ID SUH_MOUSE Reviewed; 526 AA.
AC P31266; Q80UN8; Q8C4Z3;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 27-MAR-2024, entry version 221.
DE RecName: Full=Recombining binding protein suppressor of hairless;
DE AltName: Full=J kappa-recombination signal-binding protein;
DE AltName: Full=RBP-J kappa;
GN Name=Rbpj {ECO:0000312|MGI:MGI:96522}; Synonyms=Igkjrb1, Igkrsbp, Rbpsuh;
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] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2556644; DOI=10.1038/342934a0;
RA Matsunami N., Hamaguchi Y., Yamamoto Y., Kuze K., Kangawa K., Matsuo H.,
RA Kawaichi M., Honjo T.;
RT "A protein binding to the J kappa recombination sequence of immunoglobulin
RT genes contains a sequence related to the integrase motif.";
RL Nature 342:934-937(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1740450; DOI=10.1016/s0021-9258(19)50626-3;
RA Kawaichi M., Oka C., Shibayama S., Koromilas A.E., Matsunami N.,
RA Hamaguchi Y., Honjo T.;
RT "Genomic organization of mouse J kappa recombination signal binding protein
RT (RBP-J kappa) gene.";
RL J. Biol. Chem. 267:4016-4022(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1950768; DOI=10.1007/978-1-4684-5943-2_20;
RA Hamaguchi Y., Matsunami N., Yamamoto Y., Kuze K., Kangawa K., Matsuo H.,
RA Kawaichi M., Honjo T.;
RT "Cloning and characterization of a protein binding to the J kappa
RT recombination signal sequence of immunoglobulin genes.";
RL Adv. Exp. Med. Biol. 292:177-186(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 1-341 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 FUNCTION, AND INTERACTION WITH NOTCH1.
RX PubMed=7566092; DOI=10.1038/377355a0;
RA Jarriault S., Brou C., Logeat F., Schroeter E.H., Kopan R., Israel A.;
RT "Signalling downstream of activated mammalian Notch.";
RL Nature 377:355-358(1995).
RN [7]
RP INTERACTION WITH FHL1.
RX PubMed=9418910; DOI=10.1128/mcb.18.1.644;
RA Taniguchi Y., Furukawa T., Tun T., Han H., Honjo T.;
RT "LIM protein KyoT2 negatively regulates transcription by association with
RT the RBP-J DNA-binding protein.";
RL Mol. Cell. Biol. 18:644-654(1998).
RN [8]
RP INTERACTION WITH EP300.
RX PubMed=11604511; DOI=10.1128/mcb.21.22.7761-7774.2001;
RA Oswald F., Taeuber B., Dobner T., Bourteele S., Kostezka U., Adler G.,
RA Liptay S., Schmid R.M.;
RT "p300 acts as a transcriptional coactivator for mammalian Notch-1.";
RL Mol. Cell. Biol. 21:7761-7774(2001).
RN [9]
RP INTERACTION WITH PTF1A.
RC STRAIN=ICR; TISSUE=Embryo;
RX PubMed=11318877; DOI=10.1046/j.1365-2443.2001.00422.x;
RA Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C.,
RA Kawaichi M.;
RT "p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular
RT mediator of Notch signalling, and is expressed in the neural tube of early
RT stage embryos.";
RL Genes Cells 6:345-360(2001).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH NCOR2 AND HDAC1.
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 [11]
RP INTERACTION WITH RBM15.
RX PubMed=17283045; DOI=10.1128/mcb.01339-06;
RA Ma X., Renda M.J., Wang L., Cheng E.C., Niu C., Morris S.W., Chi A.S.,
RA Krause D.S.;
RT "Rbm15 modulates Notch-induced transcriptional activation and affects
RT myeloid differentiation.";
RL Mol. Cell. Biol. 27:3056-3064(2007).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-201, 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 [13]
RP INTERACTION WITH NKAPL.
RX PubMed=25875095; DOI=10.1371/journal.pone.0124293;
RA Okuda H., Kiuchi H., Takao T., Miyagawa Y., Tsujimura A., Nonomura N.,
RA Miyata H., Okabe M., Ikawa M., Kawakami Y., Goshima N., Wada M., Tanaka H.;
RT "A novel transcriptional factor Nkapl is a germ cell-specific suppressor of
RT Notch signaling and is indispensable for spermatogenesis.";
RL PLoS ONE 10:E0124293-E0124293(2015).
RN [14]
RP FUNCTION.
RX PubMed=26194095; DOI=10.1038/ncomms8838;
RA Graham D.B., Becker C.E., Doan A., Goel G., Villablanca E.J., Knights D.,
RA Mok A., Ng A.C., Doench J.G., Root D.E., Clish C.B., Xavier R.J.;
RT "Functional genomics identifies negative regulatory nodes controlling
RT phagocyte oxidative burst.";
RL Nat. Commun. 6:7838-7838(2015).
RN [15]
RP INTERACTION WITH L3MBTL3, AND MUTAGENESIS OF PHE-128; PHE-172; ARG-186;
RP PHE-261; VAL-263; ALA-284; GLN-333; ASN-389; GLU-398; ASN-407; ARG-422 AND
RP GLU-425.
RX PubMed=29030483; DOI=10.15252/embj.201796525;
RA Xu T., Park S.S., Giaimo B.D., Hall D., Ferrante F., Ho D.M., Hori K.,
RA Anhezini L., Ertl I., Bartkuhn M., Zhang H., Milon E., Ha K., Conlon K.P.,
RA Kuick R., Govindarajoo B., Zhang Y., Sun Y., Dou Y., Basrur V.,
RA Elenitoba-Johnson K.S., Nesvizhskii A.I., Ceron J., Lee C.Y., Borggrefe T.,
RA Kovall R.A., Rual J.F.;
RT "RBPJ/CBF1 interacts with L3MBTL3/MBT1 to promote repression of Notch
RT signaling via histone demethylase KDM1A/LSD1.";
RL EMBO J. 36:3232-3249(2017).
RN [16] {ECO:0007744|PDB:3BRG}
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 53-474 IN COMPLEX WITH DNA, AND
RP FUNCTION.
RX PubMed=18381292; DOI=10.1074/jbc.m709501200;
RA Friedmann D.R., Wilson J.J., Kovall R.A.;
RT "RAM-induced allostery facilitates assembly of a notch pathway active
RT transcription complex.";
RL J. Biol. Chem. 283:14781-14791(2008).
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:7566092). Acts as a transcriptional repressor when it is not
CC associated with Notch proteins. When associated with some NICD product
CC of Notch proteins (Notch intracellular domain), it acts as a
CC transcriptional activator that activates transcription of Notch target
CC genes (By similarity) (PubMed:18381292). Probably represses or
CC activates transcription via the recruitment of chromatin remodeling
CC complexes containing histone deacetylase or histone acetylase proteins,
CC respectively. Specifically binds to the immunoglobulin kappa-type J
CC segment recombination signal sequence. Binds specifically to methylated
CC DNA. Binds to the oxygen responsive element of COX4I2 and activates its
CC transcription under hypoxia conditions (4% oxygen) (By similarity).
CC Negatively regulates the phagocyte oxidative burst in response to
CC bacterial infection by repressing transcription of NADPH oxidase
CC subunits (PubMed:26194095). {ECO:0000250|UniProtKB:P28159,
CC ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:18381292,
CC ECO:0000269|PubMed:26194095, ECO:0000269|PubMed:7566092}.
CC -!- SUBUNIT: Interacts with RITA1, leading to nuclear export, prevent the
CC interaction between RBPJ and NICD product and subsequent down-
CC regulation of the Notch signaling pathway (By similarity). Interacts
CC with activated NOTCH1, NOTCH2 and NOTCH3. Interacts with MINT/SHARP.
CC This interaction may mediate the recruitment of large corepressor
CC complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30,
CC FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. Interacts
CC with SNW1. Interacts with CHCHD2 and CXXC5. Interacts with BEND6 (via
CC BEN domain) (By similarity). Interacts with NKAPL (PubMed:25875095).
CC Interacts with ZMIZ1 (By similarity). Interacts with RBM15
CC (PubMed:17283045). Interacts with L3MBTL3; the interaction is impaired
CC by Notch-derived peptides containing the intracellular domain (NICD)
CC (PubMed:29030483). Interacts with KDM1A; the interaction with KDM1A is
CC weaker in the absence of L3MBTL3 (By similarity).
CC {ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:10640276,
CC ECO:0000269|PubMed:11318877, ECO:0000269|PubMed:11604511,
CC ECO:0000269|PubMed:17283045, ECO:0000269|PubMed:25875095,
CC ECO:0000269|PubMed:29030483, ECO:0000269|PubMed:7566092,
CC ECO:0000269|PubMed:9418910}.
CC -!- INTERACTION:
CC P31266; P97447-2: Fhl1; NbExp=4; IntAct=EBI-1392666, EBI-16082627;
CC P31266; Q01705: Notch1; NbExp=8; IntAct=EBI-1392666, EBI-1392707;
CC P31266; Q6P9Z1: Smarcd3; NbExp=3; IntAct=EBI-1392666, EBI-7525857;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Mainly
CC nuclear, upon interaction with RITA1, translocates to the cytoplasm,
CC down-regulating the Notch signaling pathway. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P31266-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P31266-2; Sequence=VSP_008392, VSP_008393;
CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
CC -!- CAUTION: Despite some similarity with the 'phage' integrase family, it
CC has no recombinase activity. {ECO:0000305}.
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DR EMBL; S63463; AAB20195.1; -; mRNA.
DR EMBL; X17459; CAA35501.1; -; mRNA.
DR EMBL; X58337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M81867; AAA39018.1; -; Genomic_DNA.
DR EMBL; M81865; AAA39018.1; JOINED; Genomic_DNA.
DR EMBL; M81866; AAA39018.1; JOINED; Genomic_DNA.
DR EMBL; M81868; AAA39019.1; -; Genomic_DNA.
DR EMBL; M81870; AAA39020.1; ALT_SEQ; Genomic_DNA.
DR EMBL; M81869; AAA39020.1; JOINED; Genomic_DNA.
DR EMBL; M81873; AAA39021.1; -; Genomic_DNA.
DR EMBL; M81872; AAA39021.1; JOINED; Genomic_DNA.
DR EMBL; M81875; AAA39022.1; -; Genomic_DNA.
DR EMBL; M81874; AAA39022.1; JOINED; Genomic_DNA.
DR EMBL; M81876; AAA39023.1; -; Genomic_DNA.
DR EMBL; M81877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051387; AAH51387.1; -; mRNA.
DR EMBL; AK080359; BAC37889.1; -; mRNA.
DR CCDS; CCDS19292.1; -. [P31266-1]
DR CCDS; CCDS51504.1; -. [P31266-2]
DR PIR; A42267; A42267.
DR PIR; A43567; A43567.
DR RefSeq; NP_001074396.1; NM_001080927.2. [P31266-2]
DR RefSeq; NP_033061.3; NM_009035.5. [P31266-1]
DR PDB; 3BRG; X-ray; 2.20 A; C=53-474.
DR PDB; 3IAG; X-ray; 2.00 A; C=53-474.
DR PDB; 4J2X; X-ray; 2.85 A; A/C=53-474.
DR PDB; 5EG6; X-ray; 2.09 A; C=53-474.
DR PDB; 6DKS; X-ray; 2.78 A; C/G=53-474.
DR PDB; 6WQU; X-ray; 2.41 A; C=53-474.
DR PDB; 7RTE; X-ray; 2.06 A; C=53-474.
DR PDB; 7RTI; X-ray; 2.05 A; C=53-474.
DR PDBsum; 3BRG; -.
DR PDBsum; 3IAG; -.
DR PDBsum; 4J2X; -.
DR PDBsum; 5EG6; -.
DR PDBsum; 6DKS; -.
DR PDBsum; 6WQU; -.
DR PDBsum; 7RTE; -.
DR PDBsum; 7RTI; -.
DR AlphaFoldDB; P31266; -.
DR SMR; P31266; -.
DR BioGRID; 202832; 13.
DR CORUM; P31266; -.
DR DIP; DIP-171N; -.
DR ELM; P31266; -.
DR IntAct; P31266; 8.
DR MINT; P31266; -.
DR STRING; 10090.ENSMUSP00000040694; -.
DR GlyGen; P31266; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P31266; -.
DR PhosphoSitePlus; P31266; -.
DR SwissPalm; P31266; -.
DR EPD; P31266; -.
DR MaxQB; P31266; -.
DR PaxDb; 10090-ENSMUSP00000040694; -.
DR PeptideAtlas; P31266; -.
DR ProteomicsDB; 254496; -. [P31266-1]
DR ProteomicsDB; 254497; -. [P31266-2]
DR Pumba; P31266; -.
DR Antibodypedia; 10265; 494 antibodies from 41 providers.
DR DNASU; 19664; -.
DR Ensembl; ENSMUST00000037618.13; ENSMUSP00000040694.7; ENSMUSG00000039191.13. [P31266-1]
DR Ensembl; ENSMUST00000113865.5; ENSMUSP00000109496.2; ENSMUSG00000039191.13. [P31266-2]
DR GeneID; 19664; -.
DR KEGG; mmu:19664; -.
DR UCSC; uc008xli.2; mouse. [P31266-1]
DR AGR; MGI:96522; -.
DR CTD; 3516; -.
DR MGI; MGI:96522; Rbpj.
DR VEuPathDB; HostDB:ENSMUSG00000039191; -.
DR eggNOG; KOG3743; Eukaryota.
DR GeneTree; ENSGT00390000005197; -.
DR InParanoid; P31266; -.
DR OMA; QRQDMPH; -.
DR OrthoDB; 1384914at2759; -.
DR PhylomeDB; P31266; -.
DR TreeFam; TF314117; -.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR BioGRID-ORCS; 19664; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Rbpj; mouse.
DR EvolutionaryTrace; P31266; -.
DR PRO; PR:P31266; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P31266; Protein.
DR Bgee; ENSMUSG00000039191; Expressed in ureter smooth muscle and 253 other cell types or tissues.
DR ExpressionAtlas; P31266; baseline and differential.
DR Genevisible; P31266; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA: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:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0003176; P:aortic valve development; IMP:BHF-UCL.
DR GO; GO:0060844; P:arterial endothelial cell fate commitment; IMP:BHF-UCL.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0036302; P:atrioventricular canal development; IMP:BHF-UCL.
DR GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0097101; P:blood vessel endothelial cell fate specification; IGI:BHF-UCL.
DR GO; GO:0072554; P:blood vessel lumenization; IMP:BHF-UCL.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0060486; P:club cell differentiation; IMP:MGI.
DR GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; TAS:BHF-UCL.
DR GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003157; P:endocardium development; IMP:BHF-UCL.
DR GO; GO:0003160; P:endocardium morphogenesis; IMP:BHF-UCL.
DR GO; GO:0009957; P:epidermal cell fate specification; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0003129; P:heart induction; TAS:BHF-UCL.
DR GO; GO:0001947; P:heart looping; TAS:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0006959; P:humoral immune response; IMP:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
DR GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:BHF-UCL.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI.
DR GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:BHF-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; IMP:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
DR GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:1901186; P:positive regulation of ERBB signaling pathway; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IGI:MGI.
DR GO; GO:0003177; P:pulmonary valve development; IMP:BHF-UCL.
DR GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IMP:BHF-UCL.
DR GO; GO:0050678; P:regulation of epithelial cell proliferation; IGI:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043467; P:regulation of generation of precursor metabolites and energy; ISO:MGI.
DR GO; GO:2000241; P:regulation of reproductive process; IGI:MGI.
DR GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
DR GO; GO:0003139; P:secondary heart field specification; IMP:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
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:SF3; RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; DNA-binding; Notch signaling pathway; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..526
FT /note="Recombining binding protein suppressor of hairless"
FT /id="PRO_0000208568"
FT DOMAIN 381..471
FT /note="IPT/TIG"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..93
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:18381292"
FT REGION 191..196
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:18381292"
FT REGION 218..223
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:18381292"
FT REGION 491..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 201
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008392"
FT VAR_SEQ 40..45
FT /note="AHAPSA -> MAPVVT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008393"
FT MUTAGEN 128
FT /note="F->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 172
FT /note="F->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 186
FT /note="R->E: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 261
FT /note="F->R: Loss of interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 263
FT /note="V->R: Decreased interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 284
FT /note="A->R: Decreased interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 333
FT /note="Q->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 389
FT /note="N->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 398
FT /note="E->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 407
FT /note="N->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 422
FT /note="R->E: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT MUTAGEN 425
FT /note="E->R: No effect on interaction with L3MBTL3."
FT /evidence="ECO:0000269|PubMed:29030483"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 124..133
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6DKS"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:5EG6"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3IAG"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 319..327
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:6WQU"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 354..368
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 382..388
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3IAG"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 439..441
FT /evidence="ECO:0007829|PDB:6DKS"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:3IAG"
FT STRAND 459..470
FT /evidence="ECO:0007829|PDB:3IAG"
SQ SEQUENCE 526 AA; 58537 MW; 8BF517CC24099E03 CRC64;
MPSGFPQSPR TSPRARPKTR ITGALPMDYS EGLSAEERPA HAPSAGKFGE RPPPKRLTRE
AMRNYLKERG DQTVLILHAK VAQKSYGNEK RFFCPPPCVY LMGSGWKKKK EQMERDGCSE
QESQPCAFIG IGNSDQEMQQ LNLEGKNYCT AKTLYISDSD KRKHFMLSVK MFYGNSDDIG
VFLSKRIKVI SKPSKKKQSL KNADLCIASG TKVALFNRLR SQTVSTRYLH VEGGNFHASS
QQWGAFYIHL LDDDESEGEE FTVRDGYIHY GQTVKLVCSV TGMALPRLII RKVDKQTALL
DADDPVSQLH KCAFYLKDTE RMYLCLSQER IIQFQATPCP KEQNKEMIND GASWTIISTD
KAEYTFYEGM GPVLAPVTPV PVVESLQLNG GGDVAMLELT GQNFTPNLRV WFGDVEAETM
YRCGESMLCV VPDISAFREG WRWVRQPVQV PVTLVRNDGV IYSTSLTFTY TPEPGPRPHC
SAAGAILRAN SSQVPSNESN TNSEGNYTNA STNSTSVTSS TATVVS
//
