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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.
22-NOV-2017, entry version 180.
RecName: Full=Recombining binding protein suppressor of hairless;
AltName: Full=J kappa-recombination signal-binding protein;
AltName: Full=RBP-J kappa;
Name=Rbpj; 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;
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).
-!- 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. 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. 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). {ECO:0000250|UniProtKB:Q06330,
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). {ECO:0000250|UniProtKB:Q06330,
ECO:0000269|PubMed:10640276, ECO:0000269|PubMed:11318877,
ECO:0000269|PubMed:11604511, ECO:0000269|PubMed:25875095,
ECO:0000269|PubMed:7566092, ECO:0000269|PubMed:9418910}.
-!- INTERACTION:
P97447-2:Fhl1; NbExp=4; IntAct=EBI-1392666, EBI-16082627;
Q01705:Notch1; NbExp=8; IntAct=EBI-1392666, EBI-1392707;
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;
Note=No experimental confirmation available.;
-!- 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]
UniGene; Mm.209292; -.
UniGene; Mm.488709; -.
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.
PDBsum; 3BRG; -.
PDBsum; 3IAG; -.
PDBsum; 4J2X; -.
PDBsum; 5EG6; -.
ProteinModelPortal; P31266; -.
SMR; P31266; -.
BioGrid; 202832; 9.
CORUM; P31266; -.
DIP; DIP-171N; -.
ELM; P31266; -.
IntAct; P31266; 7.
STRING; 10090.ENSMUSP00000040694; -.
iPTMnet; P31266; -.
PhosphoSitePlus; P31266; -.
MaxQB; P31266; -.
PaxDb; P31266; -.
PeptideAtlas; P31266; -.
PRIDE; P31266; -.
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.
eggNOG; ENOG410XV7K; LUCA.
GeneTree; ENSGT00390000005197; -.
HOGENOM; HOG000253907; -.
HOVERGEN; HBG006618; -.
InParanoid; P31266; -.
KO; K06053; -.
OMA; DMPHFGL; -.
OrthoDB; EOG091G057S; -.
PhylomeDB; P31266; -.
TreeFam; TF314117; -.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-MMU-350054; Notch-HLH transcription pathway.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
ChiTaRS; Rbpj; mouse.
EvolutionaryTrace; P31266; -.
PRO; PR:P31266; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000039191; -.
ExpressionAtlas; P31266; baseline and differential.
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:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0047485; F:protein N-terminus binding; IPI:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter 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; IPI:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
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:Clara 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:0072602; P:interleukin-4 secretion; 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 proliferation; IMP:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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 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:0045944; P:positive regulation of transcription from RNA polymerase II promoter; 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:0061344; P:regulation of cell adhesion involved in heart morphogenesis; IC:BHF-UCL.
GO; GO:0042127; P:regulation of cell 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 from RNA polymerase II promoter; 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:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.1450; -; 1.
InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
InterPro; IPR036358; BTD_sf.
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.
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;
Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding;
Notch signaling pathway; Nucleus; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation.
CHAIN 1 526 Recombining binding protein suppressor of
hairless.
/FTId=PRO_0000208568.
DOMAIN 381 471 IPT/TIG.
DNA_BIND 84 91 {ECO:0000250}.
DNA_BIND 218 227
DNA_BIND 291 323
MOD_RES 201 201 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
VAR_SEQ 1 39 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008392.
VAR_SEQ 40 45 AHAPSA -> MAPVVT (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_008393.
HELIX 59 68 {ECO:0000244|PDB:3IAG}.
STRAND 72 83 {ECO:0000244|PDB:3IAG}.
STRAND 98 103 {ECO:0000244|PDB:3IAG}.
HELIX 105 115 {ECO:0000244|PDB:3IAG}.
HELIX 120 123 {ECO:0000244|PDB:3IAG}.
STRAND 124 133 {ECO:0000244|PDB:3IAG}.
STRAND 139 141 {ECO:0000244|PDB:3BRG}.
STRAND 146 150 {ECO:0000244|PDB:3IAG}.
STRAND 163 165 {ECO:0000244|PDB:3IAG}.
STRAND 167 173 {ECO:0000244|PDB:3IAG}.
STRAND 178 183 {ECO:0000244|PDB:3IAG}.
STRAND 187 192 {ECO:0000244|PDB:3IAG}.
HELIX 200 205 {ECO:0000244|PDB:3IAG}.
STRAND 211 217 {ECO:0000244|PDB:3IAG}.
STRAND 219 221 {ECO:0000244|PDB:3IAG}.
HELIX 223 225 {ECO:0000244|PDB:3IAG}.
STRAND 227 232 {ECO:0000244|PDB:3IAG}.
STRAND 235 241 {ECO:0000244|PDB:3IAG}.
STRAND 246 250 {ECO:0000244|PDB:3IAG}.
STRAND 257 259 {ECO:0000244|PDB:3IAG}.
STRAND 273 278 {ECO:0000244|PDB:3IAG}.
TURN 279 281 {ECO:0000244|PDB:3IAG}.
STRAND 288 294 {ECO:0000244|PDB:3IAG}.
STRAND 297 301 {ECO:0000244|PDB:3IAG}.
STRAND 311 316 {ECO:0000244|PDB:3IAG}.
STRAND 319 327 {ECO:0000244|PDB:3IAG}.
STRAND 330 335 {ECO:0000244|PDB:3IAG}.
STRAND 345 347 {ECO:0000244|PDB:3IAG}.
HELIX 350 352 {ECO:0000244|PDB:3IAG}.
STRAND 354 368 {ECO:0000244|PDB:3IAG}.
STRAND 382 388 {ECO:0000244|PDB:3IAG}.
STRAND 392 394 {ECO:0000244|PDB:3IAG}.
STRAND 396 403 {ECO:0000244|PDB:3IAG}.
STRAND 408 412 {ECO:0000244|PDB:3IAG}.
STRAND 419 423 {ECO:0000244|PDB:3IAG}.
STRAND 426 430 {ECO:0000244|PDB:3IAG}.
HELIX 434 436 {ECO:0000244|PDB:3IAG}.
STRAND 448 456 {ECO:0000244|PDB:3IAG}.
STRAND 459 470 {ECO:0000244|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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