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Recombining binding protein suppressor of hairless (J kappa-recombination signal-binding protein) (RBP-J kappa)

 SUH_MOUSE               Reviewed;         526 AA.
P31266; Q80UN8; Q8C4Z3;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
07-APR-2021, entry version 207.
RecName: Full=Recombining binding protein suppressor of hairless;
AltName: Full=J kappa-recombination signal-binding protein;
AltName: Full=RBP-J kappa;
Name=Rbpj {ECO:0000312|MGI:MGI:96522}; Synonyms=Igkjrb1, Igkrsbp, Rbpsuh;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2556644; DOI=10.1038/342934a0;
Matsunami N., Hamaguchi Y., Yamamoto Y., Kuze K., Kangawa K., Matsuo H.,
Kawaichi M., Honjo T.;
"A protein binding to the J kappa recombination sequence of immunoglobulin
genes contains a sequence related to the integrase motif.";
Nature 342:934-937(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1740450;
Kawaichi M., Oka C., Shibayama S., Koromilas A.E., Matsunami N.,
Hamaguchi Y., Honjo T.;
"Genomic organization of mouse J kappa recombination signal binding protein
(RBP-J kappa) gene.";
J. Biol. Chem. 267:4016-4022(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1950768; DOI=10.1007/978-1-4684-5943-2_20;
Hamaguchi Y., Matsunami N., Yamamoto Y., Kuze K., Kangawa K., Matsuo H.,
Kawaichi M., Honjo T.;
"Cloning and characterization of a protein binding to the J kappa
recombination signal sequence of immunoglobulin genes.";
Adv. Exp. Med. Biol. 292:177-186(1991).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
FUNCTION, AND INTERACTION WITH NOTCH1.
PubMed=7566092; DOI=10.1038/377355a0;
Jarriault S., Brou C., Logeat F., Schroeter E.H., Kopan R., Israel A.;
"Signalling downstream of activated mammalian Notch.";
Nature 377:355-358(1995).
[7]
INTERACTION WITH FHL1.
PubMed=9418910; DOI=10.1128/mcb.18.1.644;
Taniguchi Y., Furukawa T., Tun T., Han H., Honjo T.;
"LIM protein KyoT2 negatively regulates transcription by association with
the RBP-J DNA-binding protein.";
Mol. Cell. Biol. 18:644-654(1998).
[8]
INTERACTION WITH EP300.
PubMed=11604511; DOI=10.1128/mcb.21.22.7761-7774.2001;
Oswald F., Taeuber B., Dobner T., Bourteele S., Kostezka U., Adler G.,
Liptay S., Schmid R.M.;
"p300 acts as a transcriptional coactivator for mammalian Notch-1.";
Mol. Cell. Biol. 21:7761-7774(2001).
[9]
INTERACTION WITH PTF1A.
STRAIN=ICR; TISSUE=Embryo;
PubMed=11318877; DOI=10.1046/j.1365-2443.2001.00422.x;
Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C.,
Kawaichi M.;
"p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular
mediator of Notch signalling, and is expressed in the neural tube of early
stage embryos.";
Genes Cells 6:345-360(2001).
[10]
IDENTIFICATION IN A COMPLEX WITH NCOR2 AND HDAC1.
PubMed=10640276;
Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
"Isolation of a novel histone deacetylase reveals that class I and class II
deacetylases promote SMRT-mediated repression.";
Genes Dev. 14:55-66(2000).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-201, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
INTERACTION WITH NKAPL.
PubMed=25875095; DOI=10.1371/journal.pone.0124293;
Okuda H., Kiuchi H., Takao T., Miyagawa Y., Tsujimura A., Nonomura N.,
Miyata H., Okabe M., Ikawa M., Kawakami Y., Goshima N., Wada M., Tanaka H.;
"A novel transcriptional factor Nkapl is a germ cell-specific suppressor of
Notch signaling and is indispensable for spermatogenesis.";
PLoS ONE 10:E0124293-E0124293(2015).
[13]
FUNCTION.
PubMed=26194095; DOI=10.1038/ncomms8838;
Graham D.B., Becker C.E., Doan A., Goel G., Villablanca E.J., Knights D.,
Mok A., Ng A.C., Doench J.G., Root D.E., Clish C.B., Xavier R.J.;
"Functional genomics identifies negative regulatory nodes controlling
phagocyte oxidative burst.";
Nat. Commun. 6:7838-7838(2015).
[14]
INTERACTION WITH RBM15.
PubMed=17283045; DOI=10.1128/mcb.01339-06;
Ma X., Renda M.J., Wang L., Cheng E.C., Niu C., Morris S.W., Chi A.S.,
Krause D.S.;
"Rbm15 modulates Notch-induced transcriptional activation and affects
myeloid differentiation.";
Mol. Cell. Biol. 27:3056-3064(2007).
[15] {ECO:0007744|PDB:3BRG}
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 53-474 IN COMPLEX WITH DNA, AND
FUNCTION.
PubMed=18381292; DOI=10.1074/jbc.M709501200;
Friedmann D.R., Wilson J.J., Kovall R.A.;
"RAM-induced allostery facilitates assembly of a notch pathway active
transcription complex.";
J. Biol. Chem. 283:14781-14791(2008).
-!- FUNCTION: Transcriptional regulator that plays a central role in Notch
signaling, a signaling pathway involved in cell-cell communication that
regulates a broad spectrum of cell-fate determinations
(PubMed:7566092). Acts as a transcriptional repressor when it is not
associated with Notch proteins. When associated with some NICD product
of Notch proteins (Notch intracellular domain), it acts as a
transcriptional activator that activates transcription of Notch target
genes (By similarity) (PubMed:18381292). Probably represses or
activates transcription via the recruitment of chromatin remodeling
complexes containing histone deacetylase or histone acetylase proteins,
respectively. Specifically binds to the immunoglobulin kappa-type J
segment recombination signal sequence. Binds specifically to methylated
DNA. Binds to the oxygen responsive element of COX4I2 and activates its
transcription under hypoxia conditions (4% oxygen) (By similarity).
Negatively regulates the phagocyte oxidative burst in response to
bacterial infection by repressing transcription of NADPH oxidase
subunits (PubMed:26194095). {ECO:0000250|UniProtKB:P28159,
ECO:0000250|UniProtKB:Q06330, ECO:0000269|PubMed:18381292,
ECO:0000269|PubMed:26194095, ECO:0000269|PubMed:7566092}.
-!- SUBUNIT: Interacts with RITA1, leading to nuclear export, prevent the
interaction between RBPJ and NICD product and subsequent down-
regulation of the Notch signaling pathway (By similarity). Interacts
with activated NOTCH1, NOTCH2 and NOTCH3. Interacts with MINT/SHARP.
This interaction may mediate the recruitment of large corepressor
complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30,
FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. Interacts
with SNW1. Interacts with CHCHD2 and CXXC5. Interacts with BEND6 (via
BEN domain) (By similarity). Interacts with NKAPL (PubMed:25875095).
Interacts with ZMIZ1 (By similarity). Interacts with RBM15
(PubMed:17283045). {ECO:0000250|UniProtKB:Q06330,
ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11318877,
ECO:0000269|PubMed:11604511, ECO:0000269|PubMed:17283045,
ECO:0000269|PubMed:25875095, ECO:0000269|PubMed:7566092,
ECO:0000269|PubMed:9418910}.
-!- INTERACTION:
P31266; P97447-2: Fhl1; NbExp=4; IntAct=EBI-1392666, EBI-16082627;
P31266; Q01705: Notch1; NbExp=8; IntAct=EBI-1392666, EBI-1392707;
P31266; Q6P9Z1: Smarcd3; NbExp=3; IntAct=EBI-1392666, EBI-7525857;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Mainly
nuclear, upon interaction with RITA1, translocates to the cytoplasm,
down-regulating the Notch signaling pathway. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31266-1; Sequence=Displayed;
Name=2;
IsoId=P31266-2; Sequence=VSP_008392, VSP_008393;
-!- SIMILARITY: Belongs to the Su(H) family. {ECO:0000305}.
-!- CAUTION: Despite some similarity with the 'phage' integrase family, it
has no recombinase activity. {ECO:0000305}.
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EMBL; S63463; AAB20195.1; -; mRNA.
EMBL; X17459; CAA35501.1; -; mRNA.
EMBL; X58337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M81867; AAA39018.1; -; Genomic_DNA.
EMBL; M81865; AAA39018.1; JOINED; Genomic_DNA.
EMBL; M81866; AAA39018.1; JOINED; Genomic_DNA.
EMBL; M81868; AAA39019.1; -; Genomic_DNA.
EMBL; M81870; AAA39020.1; ALT_SEQ; Genomic_DNA.
EMBL; M81869; AAA39020.1; JOINED; Genomic_DNA.
EMBL; M81873; AAA39021.1; -; Genomic_DNA.
EMBL; M81872; AAA39021.1; JOINED; Genomic_DNA.
EMBL; M81875; AAA39022.1; -; Genomic_DNA.
EMBL; M81874; AAA39022.1; JOINED; Genomic_DNA.
EMBL; M81876; AAA39023.1; -; Genomic_DNA.
EMBL; M81877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051387; AAH51387.1; -; mRNA.
EMBL; AK080359; BAC37889.1; -; mRNA.
CCDS; CCDS19292.1; -. [P31266-1]
CCDS; CCDS51504.1; -. [P31266-2]
PIR; A42267; A42267.
PIR; A43567; A43567.
RefSeq; NP_001074396.1; NM_001080927.2. [P31266-2]
RefSeq; NP_033061.3; NM_009035.5. [P31266-1]
PDB; 3BRG; X-ray; 2.20 A; C=53-474.
PDB; 3IAG; X-ray; 2.00 A; C=53-474.
PDB; 4J2X; X-ray; 2.85 A; A/C=53-474.
PDB; 5EG6; X-ray; 2.09 A; C=53-474.
PDB; 6DKS; X-ray; 2.78 A; C/G=53-474.
PDBsum; 3BRG; -.
PDBsum; 3IAG; -.
PDBsum; 4J2X; -.
PDBsum; 5EG6; -.
PDBsum; 6DKS; -.
SMR; P31266; -.
BioGRID; 202832; 13.
CORUM; P31266; -.
DIP; DIP-171N; -.
ELM; P31266; -.
IntAct; P31266; 7.
MINT; P31266; -.
STRING; 10090.ENSMUSP00000040694; -.
iPTMnet; P31266; -.
PhosphoSitePlus; P31266; -.
SwissPalm; P31266; -.
EPD; P31266; -.
MaxQB; P31266; -.
PaxDb; P31266; -.
PeptideAtlas; P31266; -.
PRIDE; P31266; -.
ProteomicsDB; 254496; -. [P31266-1]
ProteomicsDB; 254497; -. [P31266-2]
Antibodypedia; 10265; 360 antibodies.
Ensembl; ENSMUST00000037618; ENSMUSP00000040694; ENSMUSG00000039191. [P31266-1]
Ensembl; ENSMUST00000113865; ENSMUSP00000109496; ENSMUSG00000039191. [P31266-2]
GeneID; 19664; -.
KEGG; mmu:19664; -.
UCSC; uc008xli.2; mouse. [P31266-1]
CTD; 3516; -.
MGI; MGI:96522; Rbpj.
eggNOG; KOG3743; Eukaryota.
GeneTree; ENSGT00390000005197; -.
InParanoid; P31266; -.
OrthoDB; 444988at2759; -.
PhylomeDB; P31266; -.
TreeFam; TF314117; -.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-350054; Notch-HLH transcription pathway.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
BioGRID-ORCS; 19664; 6 hits in 50 CRISPR screens.
ChiTaRS; Rbpj; mouse.
EvolutionaryTrace; P31266; -.
PRO; PR:P31266; -.
Proteomes; UP000000589; Chromosome 5.
RNAct; P31266; protein.
Bgee; ENSMUSG00000039191; Expressed in ureter smooth muscle and 307 other tissues.
Genevisible; P31266; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0003176; P:aortic valve development; IMP:BHF-UCL.
GO; GO:0060844; P:arterial endothelial cell fate commitment; IMP:BHF-UCL.
GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
GO; GO:0036302; P:atrioventricular canal development; IMP:BHF-UCL.
GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:MGI.
GO; GO:0030183; P:B cell differentiation; IMP:MGI.
GO; GO:0097101; P:blood vessel endothelial cell fate specification; IGI:BHF-UCL.
GO; GO:0072554; P:blood vessel lumenization; IMP:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0060486; P:club cell differentiation; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0061371; P:determination of heart left/right asymmetry; TAS:BHF-UCL.
GO; GO:0035912; P:dorsal aorta morphogenesis; IMP:BHF-UCL.
GO; GO:0003157; P:endocardium development; IMP:BHF-UCL.
GO; GO:0003160; P:endocardium morphogenesis; IMP:BHF-UCL.
GO; GO:0009957; P:epidermal cell fate specification; IMP:MGI.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; IMP:BHF-UCL.
GO; GO:0048820; P:hair follicle maturation; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001947; P:heart looping; TAS:BHF-UCL.
GO; GO:0030097; P:hemopoiesis; IMP:MGI.
GO; GO:0006959; P:humoral immune response; IMP:MGI.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:BHF-UCL.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
GO; GO:0034392; P:negative regulation of smooth muscle cell apoptotic process; ISO:MGI.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
GO; GO:0060853; P:Notch signaling pathway involved in arterial endothelial cell fate commitment; IC:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
GO; GO:0021983; P:pituitary gland development; IMP:MGI.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:BHF-UCL.
GO; GO:1901297; P:positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; IMP:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; IMP:BHF-UCL.
GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:1901186; P:positive regulation of ERBB signaling pathway; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
GO; GO:0035481; P:positive regulation of Notch signaling pathway involved in heart induction; TAS:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0003177; P:pulmonary valve development; IMP:BHF-UCL.
GO; GO:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IC:BHF-UCL.
GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0048505; P:regulation of timing of cell differentiation; IMP:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; IMP:BHF-UCL.
GO; GO:0048733; P:sebaceous gland development; IMP:MGI.
GO; GO:0003139; P:secondary heart field specification; IMP:MGI.
GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
CDD; cd01176; IPT_RBP-Jkappa; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.1450; -; 1.
InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
InterPro; IPR036358; BTD_sf.
InterPro; IPR040159; CLS_fam.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
InterPro; IPR037095; RBP-J/Cbf11/Cbf12_DNA-bd_sf.
InterPro; IPR038007; RBP-Jkappa_IPT.
PANTHER; PTHR10665; PTHR10665; 2.
Pfam; PF09270; BTD; 1.
Pfam; PF09271; LAG1-DNAbind; 1.
SMART; SM01268; BTD; 1.
SMART; SM01267; LAG1_DNAbind; 1.
SUPFAM; SSF110217; SSF110217; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
Direct protein sequencing; DNA-binding; Notch signaling pathway; Nucleus;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation.
CHAIN 1..526
/note="Recombining binding protein suppressor of hairless"
/id="PRO_0000208568"
DOMAIN 381..471
/note="IPT/TIG"
REGION 83..93
/note="DNA binding"
/evidence="ECO:0000269|PubMed:18381292"
REGION 191..196
/note="DNA binding"
/evidence="ECO:0000269|PubMed:18381292"
REGION 218..223
/note="DNA binding"
/evidence="ECO:0000269|PubMed:18381292"
MOD_RES 201
/note="N6-acetyllysine"
/evidence="ECO:0007744|PubMed:23806337"
VAR_SEQ 1..39
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_008392"
VAR_SEQ 40..45
/note="AHAPSA -> MAPVVT (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_008393"
HELIX 59..68
/evidence="ECO:0007744|PDB:3IAG"
STRAND 72..83
/evidence="ECO:0007744|PDB:3IAG"
STRAND 98..103
/evidence="ECO:0007744|PDB:3IAG"
HELIX 105..115
/evidence="ECO:0007744|PDB:3IAG"
HELIX 120..123
/evidence="ECO:0007744|PDB:3IAG"
STRAND 124..133
/evidence="ECO:0007744|PDB:3IAG"
STRAND 134..136
/evidence="ECO:0007744|PDB:6DKS"
STRAND 139..141
/evidence="ECO:0007744|PDB:5EG6"
STRAND 146..150
/evidence="ECO:0007744|PDB:3IAG"
STRAND 163..165
/evidence="ECO:0007744|PDB:3IAG"
STRAND 167..173
/evidence="ECO:0007744|PDB:3IAG"
STRAND 178..183
/evidence="ECO:0007744|PDB:3IAG"
STRAND 187..192
/evidence="ECO:0007744|PDB:3IAG"
HELIX 200..205
/evidence="ECO:0007744|PDB:3IAG"
STRAND 211..217
/evidence="ECO:0007744|PDB:3IAG"
STRAND 219..221
/evidence="ECO:0007744|PDB:3IAG"
HELIX 223..225
/evidence="ECO:0007744|PDB:3IAG"
STRAND 227..232
/evidence="ECO:0007744|PDB:3IAG"
STRAND 235..241
/evidence="ECO:0007744|PDB:3IAG"
STRAND 246..250
/evidence="ECO:0007744|PDB:3IAG"
STRAND 257..259
/evidence="ECO:0007744|PDB:3IAG"
STRAND 273..278
/evidence="ECO:0007744|PDB:3IAG"
TURN 279..281
/evidence="ECO:0007744|PDB:3IAG"
STRAND 288..294
/evidence="ECO:0007744|PDB:3IAG"
STRAND 297..301
/evidence="ECO:0007744|PDB:3IAG"
STRAND 311..316
/evidence="ECO:0007744|PDB:3IAG"
STRAND 319..327
/evidence="ECO:0007744|PDB:3IAG"
STRAND 330..335
/evidence="ECO:0007744|PDB:3IAG"
STRAND 345..347
/evidence="ECO:0007744|PDB:3IAG"
HELIX 350..352
/evidence="ECO:0007744|PDB:3IAG"
STRAND 354..368
/evidence="ECO:0007744|PDB:3IAG"
STRAND 382..388
/evidence="ECO:0007744|PDB:3IAG"
STRAND 392..394
/evidence="ECO:0007744|PDB:3IAG"
STRAND 396..403
/evidence="ECO:0007744|PDB:3IAG"
STRAND 408..412
/evidence="ECO:0007744|PDB:3IAG"
STRAND 419..423
/evidence="ECO:0007744|PDB:3IAG"
STRAND 426..430
/evidence="ECO:0007744|PDB:3IAG"
HELIX 434..436
/evidence="ECO:0007744|PDB:3IAG"
STRAND 439..441
/evidence="ECO:0007744|PDB:6DKS"
STRAND 448..456
/evidence="ECO:0007744|PDB:3IAG"
STRAND 459..470
/evidence="ECO:0007744|PDB:3IAG"
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


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WP1663: Homologous recombination
WP1625: Base excision repair
WP1939: Unfolded Protein Response
WP1690: Propanoate metabolism
WP262: EBV LMP1 signaling
WP1371: G Protein Signaling Pathways
WP1694: Pyrimidine metabolism
WP1102: EBV LMP1 signaling
WP1654: gamma-Hexachlorocyclohexane degradation
WP984: EBV LMP1 signaling
WP1661: Glyoxylate and dicarboxylate metabolism
WP2152: BDNF
WP1493: Carbon assimilation C4 pathway
WP1714: Tyrosine metabolism
WP590: Cardiovascular Signaling
WP1672: Mismatch repair
WP2218: sGC
WP1243: EBV LMP1 signaling
WP1676: Non-homologous end-joining
WP232: G Protein Signaling Pathways

Related Genes :
[Rbpj Igkjrb1 Igkrsbp Rbpsuh] Recombining binding protein suppressor of hairless (J kappa-recombination signal-binding protein) (RBP-J kappa)
[RBPJ IGKJRB IGKJRB1 RBPJK RBPSUH] Recombining binding protein suppressor of hairless (CBF-1) (J kappa-recombination signal-binding protein) (RBP-J kappa) (RBP-J) (RBP-JK) (Renal carcinoma antigen NY-REN-30)
[Hivep3 KBP1 Kiaa1555 Krc Rc shn3 Zas3] Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3 homolog) (KB-binding and recognition component) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Recombinant component) (Schnurri-3) (Zinc finger protein ZAS3)
[RBPJ RBPSUH] Recombining binding protein suppressor of hairless (J kappa-recombination signal-binding protein) (RBP-J kappa)
[HIVEP3 KBP1 KIAA1555 KRC ZAS3] Transcription factor HIVEP3 (Human immunodeficiency virus type I enhancer-binding protein 3) (Kappa-B and V(D)J recombination signal sequences-binding protein) (Kappa-binding protein 1) (KBP-1) (Zinc finger protein ZAS3)
[RBPJ RBPSUH] Recombining binding protein suppressor of hairless (J kappa-recombination signal-binding protein) (RBP-J kappa)
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (NF-kappa-B1 p84/NF-kappa-B1 p98) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[NFKB2 LYT10] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (H2TF1) (Lymphocyte translocation chromosome 10 protein) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) (Oncogene Lyt-10) (Lyt10) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[Tnip2 Abin2] TNFAIP3-interacting protein 2 (A20-binding inhibitor of NF-kappa-B activation 2) (ABIN-2)
[NFKB1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit]
[Chuk Ikka] Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (IkappaB kinase) (EC 2.7.11.10) (Conserved helix-loop-helix ubiquitous kinase) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)
[Ikbkb Ikkb] Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB) (Serine/threonine protein kinase IKBKB) (EC 2.7.11.1)
[Ikbkg Nemo] NF-kappa-B essential modulator (NEMO) (IkB kinase-associated protein 1) (IKKAP1) (mFIP-3) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[Ikbke Ikke Ikki] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)
[Nfkbia Ikba] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha)
[Rela Nfkb3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[Nfkbid Ikbns] NF-kappa-B inhibitor delta (I-kappa-B-delta) (IkB-delta) (IkappaBdelta) (IkappaBNS)
[TBK1 NAK] Serine/threonine-protein kinase TBK1 (EC 2.7.11.1) (NF-kappa-B-activating kinase) (T2K) (TANK-binding kinase 1)
[TAB3 MAP3K7IP3] TGF-beta-activated kinase 1 and MAP3K7-binding protein 3 (Mitogen-activated protein kinase kinase kinase 7-interacting protein 3) (NF-kappa-B-activating protein 1) (TAK1-binding protein 3) (TAB-3) (TGF-beta-activated kinase 1-binding protein 3)
[IKBKG FIP3 NEMO] NF-kappa-B essential modulator (NEMO) (FIP-3) (IkB kinase-associated protein 1) (IKKAP1) (Inhibitor of nuclear factor kappa-B kinase subunit gamma) (I-kappa-B kinase subunit gamma) (IKK-gamma) (IKKG) (IkB kinase subunit gamma) (NF-kappa-B essential modifier)
[NFKBIA IKBA MAD3 NFKBI] NF-kappa-B inhibitor alpha (I-kappa-B-alpha) (IkB-alpha) (IkappaBalpha) (Major histocompatibility complex enhancer-binding protein MAD3)
[Nfkb1] Nuclear factor NF-kappa-B p105 subunit (DNA-binding factor KBF1) (EBP-1) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1) [Cleaved into: Nuclear factor NF-kappa-B p50 subunit] (Fragment)
[Nfkb2] Nuclear factor NF-kappa-B p100 subunit (DNA-binding factor KBF2) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2) [Cleaved into: Nuclear factor NF-kappa-B p52 subunit]
[Azi2 Az2 Nap1 Tbkp2] 5-azacytidine-induced protein 2 (NF-kappa-B-activating kinase-associated protein 1) (Nak-associated protein 1)
[TCF3 BHLHB21 E2A ITF1] Transcription factor E2-alpha (Class B basic helix-loop-helix protein 21) (bHLHb21) (Immunoglobulin enhancer-binding factor E12/E47) (Immunoglobulin transcription factor 1) (Kappa-E2-binding factor) (Transcription factor 3) (TCF-3) (Transcription factor ITF-1)
[Oprl1 Oor Oprl] Nociceptin receptor (K3 opiate receptor) (Kappa-type 3 opioid receptor) (KOR-3) (ORGC) (Orphanin FQ receptor)
[RELA NFKB3] Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)
[POLK At1g49980 F2J10.13] DNA polymerase kappa (AtPOLK) (EC 2.7.7.7)
[Cdkn2a] Tumor suppressor ARF (Alternative reading frame) (ARF) (Cyclin-dependent kinase inhibitor 2A) (p19ARF)
[IKBKE IKKE IKKI KIAA0151] Inhibitor of nuclear factor kappa-B kinase subunit epsilon (I-kappa-B kinase epsilon) (IKK-E) (IKK-epsilon) (IkBKE) (EC 2.7.11.10) (Inducible I kappa-B kinase) (IKK-i)

Bibliography :