SON_MOUSE
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 03-AUG-2022, entry version 165.
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 iPTMnet; Q9QX47; -.
DR PhosphoSitePlus; Q9QX47; -.
DR SwissPalm; Q9QX47; -.
DR EPD; Q9QX47; -.
DR jPOST; Q9QX47; -.
DR MaxQB; Q9QX47; -.
DR PaxDb; Q9QX47; -.
DR PeptideAtlas; Q9QX47; -.
DR PRIDE; Q9QX47; -.
DR ProteomicsDB; 261108; -. [Q9QX47-1]
DR ProteomicsDB; 261109; -. [Q9QX47-2]
DR ProteomicsDB; 261110; -. [Q9QX47-3]
DR ProteomicsDB; 261111; -. [Q9QX47-4]
DR Antibodypedia; 7410; 61 antibodies from 20 providers.
DR DNASU; 20658; -.
DR Ensembl; ENSMUST00000114036; ENSMUSP00000109670; ENSMUSG00000022961. [Q9QX47-2]
DR Ensembl; ENSMUST00000114037; ENSMUSP00000109671; ENSMUSG00000022961. [Q9QX47-1]
DR GeneID; 20658; -.
DR KEGG; mmu:20658; -.
DR UCSC; uc007zxy.1; mouse. [Q9QX47-2]
DR UCSC; uc007zxz.1; mouse. [Q9QX47-1]
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; ETEQCTV; -.
DR TreeFam; TF330344; -.
DR BioGRID-ORCS; 20658; 8 hits in 56 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 274 other tissues.
DR ExpressionAtlas; Q9QX47; baseline and differential.
DR Genevisible; Q9QX47; MM.
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 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; 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
