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Q06330 (SUH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Recombining binding protein suppressor of hairless
Alternative name(s):
CBF-1
J kappa-recombination signal-binding protein
RBP-J kappa
Short name=RBP-J
Short name=RBP-JK
Renal carcinoma antigen NY-REN-30
Gene names
Name:RBPJ
Synonyms:IGKJRB, IGKJRB1, RBPJK, RBPSUH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.13

Subunit structure

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. Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Nucleus. Cytoplasm. Note: Mainly nuclear, upon interaction with RITA/C12orf52, translocates to the cytoplasm, down-regulating the Notch signaling pathway. Ref.8 Ref.12

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15

Sequence similarities

Belongs to the Su(H) family.

Contains 1 IPT/TIG domain.

Caution

Despite some similarity with the "phage" integrase family, it has no recombinase activity.

Sequence caution

The sequence AAA16254.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processNotch signaling pathway
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   LigandDNA-binding
   Molecular functionActivator
Repressor
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell differentiation

Inferred from electronic annotation. Source: Ensembl

Clara cell differentiation

Inferred from electronic annotation. Source: Ensembl

DNA recombination

Non-traceable author statement Ref.1. Source: UniProtKB

Notch signaling involved in heart development

Inferred by curator PubMed 21311046. Source: BHF-UCL

Notch signaling pathway

Inferred from mutant phenotype PubMed 18663143. Source: BHF-UCL

angiogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

arterial endothelial cell fate commitment

Inferred from electronic annotation. Source: Ensembl

atrioventricular canal development

Inferred from sequence or structural similarity. Source: BHF-UCL

auditory receptor cell fate commitment

Inferred from electronic annotation. Source: Ensembl

blood vessel endothelial cell fate specification

Inferred from sequence or structural similarity. Source: BHF-UCL

blood vessel lumenization

Inferred from sequence or structural similarity. Source: BHF-UCL

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cardiac left ventricle morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

defense response to bacterium

Inferred from electronic annotation. Source: Ensembl

dorsal aorta morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

endocardium morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

epidermal cell fate specification

Inferred from electronic annotation. Source: Ensembl

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: BHF-UCL

epithelial to mesenchymal transition involved in endocardial cushion formation

Inferred from sequence or structural similarity. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

hair follicle maturation

Inferred from electronic annotation. Source: Ensembl

humoral immune response

Inferred from electronic annotation. Source: Ensembl

inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Ensembl

interleukin-4 secretion

Inferred from electronic annotation. Source: Ensembl

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

labyrinthine layer blood vessel development

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of ossification

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18663143. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10713164. Source: UniProtKB

outflow tract morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of BMP signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of ERBB signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cardiac muscle cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation involved in heart morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of ephrin receptor signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 18663143PubMed 20890042. Source: BHF-UCL

positive regulation of transcription of Notch receptor target

Inferred from direct assay Ref.12. Source: UniProtKB

regulation of timing of cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

sebaceous gland development

Inferred from electronic annotation. Source: Ensembl

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

ventricular trabecula myocardium morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentMAML1-RBP-Jkappa- ICN1 complex

Inferred from direct assay PubMed 16510869. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

nucleolus

Inferred from direct assay Ref.8. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.12Ref.8. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.8. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 18663143. Source: MGI

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 16287852. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 10713164PubMed 16510869Ref.14Ref.12Ref.8. Source: UniProtKB

recombinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.8. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN1P542537EBI-632552,EBI-930964
ATXN1LP0C7T57EBI-632552,EBI-8624731
EBNA2P129782EBI-632552,EBI-8052923From a different organism.
EBNA3P129773EBI-632552,EBI-993115From a different organism.
EBNA4P032034EBI-632552,EBI-9346250From a different organism.
EBNA6P032043EBI-632552,EBI-9255985From a different organism.
NCOR2Q9Y6183EBI-632552,EBI-80830
NOTCH1P465313EBI-632552,EBI-636374
Notch1Q017053EBI-632552,EBI-1392707From a different organism.
RITA1Q96K308EBI-632552,EBI-2836148
rita1P0CJ622EBI-632552,EBI-8517225From a different organism.
SNW1Q135732EBI-632552,EBI-632715

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform APCR-2 (identifier: Q06330-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform APCR-1 (identifier: Q06330-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.
Isoform APCR-3 (identifier: Q06330-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     90-95: DGCSEQ → MAWIKR
Isoform 4 (identifier: Q06330-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MDHTEGSPAEEPPAHAPSPG → MGGCR
Isoform 5 (identifier: Q06330-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.
Isoform 6 (identifier: Q06330-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MDHTEGSPAEEPPAHAPSPG → MAWIKR
Isoform 7 (identifier: Q06330-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MDHTEGSPAEEPPAHAPSP → MAPVVT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Recombining binding protein suppressor of hairless
PRO_0000208567

Regions

Domain355 – 44591IPT/TIG
DNA binding58 – 658 Ref.13
DNA binding192 – 20110 Ref.13
DNA binding265 – 29733 Ref.13

Amino acid modifications

Modified residue1751N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 8989Missing in isoform APCR-3.
VSP_002718
Alternative sequence1 – 7575Missing in isoform APCR-1.
VSP_002717
Alternative sequence1 – 3535Missing in isoform 5.
VSP_021572
Alternative sequence1 – 2020MDHTE…APSPG → MGGCR in isoform 4.
VSP_021573
Alternative sequence1 – 2020MDHTE…APSPG → MAWIKR in isoform 6.
VSP_021574
Alternative sequence1 – 1919MDHTE…HAPSP → MAPVVT in isoform 7.
VSP_042637
Alternative sequence90 – 956DGCSEQ → MAWIKR in isoform APCR-3.
VSP_002719
Natural variant631E → G in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. Ref.15
VAR_068929
Natural variant1691K → E in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. Ref.15
VAR_068930
Natural variant2911K → E.
Corresponds to variant rs1064372 [ dbSNP | Ensembl ].
VAR_028994
Natural variant2961M → K.
Corresponds to variant rs5011135 [ dbSNP | Ensembl ].
VAR_057243
Natural variant3341D → H.
Corresponds to variant rs1064376 [ dbSNP | Ensembl ].
VAR_028995
Natural variant4081I → V.
Corresponds to variant rs1064381 [ dbSNP | Ensembl ].
VAR_057244
Natural variant4191R → Q.
Corresponds to variant rs1064384 [ dbSNP | Ensembl ].
VAR_028996
Natural variant4251P → S.
Corresponds to variant rs1064387 [ dbSNP | Ensembl ].
VAR_028997
Natural variant4561A → V. Ref.1
Corresponds to variant rs1064402 [ dbSNP | Ensembl ].
VAR_028998

Experimental info

Sequence conflict71S → L in AAA60258. Ref.1
Sequence conflict71S → L in AAA16253. Ref.1
Sequence conflict71S → L in AAA16254. Ref.1
Sequence conflict140 – 1412ML → IF in AAA60258. Ref.1
Sequence conflict2401G → V in AAA60258. Ref.1
Sequence conflict2481V → C in AAA60258. Ref.1
Sequence conflict2651R → M in AAA60258. Ref.1
Sequence conflict2701Q → H in AAA60258. Ref.1
Sequence conflict4621R → P in AAA60258. Ref.1

Secondary structure

.................................................................................... 500
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform APCR-2 [UniParc].

Last modified June 28, 2011. Version 3.
Checksum: 91E50D2DE9087EDA

FASTA50055,637
        10         20         30         40         50         60 
MDHTEGSPAE EPPAHAPSPG KFGERPPPKR LTREAMRNYL KERGDQTVLI LHAKVAQKSY 

        70         80         90        100        110        120 
GNEKRFFCPP PCVYLMGSGW KKKKEQMERD GCSEQESQPC AFIGIGNSDQ EMQQLNLEGK 

       130        140        150        160        170        180 
NYCTAKTLYI SDSDKRKHFM LSVKMFYGNS DDIGVFLSKR IKVISKPSKK KQSLKNADLC 

       190        200        210        220        230        240 
IASGTKVALF NRLRSQTVST RYLHVEGGNF HASSQQWGAF FIHLLDDDES EGEEFTVRDG 

       250        260        270        280        290        300 
YIHYGQTVKL VCSVTGMALP RLIIRKVDKQ TALLDADDPV SQLHKCAFYL KDTERMYLCL 

       310        320        330        340        350        360 
SQERIIQFQA TPCPKEPNKE MINDGASWTI ISTDKAEYTF YEGMGPVLAP VTPVPVVESL 

       370        380        390        400        410        420 
QLNGGGDVAM LELTGQNFTP NLRVWFGDVE AETMYRCGES MLCVVPDISA FREGWRWVRQ 

       430        440        450        460        470        480 
PVQVPVTLVR NDGIIYSTSL TFTYTPEPGP RPHCSAAGAI LRANSSQVPP NESNTNSEGS 

       490        500 
YTNASTNSTS VTSSTATVVS 

« Hide

Isoform APCR-1 [UniParc].

Checksum: 31CC3FCBED8E739E
Show »

FASTA42547,180
Isoform APCR-3 [UniParc].

Checksum: F213446BAF8AA7BF
Show »

FASTA41145,642
Isoform 4 [UniParc].

Checksum: F0907B0A36490025
Show »

FASTA48554,146
Isoform 5 [UniParc].

Checksum: 683E1FC7CC0FACC8
Show »

FASTA46551,877
Isoform 6 [UniParc].

Checksum: 31FD3B3D01B13C4C
Show »

FASTA48654,427
Isoform 7 [UniParc].

Checksum: BF5DE1E391B0E947
Show »

FASTA48754,297

References

« Hide 'large scale' references
[1]"Human Jk recombination signal binding protein gene (IGKJRB): comparison with its mouse homologue."
Amakawa R., Jing W., Ozawa K., Matsunami N., Hamaguchi Y., Matsuda F., Kawaichi M., Honjo T.
Genomics 17:306-315(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS APCR-1; APCR-2 AND APCR-3), VARIANT VAL-456.
Tissue: Placenta.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Testis.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
Tissue: Eye.
[5]"Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein J kappa."
Henkel T., Ling P.D., Hayward S.D., Peterson M.G.
Science 265:92-95(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV EBNA2.
[6]"The amino-terminal domains of Epstein-Barr virus nuclear proteins 3A, 3B, and 3C interact with RBPJ(kappa)."
Robertson E.S., Lin J., Kieff E.
J. Virol. 70:3068-3074(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV EBNA3; EBV EBNA4 AND EBV EBNA6.
[7]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
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.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
[8]"CIR, a corepressor linking the DNA binding factor CBF1 to the histone deacetylase complex."
Hsieh J.J.-D., Zhou S., Chen L., Young D.B., Hayward S.D.
Proc. Natl. Acad. Sci. U.S.A. 96:23-28(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CIR1, SUBCELLULAR LOCATION.
[9]"A role for SKIP in EBNA2 activation of CBF1-repressed promoters."
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.
J. Virol. 74:1939-1947(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNW1.
[10]"Intracellular forms of human NOTCH1 interact at distinctly different levels with RBP-jkappa in human B and T cells."
Callahan J., Aster J., Sklar J., Kieff E., Robertson E.S.
Leukemia 14:84-92(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOTCH1.
[11]"SHARP is a novel component of the Notch/RBP-Jkappa signalling pathway."
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.
EMBO J. 21:5417-5426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MINT.
[12]"RITA, a novel modulator of Notch signalling, acts via nuclear export of RBP-J."
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.
EMBO J. 30:43-56(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH C12ORF52, SUBCELLULAR LOCATION.
[13]"A SILAC-based screen for Methyl-CpG binding proteins identifies RBP-J as a DNA methylation and sequence-specific binding protein."
Bartels S.J., Spruijt C.G., Brinkman A.B., Jansen P.W., Vermeulen M., Stunnenberg H.G.
PLoS ONE 6:E25884-E25884(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, METHYLATED DNA-BINDING.
[14]"Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes."
Nam Y., Sliz P., Song L., Aster J.C., Blacklow S.C.
Cell 124:973-983(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA; MAML1 AND NOTCH1.
[15]"RBPJ mutations identified in two families affected by Adams-Oliver syndrome."
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.
Am. J. Hum. Genet. 91:391-395(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AOS3 GLY-63 AND GLU-169, CHARACTERIZATION OF VARIANTS AOS3 GLY-63 AND GLU-169.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L07872 mRNA. Translation: AAA60258.1.
L07874 mRNA. Translation: AAA16253.1.
L07875 mRNA. Translation: AAA16254.1. Different initiation.
L07876 mRNA. Translation: AAA16356.1.
AK302230 mRNA. Translation: BAG63584.1.
AC093637 Genomic DNA. No translation available.
AC097109 Genomic DNA. No translation available.
AC097714 Genomic DNA. No translation available.
AC111003 Genomic DNA. No translation available.
BC020780 mRNA. Translation: AAH20780.1.
BC053531 mRNA. No translation available.
BC064976 mRNA. Translation: AAH64976.1.
CCDSCCDS33969.1. [Q06330-6]
CCDS3436.1. [Q06330-4]
CCDS3437.1. [Q06330-1]
CCDS43219.1. [Q06330-7]
PIRA47214.
RefSeqNP_005340.2. NM_005349.3. [Q06330-1]
NP_056958.3. NM_015874.4. [Q06330-7]
NP_976028.1. NM_203283.2. [Q06330-4]
NP_976029.1. NM_203284.2. [Q06330-6]
XP_005248218.1. XM_005248161.2. [Q06330-6]
XP_006714025.1. XM_006713962.1. [Q06330-6]
XP_006714026.1. XM_006713963.1. [Q06330-5]
UniGeneHs.479396.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2F8XX-ray3.25C23-449[»]
3NBNX-ray3.45A/D23-448[»]
3V79X-ray3.85C23-449[»]
ProteinModelPortalQ06330.
SMRQ06330. Positions 25-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109736. 35 interactions.
DIPDIP-33326N.
IntActQ06330. 25 interactions.
MINTMINT-1327001.
STRING9606.ENSP00000345206.

PTM databases

PhosphoSiteQ06330.

Polymorphism databases

DMDM338817983.

Proteomic databases

MaxQBQ06330.
PaxDbQ06330.
PRIDEQ06330.

Protocols and materials databases

DNASU3516.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342295; ENSP00000345206; ENSG00000168214. [Q06330-1]
ENST00000342320; ENSP00000340124; ENSG00000168214. [Q06330-6]
ENST00000345843; ENSP00000305815; ENSG00000168214. [Q06330-4]
ENST00000348160; ENSP00000339699; ENSG00000168214. [Q06330-7]
ENST00000355476; ENSP00000347659; ENSG00000168214. [Q06330-6]
ENST00000361572; ENSP00000354528; ENSG00000168214. [Q06330-1]
ENST00000507561; ENSP00000423907; ENSG00000168214. [Q06330-5]
GeneID3516.
KEGGhsa:3516.
UCSCuc003grx.2. human. [Q06330-1]
uc003gry.2. human. [Q06330-4]
uc003gsa.2. human. [Q06330-6]
uc003gsb.2. human. [Q06330-7]

Organism-specific databases

CTD3516.
GeneCardsGC04P026165.
HGNCHGNC:5724. RBPJ.
MIM147183. gene.
614814. phenotype.
neXtProtNX_Q06330.
Orphanet974. Adams-Oliver syndrome.
PharmGKBPA34292.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295376.
HOGENOMHOG000253907.
HOVERGENHBG006618.
InParanoidQ06330.
KOK06053.
OMAMGPVHAP.
PhylomeDBQ06330.
TreeFamTF314117.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.
SignaLinkQ06330.

Gene expression databases

ArrayExpressQ06330.
BgeeQ06330.
CleanExHS_RBPJ.
GenevestigatorQ06330.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProIPR015350. Beta-trefoil_DNA-bd_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR015351. LAG1_DNA-bd.
IPR008967. p53-like_TF_DNA-bd.
[Graphical view]
PfamPF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SUPFAMSSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRBPJ. human.
EvolutionaryTraceQ06330.
GeneWikiRBPJ.
GenomeRNAi3516.
NextBio13784.
PROQ06330.
SOURCESearch...

Entry information

Entry nameSUH_HUMAN
AccessionPrimary (citable) accession number: Q06330
Secondary accession number(s): B4DY22, Q5XKH9, Q6P1N3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 28, 2011
Last modified: July 9, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM