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 23-FEB-2022, entry version 207. 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 {ECO:0000312|HGNC:HGNC:5724}; GN Synonyms=IGKJRB, IGKJRB1, RBPJK, RBPSUH; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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): comparison RT 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 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 project: RT 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 recombination RT 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; DOI=10.1128/jvi.70.5.3068-3074.1996; RA Robertson E.S., Lin J., Kieff E.; RT "The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, RT 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-cell RT 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 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., Wiedenmann J., RA Clauss K., Nienhaus G.U., Hameister H., Baumann B., Borggrefe T., RA Knochel W., Oswald F.; RT "RITA, a novel modulator of Notch signalling, acts via nuclear export of RT 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 as a RT DNA methylation and sequence-specific binding protein."; RL PLoS ONE 6:E25884-E25884(2011). RN [14] RP INTERACTION WITH BEND6. RX PubMed=23571214; DOI=10.1242/dev.087502; RA Dai Q., Andreu-Agullo C., Insolera R., Wong L.C., Shi S.H., Lai E.C.; RT "BEND6 is a nuclear antagonist of Notch signaling during self-renewal of RT neural stem cells."; RL Development 140:1892-1902(2013). RN [15] RP FUNCTION IN COX4I2 TRANSCRIPTION, AND INTERACTION WITH CHCHD2 AND CXXC5. RX PubMed=23303788; DOI=10.1093/nar/gks1454; RA Aras S., Pak O., Sommer N., Finley R. Jr., Huttemann M., Weissmann N., RA Grossman L.I.; RT "Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene RT expression is mediated by transcription factors RBPJ, CXXC5 and CHCHD2."; RL Nucleic Acids Res. 41:2255-2266(2013). RN [16] RP INTERACTION WITH ZMIZ1. RX PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007; RA Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y., Alarcon A.S., RA Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S., Maillard I., RA Samuelson L.C., Cierpicki T., Chiang M.Y.; RT "The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of RT Notch1 in T cell development and leukemia."; RL Immunity 43:870-883(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA; MAML1 RP 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 coactivators to RT Notch transcription complexes."; RL Cell 124:973-983(2006). RN [18] RP VARIANTS AOS3 GLY-63 AND GLU-169, AND CHARACTERIZATION OF VARIANTS AOS3 RP 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 Notch CC signaling, a signaling pathway involved in cell-cell communication that CC regulates a broad spectrum of cell-fate determinations. Acts as a CC transcriptional repressor when it is not associated with Notch CC proteins. When associated with some NICD product of Notch proteins CC (Notch intracellular domain), it acts as a transcriptional activator CC that activates transcription of Notch target genes. Probably represses CC or 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 (PubMed:21991380). Binds to the oxygen responsive element of COX4I2 CC and activates its transcription under hypoxia conditions (4% oxygen) CC (PubMed:23303788). Negatively regulates the phagocyte oxidative burst CC in response to bacterial infection by repressing transcription of NADPH CC oxidase subunits (By similarity). {ECO:0000250|UniProtKB:P31266, CC ECO:0000269|PubMed:21991380, ECO:0000269|PubMed:23303788}. CC -!- SUBUNIT: Interacts with activated NOTCH1, NOTCH2 or NOTCH3. Interacts CC with MINT/SHARP. This interaction may mediate the recruitment of large CC corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2, CC SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. CC Interacts with Epstein-Barr virus EBNA2, EBNA3, EBNA4 and EBNA6. CC Interacts with RITA1/C12orf52, leading to nuclear export, prevent the CC interaction between RBPJ and NICD product and subsequent down- CC regulation of the Notch signaling pathway. Interacts with SNW1. CC Interacts with CHCHD2 and CXXC5 (PubMed:23303788). Interacts with BEND6 CC (via BEN domain). Interacts with NKAPL (By similarity). Interacts with CC ZMIZ1. Interacts with RBM15 (By similarity). CC {ECO:0000250|UniProtKB:P31266, ECO:0000269|PubMed:10637481, CC ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:12374742, CC ECO:0000269|PubMed:16530044, ECO:0000269|PubMed:21102556, CC ECO:0000269|PubMed:23303788, ECO:0000269|PubMed:23571214, CC ECO:0000269|PubMed:26522984, ECO:0000269|PubMed:8016657, CC ECO:0000269|PubMed:8627785, ECO:0000269|PubMed:9874765}. CC -!- INTERACTION: CC Q06330; P54253: ATXN1; NbExp=7; IntAct=EBI-632552, EBI-930964; CC Q06330; P0C7T5: ATXN1L; NbExp=7; IntAct=EBI-632552, EBI-8624731; CC Q06330; Q6P3S6: FBXO42; NbExp=3; IntAct=EBI-632552, EBI-2506081; CC Q06330; O60341: KDM1A; NbExp=4; IntAct=EBI-632552, EBI-710124; CC Q06330; Q9Y618: NCOR2; NbExp=3; IntAct=EBI-632552, EBI-80830; CC Q06330; P46531: NOTCH1; NbExp=12; IntAct=EBI-632552, EBI-636374; CC Q06330; Q9UPP1: PHF8; NbExp=2; IntAct=EBI-632552, EBI-1560800; CC Q06330; Q96K30: RITA1; NbExp=10; IntAct=EBI-632552, EBI-2836148; CC Q06330; P51532: SMARCA4; NbExp=2; IntAct=EBI-632552, EBI-302489; CC Q06330; Q13573: SNW1; NbExp=2; IntAct=EBI-632552, EBI-632715; CC Q06330; Q96T58: SPEN; NbExp=2; IntAct=EBI-632552, EBI-765739; CC Q06330; P04637: TP53; NbExp=5; IntAct=EBI-632552, EBI-366083; CC Q06330; P12978: EBNA2; Xeno; NbExp=2; IntAct=EBI-632552, EBI-8052923; CC Q06330; P12977: EBNA3; Xeno; NbExp=4; IntAct=EBI-632552, EBI-993115; CC Q06330; P03203: EBNA4; Xeno; NbExp=4; IntAct=EBI-632552, EBI-9346250; CC Q06330; P03204: EBNA6; Xeno; NbExp=3; IntAct=EBI-632552, EBI-9255985; CC Q06330; Q01705: Notch1; Xeno; NbExp=3; IntAct=EBI-632552, EBI-1392707; CC Q06330; P0CJ62: rita1; Xeno; NbExp=2; IntAct=EBI-632552, EBI-8517225; CC Q06330-6; P46531: NOTCH1; NbExp=6; IntAct=EBI-12599287, EBI-636374; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear, upon CC interaction with RITA/C12orf52, translocates to the cytoplasm, down- CC 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 by the CC congenital absence of skin (aplasia cutis congenita) in combination CC with transverse limb defects. Aplasia cutis congenita can be located CC anywhere on the body, but in the vast majority of the cases, it is CC present on the posterior parietal region where it is often associated CC with an underlying defect of the parietal bones. Limb abnormalities are CC typically limb truncation defects affecting the distal phalanges or CC entire digits (true ectrodactyly). Only rarely, metatarsals/metacarpals CC or more proximal limb structures are also affected. Apart from CC transverse limb defects, syndactyly, most commonly of second and third CC toes, can also be observed. The clinical features are highly variable CC and can also include cardiovascular malformations, brain abnormalities CC and vascular defects such as cutis marmorata and dilated scalp veins. CC AOS3 patients manifest characteristic vertex scalp defects and terminal CC limb defects, but without congenital heart defects, other associated CC defects, or immune defects. {ECO:0000269|PubMed:22883147}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA16254.1; 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; 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; -. [Q06330-5] DR CCDS; CCDS3437.1; -. [Q06330-1] DR CCDS; CCDS43219.1; -. [Q06330-7] DR CCDS; CCDS87214.1; -. [Q06330-5] 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_005248161.3. DR RefSeq; XP_011512142.1; XM_011513840.2. [Q06330-6] DR RefSeq; XP_016863661.1; XM_017008172.1. DR RefSeq; XP_016863662.1; XM_017008173.1. DR RefSeq; XP_016863663.1; XM_017008174.1. [Q06330-6] DR RefSeq; XP_016863664.1; XM_017008175.1. 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 PDB; 6PY8; X-ray; 3.75 A; C/E=23-466. DR PDBsum; 2F8X; -. DR PDBsum; 3NBN; -. DR PDBsum; 3V79; -. DR PDBsum; 6PY8; -. DR SMR; Q06330; -. DR BioGRID; 109736; 150. DR CORUM; Q06330; -. DR DIP; DIP-33326N; -. DR ELM; Q06330; -. DR IntAct; Q06330; 125. DR MINT; Q06330; -. DR STRING; 9606.ENSP00000345206; -. DR BindingDB; Q06330; -. DR ChEMBL; CHEMBL4105709; -. DR GlyGen; Q06330; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q06330; -. DR PhosphoSitePlus; Q06330; -. DR BioMuta; RBPJ; -. DR DMDM; 338817983; -. DR EPD; Q06330; -. DR jPOST; Q06330; -. DR MassIVE; Q06330; -. DR MaxQB; Q06330; -. DR PaxDb; Q06330; -. DR PeptideAtlas; Q06330; -. DR PRIDE; Q06330; -. DR ProteomicsDB; 58432; -. [Q06330-1] DR ProteomicsDB; 58433; -. [Q06330-2] DR ProteomicsDB; 58434; -. [Q06330-3] DR ProteomicsDB; 58435; -. [Q06330-4] DR ProteomicsDB; 58436; -. [Q06330-5] DR ProteomicsDB; 58437; -. [Q06330-6] DR ProteomicsDB; 58438; -. [Q06330-7] DR TopDownProteomics; Q06330-3; -. [Q06330-3] DR Antibodypedia; 10265; 437 antibodies from 41 providers. DR DNASU; 3516; -. DR Ensembl; ENST00000342295; ENSP00000345206; ENSG00000168214. DR Ensembl; ENST00000342320; ENSP00000340124; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000345843; ENSP00000305815; ENSG00000168214. [Q06330-5] DR Ensembl; ENST00000348160; ENSP00000339699; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000355476; ENSP00000347659; ENSG00000168214. [Q06330-7] DR Ensembl; ENST00000361572; ENSP00000354528; ENSG00000168214. DR Ensembl; ENST00000504423; ENSP00000421804; ENSG00000168214. [Q06330-5] DR Ensembl; ENST00000505958; ENSP00000426872; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000507561; ENSP00000423907; ENSG00000168214. [Q06330-5] DR Ensembl; ENST00000512671; ENSP00000423644; ENSG00000168214. DR Ensembl; ENST00000680928; ENSP00000505493; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000681093; ENSP00000504964; ENSG00000168214. [Q06330-6] DR Ensembl; ENST00000681264; ENSP00000505255; ENSG00000168214. [Q06330-5] DR Ensembl; ENST00000681484; ENSP00000505636; ENSG00000168214. [Q06330-5] DR GeneID; 3516; -. DR KEGG; hsa:3516; -. DR MANE-Select; ENST00000355476.8; ENSP00000347659.4; NM_015874.6; NP_056958.3. [Q06330-7] DR UCSC; uc003grx.3; human. [Q06330-1] DR CTD; 3516; -. DR DisGeNET; 3516; -. DR GeneCards; RBPJ; -. DR GeneReviews; RBPJ; -. DR HGNC; HGNC:5724; RBPJ. DR HPA; ENSG00000168214; Low tissue specificity. DR MalaCards; RBPJ; -. DR MIM; 147183; gene. DR MIM; 614814; phenotype. DR neXtProt; NX_Q06330; -. DR OpenTargets; ENSG00000168214; -. DR Orphanet; 974; Adams-Oliver syndrome. DR PharmGKB; PA34292; -. DR VEuPathDB; HostDB:ENSG00000168214; -. DR eggNOG; KOG3743; Eukaryota. DR GeneTree; ENSGT00390000005197; -. DR HOGENOM; CLU_022207_2_1_1; -. DR InParanoid; Q06330; -. DR OMA; ISEVQWN; -. DR OrthoDB; 444988at2759; -. DR PhylomeDB; Q06330; -. DR TreeFam; TF314117; -. DR PathwayCommons; Q06330; -. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-350054; Notch-HLH transcription pathway. DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling. DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription. DR SignaLink; Q06330; -. DR SIGNOR; Q06330; -. DR BioGRID-ORCS; 3516; 23 hits in 1051 CRISPR screens. DR ChiTaRS; RBPJ; human. DR EvolutionaryTrace; Q06330; -. DR GeneWiki; RBPJ; -. DR GenomeRNAi; 3516; -. DR Pharos; Q06330; Tbio. DR PRO; PR:Q06330; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q06330; protein. DR Bgee; ENSG00000168214; Expressed in corpus callosum and 255 other tissues. DR ExpressionAtlas; Q06330; baseline and differential. DR Genevisible; Q06330; HS. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. 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; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IDA:CAFA. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IDA:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:CAFA. DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL. DR GO; GO:0003176; P:aortic valve development; IEA:Ensembl. 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:club cell differentiation; IEA:Ensembl. DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl. 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: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:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0060716; P:labyrinthine layer blood vessel development; ISS:BHF-UCL. DR GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl. DR GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0030279; P:negative regulation of ossification; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; 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:0010628; P:positive regulation of gene expression; ISS:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB. DR GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:UniProtKB. DR GO; GO:0003177; P:pulmonary valve development; IEA:Ensembl. 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 population maintenance; IEA:Ensembl. DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl. DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl. DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL. DR CDD; cd01176; IPT_RBP-Jkappa; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 2.60.40.1450; -; 1. DR IDEAL; IID00380; -. 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. 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; PTHR10665; 2. 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; 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; Cytoplasm; KW Disease variant; DNA-binding; Notch signaling pathway; Nucleus; KW Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1..500 FT /note="Recombining binding protein suppressor of hairless" FT /id="PRO_0000208567" FT DOMAIN 355..445 FT /note="IPT/TIG" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 57..67 FT /note="DNA binding" FT /evidence="ECO:0000269|PubMed:16530044" FT REGION 165..170 FT /note="DNA binding" FT /evidence="ECO:0000269|PubMed:16530044" FT REGION 192..197 FT /note="DNA binding" FT /evidence="ECO:0000269|PubMed:16530044" FT REGION 465..500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 175 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P31266" FT VAR_SEQ 1..89 FT /note="Missing (in isoform APCR-3)" FT /evidence="ECO:0000303|PubMed:8406481" FT /id="VSP_002718" FT VAR_SEQ 1..75 FT /note="Missing (in isoform APCR-1)" FT /evidence="ECO:0000303|PubMed:8406481" FT /id="VSP_002717" FT VAR_SEQ 1..35 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021572" FT VAR_SEQ 1..20 FT /note="MDHTEGSPAEEPPAHAPSPG -> MGGCR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021573" FT VAR_SEQ 1..20 FT /note="MDHTEGSPAEEPPAHAPSPG -> MAWIKR (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_021574" FT VAR_SEQ 1..19 FT /note="MDHTEGSPAEEPPAHAPSP -> MAPVVT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042637" FT VAR_SEQ 90..95 FT /note="DGCSEQ -> MAWIKR (in isoform APCR-3)" FT /evidence="ECO:0000303|PubMed:8406481" FT /id="VSP_002719" FT VARIANT 63 FT /note="E -> G (in AOS3; shows decreased binding to the HES1 FT promoter compared to wild-type; dbSNP:rs387907270)" FT /evidence="ECO:0000269|PubMed:22883147" FT /id="VAR_068929" FT VARIANT 169 FT /note="K -> E (in AOS3; shows decreased binding to the HES1 FT promoter compared to wild-type; dbSNP:rs387907271)" FT /evidence="ECO:0000269|PubMed:22883147" FT /id="VAR_068930" FT VARIANT 291 FT /note="K -> E (in dbSNP:rs1064372)" FT /id="VAR_028994" FT VARIANT 334 FT /note="D -> H (in dbSNP:rs1064376)" FT /id="VAR_028995" FT VARIANT 408 FT /note="I -> V (in dbSNP:rs1064381)" FT /id="VAR_057244" FT VARIANT 419 FT /note="R -> Q (in dbSNP:rs1064384)" FT /id="VAR_028996" FT VARIANT 425 FT /note="P -> S (in dbSNP:rs1064387)" FT /id="VAR_028997" FT VARIANT 456 FT /note="A -> V (in dbSNP:rs1064402)" FT /evidence="ECO:0000269|PubMed:8406481" FT /id="VAR_028998" FT CONFLICT 7 FT /note="S -> L (in Ref. 1; AAA60258/AAA16253/AAA16254)" FT /evidence="ECO:0000305" FT CONFLICT 140..141 FT /note="ML -> IF (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT CONFLICT 240 FT /note="G -> V (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="V -> C (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT CONFLICT 265 FT /note="R -> M (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="Q -> H (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT CONFLICT 462 FT /note="R -> P (in Ref. 1; AAA60258)" FT /evidence="ECO:0000305" FT HELIX 33..41 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 50..57 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:3NBN" FT HELIX 79..88 FT /evidence="ECO:0007829|PDB:2F8X" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:3NBN" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:3NBN" FT STRAND 137..139 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 178..180 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:2F8X" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:2F8X" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 231..234 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 246..255 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 262..268 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 271..275 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 284..289 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 291..295 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:3NBN" FT STRAND 302..306 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 328..336 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 343..345 FT /evidence="ECO:0007829|PDB:3NBN" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:2F8X" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 370..377 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 382..386 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 389..391 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 393..397 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 400..404 FT /evidence="ECO:0007829|PDB:2F8X" FT HELIX 408..411 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 426..430 FT /evidence="ECO:0007829|PDB:2F8X" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:3NBN" FT STRAND 435..437 FT /evidence="ECO:0007829|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 //