ID SUH_DROME Reviewed; 594 AA. AC P28159; Q3S1M8; Q9TVK8; Q9TVY7; Q9TW34; Q9U8F9; Q9V446; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 24-JAN-2024, entry version 210. DE RecName: Full=Suppressor of hairless protein; DE AltName: Full=J kappa-recombination signal-binding protein; DE AltName: Full=RBP-J kappa; GN Name=Su(H); Synonyms=dRBP-JK; ORFNames=CG3497; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION. RC TISSUE=Embryo; RX PubMed=1744127; DOI=10.1016/s0021-9258(18)54501-4; RA Furukawa T., Kawaichi M., Matsunami N., Ryo H., Nishida Y., Honjo T.; RT "The Drosophila RBP-J kappa gene encodes the binding protein for the RT immunoglobulin J kappa recombination signal sequence."; RL J. Biol. Chem. 266:23334-23340(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION RP PHENOTYPE. RC TISSUE=Imaginal disk; RX PubMed=1617730; DOI=10.1016/0092-8674(92)90641-o; RA Schweisguth F., Posakony J.W.; RT "Suppressor of Hairless, the Drosophila homolog of the mouse recombination RT signal-binding protein gene, controls sensory organ cell fates."; RL Cell 69:1199-1212(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10471707; DOI=10.1093/genetics/153.1.179; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R., RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., RA Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [5] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-128. RC STRAIN=LAMTO 101, LAMTO 106, LAMTO 111, LAMTO 12, LAMTO 120, LAMTO RC 124, LAMTO 13, LAMTO 134, LAMTO 19, LAMTO 21, LAMTO 27, LAMTO 28, RC LAMTO 3, LAMTO 31, LAMTO 33, LAMTO 35, LAMTO 37, LAMTO 4, LAMTO 5, and RC LAMTP 18; RX PubMed=10388820; DOI=10.1093/genetics/152.3.1017; RA Depaulis F., Brazier L., Veuille M.; RT "Selective sweep at the Drosophila melanogaster Suppressor of Hairless RT locus and its association with the In(2L)t inversion polymorphism."; RL Genetics 152:1017-1024(1999). RN [8] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=1617729; DOI=10.1016/0092-8674(92)90640-x; RA Furukawa T., Maruyama S., Kawaichi M., Honjo T.; RT "The Drosophila homolog of the immunoglobulin recombination signal-binding RT protein regulates peripheral nervous system development."; RL Cell 69:1191-1197(1992). RN [9] RP FUNCTION, AND MUTAGENESIS OF TYR-315. RX PubMed=7813798; DOI=10.1006/dbio.1994.1359; RA Schweisguth F., Nero P., Posakony J.W.; RT "The sequence similarity of the Drosophila suppressor of hairless protein RT to the integrase domain has no functional significance in vivo."; RL Dev. Biol. 166:812-814(1994). RN [10] RP INTERACTION WITH HAIRLESS. RX PubMed=7958912; DOI=10.1101/gad.8.20.2491; RA Brou C., Logeat F., Lecourtois M., Vandekerckhove J., Kourilsky P., RA Schweisguth F., Israel A.; RT "Inhibition of the DNA-binding activity of Drosophila suppressor of RT hairless and of its human homolog, KBF2/RBP-J kappa, by direct protein- RT protein interaction with Drosophila hairless."; RL Genes Dev. 8:2491-2503(1994). RN [11] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8674407; DOI=10.1242/dev.122.6.1673; RA Gho M., Lecourtois M., Geraud G., Posakony J.W., Schweisguth F.; RT "Subcellular localization of Suppressor of Hairless in Drosophila sense RT organ cells during Notch signalling."; RL Development 122:1673-1682(1996). RN [12] RP FUNCTION, AND DNA-BINDING. RX PubMed=10673509; RA Morel V., Schweisguth F.; RT "Repression by suppressor of hairless and activation by Notch are required RT to define a single row of single-minded expressing cells in the Drosophila RT embryo."; RL Genes Dev. 14:377-388(2000). RN [13] RP FUNCTION. RX PubMed=12642500; DOI=10.1242/dev.00426; RA Koelzer S., Klein T.; RT "A Notch-independent function of Suppressor of Hairless during the RT development of the bristle sensory organ precursor cell of Drosophila."; RL Development 130:1973-1988(2003). RN [14] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=21262215; DOI=10.1016/j.ydbio.2011.01.019; RA San-Juan B.P., Baonza A.; RT "The bHLH factor deadpan is a direct target of Notch signaling and RT regulates neuroblast self-renewal in Drosophila."; RL Dev. Biol. 352:70-82(2011). RN [15] RP INTERACTION WITH INSV. RX PubMed=21765394; DOI=10.1038/emboj.2011.218; RA Duan H., Dai Q., Kavaler J., Bejarano F., Medranda G., Negre N., Lai E.C.; RT "Insensitive is a corepressor for Suppressor of Hairless and regulates RT Notch signalling during neural development."; RL EMBO J. 30:3120-3133(2011). CC -!- FUNCTION: Transcriptional regulator that plays a central role in Notch CC signaling, a signaling pathway involved in cell-cell communication that CC regulates a broad spectrum of cell-fate determinations CC (PubMed:21262215, PubMed:1617729, PubMed:8674407, PubMed:10673509). CC Binds directly the 5'-GTGRGAR-3' DNA consensus sequence, which is CC present in the regulatory region of several genes (PubMed:10673509). CC Acts as a transcriptional repressor when it is not associated with CC Notch proteins (PubMed:10673509). When associated with some Notch CC protein, it acts as a transcriptional activator that activates CC transcription of Notch target genes (PubMed:10673509). Required for CC transcription of Sim (PubMed:10673509). Specifically binds to the CC immunoglobulin kappa-type J segment recombination signal sequence CC (PubMed:1744127, PubMed:1617730, PubMed:1617729). Required for CC neurogenesis in imaginal disks (PubMed:1617730, PubMed:7813798). In the CC larval brain, might play a role as a transducer of Notch signaling CC during type II neuroblast development (PubMed:21262215). Also functions CC independently of the Notch pathway, in the development of the bristle CC sensory organ precursor cell (PubMed:12642500). CC {ECO:0000269|PubMed:10673509, ECO:0000269|PubMed:12642500, CC ECO:0000269|PubMed:1617729, ECO:0000269|PubMed:1617730, CC ECO:0000269|PubMed:1744127, ECO:0000269|PubMed:21262215, CC ECO:0000269|PubMed:7813798, ECO:0000269|PubMed:8674407}. CC -!- SUBUNIT: Interacts with activated cleaved Notch. Interacts with CC Hairless, this interaction preventing its DNA-binding activity. CC Interacts with insv (via BEN domain). {ECO:0000269|PubMed:21765394, CC ECO:0000269|PubMed:7958912}. CC -!- INTERACTION: CC P28159; Q8SYK5: insv; NbExp=4; IntAct=EBI-92180, EBI-192407; CC P28159; P07207: N; NbExp=7; IntAct=EBI-92180, EBI-103438; CC P28159; Q01705: Notch1; Xeno; NbExp=3; IntAct=EBI-92180, EBI-1392707; CC P28159; P20226: TBP; Xeno; NbExp=2; IntAct=EBI-92180, EBI-355371; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8674407}. Cytoplasm CC {ECO:0000269|PubMed:8674407}. Note=In imaginal disk, at the onset of CC differentiation of socket cell, it is also present in the cytoplasm. CC {ECO:0000269|PubMed:8674407}. CC -!- DEVELOPMENTAL STAGE: Expressed in early syncytial embryo CC (PubMed:1617730, PubMed:1617729). During cellularization, transient CC accumulation in a striped pattern (PubMed:1617730, PubMed:1617729). CC From late stage 11 onward, expressed gradually in a small number of CC segmentally reiterated cells of the peripheral nervous system (PNS) CC (PubMed:1617730, PubMed:1617729). This expression is specific to the CC external sensory organs (PubMed:1617730). In the thoracic and abdominal CC segments, expressed in the trichogen and tormogen cells, two outer CC accessory cells present in all larval external sensory organs CC (PubMed:1617730). During the late third larval instar, expressed in CC many larval and imaginal tissues (PubMed:1617730). Broadly distributed CC in the disks, but most abundant in the posterior region of the wing CC pouch (PubMed:1617730). In the leg disk, predominant in a zone largely CC overlapping the posterior region (PubMed:1617730). In the eye-antenna CC disk, low level in both the retinal field posterior to the CC morphogenetic furrow and the central antenna region, while higher CC levels appears on the margins of the disk and in the vicinity of the CC morphogenetic furrow (PubMed:1617730). In pupae, expressed in many CC tissues at this stage, including developing muscle and epidermis CC (PubMed:1617730). In both microchaetes and macrochaetes of 24 hr pupae, CC expressed on the notum and the head (PubMed:1617730). Expressed in the CC tormogen cell and in specific bristle cells (PubMed:1617730). CC {ECO:0000269|PubMed:1617729, ECO:0000269|PubMed:1617730}. CC -!- DISRUPTION PHENOTYPE: Lethal during the first day of pupal development CC (PubMed:1617730). At the larval stage, results in a 'neurogenic' CC phenotype in imaginal disks, in which too many cells adopt the sensory CC organ precursor cell fate (PubMed:1617730). RNAi-mediated knockdown in CC type II neuroblasts, results in smaller cells (PubMed:1617730). CC {ECO:0000269|PubMed:1617730, ECO:0000269|PubMed:21262215}. CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}. CC -!- CAUTION: Despite some similarity with the 'phage' integrase family, CC PubMed:7958912 showed that it has no recombinase activity. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA06211.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA41282.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; S69213; AAA06211.1; ALT_FRAME; Genomic_DNA. DR EMBL; X58393; CAA41282.1; ALT_INIT; mRNA. DR EMBL; M94383; AAA28919.1; -; mRNA. DR EMBL; AE014134; AAF53434.1; -; Genomic_DNA. DR EMBL; AY069091; AAL39236.1; -; mRNA. DR EMBL; AF088255; AAD39698.1; -; Genomic_DNA. DR EMBL; AF088256; AAD39699.1; -; Genomic_DNA. DR EMBL; AF088257; AAD39700.1; -; Genomic_DNA. DR EMBL; AF088258; AAD39701.1; -; Genomic_DNA. DR EMBL; AF088259; AAD39702.1; -; Genomic_DNA. DR EMBL; AF088260; AAD39703.1; -; Genomic_DNA. DR EMBL; AF088261; AAD39704.1; -; Genomic_DNA. DR EMBL; AF088262; AAD39705.1; -; Genomic_DNA. DR EMBL; AF088263; AAD39706.1; -; Genomic_DNA. DR EMBL; AF088264; AAD39707.1; -; Genomic_DNA. DR EMBL; AF088265; AAD39708.1; -; Genomic_DNA. DR EMBL; AF088266; AAD39709.1; -; Genomic_DNA. DR EMBL; AF088267; AAD39710.1; -; Genomic_DNA. DR EMBL; AF088268; AAD39711.1; -; Genomic_DNA. DR EMBL; AF088269; AAD39712.1; -; Genomic_DNA. DR EMBL; AF088270; AAD39713.1; -; Genomic_DNA. DR EMBL; AF088271; AAD39714.1; -; Genomic_DNA. DR EMBL; AF088272; AAD39715.1; -; Genomic_DNA. DR EMBL; AF088273; AAD39716.1; -; Genomic_DNA. DR EMBL; AF088274; AAD39717.1; -; Genomic_DNA. DR PIR; A41585; A41585. DR PIR; A42770; A42770. DR RefSeq; NP_001285948.1; NM_001299019.1. DR RefSeq; NP_476868.1; NM_057520.4. DR PDB; 5E24; X-ray; 2.14 A; E/F=99-522. DR PDBsum; 5E24; -. DR AlphaFoldDB; P28159; -. DR SMR; P28159; -. DR BioGRID; 60899; 85. DR ComplexPortal; CPX-2337; CSL-Notch-Mastermind transcriptional activation complex. DR DIP; DIP-177N; -. DR IntAct; P28159; 23. DR MINT; P28159; -. DR STRING; 7227.FBpp0080261; -. DR iPTMnet; P28159; -. DR PaxDb; 7227-FBpp0080261; -. DR EnsemblMetazoa; FBtr0080700; FBpp0080261; FBgn0004837. DR EnsemblMetazoa; FBtr0346621; FBpp0312201; FBgn0004837. DR GeneID; 34881; -. DR KEGG; dme:Dmel_CG3497; -. DR AGR; FB:FBgn0004837; -. DR CTD; 34881; -. DR FlyBase; FBgn0004837; Su(H). DR VEuPathDB; VectorBase:FBgn0004837; -. DR eggNOG; KOG3743; Eukaryota. DR HOGENOM; CLU_022207_2_1_1; -. DR InParanoid; P28159; -. DR OMA; QRQDMPH; -. DR OrthoDB; 1384914at2759; -. DR PhylomeDB; P28159; -. DR Reactome; R-DME-350054; Notch-HLH transcription pathway. DR SignaLink; P28159; -. DR BioGRID-ORCS; 34881; 0 hits in 3 CRISPR screens. DR GenomeRNAi; 34881; -. DR PRO; PR:P28159; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0004837; Expressed in outer epithelium and 71 other cell types or tissues. DR ExpressionAtlas; P28159; baseline and differential. DR GO; GO:1990433; C:CSL-Notch-Mastermind transcription factor complex; IDA:FlyBase. DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:FlyBase. DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase. DR GO; GO:0032991; C:protein-containing complex; IPI:FlyBase. DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IPI:FlyBase. DR GO; GO:0017053; C:transcription repressor complex; IGI:FlyBase. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:FlyBase. DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:FlyBase. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:FlyBase. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase. DR GO; GO:0008356; P:asymmetric cell division; TAS:FlyBase. DR GO; GO:0001709; P:cell fate determination; TAS:FlyBase. DR GO; GO:0042688; P:crystal cell differentiation; IMP:FlyBase. DR GO; GO:0030097; P:hemopoiesis; TAS:FlyBase. DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase. DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase. DR GO; GO:0007616; P:long-term memory; IMP:FlyBase. DR GO; GO:0042683; P:negative regulation of compound eye cone cell fate specification; TAS:FlyBase. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; TAS:FlyBase. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:FlyBase. DR GO; GO:0007219; P:Notch signaling pathway; IDA:FlyBase. DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:FlyBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase. DR GO; GO:0016360; P:sensory organ precursor cell fate determination; IMP:UniProtKB. DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IMP:FlyBase. DR CDD; cd01176; IPT_RBP-Jkappa; 1. DR Gene3D; 2.80.10.50; -; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 2.60.40.1450; LAG1, DNA binding domain; 1. DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom. DR InterPro; IPR036358; BTD_sf. DR InterPro; IPR040159; CLS_fam. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf. DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd. DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf. DR InterPro; IPR038007; RBP-Jkappa_IPT. DR PANTHER; PTHR10665; RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS; 1. DR PANTHER; PTHR10665:SF0; SUPPRESSOR OF HAIRLESS PROTEIN; 1. DR Pfam; PF09270; BTD; 1. DR Pfam; PF09271; LAG1-DNAbind; 1. DR Pfam; PF20144; TIG_SUH; 1. DR SMART; SM01268; BTD; 1. DR SMART; SM01267; LAG1_DNAbind; 1. DR SUPFAM; SSF110217; DNA-binding protein LAG-1 (CSL); 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF49417; p53-like transcription factors; 1. DR Genevisible; P28159; DM. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cytoplasm; Developmental protein; DNA-binding; KW Notch signaling pathway; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..594 FT /note="Suppressor of hairless protein" FT /id="PRO_0000208572" FT DOMAIN 429..519 FT /note="IPT/TIG" FT REGION 20..87 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 131..141 FT /note="DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q06330" FT REGION 239..244 FT /note="DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q06330" FT REGION 266..271 FT /note="DNA-binding" FT /evidence="ECO:0000250|UniProtKB:Q06330" FT REGION 542..594 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 22..46 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 53..87 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 80..82 FT /note="Missing (in strain: LAMTO 3, LAMTO 4, LAMTO 12, FT LAMTO 18, LAMTO 19, LAMTO 21, LAMTO 31, LAMTO 35, LAMTO 101 FT and LAMTO 111)" FT VARIANT 81..82 FT /note="Missing (in strain: LAMTO 13, LAMTO 37 and LAMTO FT 134)" FT VARIANT 82 FT /note="Missing (in strain: LAMTO 124)" FT MUTAGEN 315 FT /note="Y->F: No effect." FT /evidence="ECO:0000269|PubMed:7813798" FT CONFLICT 116..117 FT /note="ER -> DG (in Ref. 1; AAA06211/CAA41282)" FT /evidence="ECO:0000305" FT CONFLICT 492 FT /note="V -> A (in Ref. 1; AAA06211/CAA41282)" FT /evidence="ECO:0000305" FT HELIX 107..116 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 120..131 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:5E24" FT HELIX 153..163 FT /evidence="ECO:0007829|PDB:5E24" FT HELIX 167..171 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 172..178 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 195..198 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 216..221 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 226..231 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 235..238 FT /evidence="ECO:0007829|PDB:5E24" FT HELIX 248..250 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 259..266 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 274..280 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 283..289 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 321..326 FT /evidence="ECO:0007829|PDB:5E24" FT TURN 327..329 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 336..342 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 345..347 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 367..375 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 378..383 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 388..395 FT /evidence="ECO:0007829|PDB:5E24" FT HELIX 398..400 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 402..416 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 430..437 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 439..442 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 444..450 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 456..460 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 467..471 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 474..477 FT /evidence="ECO:0007829|PDB:5E24" FT HELIX 483..488 FT /evidence="ECO:0007829|PDB:5E24" FT TURN 489..491 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 492..494 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 498..504 FT /evidence="ECO:0007829|PDB:5E24" FT STRAND 507..520 FT /evidence="ECO:0007829|PDB:5E24" SQ SEQUENCE 594 AA; 66924 MW; 145144F336CD8F4C CRC64; MKSYSQFNLN AAAPPAIAYE TTVVNPNGSP LDPHQQQQQQ SQDMPHFGLP GPQPPSSQQQ QQQLQVHHQQ QQQQQQQQQQ QQHQQQMQMS LLPGPYRPHI EEKKLTRDAM EKYMRERNDM VIVILHAKVA QKSYGNEKRF FCPPPCIYLF GSGWRRRYEE MLQQGEGEQG AQLCAFIGIG SSDQDMQQLD LNGKQYCAAK TLFISDSDKR KHFMLSVKMF YGNGHDIGVF NSKRIKVISK PSKKKQSLKN ADLCIASGTN VALFNRLRSQ TVSTRYLHVE NGHFHASSTQ WGAFTIHLLD DNESESEEFQ VRDGYIHYGA TVKLVCSVTG MALPRLIIRK VDKQMALLEA DDPVSQLHKC AFYMKDTDRM YLCLSQEKII QFQATPCPKE PNKEMINDGA CWTIISTDKA EYQFYEGMGP VASPVTPVPI VNSLNLNGGG DVAMLELSGD NFTPHLQVWF GDVEAETMYR CTETLLCVVP EISQFRGEWL WVRQPTQVPI SLVRNDGIIY ATGLTFTYTP EPGPRPHCNT QAEDVMRARQ NNNNNNITSI SNNNNSNNAG SPAAGGGLQQ QQQQHQALPS ISEVQWNSHG SGLS //