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 24-JAN-2024, entry version 201. 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, RC Pancreas, 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; 25. DR CORUM; Q9WU42; -. DR DIP; DIP-42595N; -. DR IntAct; Q9WU42; 8. DR MINT; Q9WU42; -. DR STRING; 10090.ENSMUSP00000083250; -. DR GlyGen; Q9WU42; 14 sites, 1 O-linked glycan (14 sites). DR iPTMnet; Q9WU42; -. DR PhosphoSitePlus; Q9WU42; -. DR EPD; Q9WU42; -. DR jPOST; Q9WU42; -. DR MaxQB; Q9WU42; -. DR PaxDb; 10090-ENSMUSP00000107033; -. DR PeptideAtlas; Q9WU42; -. DR ProteomicsDB; 252659; -. [Q9WU42-1] DR ProteomicsDB; 252660; -. [Q9WU42-2] DR Pumba; Q9WU42; -. DR Antibodypedia; 1103; 315 antibodies from 36 providers. DR DNASU; 20602; -. DR Ensembl; ENSMUST00000111394.8; ENSMUSP00000107025.2; ENSMUSG00000029478.17. [Q9WU42-2] DR Ensembl; ENSMUST00000111398.8; ENSMUSP00000107029.2; ENSMUSG00000029478.17. [Q9WU42-1] DR GeneID; 20602; -. DR KEGG; mmu:20602; -. DR UCSC; uc008zra.2; mouse. [Q9WU42-2] DR AGR; MGI:1337080; -. DR CTD; 9612; -. DR MGI; MGI:1337080; Ncor2. DR VEuPathDB; HostDB:ENSMUSG00000029478; -. DR eggNOG; KOG1878; Eukaryota. DR GeneTree; ENSGT00940000159022; -. DR InParanoid; Q9WU42; -. DR OrthoDB; 5482374at2759; -. DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-MMU-350054; Notch-HLH transcription pathway. DR Reactome; R-MMU-381340; Transcriptional regulation of white adipocyte differentiation. 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 84 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 270 other cell types or tissues. DR ExpressionAtlas; Q9WU42; baseline and differential. 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:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded 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:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI. DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0090312; P:positive regulation of 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: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 Gene3D; 1.20.5.430; -; 1. DR Gene3D; 1.20.58.1880; -; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 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 PANTHER; PTHR13992; NUCLEAR RECEPTOR CO-REPRESSOR RELATED NCOR; 1. DR PANTHER; PTHR13992:SF21; NUCLEAR RECEPTOR COREPRESSOR 2; 1. DR Pfam; PF15784; GPS2_interact; 1. DR Pfam; PF00249; Myb_DNA-binding; 2. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS51293; SANT; 2. DR Genevisible; Q9WU42; MM. 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; FT AAD20944/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 //