT REPEAT 1071..1076 FT /note="1-9" FT REPEAT 1080..1085 FT /note="1-10" FT REPEAT 1089..1094 FT /note="1-11" FT REPEAT 1100..1105 FT /note="1-12" FT REPEAT 1111..1116 FT /note="1-13" FT REPEAT 1121..1126 FT /note="1-14" FT REPEAT 1925..1931 FT /note="2-1" FT REPEAT 1934..1952 FT /note="3-1" FT REPEAT 1953..1959 FT /note="2-2" FT REPEAT 1960..1966 FT /note="2-3" FT REPEAT 1967..1973 FT /note="2-4" FT REPEAT 1974..1980 FT /note="2-5" FT REPEAT 1981..1987 FT /note="2-6" FT REPEAT 1988..1994 FT /note="2-7" FT REPEAT 1995..2013 FT /note="3-2" FT DOMAIN 2305..2351 FT /note="G-patch" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092" FT DOMAIN 2371..2426 FT /note="DRBM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266" FT REGION 24..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 77..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..328 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 406..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 726..895 FT /note="17 X 10 AA tandem repeats of L-A-[ST]-[NSG]-[TS]- FT MDSQM" FT REGION 912..988 FT /note="11 X 7 AA tandem repeats of [DR]-P-Y-R- FT [LI][AG][QHP]" FT REGION 1006..1126 FT /note="14 X 6 AA repeats of [ED]-R-S-M-M-S" FT REGION 1144..1236 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1147..1179 FT /note="3 X 11 AA tandem repats of P-P-L-P-P-E-E-P-P-[TME]- FT [MTG]" FT REGION 1359..1390 FT /note="4 X 8 AA tandem repeats of V-L-E-SS-[AVT]-VT" FT REGION 1645..1722 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1754..2054 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1925..1994 FT /note="7 X 7 AA repeats of P-S-R-R-S-R-[TS]" FT REGION 1934..2013 FT /note="2 X 19 AA repeats of P-S-R-R-R-R-S-R-S-V-V-R-R-R-S- FT F-S-I-S" FT REGION 2013..2039 FT /note="3 X tandem repeats of [ST]-P-[VLI]-R-[RL]-[RK]-[RF]- FT S-R" FT REGION 2200..2220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..45 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 77..91 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 107..127 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 128..155 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1147..1180 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1186..1236 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1780..1827 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1841..1914 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1921..1945 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1958..2006 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2019..2043 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22814378" FT MOD_RES 16 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 94 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 142 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 288 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 400 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 950 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 959 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 998 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1007 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9QX47" FT MOD_RES 1022 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9QX47" FT MOD_RES 1035 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1043 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1060 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1068 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1082 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1556 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1651 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1697 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1701 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1747 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1759 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1766 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 1769 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1782 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1783 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1948 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1950 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1952 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2009 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2011 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 2013 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 2029 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2031 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2055 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 2129 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2163 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 2238 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 64 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2055 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2092 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 2149 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 687..689 FT /note="VAQ -> NVP (in isoform H)" FT /evidence="ECO:0000303|PubMed:14637006" FT /id="VSP_004411" FT VAR_SEQ 687 FT /note="V -> Q (in isoform A)" FT /evidence="ECO:0000303|PubMed:11707072, FT ECO:0000303|PubMed:1944255, ECO:0000303|PubMed:3054499" FT /id="VSP_004401" FT VAR_SEQ 688..1006 FT /note="Missing (in isoform A)" FT /evidence="ECO:0000303|PubMed:11707072, FT ECO:0000303|PubMed:1944255, ECO:0000303|PubMed:3054499" FT /id="VSP_004402" FT VAR_SEQ 690..2416 FT /note="Missing (in isoform H)" FT /evidence="ECO:0000303|PubMed:14637006" FT /id="VSP_004412" FT VAR_SEQ 748..787 FT /note="Missing (in isoform G)" FT /evidence="ECO:0000303|PubMed:11306577" FT /id="VSP_004410" FT VAR_SEQ 770 FT /note="S -> SMDSQMLASNTMDSQMLASNTMDSQMLASSTMDSQMLATSS (in FT isoform I)" FT /evidence="ECO:0000303|PubMed:1435774" FT /id="VSP_004413" FT VAR_SEQ 2108 FT /note="K -> F (in isoform E)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_004408" FT VAR_SEQ 2109..2426 FT /note="Missing (in isoform E)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_004409" FT VAR_SEQ 2220..2303 FT /note="PVDISTAMSERALAQKRLSENAFDLEAMSMLNRAQERIDAWAQLNSIPGQFT FT GSTGVQVLTQEQLANTGAQAWIKKDQFLRAAP -> GRVKRQGRVRRQMKQPAASHLTV FT TRCNSLCGTKPQSEKHRIAENSVITSLPNIGPSLHLWEGSPRYNYLASRFASRLYSSRF FT WW (in isoform B)" FT /evidence="ECO:0000303|PubMed:10470851, FT ECO:0000303|PubMed:11707072" FT /id="VSP_004404" FT VAR_SEQ 2257..2282 FT /note="IDAWAQLNSIPGQFTGSTGVQVLTQE -> VCSSFLKKIIIYHQPTHTNVPV FT LMSK (in isoform J)" FT /evidence="ECO:0000303|PubMed:10509013" FT /id="VSP_004414" FT VAR_SEQ 2283..2426 FT /note="Missing (in isoform J)" FT /evidence="ECO:0000303|PubMed:10509013" FT /id="VSP_004415" FT VAR_SEQ 2296..2325 FT /note="DQFLRAAPVTGGMGAVLMRKMGWREGEGLG -> GQILVAVFLPRSVPAVLF FT TTLLLPRPRISS (in isoform C)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_004406" FT VAR_SEQ 2304..2426 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:10470851, FT ECO:0000303|PubMed:11707072" FT /id="VSP_004405" FT VAR_SEQ 2326..2426 FT /note="Missing (in isoform C)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_004407" FT VAR_SEQ 2410..2426 FT /note="RNGALTRPNCMFFLNRY -> INGSAYQPSFASPNKKHAKATAATVVLQAMG FT LVPKDLMANATCFRSASRR (in isoform A and isoform D)" FT /evidence="ECO:0000303|PubMed:11707072, FT ECO:0000303|PubMed:1944255, ECO:0000303|PubMed:3054499" FT /id="VSP_004403" FT VARIANT 473 FT /note="P -> S (in dbSNP:rs35622138)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:11306577, ECO:0000269|PubMed:11707072, FT ECO:0000269|PubMed:1424986, ECO:0000269|PubMed:1435773, FT ECO:0000269|Ref.5" FT /id="VAR_065456" FT VARIANT 555 FT /note="T -> M (in dbSNP:rs13049658)" FT /id="VAR_065457" FT VARIANT 870 FT /note="T -> A (in dbSNP:rs11908823)" FT /id="VAR_056990" FT VARIANT 1202 FT /note="S -> L (in dbSNP:rs13433428)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:11306577, ECO:0000269|PubMed:11707072, FT ECO:0000269|PubMed:1424986, ECO:0000269|PubMed:1435773" FT /id="VAR_065458" FT VARIANT 1575 FT /note="R -> C (in dbSNP:rs13047599)" FT /evidence="ECO:0000269|PubMed:10470851, FT ECO:0000269|PubMed:11306577, ECO:0000269|Ref.8" FT /id="VAR_056991" FT VARIANT 1637 FT /note="T -> S (in ZTTKS; uncertain significance; de novo FT mutation associated in cis with Y-1843)" FT /evidence="ECO:0000269|PubMed:27545676" FT /id="VAR_077864" FT VARIANT 1843 FT /note="S -> Y (in ZTTKS; uncertain significance; de novo FT mutation associated in cis with S-1637)" FT /evidence="ECO:0000269|PubMed:27545676" FT /id="VAR_077865" FT CONFLICT 126 FT /note="E -> K (in Ref. 7; BAB14985)" FT /evidence="ECO:0000305" FT CONFLICT 129 FT /note="Y -> K (in Ref. 7; BAB14985)" FT /evidence="ECO:0000305" FT CONFLICT 1402 FT /note="Y -> S (in Ref. 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 1495 FT /note="N -> I (in Ref. 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 1538 FT /note="N -> S (in Ref. 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 1643 FT /note="I -> II (in Ref. 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 1692 FT /note="L -> I (in Ref. 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 1693 FT /note="A -> R (in Ref. 14; AAA36624)" FT /evidence="ECO:0000305" FT CONFLICT 1820..1821 FT /note="SS -> PH (in Ref. 12; CAA45282 and 14; AAA36624)" FT /evidence="ECO:0000305" FT CONFLICT 1939 FT /note="R -> S (in Ref. 15; AAD50078)" FT /evidence="ECO:0000305" FT CONFLICT 2090 FT /note="E -> V (in Ref. 2; AAK07692 and 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 2148 FT /note="P -> F (in Ref. 2; AAK07692 and 12; CAA45282)" FT /evidence="ECO:0000305" FT CONFLICT 2413..2416 FT /note="ALTR -> SPYQ (in Ref. 2; AAK07692)" FT /evidence="ECO:0000305" SQ SEQUENCE 2426 AA; 263830 MW; AE53B1157A37657D CRC64; MATNIEQIFR SFVVSKFREI QQELSSGRNE GQLNGETNTP IEGNQAGDAA ASARSLPNEE IVQKIEEVLS GVLDTELRYK PDLKEGSRKS RCVSVQTDPT DEIPTKKSKK HKKHKNKKKK KKKEKEKKYK RQPEESESKT KSHDDGNIDL ESDSFLKFDS EPSAVALELP TRAFGPSETN ESPAVVLEPP VVSMEVSEPH ILETLKPATK TAELSVVSTS VISEQSEQSV AVMPEPSMTK ILDSFAAAPV PTTTLVLKSS EPVVTMSVEY QMKSVLKSVE STSPEPSKIM LVEPPVAKVL EPSETLVVSS ETPTEVYPEP STSTTMDFPE SSAIEALRLP EQPVDVPSEI ADSSMTRPQE LPELPKTTAL ELQESSVASA MELPGPPATS MPELQGPPVT PVLELPGPSA TPVPELPGPL STPVPELPGP PATAVPELPG PSVTPVPQLS QELPGLPAPS MGLEPPQEVP EPPVMAQELP GLPLVTAAVE LPEQPAVTVA MELTEQPVTT TELEQPVGMT TVEHPGHPEV TTATGLLGQP EATMVLELPG QPVATTALEL PGQPSVTGVP ELPGLPSATR ALELSGQPVA TGALELPGPL MAAGALEFSG QSGAAGALEL LGQPLATGVL ELPGQPGAPE LPGQPVATVA LEISVQSVVT TSELSTMTVS QSLEVPSTTA LESYNTVAQE LPTTLVGETS VTVGVDPLMA PESHILASNT METHILASNT MDSQMLASNT MDSQMLASNT MDSQMLASST MDSQMLATSS MDSQMLATSS MDSQMLATST MDSQMLATSS MDSQMLATSS MDSQMLATSS MDSQMLATSS MDSQMLATST MDSQMLATST MDSQMLATSS MDSQMLASGT MDSQMLASGT MDAQMLASGT MDAQMLASST QDSAMLGSKS PDPYRLAQDP YRLAQDPYRL GHDPYRLGHD AYRLGQDPYR LGHDPYRLTP DPYRMSPRPY RIAPRSYRIA PRPYRLAPRP LMLASRRSMM MSYAAERSMM SSYERSMMSY ERSMMSPMAE RSMMSAYERS MMSAYERSMM SPMAERSMMS AYERSMMSAY ERSMMSPMAD RSMMSMGADR SMMSSYSAAD RSMMSSYSAA DRSMMSSYTA DRSMMSMAAD SYTDSYTDTY TEAYMVPPLP PEEPPTMPPL PPEEPPMTPP LPPEEPPEGP ALPTEQSALT AENTWPTEVP SSPSEESVSQ PEPPVSQSEI SEPSAVPTDY SVSASDPSVL VSEAAVTVPE PPPEPESSIT LTPVESAVVA EEHEVVPERP VTCMVSETPA MSAEPTVLAS EPPVMSETAE TFDSMRASGH VASEVSTSLL VPAVTTPVLA ESILEPPAMA APESSAMAVL ESSAVTVLES STVTVLESST VTVLEPSVVT VPEPPVVAEP DYVTIPVPVV SALEPSVPVL EPAVSVLQPS MIVSEPSVSV QESTVTVSEP AVTVSEQTQV IPTEVAIEST PMILESSIMS SHVMKGINLS SGDQNLAPEI GMQEIALHSG EEPHAEEHLK GDFYESEHGI NIDLNINNHL IAKEMEHNTV CAAGTSPVGE IGEEKILPTS ETKQRTVLDT YPGVSEADAG ETLSSTGPFA LEPDATGTSK GIEFTTASTL SLVNKYDVDL SLTTQDTEHD MVISTSPSGG SEADIEGPLP AKDIHLDLPS NNNLVSKDTE EPLPVKESDQ TLAALLSPKE SSGGEKEVPP PPKETLPDSG FSANIEDINE ADLVRPLLPK DMERLTSLRA GIEGPLLASD VGRDRSAASP VVSSMPERAS ESSSEEKDDY EIFVKVKDTH EKSKKNKNRD KGEKEKKRDS SLRSRSKRSK SSEHKSRKRT SESRSRARKR SSKSKSHRSQ TRSRSRSRRR RRSSRSRSKS RGRRSVSKEK RKRSPKHRSK SRERKRKRSS SRDNRKTVRA RSRTPSRRSR SHTPSRRRRS RSVGRRRSFS ISPSRRSRTP SRRSRTPSRR SRTPSRRSRT PSRRSRTPSR RSRTPSRRRR SRSVVRRRSF SISPVRLRRS RTPLRRRFSR SPIRRKRSRS SERGRSPKRL TDLDKAQLLE IAKANAAAMC AKAGVPLPPN LKPAPPPTIE EKVAKKSGGA TIEELTEKCK QIAQSKEDDD VIVNKPHVSD EEEEEPPFYH HPFKLSEPKP IFFNLNIAAA KPTPPKSQVT LTKEFPVSSG SQHRKKEADS VYGEWVPVEK NGEENKDDDN VFSSNLPSEP VDISTAMSER ALAQKRLSEN AFDLEAMSML NRAQERIDAW AQLNSIPGQF TGSTGVQVLT QEQLANTGAQ AWIKKDQFLR AAPVTGGMGA VLMRKMGWRE GEGLGKNKEG NKEPILVDFK TDRKGLVAVG ERAQKRSGNF SAAMKDLSGK HPVSALMEIC NKRRWQPPEF LLVHDSGPDH RKHFLFRVLR NGALTRPNCM FFLNRY //