ID   SON_MOUSE               Reviewed;        2444 AA.
AC   Q9QX47; E3WC91; E9PXW2; E9Q3H8; E9Q3I0; E9Q6M4; E9Q7G2; E9QAR8; E9QMT0;
AC   Q811G3; Q9CQ12; Q9CQK6; Q9QXP5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   27-MAR-2024, entry version 174.
DE   RecName: Full=Protein SON;
DE   AltName: Full=Negative regulatory element-binding protein;
DE            Short=NRE-binding protein;
GN   Name=Son; Synonyms=Nrebp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 1-2125 (ISOFORM 3), AND SUBCELLULAR LOCATION.
RC   STRAIN=129/Sv;
RX   PubMed=10950926; DOI=10.1006/geno.2000.6254;
RA   Wynn S.L., Fisher R.A., Pagel C., Price M., Liu Q.Y., Khan I.M., Zammit P.,
RA   Dadrah K., Mazrani W., Kessling A., Lee J.S., Buluwela L.;
RT   "Organization and conservation of the GART/SON/DONSON locus in mouse and
RT   human genomes.";
RL   Genomics 68:57-62(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=20876580; DOI=10.1074/jbc.m110.148973;
RA   Komori T., Doi A., Furuta H., Wakao H., Nakao N., Nakazato M., Nanjo K.,
RA   Senba E., Morikawa Y.;
RT   "Regulation of ghrelin signaling by a leptin-induced gene, negative
RT   regulatory element-binding protein, in the hypothalamic neurons.";
RL   J. Biol. Chem. 285:37884-37894(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1827 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Small intestine, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1723, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1723, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-993; SER-1723; SER-2147 AND
RP   SER-2256, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2073, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1002 AND ARG-1017, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
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).
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' (By similarity).
CC       Essential for correct RNA splicing of multiple genes critical for brain
CC       development, neuronal migration and metabolism, including TUBG1, FLNA,
CC       PNKP, WDR62, PSMD3, PCK2, PFKL, IDH2, and ACY1 (By similarity). May
CC       also regulate the ghrelin signaling in hypothalamic neuron by acting as
CC       a negative regulator of GHSR expression (PubMed:20876580).
CC       {ECO:0000250|UniProtKB:P18583, ECO:0000269|PubMed:20876580}.
CC   -!- SUBUNIT: Interacts with SRSF2. Associates with the spliceosome.
CC       Interacts with USH1G. {ECO:0000250|UniProtKB:P18583}.
CC   -!- INTERACTION:
CC       Q9QX47; Q06455: RUNX1T1; Xeno; NbExp=4; IntAct=EBI-643037, EBI-743342;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P18583}.
CC       Note=Colocalizes with the pre-mRNA splicing factor SRSF2.
CC       {ECO:0000250|UniProtKB:P18583}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9QX47-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QX47-2; Sequence=VSP_004416, VSP_004417;
CC       Name=3;
CC         IsoId=Q9QX47-3; Sequence=VSP_041557;
CC       Name=4;
CC         IsoId=Q9QX47-4; Sequence=VSP_041557, VSP_041558;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, heart,
CC       spleen, liver, skeletal muscle, kidney and testis.
CC       {ECO:0000269|PubMed:20876580}.
CC   -!- INDUCTION: By leptin. Highly expressed in hypothalamus following leptin
CC       injection. {ECO:0000269|PubMed:20876580}.
CC   -!- DOMAIN: Contains 8 types of repeats which are distributed in 3 regions.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46419.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AF193606; AAF23120.1; -; Genomic_DNA.
DR   EMBL; AF193595; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193596; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193597; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193598; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193599; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193600; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193601; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193602; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193603; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193604; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193605; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193607; AAF23121.1; -; mRNA.
DR   EMBL; AB546195; BAJ40169.1; -; mRNA.
DR   EMBL; AC131691; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046419; AAH46419.1; ALT_SEQ; mRNA.
DR   EMBL; AK019312; BAB31659.1; -; mRNA.
DR   EMBL; AK019081; BAB31536.1; -; mRNA.
DR   EMBL; AK008478; BAB25691.1; -; mRNA.
DR   EMBL; AK008256; BAB25562.1; -; mRNA.
DR   CCDS; CCDS37399.1; -. [Q9QX47-1]
DR   CCDS; CCDS37400.1; -. [Q9QX47-2]
DR   RefSeq; NP_849211.3; NM_178880.4. [Q9QX47-1]
DR   AlphaFoldDB; Q9QX47; -.
DR   BioGRID; 203390; 10.
DR   DIP; DIP-49510N; -.
DR   IntAct; Q9QX47; 6.
DR   MINT; Q9QX47; -.
DR   STRING; 10090.ENSMUSP00000109671; -.
DR   GlyGen; Q9QX47; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q9QX47; -.
DR   PhosphoSitePlus; Q9QX47; -.
DR   SwissPalm; Q9QX47; -.
DR   EPD; Q9QX47; -.
DR   jPOST; Q9QX47; -.
DR   MaxQB; Q9QX47; -.
DR   PaxDb; 10090-ENSMUSP00000109671; -.
DR   PeptideAtlas; Q9QX47; -.
DR   ProteomicsDB; 261108; -. [Q9QX47-1]
DR   ProteomicsDB; 261109; -. [Q9QX47-2]
DR   ProteomicsDB; 261110; -. [Q9QX47-3]
DR   ProteomicsDB; 261111; -. [Q9QX47-4]
DR   Pumba; Q9QX47; -.
DR   Antibodypedia; 7410; 70 antibodies from 20 providers.
DR   DNASU; 20658; -.
DR   Ensembl; ENSMUST00000114036.9; ENSMUSP00000109670.3; ENSMUSG00000022961.19. [Q9QX47-2]
DR   Ensembl; ENSMUST00000114037.9; ENSMUSP00000109671.3; ENSMUSG00000022961.19. [Q9QX47-1]
DR   GeneID; 20658; -.
DR   KEGG; mmu:20658; -.
DR   UCSC; uc007zxy.1; mouse. [Q9QX47-2]
DR   UCSC; uc007zxz.1; mouse. [Q9QX47-1]
DR   AGR; MGI:98353; -.
DR   CTD; 6651; -.
DR   MGI; MGI:98353; Son.
DR   VEuPathDB; HostDB:ENSMUSG00000022961; -.
DR   eggNOG; ENOG502QPQ7; Eukaryota.
DR   GeneTree; ENSGT00730000111141; -.
DR   HOGENOM; CLU_230016_0_0_1; -.
DR   InParanoid; Q9QX47; -.
DR   OMA; NETEQCT; -.
DR   OrthoDB; 2882949at2759; -.
DR   TreeFam; TF330344; -.
DR   BioGRID-ORCS; 20658; 9 hits in 59 CRISPR screens.
DR   ChiTaRS; Son; mouse.
DR   PRO; PR:Q9QX47; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9QX47; Protein.
DR   Bgee; ENSMUSG00000022961; Expressed in aorta tunica media and 278 other cell types or tissues.
DR   ExpressionAtlas; Q9QX47; baseline and differential.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   CDD; cd19870; DSRM_SON-like; 1.
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; Q9QX47; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; DNA-binding;
KW   Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   CHAIN           2..2444
FT                   /note="Protein SON"
FT                   /id="PRO_0000072038"
FT   REPEAT          1001..1006
FT                   /note="1-1"
FT   REPEAT          1009..1014
FT                   /note="1-2"
FT   REPEAT          1016..1021
FT                   /note="1-3"
FT   REPEAT          1025..1030
FT                   /note="1-4"
FT   REPEAT          1033..1038
FT                   /note="1-5"
FT   REPEAT          1041..1046
FT                   /note="1-6"
FT   REPEAT          1050..1055
FT                   /note="1-7"
FT   REPEAT          1058..1063
FT                   /note="1-8"
FT   REPEAT          1066..1071
FT                   /note="1-9"
FT   REPEAT          1075..1080
FT                   /note="1-10"
FT   REPEAT          1084..1089
FT                   /note="1-11"
FT   REPEAT          1095..1100
FT                   /note="1-12"
FT   REPEAT          1106..1111
FT                   /note="1-13"
FT   REPEAT          1115..1120
FT                   /note="1-14"
FT   REPEAT          1950..1956
FT                   /note="2-1"
FT   REPEAT          1959..1977
FT                   /note="3-1"
FT   REPEAT          1978..1984
FT                   /note="2-2"
FT   REPEAT          1985..1991
FT                   /note="2-3"
FT   REPEAT          1992..1998
FT                   /note="2-4"
FT   REPEAT          1999..2005
FT                   /note="2-5"
FT   REPEAT          2006..2012
FT                   /note="2-6"
FT   REPEAT          2013..2019
FT                   /note="2-7; approximate"
FT   REPEAT          2020..2030
FT                   /note="3-2; approximate"
FT   DOMAIN          2323..2369
FT                   /note="G-patch"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT   DOMAIN          2389..2444
FT                   /note="DRBM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          23..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          301..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          391..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..850
FT                   /note="13 X 10 AA tandem repeats of L-A-[ST]-[NSG]-[TS]-
FT                   MDSQM"
FT   REGION          907..983
FT                   /note="11 X 7 AA tandem repeats of [DR]-P-Y-R-
FT                   [LI][AG][QHP]"
FT   REGION          1001..1120
FT                   /note="14 X 6 AA repeats of [ED]-R-S-M-M-S"
FT   REGION          1141..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1141..1173
FT                   /note="3 X 11 AA tandem repats of P-P-L-P-P-E-E-P-P-[TME]-
FT                   [MTG]"
FT   REGION          1802..2072
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1950..2019
FT                   /note="7 X 7 AA repeats of P-S-R-R-S-R-[TS]"
FT   REGION          1959..2030
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          2031..2057
FT                   /note="3 X tandem repeats of [ST]-P-[VLI]-R-[RL]-[RK]-[RF]-
FT                   S-R"
FT   REGION          2192..2238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..52
FT                   /note="Polar 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..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        301..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..438
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..467
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1173
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1177..1213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1805..1852
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1866..1939
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1946..1970
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1983..2024
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2037..2061
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2197..2228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         16
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         150
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         152
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         158
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         284
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         395
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         945
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         954
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         993
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1002
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1017
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         1030
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1038
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1055
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1063
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1077
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1678
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1723
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         1727
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1772
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1784
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1791
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1794
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1807
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1808
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1973
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1975
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         1977
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2027
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2029
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2031
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2047
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2049
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2073
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         2147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         2181
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   MOD_RES         2256
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        64
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   CROSSLNK        2073
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   CROSSLNK        2110
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   CROSSLNK        2167
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P18583"
FT   VAR_SEQ         776..815
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10950926,
FT                   ECO:0000303|PubMed:20876580"
FT                   /id="VSP_041557"
FT   VAR_SEQ         2126
FT                   /note="K -> F (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004416"
FT   VAR_SEQ         2127..2444
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_004417"
FT   VAR_SEQ         2238..2444
FT                   /note="PVDISTAMSERALAQKRLSENAFDLEAMSMLNRAQERIDAWAQLNSIPGQFT
FT                   GSTGVQVLTQEQLANTGAQAWIKKDQFLRAAPVTGGMGAVLMRKMGWREGEGLGKNKEG
FT                   NKEPILVDFKTDRKGLVAVGERAQKRSGNFSAAMKDLSGKHPVSALMEICNKRRWQPPE
FT                   FLLVHDSGPDHRKHFLFRVLRNGSPYQPNCMFFLNRY -> GRVKRQGRVKRQMKQPAA
FT                   SHLTVTRCNSLCGTKPQSEKHRIAEKSVITSLPNIGPSMHLWEGSPRYNYLASRFASRL
FT                   YSSRFWW (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:20876580"
FT                   /id="VSP_041558"
FT   CONFLICT        857
FT                   /note="D -> E (in Ref. 1; AAF23120/AAF23121 and 2;
FT                   BAJ40169)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1333
FT                   /note="N -> D (in Ref. 1; AAF23120/AAF23121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1734
FT                   /note="P -> L (in Ref. 1; AAF23120/AAF23121)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1966
FT                   /note="R -> I (in Ref. 1; AAF23120/AAF23121)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2444 AA;  265651 MW;  E873ADCB51B7123B CRC64;
     MAADIEQVFR SFVVSKFREI QQELSSGRSE GQLNGETNPP IEGNQAGDTA ASARSLPNEE
     IVQKIEEVLS GVLDTELRYK PDLKEASRKS RCVSVQTDPT DEVPTKKSKK HKKHKNKKKK
     KKKEKEKKYK RQPEESESKL KSHHDGNLES DSFLKFDSEP SAAALEHPVR AFGLSEASET
     ALVLEPPVVS MEVQESHVLE TLKPATKAAE LSVVSTSVIS EQSEQPMPGM LEPSMTKILD
     SFTAAPVPMS TAALKSPEPV VTMSVEYQKS VLKSLETMPP ETSKTTLVEL PIAKVVEPSE
     TLTIVSETPT EVHPEPSPST MDFPESSTTD VQRLPEQPVE APSEIADSSM TRPQESLELP
     KTTAVELQES TVASALELPG PPATSILELQ GPPVTPVPEL PGPSATPVPE LSGPLSTPVP
     ELPGPPATVV PELPGPSVTP VPQLSQELPG PPAPSMGLEP PQEVPEPPVM AQELSGVPAV
     SAAIELTGQP AVTVAMELTE QPVTTTEFEQ PVAMTTVEHP GHPEVTTATG LLGQPEAAMV
     LELPGQPVAT TALELSGQPS VTGVPELSGL PSATRALELS GQSVATGALE LPGQLMATGA
     LEFSGQSGAA GALELLGQPL ATGVLELPGQ PGAPELPGQP VATVALEISV QSVVTTSELS
     TMTVSQSLEV PSTTALESYN TVAQELPTTL VGETSVTVGV DPLMAQESHM LASNTMETHM
     LASNTMDSQM LASNTMDSQM LASNTMDSQM LASSTMDSQM LASSTMDSQM LATSTMDSQM
     LATSSMDSQM LATSSMDSQM LATSSMDSQM LATSSMDSQM LATSSMDSQM LATSSMDSQM
     LATSSMDSQM LATSSMDSQM LASGAMDSQM LASGTMDAQM LASGTMDAQM LASSTQDSAM
     MGSKSPDPYR LAQDPYRLAQ DPYRLGHDPY RLGHDAYRLG QDPYRLGHDP YRLTPDPYRV
     SPRPYRIAPR SYRIAPRPYR LAPRPLMLAS RRSMMMSYAA ERSMMSSYER SMMSYERSMM
     SPMAERSMMS AYERSMMSAY ERSMMSPMAE RSMMSAYERS MMSAYERSMM SPMADRSMMS
     MGADRSMMSS YSAADRSMMS SYSAADRSMM SSYTDRSMMS MAADSYTDSY TDSYTEAYMV
     PPLPPEEPPT MPPLPPEEPP MTPPLPPEEP PEGPALSTEQ SALTADNTWS TEVTLSTGES
     LSQPEPPVSQ SEISEPMAVP ANYSMSESET SMLASEAVMT VPEPAREPES SVTSAPVESA
     VVAEHEMVPE RPMTYMVSET TMSVEPAVLT SEASVISETS ETYDSMRPSG HAISEVTMSL
     LEPAVTISQP AENSLELPSM TVPAPSTMTT TESPVVAVTE IPPVAVPEPP IMAVPELPTM
     AVVKTPAVAV PEPLVAAPEP PTMATPELCS LSVSEPPVAV SELPALADPE HAITAVSGVS
     SLEPSVPILE PAVSVLQPVM IVSEPSVPVQ EPTVAVSEPA VIVSEHTQIT SPEMAVESSP
     VIVDSSVMSS QIMKGMNLLG GDENLGPEVG MQETLLHPGE EPRDGGHLKS DLYENEYDRN
     ADLTVNSHLI VKDAEHNTVC ATTVGPVGEA SEEKILPISE TKEITELATC AAVSEADIGR
     SLSSQLALEL DTVGTSKGFE FVTASALISE SKYDVEVSVT TQDTEHDMVI STSPSGGSEA
     DIEGPLPAKD IHLDLPSTNF VCKDVEDSLP IKESAQAVAV ALSPKESSED TEVPLPNKEI
     VPESGYSASI DEINEADLVR PLLPKDMERL TSLRAGIEGP LLASEVERDK SAASPVVISI
     PERASESSSE EKDDYEIFVK VKDTHEKSKK NKNRDKGEKE KKRDSSLRSR SKRSKSSEHK
     SRKRTSESRS RARKRSSKSK SHRSQTRSRS RSRRRRRSSR SRSKSRGRRS VSKEKRKRSP
     KHRSKSRERK RKRSSSRDNR KAARARSRTP SRRSRSHTPS RRRRSRSVGR RRSFSISPSR
     RSRTPSRRSR TPSRRSRTPS RRSRTPSRRS RTPSRRRRSR SAVRRRSFSI SPVRLRRSRT
     PLRRRFSRSP IRRKRSRSSE RGRSPKRLTD LDKAQLLEIA KANAAAMCAK AGVPLPPNLK
     PAPPPTIEEK VAKKSGGATI EELTEKCKQI AQSKEDDDVI VNKPHVSDEE EEEPPFYHHP
     FKLSEPKPIF FNLNIAAAKP TPPKSQVTLT KEFPVSSGSQ HRKKEADSVY GEWVPVEKNG
     EESKDDDNVF SSSLPSEPVD ISTAMSERAL AQKRLSENAF DLEAMSMLNR AQERIDAWAQ
     LNSIPGQFTG STGVQVLTQE QLANTGAQAW IKKDQFLRAA PVTGGMGAVL MRKMGWREGE
     GLGKNKEGNK EPILVDFKTD RKGLVAVGER AQKRSGNFSA AMKDLSGKHP VSALMEICNK
     RRWQPPEFLL VHDSGPDHRK HFLFRVLRNG SPYQPNCMFF LNRY
//