NCOR2_MOUSE
ID NCOR2_MOUSE Reviewed; 2472 AA.
AC Q9WU42; E9Q9V0; Q9WU43; Q9WUC1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Nuclear receptor corepressor 2;
DE Short=N-CoR2;
DE AltName: Full=Silencing mediator of retinoic acid and thyroid hormone receptor;
DE Short=SMRT;
DE Short=SMRTe;
DE AltName: Full=T3 receptor-associating factor;
DE Short=TRAC;
DE AltName: Full=Thyroid-, retinoic-acid-receptor-associated corepressor;
GN Name=Ncor2; Synonyms=Smrt;
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 [MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Brain, and Spleen;
RX PubMed=10077563; DOI=10.1073/pnas.96.6.2639;
RA Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M.;
RT "Unique forms of human and mouse nuclear receptor corepressor SMRT.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Embryo;
RX PubMed=10097068; DOI=10.1073/pnas.96.7.3519;
RA Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D.;
RT "SMRTe, a silencing mediator for retinoid and thyroid hormone receptors-
RT extended isoform that is more related to the nuclear receptor
RT corepressor.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999).
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 INTERACTION WITH C1D.
RX PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G., Lazar M.A.;
RT "Cloning and characterization of a corepressor and potential component of
RT the nuclear hormone receptor repression complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
RN [5]
RP INTERACTION WITH HDAC7.
RX PubMed=10640276;
RA Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT "Isolation of a novel histone deacetylase reveals that class I and class II
RT deacetylases promote SMRT-mediated repression.";
RL Genes Dev. 14:55-66(2000).
RN [6]
RP INTERACTION WITH CBFA2T3.
RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001;
RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA Downing J.R., Meyers S., Hiebert S.W.;
RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with
RT multiple histone deacetylases and binds mSin3A through its oligomerization
RT domain.";
RL Mol. Cell. Biol. 21:6470-6483(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550 AND SER-2215, AND
RP IDENTIFICATION BY 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 [8]
RP FUNCTION, AND INTERACTION WITH NR4A2.
RX PubMed=19144721; DOI=10.1242/dev.029769;
RA Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P.,
RA Smidt M.P.;
RT "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
RT through release of SMRT-mediated repression.";
RL Development 136:531-540(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2181, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; THR-549;
RP SER-550; SER-747; SER-750; THR-1350; SER-1565; SER-1749; SER-2004;
RP SER-2012; SER-2015; SER-2016; SER-2018; THR-2020; SER-2181 AND SER-2215,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1983, 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 [12]
RP INTERACTION WITH MECP2.
RX PubMed=23770565; DOI=10.1038/nn.3434;
RA Lyst M.J., Ekiert R., Ebert D.H., Merusi C., Nowak J., Selfridge J.,
RA Guy J., Kastan N.R., Robinson N.D., de Lima Alves F., Rappsilber J.,
RA Greenberg M.E., Bird A.;
RT "Rett syndrome mutations abolish the interaction of MeCP2 with the
RT NCoR/SMRT co-repressor.";
RL Nat. Neurosci. 16:898-902(2013).
RN [13]
RP DNA-BINDING, AND INTERACTION WITH BCL6.
RX PubMed=23455674; DOI=10.1038/ni.2543;
RA Huang C., Hatzi K., Melnick A.;
RT "Lineage-specific functions of Bcl-6 in immunity and inflammation are
RT mediated by distinct biochemical mechanisms.";
RL Nat. Immunol. 14:380-388(2013).
RN [14]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-18 AND ARG-1854, 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).
RN [15]
RP INTERACTION WITH SANBR.
RX PubMed=33831416; DOI=10.1016/j.jbc.2021.100625;
RA Zheng S., Matthews A.J., Rahman N., Herrick-Reynolds K., Sible E.,
RA Choi J.E., Wishnie A., Ng Y.K., Rhodes D., Elledge S.J., Vuong B.Q.;
RT "The uncharacterized SANT and BTB domain-containing protein SANBR inhibits
RT class switch recombination.";
RL J. Biol. Chem. 296:100625-100625(2021).
CC -!- FUNCTION: Transcriptional corepressor. Mediates the transcriptional
CC repression activity of some nuclear receptors by promoting chromatin
CC condensation, thus preventing access of the basal transcription.
CC Isoform 1 and isoform 5 have different affinities for different nuclear
CC receptors. Involved in the regulation BCL6-dependent of the germinal
CC center (GC) reactions, mainly through the control of the GC B-cells
CC proliferation and survival. Recruited by ZBTB7A to the androgen
CC response elements/ARE on target genes, negatively regulates androgen
CC receptor signaling and androgen-induced cell proliferation.
CC {ECO:0000250|UniProtKB:Q9Y618, ECO:0000269|PubMed:19144721}.
CC -!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B and
CC histone deacetylases HDAC1 and HDAC2. This complex associates with the
CC thyroid (TR) and the retinoid acid receptors (RAR) in the absence of
CC ligand, and may stabilize their interaction with TFIIB. Interacts
CC directly with RARA in the absence of ligand; the interaction represses
CC RARA activity. Interacts (isoform SMRT) with HDAC10. Interacts with
CC MINT. Component of the N-Cor repressor complex, at least composed of
CC NCOR1, NCOR2, HDAC3, TBL1X, TBL1R, CORO2A and GPS2. Interacts with
CC CBFA2T3 and ATXN1L. Interacts with RARB; the interaction is weak and
CC does not repress RARB transactivational activity. Interacts with HDAC7
CC and C1D. Interacts with NR4A2; this interaction increases in the
CC absence of PITX3. Interacts with BCL6 (via the BTB domain), required
CC for BCL6 transcriptional repressor activity on a subset of target
CC genes. Forms ternary complexes with BCOR and BCL6 on target gene
CC promoters but, on enhancer elements, interacts with BCL6 and HDAC3 to
CC repress proximal gene expression. May interact with DEAF1. Interacts
CC with RXRA. Interacts with MECP2. Interacts with ZBTB7A (By similarity).
CC Interacts with AR (By similarity). Interacts with TBL1Y (By
CC similarity). Interacts with SANBR (via the BTB domain)
CC (PubMed:33831416). {ECO:0000250|UniProtKB:Q9Y618,
CC ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11533236,
CC ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:23455674,
CC ECO:0000269|PubMed:23770565, ECO:0000269|PubMed:33831416,
CC ECO:0000269|PubMed:9405624}.
CC -!- INTERACTION:
CC Q9WU42; P51608: MECP2; Xeno; NbExp=4; IntAct=EBI-6673326, EBI-1189067;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9WU42-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9WU42-2; Sequence=VSP_003414;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Also widely expressed in early embryos.
CC -!- DOMAIN: The N-terminal region contains repression functions that are
CC divided into three independent repression domains (RD1, RD2 and RD3).
CC The C-terminal region contains the nuclear receptor-interacting domains
CC that are divided in two separate interaction domains (ID1 and ID2).
CC -!- DOMAIN: The two interaction domains (ID) contain a conserved sequence
CC referred to as the CORNR box. This motif is required and sufficient to
CC permit binding to unligated TR and RARS. Sequences flanking the CORNR
CC box determine nuclear hormone receptor specificity.
CC -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF113001; AAD20944.1; -; mRNA.
DR EMBL; AF113002; AAD20945.1; -; mRNA.
DR EMBL; AF125671; AAD22972.1; -; mRNA.
DR EMBL; AC132118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS57382.1; -. [Q9WU42-2]
DR RefSeq; NP_001240833.1; NM_001253904.1.
DR RefSeq; NP_001240834.1; NM_001253905.1. [Q9WU42-2]
DR RefSeq; XP_011239133.1; XM_011240831.2. [Q9WU42-1]
DR AlphaFoldDB; Q9WU42; -.
DR BMRB; Q9WU42; -.
DR SMR; Q9WU42; -.
DR BioGRID; 203350; 24.
DR CORUM; Q9WU42; -.
DR DIP; DIP-42595N; -.
DR IntAct; Q9WU42; 7.
DR MINT; Q9WU42; -.
DR STRING; 10090.ENSMUSP00000107033; -.
DR iPTMnet; Q9WU42; -.
DR PhosphoSitePlus; Q9WU42; -.
DR EPD; Q9WU42; -.
DR jPOST; Q9WU42; -.
DR MaxQB; Q9WU42; -.
DR PaxDb; Q9WU42; -.
DR PeptideAtlas; Q9WU42; -.
DR PRIDE; Q9WU42; -.
DR ProteomicsDB; 252659; -. [Q9WU42-1]
DR ProteomicsDB; 252660; -. [Q9WU42-2]
DR Antibodypedia; 1103; 279 antibodies from 36 providers.
DR DNASU; 20602; -.
DR Ensembl; ENSMUST00000111394; ENSMUSP00000107025; ENSMUSG00000029478. [Q9WU42-2]
DR Ensembl; ENSMUST00000111398; ENSMUSP00000107029; ENSMUSG00000029478. [Q9WU42-1]
DR GeneID; 20602; -.
DR KEGG; mmu:20602; -.
DR UCSC; uc008zra.2; mouse. [Q9WU42-2]
DR CTD; 9612; -.
DR MGI; MGI:1337080; Ncor2.
DR VEuPathDB; HostDB:ENSMUSG00000029478; -.
DR eggNOG; KOG1878; Eukaryota.
DR GeneTree; ENSGT00940000159022; -.
DR InParanoid; Q9WU42; -.
DR OrthoDB; 12227at2759; -.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-MMU-3214815; HDACs deacetylate histones.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR Reactome; R-MMU-9623433; NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 20602; 9 hits in 78 CRISPR screens.
DR ChiTaRS; Ncor2; mouse.
DR PRO; PR:Q9WU42; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9WU42; protein.
DR Bgee; ENSMUSG00000029478; Expressed in superior frontal gyrus and 267 other tissues.
DR ExpressionAtlas; Q9WU42; baseline and differential.
DR Genevisible; Q9WU42; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; IDA:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0005112; F:Notch binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IGI:MGI.
DR GO; GO:0061436; P:establishment of skin barrier; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IGI:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:1903799; P:negative regulation of miRNA maturation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; IDA:MGI.
DR GO; GO:0006476; P:protein deacetylation; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IGI:MGI.
DR GO; GO:0010565; P:regulation of cellular ketone metabolic process; ISO:MGI.
DR GO; GO:1901725; P:regulation of histone deacetylase activity; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IMP:MGI.
DR GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR031557; N-CoR_GPS2_interact.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF15784; GPS2_interact; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..2472
FT /note="Nuclear receptor corepressor 2"
FT /id="PRO_0000055623"
FT DOMAIN 427..478
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 606..657
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..312
FT /note="Interaction with SIN3A/B"
FT /evidence="ECO:0000250"
FT REGION 487..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1254..1277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1479..1578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1857..1878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2001..2078
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2086..2090
FT /note="Required for interaction with RARA in the absence of
FT its ligand"
FT /evidence="ECO:0000250"
FT REGION 2132..2226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2343..2459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 165..207
FT /evidence="ECO:0000255"
FT COILED 492..560
FT /evidence="ECO:0000255"
FT COILED 658..682
FT /evidence="ECO:0000255"
FT MOTIF 2094..2098
FT /note="CORNR box of ID1"
FT MOTIF 2296..2300
FT /note="CORNR box of ID2"
FT COMPBIAS 53..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..563
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..717
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..811
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1002
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1060
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1362
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1554..1578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1738..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1762..1781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1926..1951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2024..2047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2212..2226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2383..2397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 549
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 878
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 938
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 945
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 958
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1181
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1350
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1624
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1819
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1854
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1920
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1963
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 1983
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2012
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2020
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2035
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 2161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT MOD_RES 2181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y618"
FT VAR_SEQ 36..254
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10077563"
FT /id="VSP_003414"
FT CONFLICT 176
FT /note="M -> RL (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..402
FT /note="PPMLYDA -> RHVVRR (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="D -> H (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
FT CONFLICT 756
FT /note="T -> M (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="V -> A (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 806..846
FT /note="PSPAAPPATVDKDEQEAPAAPAPQTEDAKEQKSEAEEIDVG -> HHLPHPR
FT LLWTRMNKKPRLLQLPRQRMPRSRSLRPRRSMWE (in Ref. 1; AAD20944/
FT AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 856
FT /note="E -> K (in Ref. 1; AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="E -> K (in Ref. 1; AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 867
FT /note="E -> K (in Ref. 1; AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 895
FT /note="E -> K (in Ref. 1; AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="S -> F (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
FT CONFLICT 975
FT /note="I -> IQ (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046..1063
FT /note="PKLPTEPPRWSSGLPFPI -> QSYRLSPHAGHRLPSH (in Ref. 2;
FT AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073..1080
FT /note="PHAADPSA -> TRADPL (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1133
FT /note="Missing (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="Missing (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1157
FT /note="G -> E (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1172..1201
FT /note="GSATSGSITKGLPSTRAADGPSYRGSITHG -> APPPVEASPRASQYPGCR
FT RPQLQRLYHPR (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="A -> S (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1855..1857
FT /note="Missing (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1909
FT /note="P -> A (in Ref. 1; AAD20944/AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 1913
FT /note="A -> G (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1923
FT /note="A -> G (in Ref. 1; AAD20944/AAD20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 1956
FT /note="N -> S (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 1968
FT /note="A -> G (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 2195..2196
FT /note="TA -> AV (in Ref. 2; AAD22972)"
FT /evidence="ECO:0000305"
FT CONFLICT 2213..2214
FT /note="SK -> LE (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
FT CONFLICT 2224
FT /note="A -> T (in Ref. 1; AAD20944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2472 AA; 269807 MW; 8068020DF0AAB9B7 CRC64;
MSGSTQPVAQ TWRAAEPRYP PHGISYPVQI ARSHTDVGLL EYQHHPRDYT SHLSPGSIIQ
PQRRRPSLLS EFQPGSERSQ ELHLRPESRT FLPELGKPDI EFTESKRPRL ELLPDTLLRP
SPLLATGQPS GSEDLTKDRS LAGKLEPVSP PSPPHADPEL ELAPSRLSKE ELIQNMDRVD
REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA
AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQRFCQ
RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG
LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMDDPM
KVYKDRQVTN MWSEQERDTF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK
SLVRRSYRRR GKSQQQQQQQ QQQQQQQMAR SSQEEKEEKE KEKEADKEEE KQDAENEKEE
LSKEKTDDTS GEDNDEKEAV ASKGRKTANS QGRRKGRITR SMANEANHEE TATPQQSSEL
ASMEMNESSR WTEEEMETAK KGLLEHGRNW SAIARMVGSK TVSQCKNFYF NYKKRQNLDE
ILQQHKLKME KERNARRKKK KTPAAASEET AFPPAAEDEE MEASGASANE EELAEEAEAS
QASGNEVPRV GECSGPAAVN NSSDTESVPS PRSEATKDTG PKPTGTEALP AATQPPVPPP
EEPAVAPAEP SPVPDASGPP SPEPSPSPAA PPATVDKDEQ EAPAAPAPQT EDAKEQKSEA
EEIDVGKPEE PEASEEPPES VKSDHKEETE EEPEDKAKGT EAIETVSEAP LKVEEAGSKA
AVTKGSSSGA TQDSDSSATC SADEVDEPEG GDKGRLLSPR PSLLTPAGDP RASTSPQKPL
DLKQLKQRAA AIPPIVTKVH EPPREDTVPP KPVPPVPPPT QHLQPEGDVS QQSGGSPRGK
SRSPVPPAEK EAEKPAFFPA FPTEGPKLPT EPPRWSSGLP FPIPPREVIK TSPHAADPSA
FSYTPPGHPL PLGLHDSARP VLPRPPISNP PPLISSAKHP GVLERQLGAI SQQGMSVQLR
VPHSEHAKAP MGPLTMGLPL AVDPKKLGTA LGSATSGSIT KGLPSTRAAD GPSYRGSITH
GTPADVLYKG TISRIVGEDS PSRLDRARED TLPKGHVIYE GKKGHVLSYE GGMSVSQCSK
EDGRSSSGPP HETAAPKRTY DMMEGRVGRT VTSASIEGLM GRAIPEQHSP HLKEQHHIRG
SITQGIPRSY VEAQEDYLRR EAKLLKREGT PPPPPPPRDL TETYKPRPLD PLGPLKLKPT
HEGVVATVKE AGRSIHEIPR EELRRTPELP LAPRPLKEGS ITQGTPLKYD SGAPSTGTKK
HDVRSIIGSP GRPFPALHPL DIMADARALE RACYEESLKS RSGTSSGAGG SITRGAPVVV
PELGKPRQSP LTYEDHGAPF TSHLPRGSPV TTREPTPRLQ EGSLLSSKAS QDRKLTSTPR
EIAKSPHSTV PEHHPHPISP YEHLLRGVTG VDLYRGHIPL AFDPTSIPRG IPLEAAAAAY
YLPRHLAPSP TYPHLYPPYL IRGYPDTAAL ENRQTIINDY ITSQQMHHNA ASAMAQRADM
LRGLSPRESS LALNYAAGPR GIIDLSQVPH LPVLVPPTPG TPATAIDRLA YLPTAPPPFS
SRHSSSPLSP GGPTHLAKPT ATSSSERERE RERERDKSIL TSTTTVEHAP IWRPGTEQSS
GAGGSSRPAS HTHQHSPISP RTQDALQQRP SVLHNTSMKG VVTSVEPGTP TVLRWARSTS
TSSPVRPAAT FPPATHCPLG GTLEGVYPTL MEPVLLPKET SRVARPERPR VDAGHAFLTK
PPAREPASSP SKSSEPRSLA PPSSSHTAIA RTPAKNLAPH HASPDPPAPT SASDLHREKT
QSKPFSIQEL ELRSLGYHSG AGYSPDGVEP ISPVSSPSLT HDKGLSKPLE ELEKSHLEGE
LRHKQPGPMK LSAEAAHLPH LRPLPESQPS SSPLLQTAPG IKGHQRVVTL AQHISEVITQ
DYTRHHPQQL SGPLPAPLYS FPGASCPVLD LRRPPSDLYL PPPDHGTPAR GSPHSEGGKR
SPEPSKTSVL GSSEDAIEPV SPPEGMTEPG HARSTAYPLL YRDGEQGEPR MGSKSPGNTS
QPPAFFSKLT ESNSAMVKSK KQEINKKLNT HNRNEPEYNI GQPGTEIFNM PAITGAGLMT
CRSQAVQEHA STNMGLEAII RKALMGKYDQ WEEPPPLGAN AFNPLNASAS LPAAAMPITT
ADGRSDHALT SPGGGGKAKV SGRPSSRKAK SPAPGLASGD RPPSVSSVHS EGDCNRRTPL
TNRVWEDRPS SAGSTPFPYN PLIMRLQAGV MASPPPPGLA AGSGPLAGPH HAWDEEPKPL
LCSQYETLSD SE
