ID SUH_HUMAN Reviewed; 500 AA. AC Q06330; B4DY22; Q5XKH9; Q6P1N3; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 3. DT 07-JAN-2015, entry version 149. DE RecName: Full=Recombining binding protein suppressor of hairless; DE AltName: Full=CBF-1; DE AltName: Full=J kappa-recombination signal-binding protein; DE AltName: Full=RBP-J kappa; DE Short=RBP-J; DE Short=RBP-JK; DE AltName: Full=Renal carcinoma antigen NY-REN-30; GN Name=RBPJ; Synonyms=IGKJRB, IGKJRB1, RBPJK, RBPSUH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS APCR-1; APCR-2 AND APCR-3), AND RP VARIANT VAL-456. RC TISSUE=Placenta; RX PubMed=8406481; DOI=10.1006/geno.1993.1326; RA Amakawa R., Jing W., Ozawa K., Matsunami N., Hamaguchi Y., Matsuda F., RA Kawaichi M., Honjo T.; RT "Human Jk recombination signal binding protein gene (IGKJRB): RT comparison with its mouse homologue."; RL Genomics 17:306-315(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6). RC TISSUE=Eye; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP INTERACTION WITH EBV EBNA2. RX PubMed=8016657; DOI=10.1126/science.8016657; RA Henkel T., Ling P.D., Hayward S.D., Peterson M.G.; RT "Mediation of Epstein-Barr virus EBNA2 transactivation by RT recombination signal-binding protein J kappa."; RL Science 265:92-95(1994). RN [6] RP INTERACTION WITH EBV EBNA3; EBV EBNA4 AND EBV EBNA6. RX PubMed=8627785; RA Robertson E.S., Lin J., Kieff E.; RT "The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, RT 3B, and 3C interact with RBPJ(kappa)."; RL J. Virol. 70:3068-3074(1996). RN [7] RP IDENTIFICATION AS A RENAL CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [8] RP INTERACTION WITH CIR1, AND SUBCELLULAR LOCATION. RX PubMed=9874765; DOI=10.1073/pnas.96.1.23; RA Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.; RT "CIR, a corepressor linking the DNA binding factor CBF1 to the histone RT deacetylase complex."; RL Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999). RN [9] RP INTERACTION WITH SNW1. RX PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000; RA Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.; RT "A role for SKIP in EBNA2 activation of CBF1-repressed promoters."; RL J. Virol. 74:1939-1947(2000). RN [10] RP INTERACTION WITH NOTCH1. RX PubMed=10637481; DOI=10.1038/sj.leu.2401630; RA Callahan J., Aster J., Sklar J., Kieff E., Robertson E.S.; RT "Intracellular forms of human NOTCH1 interact at distinctly different RT levels with RBP-jkappa in human B and T cells."; RL Leukemia 14:84-92(2000). RN [11] RP INTERACTION WITH MINT. RX PubMed=12374742; DOI=10.1093/emboj/cdf549; RA Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K., RA Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S., RA Schmid R.M.; RT "SHARP is a novel component of the Notch/RBP-Jkappa signalling RT pathway."; RL EMBO J. 21:5417-5426(2002). RN [12] RP INTERACTION WITH C12ORF52, AND SUBCELLULAR LOCATION. RX PubMed=21102556; DOI=10.1038/emboj.2010.289; RA Wacker S.A., Alvarado C., von Wichert G., Knippschild U., RA Wiedenmann J., Clauss K., Nienhaus G.U., Hameister H., Baumann B., RA Borggrefe T., Knochel W., Oswald F.; RT "RITA, a novel modulator of Notch signalling, acts via nuclear export RT of RBP-J."; RL EMBO J. 30:43-56(2011). RN [13] RP FUNCTION, AND METHYLATED DNA-BINDING. RX PubMed=21991380; DOI=10.1371/journal.pone.0025884; RA Bartels S.J., Spruijt C.G., Brinkman A.B., Jansen P.W., Vermeulen M., RA Stunnenberg H.G.; RT "A SILAC-based screen for Methyl-CpG binding proteins identifies RBP-J RT as a DNA methylation and sequence-specific binding protein."; RL PLoS ONE 6:E25884-E25884(2011). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA; RP MAML1 AND NOTCH1. RX PubMed=16530044; DOI=10.1016/j.cell.2005.12.037; RA Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.; RT "Structural basis for cooperativity in recruitment of MAML RT coactivators to Notch transcription complexes."; RL Cell 124:973-983(2006). RN [15] RP VARIANTS AOS3 GLY-63 AND GLU-169, AND CHARACTERIZATION OF VARIANTS RP AOS3 GLY-63 AND GLU-169. RX PubMed=22883147; DOI=10.1016/j.ajhg.2012.07.005; RA Hassed S.J., Wiley G.B., Wang S., Lee J.Y., Li S., Xu W., Zhao Z.J., RA Mulvihill J.J., Robertson J., Warner J., Gaffney P.M.; RT "RBPJ mutations identified in two families affected by Adams-Oliver RT syndrome."; RL Am. J. Hum. Genet. 91:391-395(2012). CC -!- FUNCTION: Transcriptional regulator that plays a central role in CC Notch signaling, a signaling pathway involved in cell-cell CC communication that regulates a broad spectrum of cell-fate CC determinations. Acts as a transcriptional repressor when it is not CC associated with Notch proteins. When associated with some NICD CC product of Notch proteins (Notch intracellular domain), it acts as CC a transcriptional activator that activates transcription of Notch CC target genes. Probably represses or activates transcription via CC the recruitment of chromatin remodeling complexes containing CC histone deacetylase or histone acetylase proteins, respectively. CC Specifically binds to the immunoglobulin kappa-type J segment CC recombination signal sequence. Binds specifically to methylated CC DNA. {ECO:0000269|PubMed:21991380}. CC -!- SUBUNIT: Interacts with activated NOTCH1, NOTCH2 or NOTCH3. CC Interacts with MINT/SHARP. This interaction may mediate the CC recruitment of large corepressor complexes containing proteins CC such as HDAC1, HDAC2, NCOR2, SAP30, FHL1/KYOT2 and CIR1. Interacts CC with EP300, MAML1 and PTF1A. Interacts with Epstein-Barr virus CC EBNA2, EBNA3, EBNA4 and EBNA6. Interacts with RITA1/C12orf52, CC leading to nuclear export, prevent the interaction between RBPJ CC and NICD product and subsequent down-regulation of the Notch CC signaling pathway. Interacts with SNW1. CC {ECO:0000269|PubMed:10637481, ECO:0000269|PubMed:10644367, CC ECO:0000269|PubMed:12374742, ECO:0000269|PubMed:16530044, CC ECO:0000269|PubMed:21102556, ECO:0000269|PubMed:8016657, CC ECO:0000269|PubMed:8627785, ECO:0000269|PubMed:9874765}. CC -!- INTERACTION: CC P54253:ATXN1; NbExp=7; IntAct=EBI-632552, EBI-930964; CC P0C7T5:ATXN1L; NbExp=7; IntAct=EBI-632552, EBI-8624731; CC P12978:EBNA2 (xeno); NbExp=2; IntAct=EBI-632552, EBI-8052923; CC P12977:EBNA3 (xeno); NbExp=3; IntAct=EBI-632552, EBI-993115; CC P03203:EBNA4 (xeno); NbExp=4; IntAct=EBI-632552, EBI-9346250; CC P03204:EBNA6 (xeno); NbExp=3; IntAct=EBI-632552, EBI-9255985; CC Q9Y618:NCOR2; NbExp=3; IntAct=EBI-632552, EBI-80830; CC P46531:NOTCH1; NbExp=3; IntAct=EBI-632552, EBI-636374; CC Q01705:Notch1 (xeno); NbExp=3; IntAct=EBI-632552, EBI-1392707; CC Q96K30:RITA1; NbExp=8; IntAct=EBI-632552, EBI-2836148; CC P0CJ62:rita1 (xeno); NbExp=2; IntAct=EBI-632552, EBI-8517225; CC Q13573:SNW1; NbExp=2; IntAct=EBI-632552, EBI-632715; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear, CC upon interaction with RITA/C12orf52, translocates to the CC cytoplasm, down-regulating the Notch signaling pathway. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=APCR-2; CC IsoId=Q06330-1; Sequence=Displayed; CC Name=APCR-1; CC IsoId=Q06330-2; Sequence=VSP_002717; CC Name=APCR-3; CC IsoId=Q06330-3; Sequence=VSP_002718, VSP_002719; CC Name=4; CC IsoId=Q06330-4; Sequence=VSP_021573; CC Name=5; CC IsoId=Q06330-5; Sequence=VSP_021572; CC Name=6; CC IsoId=Q06330-6; Sequence=VSP_021574; CC Name=7; CC IsoId=Q06330-7; Sequence=VSP_042637; CC -!- DISEASE: Adams-Oliver syndrome 3 (AOS3) [MIM:614814]: An autosomal CC dominant form of Adams-Oliver syndrome, a disorder characterized CC by the congenital absence of skin (aplasia cutis congenita) in CC combination with transverse limb defects. Aplasia cutis congenita CC can be located anywhere on the body, but in the vast majority of CC the cases, it is present on the posterior parietal region where it CC is often associated with an underlying defect of the parietal CC bones. Limb abnormalities are typically limb truncation defects CC affecting the distal phalanges or entire digits (true CC ectrodactyly). Only rarely, metatarsals/metacarpals or more CC proximal limb structures are also affected. Apart from transverse CC limb defects, syndactyly, most commonly of second and third toes, CC can also be observed. The clinical features are highly variable CC and can also include cardiovascular malformations, brain CC abnormalities and vascular defects such as cutis marmorata and CC dilated scalp veins. AOS3 patients manifest characteristic vertex CC scalp defects and terminal limb defects, but without congenital CC heart defects, other associated defects, or immune defects. CC {ECO:0000269|PubMed:22883147}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 IPT/TIG domain. {ECO:0000305}. CC -!- CAUTION: Despite some similarity with the "phage" integrase CC family, it has no recombinase activity. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA16254.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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; L07872; AAA60258.1; -; mRNA. DR EMBL; L07874; AAA16253.1; -; mRNA. DR EMBL; L07875; AAA16254.1; ALT_INIT; mRNA. DR EMBL; L07876; AAA16356.1; -; mRNA. DR EMBL; AK302230; BAG63584.1; -; mRNA. DR EMBL; AC093637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097109; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC097714; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC111003; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020780; AAH20780.1; -; mRNA. DR EMBL; BC053531; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC064976; AAH64976.1; -; mRNA. DR CCDS; CCDS33969.1; -. [Q06330-6] DR CCDS; CCDS3436.1; -. [Q06330-4] DR CCDS; CCDS3437.1; -. [Q06330-1] DR CCDS; CCDS43219.1; -. [Q06330-7] DR PIR; A47214; A47214. DR RefSeq; NP_005340.2; NM_005349.3. [Q06330-1] DR RefSeq; NP_056958.3; NM_015874.4. [Q06330-7] DR RefSeq; NP_976028.1; NM_203283.2. [Q06330-4] DR RefSeq; NP_976029.1; NM_203284.2. [Q06330-6] DR RefSeq; XP_005248218.1; XM_005248161.2. [Q06330-6] DR RefSeq; XP_006714025.1; XM_006713962.1. [Q06330-6] DR RefSeq; XP_006714026.1; XM_006713963.1. [Q06330-5] DR UniGene; Hs.479396; -. DR PDB; 2F8X; X-ray; 3.25 A; C=23-449. DR PDB; 3NBN; X-ray; 3.45 A; A/D=23-448. DR PDB; 3V79; X-ray; 3.85 A; C=23-449. DR PDBsum; 2F8X; -. DR PDBsum; 3NBN; -. DR PDBsum; 3V79; -. DR ProteinModelPortal; Q06330; -. DR SMR; Q06330; 25-448. DR BioGrid; 109736; 42. DR DIP; DIP-33326N; -. DR IntAct; Q06330; 26. DR MINT; MINT-1327001; -. DR STRING; 9606.ENSP00000345206; -. DR PhosphoSite; Q06330; -. DR DMDM; 338817983; -. DR MaxQB; Q06330; -. DR PaxDb; Q06330; -. DR PRIDE; Q06330; -. DR DNASU; 3516; -. DR Ensembl; ENST00000342295; ENSP00000345206; ENSG00000168214. [Q06330-1] DR Ensembl; ENST00000342320; ENSP00000340124; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000345843; ENSP00000305815; ENSG00000168214. [Q06330-4] DR Ensembl; ENST00000348160; ENSP00000339699; ENSG00000168214. [Q06330-7] DR Ensembl; ENST00000355476; ENSP00000347659; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000361572; ENSP00000354528; ENSG00000168214. [Q06330-1] DR Ensembl; ENST00000507561; ENSP00000423907; ENSG00000168214. [Q06330-5] DR GeneID; 3516; -. DR KEGG; hsa:3516; -. DR UCSC; uc003grx.2; human. [Q06330-1] DR UCSC; uc003gry.2; human. [Q06330-4] DR UCSC; uc003gsa.2; human. [Q06330-6] DR UCSC; uc003gsb.2; human. [Q06330-7] DR CTD; 3516; -. DR GeneCards; GC04P026165; -. DR HGNC; HGNC:5724; RBPJ. DR MIM; 147183; gene. DR MIM; 614814; phenotype. DR neXtProt; NX_Q06330; -. DR Orphanet; 974; Adams-Oliver syndrome. DR PharmGKB; PA34292; -. DR eggNOG; NOG295376; -. DR GeneTree; ENSGT00390000005197; -. DR HOGENOM; HOG000253907; -. DR HOVERGEN; HBG006618; -. DR InParanoid; Q06330; -. DR KO; K06053; -. DR OMA; MGPVHAP; -. DR PhylomeDB; Q06330; -. DR TreeFam; TF314117; -. DR Reactome; REACT_118568; Pre-NOTCH Transcription and Translation. DR Reactome; REACT_118780; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; REACT_13673; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells. DR Reactome; REACT_14835; Notch-HLH transcription pathway. DR Reactome; REACT_160243; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; REACT_160254; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; REACT_163910; NOTCH2 intracellular domain regulates transcription. DR SignaLink; Q06330; -. DR ChiTaRS; RBPJ; human. DR EvolutionaryTrace; Q06330; -. DR GeneWiki; RBPJ; -. DR GenomeRNAi; 3516; -. DR NextBio; 13784; -. DR PRO; PR:Q06330; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; Q06330; -. DR CleanEx; HS_RBPJ; -. DR ExpressionAtlas; Q06330; baseline and differential. DR Genevestigator; Q06330; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005667; C:transcription factor complex; IEA:Ensembl. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB. DR GO; GO:0000150; F:recombinase activity; NAS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:MGI. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL. DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:UniProtKB. DR GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL. DR GO; GO:0060844; P:arterial endothelial cell fate commitment; IEA:Ensembl. DR GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL. DR GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl. DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl. DR GO; GO:0097101; P:blood vessel endothelial cell fate specification; ISS:BHF-UCL. DR GO; GO:0072554; P:blood vessel lumenization; ISS:BHF-UCL. DR GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl. DR GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL. DR GO; GO:0060486; P:Clara cell differentiation; IEA:Ensembl. DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl. DR GO; GO:0006310; P:DNA recombination; NAS:UniProtKB. DR GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL. DR GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL. DR GO; GO:0009957; P:epidermal cell fate specification; IEA:Ensembl. DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL. DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL. DR GO; GO:0010467; P:gene expression; TAS:Reactome. DR GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl. DR GO; GO:0006959; P:humoral immune response; IEA:Ensembl. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl. DR GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISS:BHF-UCL. DR GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl. DR GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0061314; P:Notch signaling involved in heart development; IC:BHF-UCL. DR GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL. DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL. DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:BHF-UCL. DR GO; GO:1901297; P:positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; IEA:Ensembl. DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL. DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL. DR GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; ISS:BHF-UCL. DR GO; GO:1901186; P:positive regulation of ERBB signaling pathway; ISS:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL. DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:UniProtKB. DR GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl. DR GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL. DR GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl. DR GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl. DR GO; GO:0035019; P:somatic stem cell maintenance; IEA:Ensembl. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome. DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.1450; -; 1. DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR014756; Ig_E-set. DR InterPro; IPR002909; IPT. DR InterPro; IPR015351; LAG1_DNA-bd. DR InterPro; IPR008967; p53-like_TF_DNA-bd. DR Pfam; PF09270; BTD; 1. DR Pfam; PF09271; LAG1-DNAbind; 1. DR Pfam; PF01833; TIG; 1. DR SUPFAM; SSF110217; SSF110217; 1. DR SUPFAM; SSF49417; SSF49417; 1. DR SUPFAM; SSF81296; SSF81296; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Complete proteome; Cytoplasm; Disease mutation; DNA-binding; KW Notch signaling pathway; Nucleus; Polymorphism; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation. FT CHAIN 1 500 Recombining binding protein suppressor of FT hairless. FT /FTId=PRO_0000208567. FT DOMAIN 355 445 IPT/TIG. FT DNA_BIND 58 65 FT DNA_BIND 192 201 FT DNA_BIND 265 297 FT MOD_RES 175 175 N6-acetyllysine. {ECO:0000250}. FT VAR_SEQ 1 89 Missing (in isoform APCR-3). FT {ECO:0000303|PubMed:8406481}. FT /FTId=VSP_002718. FT VAR_SEQ 1 75 Missing (in isoform APCR-1). FT {ECO:0000303|PubMed:8406481}. FT /FTId=VSP_002717. FT VAR_SEQ 1 35 Missing (in isoform 5). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_021572. FT VAR_SEQ 1 20 MDHTEGSPAEEPPAHAPSPG -> MGGCR (in isoform FT 4). {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_021573. FT VAR_SEQ 1 20 MDHTEGSPAEEPPAHAPSPG -> MAWIKR (in FT isoform 6). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_021574. FT VAR_SEQ 1 19 MDHTEGSPAEEPPAHAPSP -> MAPVVT (in isoform FT 7). {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_042637. FT VAR_SEQ 90 95 DGCSEQ -> MAWIKR (in isoform APCR-3). FT {ECO:0000303|PubMed:8406481}. FT /FTId=VSP_002719. FT VARIANT 63 63 E -> G (in AOS3; shows decreased binding FT to the HES1 promoter compared to wild- FT type). {ECO:0000269|PubMed:22883147}. FT /FTId=VAR_068929. FT VARIANT 169 169 K -> E (in AOS3; shows decreased binding FT to the HES1 promoter compared to wild- FT type). {ECO:0000269|PubMed:22883147}. FT /FTId=VAR_068930. FT VARIANT 291 291 K -> E (in dbSNP:rs1064372). FT /FTId=VAR_028994. FT VARIANT 296 296 M -> K (in dbSNP:rs5011135). FT /FTId=VAR_057243. FT VARIANT 334 334 D -> H (in dbSNP:rs1064376). FT /FTId=VAR_028995. FT VARIANT 408 408 I -> V (in dbSNP:rs1064381). FT /FTId=VAR_057244. FT VARIANT 419 419 R -> Q (in dbSNP:rs1064384). FT /FTId=VAR_028996. FT VARIANT 425 425 P -> S (in dbSNP:rs1064387). FT /FTId=VAR_028997. FT VARIANT 456 456 A -> V (in dbSNP:rs1064402). FT {ECO:0000269|PubMed:8406481}. FT /FTId=VAR_028998. FT CONFLICT 7 7 S -> L (in Ref. 1; AAA60258/AAA16253/ FT AAA16254). {ECO:0000305}. FT CONFLICT 140 141 ML -> IF (in Ref. 1; AAA60258). FT {ECO:0000305}. FT CONFLICT 240 240 G -> V (in Ref. 1; AAA60258). FT {ECO:0000305}. FT CONFLICT 248 248 V -> C (in Ref. 1; AAA60258). FT {ECO:0000305}. FT CONFLICT 265 265 R -> M (in Ref. 1; AAA60258). FT {ECO:0000305}. FT CONFLICT 270 270 Q -> H (in Ref. 1; AAA60258). FT {ECO:0000305}. FT CONFLICT 462 462 R -> P (in Ref. 1; AAA60258). FT {ECO:0000305}. FT HELIX 33 41 {ECO:0000244|PDB:2F8X}. FT STRAND 50 57 {ECO:0000244|PDB:2F8X}. FT STRAND 72 74 {ECO:0000244|PDB:3NBN}. FT HELIX 79 88 {ECO:0000244|PDB:2F8X}. FT TURN 89 91 {ECO:0000244|PDB:3NBN}. FT TURN 94 96 {ECO:0000244|PDB:2F8X}. FT STRAND 102 105 {ECO:0000244|PDB:2F8X}. FT STRAND 118 121 {ECO:0000244|PDB:3NBN}. FT STRAND 137 139 {ECO:0000244|PDB:2F8X}. FT STRAND 141 146 {ECO:0000244|PDB:2F8X}. FT STRAND 152 157 {ECO:0000244|PDB:2F8X}. FT STRAND 161 166 {ECO:0000244|PDB:2F8X}. FT STRAND 174 176 {ECO:0000244|PDB:2F8X}. FT STRAND 178 180 {ECO:0000244|PDB:2F8X}. FT STRAND 185 191 {ECO:0000244|PDB:2F8X}. FT HELIX 193 195 {ECO:0000244|PDB:2F8X}. FT TURN 197 199 {ECO:0000244|PDB:2F8X}. FT STRAND 204 206 {ECO:0000244|PDB:2F8X}. FT STRAND 209 211 {ECO:0000244|PDB:2F8X}. FT STRAND 220 225 {ECO:0000244|PDB:2F8X}. FT STRAND 231 234 {ECO:0000244|PDB:2F8X}. FT STRAND 246 255 {ECO:0000244|PDB:2F8X}. FT STRAND 262 268 {ECO:0000244|PDB:2F8X}. FT STRAND 271 275 {ECO:0000244|PDB:2F8X}. FT STRAND 284 289 {ECO:0000244|PDB:2F8X}. FT STRAND 291 295 {ECO:0000244|PDB:2F8X}. FT STRAND 297 299 {ECO:0000244|PDB:3NBN}. FT STRAND 302 306 {ECO:0000244|PDB:2F8X}. FT STRAND 319 321 {ECO:0000244|PDB:2F8X}. FT STRAND 328 336 {ECO:0000244|PDB:2F8X}. FT STRAND 343 345 {ECO:0000244|PDB:3NBN}. FT STRAND 356 362 {ECO:0000244|PDB:2F8X}. FT HELIX 366 368 {ECO:0000244|PDB:2F8X}. FT STRAND 370 377 {ECO:0000244|PDB:2F8X}. FT STRAND 382 386 {ECO:0000244|PDB:2F8X}. FT STRAND 389 391 {ECO:0000244|PDB:2F8X}. FT STRAND 393 397 {ECO:0000244|PDB:2F8X}. FT STRAND 400 404 {ECO:0000244|PDB:2F8X}. FT HELIX 408 411 {ECO:0000244|PDB:2F8X}. FT STRAND 412 414 {ECO:0000244|PDB:2F8X}. FT STRAND 426 430 {ECO:0000244|PDB:2F8X}. FT STRAND 431 433 {ECO:0000244|PDB:3NBN}. FT STRAND 435 437 {ECO:0000244|PDB:2F8X}. SQ SEQUENCE 500 AA; 55637 MW; 91E50D2DE9087EDA CRC64; MDHTEGSPAE EPPAHAPSPG KFGERPPPKR LTREAMRNYL KERGDQTVLI LHAKVAQKSY GNEKRFFCPP PCVYLMGSGW KKKKEQMERD GCSEQESQPC AFIGIGNSDQ EMQQLNLEGK NYCTAKTLYI SDSDKRKHFM LSVKMFYGNS DDIGVFLSKR IKVISKPSKK KQSLKNADLC IASGTKVALF NRLRSQTVST RYLHVEGGNF HASSQQWGAF FIHLLDDDES EGEEFTVRDG YIHYGQTVKL VCSVTGMALP RLIIRKVDKQ TALLDADDPV SQLHKCAFYL KDTERMYLCL SQERIIQFQA TPCPKEPNKE MINDGASWTI ISTDKAEYTF YEGMGPVLAP VTPVPVVESL QLNGGGDVAM LELTGQNFTP NLRVWFGDVE AETMYRCGES MLCVVPDISA FREGWRWVRQ PVQVPVTLVR NDGIIYSTSL TFTYTPEPGP RPHCSAAGAI LRANSSQVPP NESNTNSEGS YTNASTNSTS VTSSTATVVS //