SON_HUMAN
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 03-AUG-2022, entry version 214.
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 -!- INTERACTION:
CC P18583; Q93009: USP7; NbExp=2; IntAct=EBI-1053513, EBI-302474;
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};
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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 AlphaFoldDB; P18583; -.
DR BioGRID; 112534; 151.
DR DIP; DIP-42289N; -.
DR IntAct; P18583; 49.
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-Linked glycan (2 sites). [P18583-1]
DR GlyGen; P18583; 10 sites, 2 O-linked glycans (10 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; P18583; -.
DR PeptideAtlas; P18583; -.
DR PRIDE; 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 Antibodypedia; 7410; 61 antibodies from 20 providers.
DR DNASU; 6651; -.
DR Ensembl; ENST00000300278.8; ENSP00000300278.2; ENSG00000159140.21. [P18583-3]
DR Ensembl; ENST00000356577.10; ENSP00000348984.4; ENSG00000159140.21. [P18583-1]
DR Ensembl; ENST00000381679.8; ENSP00000371095.4; ENSG00000159140.21. [P18583-6]
DR Ensembl; ENST00000455528.5; ENSP00000399783.1; ENSG00000159140.21. [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 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; ETEQCTV; -.
DR OrthoDB; 30934at2759; -.
DR PhylomeDB; P18583; -.
DR TreeFam; TF330344; -.
DR PathwayCommons; P18583; -.
DR SignaLink; P18583; -.
DR SIGNOR; P18583; -.
DR BioGRID-ORCS; 6651; 681 hits in 1091 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 209 other tissues.
DR ExpressionAtlas; P18583; baseline and differential.
DR Genevisible; P18583; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
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 InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR032922; SON.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR46528; PTHR46528; 1.
DR Pfam; PF01585; G-patch; 1.
DR SMART; SM00443; G_patch; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50137; DS_RBD; 1.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Disease variant;
KW DNA-binding; Intellectual disability; Isopeptide bond; Methylation;
KW 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; unknown pathological significance;
FT de novo 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; unknown pathological significance;
FT de novo 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
