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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)

 SUH_HUMAN               Reviewed;         500 AA.
Q06330; B4DY22; Q5XKH9; Q6P1N3;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
28-JUN-2011, sequence version 3.
25-OCT-2017, entry version 176.
RecName: Full=Recombining binding protein suppressor of hairless;
AltName: Full=CBF-1;
AltName: Full=J kappa-recombination signal-binding protein;
AltName: Full=RBP-J kappa;
Short=RBP-J;
Short=RBP-JK;
AltName: Full=Renal carcinoma antigen NY-REN-30;
Name=RBPJ; Synonyms=IGKJRB, IGKJRB1, RBPJK, RBPSUH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS APCR-1; APCR-2 AND APCR-3), AND
VARIANT VAL-456.
TISSUE=Placenta;
PubMed=8406481; DOI=10.1006/geno.1993.1326;
Amakawa R., Jing W., Ozawa K., Matsunami N., Hamaguchi Y., Matsuda F.,
Kawaichi M., Honjo T.;
"Human Jk recombination signal binding protein gene (IGKJRB):
comparison with its mouse homologue.";
Genomics 17:306-315(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
TISSUE=Eye;
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]
INTERACTION WITH EBV EBNA2.
PubMed=8016657; DOI=10.1126/science.8016657;
Henkel T., Ling P.D., Hayward S.D., Peterson M.G.;
"Mediation of Epstein-Barr virus EBNA2 transactivation by
recombination signal-binding protein J kappa.";
Science 265:92-95(1994).
[6]
INTERACTION WITH EBV EBNA3; EBV EBNA4 AND EBV EBNA6.
PubMed=8627785;
Robertson E.S., Lin J., Kieff E.;
"The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A,
3B, and 3C interact with RBPJ(kappa).";
J. Virol. 70:3068-3074(1996).
[7]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[8]
INTERACTION WITH CIR1, AND SUBCELLULAR LOCATION.
PubMed=9874765; DOI=10.1073/pnas.96.1.23;
Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.;
"CIR, a corepressor linking the DNA binding factor CBF1 to the histone
deacetylase complex.";
Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999).
[9]
INTERACTION WITH SNW1.
PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
"A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
J. Virol. 74:1939-1947(2000).
[10]
INTERACTION WITH NOTCH1.
PubMed=10637481; DOI=10.1038/sj.leu.2401630;
Callahan J., Aster J., Sklar J., Kieff E., Robertson E.S.;
"Intracellular forms of human NOTCH1 interact at distinctly different
levels with RBP-jkappa in human B and T cells.";
Leukemia 14:84-92(2000).
[11]
INTERACTION WITH MINT.
PubMed=12374742; DOI=10.1093/emboj/cdf549;
Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K.,
Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S.,
Schmid R.M.;
"SHARP is a novel component of the Notch/RBP-Jkappa signalling
pathway.";
EMBO J. 21:5417-5426(2002).
[12]
INTERACTION WITH C12ORF52, AND SUBCELLULAR LOCATION.
PubMed=21102556; DOI=10.1038/emboj.2010.289;
Wacker S.A., Alvarado C., von Wichert G., Knippschild U.,
Wiedenmann J., Clauss K., Nienhaus G.U., Hameister H., Baumann B.,
Borggrefe T., Knochel W., Oswald F.;
"RITA, a novel modulator of Notch signalling, acts via nuclear export
of RBP-J.";
EMBO J. 30:43-56(2011).
[13]
FUNCTION, AND METHYLATED DNA-BINDING.
PubMed=21991380; DOI=10.1371/journal.pone.0025884;
Bartels S.J., Spruijt C.G., Brinkman A.B., Jansen P.W., Vermeulen M.,
Stunnenberg H.G.;
"A SILAC-based screen for Methyl-CpG binding proteins identifies RBP-J
as a DNA methylation and sequence-specific binding protein.";
PLoS ONE 6:E25884-E25884(2011).
[14]
INTERACTION WITH BEND6.
PubMed=23571214; DOI=10.1242/dev.087502;
Dai Q., Andreu-Agullo C., Insolera R., Wong L.C., Shi S.H., Lai E.C.;
"BEND6 is a nuclear antagonist of Notch signaling during self-renewal
of neural stem cells.";
Development 140:1892-1902(2013).
[15]
FUNCTION IN COX4I2 TRANSCRIPTION, AND INTERACTION WITH CHCHD2 AND
CXXC5.
PubMed=23303788; DOI=10.1093/nar/gks1454;
Aras S., Pak O., Sommer N., Finley R. Jr., Huttemann M., Weissmann N.,
Grossman L.I.;
"Oxygen-dependent expression of cytochrome c oxidase subunit 4-2 gene
expression is mediated by transcription factors RBPJ, CXXC5 and
CHCHD2.";
Nucleic Acids Res. 41:2255-2266(2013).
[16]
INTERACTION WITH ZMIZ1.
PubMed=26522984; DOI=10.1016/j.immuni.2015.10.007;
Pinnell N., Yan R., Cho H.J., Keeley T., Murai M.J., Liu Y.,
Alarcon A.S., Qin J., Wang Q., Kuick R., Elenitoba-Johnson K.S.,
Maillard I., Samuelson L.C., Cierpicki T., Chiang M.Y.;
"The PIAS-like coactivator Zmiz1 is a direct and selective cofactor of
Notch1 in T cell development and leukemia.";
Immunity 43:870-883(2015).
[17]
X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA;
MAML1 AND NOTCH1.
PubMed=16530044; DOI=10.1016/j.cell.2005.12.037;
Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.;
"Structural basis for cooperativity in recruitment of MAML
coactivators to Notch transcription complexes.";
Cell 124:973-983(2006).
[18]
VARIANTS AOS3 GLY-63 AND GLU-169, AND CHARACTERIZATION OF VARIANTS
AOS3 GLY-63 AND GLU-169.
PubMed=22883147; DOI=10.1016/j.ajhg.2012.07.005;
Hassed S.J., Wiley G.B., Wang S., Lee J.Y., Li S., Xu W., Zhao Z.J.,
Mulvihill J.J., Robertson J., Warner J., Gaffney P.M.;
"RBPJ mutations identified in two families affected by Adams-Oliver
syndrome.";
Am. J. Hum. Genet. 91:391-395(2012).
-!- 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)
(PubMed:23303788). {ECO:0000269|PubMed:21991380,
ECO:0000269|PubMed:23303788}.
-!- SUBUNIT: Interacts with activated NOTCH1, NOTCH2 or 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 Epstein-Barr virus
EBNA2, EBNA3, EBNA4 and EBNA6. Interacts with RITA1/C12orf52,
leading to nuclear export, prevent the interaction between RBPJ
and NICD product and subsequent down-regulation of the Notch
signaling pathway. Interacts with SNW1. Interacts with CHCHD2 and
CXXC5 (PubMed:23303788). Interacts with BEND6 (via BEN domain).
Interacts with NKAPL (By similarity). Interacts with ZMIZ1.
{ECO:0000250|UniProtKB:P31266, ECO:0000269|PubMed:10637481,
ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:12374742,
ECO:0000269|PubMed:16530044, ECO:0000269|PubMed:21102556,
ECO:0000269|PubMed:23303788, ECO:0000269|PubMed:23571214,
ECO:0000269|PubMed:26522984, ECO:0000269|PubMed:8016657,
ECO:0000269|PubMed:8627785, ECO:0000269|PubMed:9874765}.
-!- INTERACTION:
P54253:ATXN1; NbExp=7; IntAct=EBI-632552, EBI-930964;
P0C7T5:ATXN1L; NbExp=7; IntAct=EBI-632552, EBI-8624731;
P12978:EBNA2 (xeno); NbExp=2; IntAct=EBI-632552, EBI-8052923;
P12977:EBNA3 (xeno); NbExp=4; IntAct=EBI-632552, EBI-993115;
P03203:EBNA4 (xeno); NbExp=4; IntAct=EBI-632552, EBI-9346250;
P03204:EBNA6 (xeno); NbExp=3; IntAct=EBI-632552, EBI-9255985;
Q6P3S6:FBXO42; NbExp=3; IntAct=EBI-632552, EBI-2506081;
O60341:KDM1A; NbExp=4; IntAct=EBI-632552, EBI-710124;
Q9Y618:NCOR2; NbExp=3; IntAct=EBI-632552, EBI-80830;
P46531:NOTCH1; NbExp=12; IntAct=EBI-632552, EBI-636374;
Q01705:Notch1 (xeno); NbExp=3; IntAct=EBI-632552, EBI-1392707;
Q9UPP1:PHF8; NbExp=2; IntAct=EBI-632552, EBI-1560800;
Q96K30:RITA1; NbExp=10; IntAct=EBI-632552, EBI-2836148;
P0CJ62:rita1 (xeno); NbExp=2; IntAct=EBI-632552, EBI-8517225;
P51532:SMARCA4; NbExp=2; IntAct=EBI-632552, EBI-302489;
Q13573:SNW1; NbExp=2; IntAct=EBI-632552, EBI-632715;
Q96T58:SPEN; NbExp=2; IntAct=EBI-632552, EBI-765739;
P04637:TP53; NbExp=5; IntAct=EBI-632552, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Mainly nuclear,
upon interaction with RITA/C12orf52, translocates to the
cytoplasm, down-regulating the Notch signaling pathway.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=APCR-2;
IsoId=Q06330-1; Sequence=Displayed;
Name=APCR-1;
IsoId=Q06330-2; Sequence=VSP_002717;
Name=APCR-3;
IsoId=Q06330-3; Sequence=VSP_002718, VSP_002719;
Name=4;
IsoId=Q06330-4; Sequence=VSP_021573;
Name=5;
IsoId=Q06330-5; Sequence=VSP_021572;
Name=6;
IsoId=Q06330-6; Sequence=VSP_021574;
Name=7;
IsoId=Q06330-7; Sequence=VSP_042637;
-!- DISEASE: Adams-Oliver syndrome 3 (AOS3) [MIM:614814]: An autosomal
dominant form of Adams-Oliver syndrome, a disorder characterized
by the congenital absence of skin (aplasia cutis congenita) in
combination with transverse limb defects. Aplasia cutis congenita
can be located anywhere on the body, but in the vast majority of
the cases, it is present on the posterior parietal region where it
is often associated with an underlying defect of the parietal
bones. Limb abnormalities are typically limb truncation defects
affecting the distal phalanges or entire digits (true
ectrodactyly). Only rarely, metatarsals/metacarpals or more
proximal limb structures are also affected. Apart from transverse
limb defects, syndactyly, most commonly of second and third toes,
can also be observed. The clinical features are highly variable
and can also include cardiovascular malformations, brain
abnormalities and vascular defects such as cutis marmorata and
dilated scalp veins. AOS3 patients manifest characteristic vertex
scalp defects and terminal limb defects, but without congenital
heart defects, other associated defects, or immune defects.
{ECO:0000269|PubMed:22883147}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA16254.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; L07872; AAA60258.1; -; mRNA.
EMBL; L07874; AAA16253.1; -; mRNA.
EMBL; L07875; AAA16254.1; ALT_INIT; mRNA.
EMBL; L07876; AAA16356.1; -; mRNA.
EMBL; AK302230; BAG63584.1; -; mRNA.
EMBL; AC093637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC097109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC097714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC111003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC020780; AAH20780.1; -; mRNA.
EMBL; BC053531; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC064976; AAH64976.1; -; mRNA.
CCDS; CCDS33969.1; -. [Q06330-6]
CCDS; CCDS3436.1; -. [Q06330-4]
CCDS; CCDS3437.1; -. [Q06330-1]
CCDS; CCDS43219.1; -. [Q06330-7]
PIR; A47214; A47214.
RefSeq; NP_005340.2; NM_005349.3. [Q06330-1]
RefSeq; NP_056958.3; NM_015874.4. [Q06330-7]
RefSeq; NP_976028.1; NM_203283.2. [Q06330-4]
RefSeq; NP_976029.1; NM_203284.2. [Q06330-6]
RefSeq; XP_005248218.1; XM_005248161.3. [Q06330-6]
RefSeq; XP_011512142.1; XM_011513840.2. [Q06330-6]
RefSeq; XP_016863661.1; XM_017008172.1. [Q06330-1]
RefSeq; XP_016863662.1; XM_017008173.1. [Q06330-6]
RefSeq; XP_016863663.1; XM_017008174.1. [Q06330-6]
RefSeq; XP_016863664.1; XM_017008175.1. [Q06330-6]
UniGene; Hs.479396; -.
PDB; 2F8X; X-ray; 3.25 A; C=23-449.
PDB; 3NBN; X-ray; 3.45 A; A/D=23-448.
PDB; 3V79; X-ray; 3.85 A; C=23-449.
PDBsum; 2F8X; -.
PDBsum; 3NBN; -.
PDBsum; 3V79; -.
ProteinModelPortal; Q06330; -.
SMR; Q06330; -.
BioGrid; 109736; 132.
CORUM; Q06330; -.
DIP; DIP-33326N; -.
ELM; Q06330; -.
IntAct; Q06330; 114.
MINT; MINT-1327001; -.
STRING; 9606.ENSP00000345206; -.
BindingDB; Q06330; -.
iPTMnet; Q06330; -.
PhosphoSitePlus; Q06330; -.
BioMuta; RBPJ; -.
DMDM; 338817983; -.
EPD; Q06330; -.
MaxQB; Q06330; -.
PaxDb; Q06330; -.
PeptideAtlas; Q06330; -.
PRIDE; Q06330; -.
TopDownProteomics; Q06330-3; -. [Q06330-3]
DNASU; 3516; -.
Ensembl; ENST00000342295; ENSP00000345206; ENSG00000168214. [Q06330-1]
Ensembl; ENST00000342320; ENSP00000340124; ENSG00000168214. [Q06330-6]
Ensembl; ENST00000345843; ENSP00000305815; ENSG00000168214. [Q06330-4]
Ensembl; ENST00000348160; ENSP00000339699; ENSG00000168214. [Q06330-7]
Ensembl; ENST00000355476; ENSP00000347659; ENSG00000168214. [Q06330-6]
Ensembl; ENST00000361572; ENSP00000354528; ENSG00000168214. [Q06330-1]
Ensembl; ENST00000507561; ENSP00000423907; ENSG00000168214. [Q06330-5]
GeneID; 3516; -.
KEGG; hsa:3516; -.
UCSC; uc003grx.3; human. [Q06330-1]
CTD; 3516; -.
DisGeNET; 3516; -.
EuPathDB; HostDB:ENSG00000168214.20; -.
GeneCards; RBPJ; -.
HGNC; HGNC:5724; RBPJ.
HPA; HPA060647; -.
MalaCards; RBPJ; -.
MIM; 147183; gene.
MIM; 614814; phenotype.
neXtProt; NX_Q06330; -.
OpenTargets; ENSG00000168214; -.
Orphanet; 974; Adams-Oliver syndrome.
PharmGKB; PA34292; -.
eggNOG; KOG3743; Eukaryota.
eggNOG; ENOG410XV7K; LUCA.
GeneTree; ENSGT00390000005197; -.
HOGENOM; HOG000253907; -.
HOVERGEN; HBG006618; -.
InParanoid; Q06330; -.
KO; K06053; -.
OMA; DMPHFGL; -.
OrthoDB; EOG091G057S; -.
PhylomeDB; Q06330; -.
TreeFam; TF314117; -.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2197563; NOTCH2 intracellular domain regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
SignaLink; Q06330; -.
SIGNOR; Q06330; -.
ChiTaRS; RBPJ; human.
EvolutionaryTrace; Q06330; -.
GeneWiki; RBPJ; -.
GenomeRNAi; 3516; -.
PRO; PR:Q06330; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000168214; -.
CleanEx; HS_RBPJ; -.
ExpressionAtlas; Q06330; baseline and differential.
Genevisible; Q06330; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0002193; C:MAML1-RBP-Jkappa- ICN1 complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IDA:CAFA.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0000150; F:recombinase activity; NAS:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:CAFA.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:CAFA.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IPI:BHF-UCL.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; TAS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:MGI.
GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL.
GO; GO:0060844; P:arterial endothelial cell fate commitment; IEA:Ensembl.
GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL.
GO; GO:0009912; P:auditory receptor cell fate commitment; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0097101; P:blood vessel endothelial cell fate specification; ISS:BHF-UCL.
GO; GO:0072554; P:blood vessel lumenization; ISS:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0003214; P:cardiac left ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0060486; P:Clara cell differentiation; IEA:Ensembl.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0003160; P:endocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0009957; P:epidermal cell fate specification; IEA:Ensembl.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:BHF-UCL.
GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
GO; GO:0006959; P:humoral immune response; IEA:Ensembl.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0072602; P:interleukin-4 secretion; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl.
GO; GO:0060716; P:labyrinthine layer blood vessel development; ISS:BHF-UCL.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0030279; P:negative regulation of ossification; ISS: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:UniProtKB.
GO; GO:0061314; P:Notch signaling involved in heart development; IC:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IMP:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:BHF-UCL.
GO; GO:1901297; P:positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment; IEA:Ensembl.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISS:BHF-UCL.
GO; GO:1901189; P:positive regulation of ephrin receptor signaling pathway; ISS:BHF-UCL.
GO; GO:1901186; P:positive regulation of ERBB signaling pathway; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0061419; P:positive regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:UniProtKB.
GO; GO:0048505; P:regulation of timing of cell differentiation; IEA:Ensembl.
GO; GO:0003256; P:regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation; ISS:BHF-UCL.
GO; GO:0048733; P:sebaceous gland development; IEA:Ensembl.
GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS: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; Disease mutation; DNA-binding;
Notch signaling pathway; Nucleus; Polymorphism; Reference proteome;
Repeat; Repressor; Transcription; Transcription regulation.
CHAIN 1 500 Recombining binding protein suppressor of
hairless.
/FTId=PRO_0000208567.
DOMAIN 355 445 IPT/TIG.
DNA_BIND 58 65
DNA_BIND 192 201
DNA_BIND 265 297
MOD_RES 175 175 N6-acetyllysine.
{ECO:0000250|UniProtKB:P31266}.
VAR_SEQ 1 89 Missing (in isoform APCR-3).
{ECO:0000303|PubMed:8406481}.
/FTId=VSP_002718.
VAR_SEQ 1 75 Missing (in isoform APCR-1).
{ECO:0000303|PubMed:8406481}.
/FTId=VSP_002717.
VAR_SEQ 1 35 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021572.
VAR_SEQ 1 20 MDHTEGSPAEEPPAHAPSPG -> MGGCR (in isoform
4). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_021573.
VAR_SEQ 1 20 MDHTEGSPAEEPPAHAPSPG -> MAWIKR (in
isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_021574.
VAR_SEQ 1 19 MDHTEGSPAEEPPAHAPSP -> MAPVVT (in isoform
7). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_042637.
VAR_SEQ 90 95 DGCSEQ -> MAWIKR (in isoform APCR-3).
{ECO:0000303|PubMed:8406481}.
/FTId=VSP_002719.
VARIANT 63 63 E -> G (in AOS3; shows decreased binding
to the HES1 promoter compared to wild-
type; dbSNP:rs387907270).
{ECO:0000269|PubMed:22883147}.
/FTId=VAR_068929.
VARIANT 169 169 K -> E (in AOS3; shows decreased binding
to the HES1 promoter compared to wild-
type; dbSNP:rs387907271).
{ECO:0000269|PubMed:22883147}.
/FTId=VAR_068930.
VARIANT 291 291 K -> E (in dbSNP:rs1064372).
/FTId=VAR_028994.
VARIANT 334 334 D -> H (in dbSNP:rs1064376).
/FTId=VAR_028995.
VARIANT 408 408 I -> V (in dbSNP:rs1064381).
/FTId=VAR_057244.
VARIANT 419 419 R -> Q (in dbSNP:rs1064384).
/FTId=VAR_028996.
VARIANT 425 425 P -> S (in dbSNP:rs1064387).
/FTId=VAR_028997.
VARIANT 456 456 A -> V (in dbSNP:rs1064402).
{ECO:0000269|PubMed:8406481}.
/FTId=VAR_028998.
CONFLICT 7 7 S -> L (in Ref. 1; AAA60258/AAA16253/
AAA16254). {ECO:0000305}.
CONFLICT 140 141 ML -> IF (in Ref. 1; AAA60258).
{ECO:0000305}.
CONFLICT 240 240 G -> V (in Ref. 1; AAA60258).
{ECO:0000305}.
CONFLICT 248 248 V -> C (in Ref. 1; AAA60258).
{ECO:0000305}.
CONFLICT 265 265 R -> M (in Ref. 1; AAA60258).
{ECO:0000305}.
CONFLICT 270 270 Q -> H (in Ref. 1; AAA60258).
{ECO:0000305}.
CONFLICT 462 462 R -> P (in Ref. 1; AAA60258).
{ECO:0000305}.
HELIX 33 41 {ECO:0000244|PDB:2F8X}.
STRAND 50 57 {ECO:0000244|PDB:2F8X}.
STRAND 72 74 {ECO:0000244|PDB:3NBN}.
HELIX 79 88 {ECO:0000244|PDB:2F8X}.
TURN 89 91 {ECO:0000244|PDB:3NBN}.
TURN 94 96 {ECO:0000244|PDB:2F8X}.
STRAND 102 105 {ECO:0000244|PDB:2F8X}.
STRAND 118 121 {ECO:0000244|PDB:3NBN}.
STRAND 137 139 {ECO:0000244|PDB:2F8X}.
STRAND 141 146 {ECO:0000244|PDB:2F8X}.
STRAND 152 157 {ECO:0000244|PDB:2F8X}.
STRAND 161 166 {ECO:0000244|PDB:2F8X}.
STRAND 174 176 {ECO:0000244|PDB:2F8X}.
STRAND 178 180 {ECO:0000244|PDB:2F8X}.
STRAND 185 191 {ECO:0000244|PDB:2F8X}.
HELIX 193 195 {ECO:0000244|PDB:2F8X}.
TURN 197 199 {ECO:0000244|PDB:2F8X}.
STRAND 204 206 {ECO:0000244|PDB:2F8X}.
STRAND 209 211 {ECO:0000244|PDB:2F8X}.
STRAND 220 225 {ECO:0000244|PDB:2F8X}.
STRAND 231 234 {ECO:0000244|PDB:2F8X}.
STRAND 246 255 {ECO:0000244|PDB:2F8X}.
STRAND 262 268 {ECO:0000244|PDB:2F8X}.
STRAND 271 275 {ECO:0000244|PDB:2F8X}.
STRAND 284 289 {ECO:0000244|PDB:2F8X}.
STRAND 291 295 {ECO:0000244|PDB:2F8X}.
STRAND 297 299 {ECO:0000244|PDB:3NBN}.
STRAND 302 306 {ECO:0000244|PDB:2F8X}.
STRAND 319 321 {ECO:0000244|PDB:2F8X}.
STRAND 328 336 {ECO:0000244|PDB:2F8X}.
STRAND 343 345 {ECO:0000244|PDB:3NBN}.
STRAND 356 362 {ECO:0000244|PDB:2F8X}.
HELIX 366 368 {ECO:0000244|PDB:2F8X}.
STRAND 370 377 {ECO:0000244|PDB:2F8X}.
STRAND 382 386 {ECO:0000244|PDB:2F8X}.
STRAND 389 391 {ECO:0000244|PDB:2F8X}.
STRAND 393 397 {ECO:0000244|PDB:2F8X}.
STRAND 400 404 {ECO:0000244|PDB:2F8X}.
HELIX 408 411 {ECO:0000244|PDB:2F8X}.
STRAND 412 414 {ECO:0000244|PDB:2F8X}.
STRAND 426 430 {ECO:0000244|PDB:2F8X}.
STRAND 431 433 {ECO:0000244|PDB:3NBN}.
STRAND 435 437 {ECO:0000244|PDB:2F8X}.
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


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