Q06330 (SUH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Protein existence	Evidence 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 RITA/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 process	Notch signaling pathway Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Notch signaling involved in heart development Inferred by curator PubMed 21311046. Source: BHF-UCL angiogenesis Inferred from sequence or structural similarity. Source: BHF-UCL atrioventricular canal development Inferred from sequence or structural similarity. Source: BHF-UCL 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 cardiac left ventricle morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL dorsal aorta morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL endocardium morphogenesis 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 labyrinthine layer blood vessel development Inferred from sequence or structural similarity. Source: BHF-UCL 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 outflow tract morphogenesis Inferred from sequence or structural similarity. Source: BHF-UCL 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 of Notch receptor target Inferred from direct assay Ref.12. Source: UniProtKB regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Inferred from sequence or structural similarity. Source: BHF-UCL 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_component	MAML1-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
Molecular_function	DNA 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 recombinase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NOTCH1	P46531	2	EBI-632552,EBI-636374
SNW1	Q13573	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 500

500

Recombining binding protein suppressor of hairless

PRO_0000208567

Regions

Domain

355 – 445

91

IPT/TIG

DNA binding

58 – 65

8

Ref.13

DNA binding

192 – 201

10

Ref.13

DNA binding

265 – 297

33

Ref.13

Natural variations

Alternative sequence

1 – 89

89

Missing in isoform APCR-3.

VSP_002718

Alternative sequence

1 – 75

75

Missing in isoform APCR-1.

VSP_002717

Alternative sequence

1 – 35

35

Missing in isoform 5.

VSP_021572

Alternative sequence

1 – 20

20

MDHTE…APSPG → MGGCR in isoform 4.

VSP_021573

Alternative sequence

1 – 20

20

MDHTE…APSPG → MAWIKR in isoform 6.

VSP_021574

Alternative sequence

1 – 19

19

MDHTE…HAPSP → MAPVVT in isoform 7.

VSP_042637

Alternative sequence

90 – 95

6

DGCSEQ → MAWIKR in isoform APCR-3.

VSP_002719

Natural variant

63

1

E → G in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. Ref.15

VAR_068929

Natural variant

169

1

K → E in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. Ref.15

VAR_068930

Natural variant

291

1

K → E.
Corresponds to variant rs1064372 [ dbSNP | Ensembl ].

VAR_028994

Natural variant

296

1

M → K.
Corresponds to variant rs5011135 [ dbSNP | Ensembl ].

VAR_057243

Natural variant

334

1

D → H.
Corresponds to variant rs1064376 [ dbSNP | Ensembl ].

VAR_028995

Natural variant

408

1

I → V.
Corresponds to variant rs1064381 [ dbSNP | Ensembl ].

VAR_057244

Natural variant

419

1

R → Q.
Corresponds to variant rs1064384 [ dbSNP | Ensembl ].

VAR_028996

Natural variant

425

1

P → S.
Corresponds to variant rs1064387 [ dbSNP | Ensembl ].

VAR_028997

Natural variant

456

1

A → V. Ref.1
Corresponds to variant rs1064402 [ dbSNP | Ensembl ].

VAR_028998

Experimental info

Sequence conflict

7

1

S → L in AAA60258. Ref.1

Sequence conflict

7

1

S → L in AAA16253. Ref.1

Sequence conflict

7

1

S → L in AAA16254. Ref.1

Sequence conflict

140 – 141

2

ML → IF in AAA60258. Ref.1

Sequence conflict

240

1

G → V in AAA60258. Ref.1

Sequence conflict

248

1

V → C in AAA60258. Ref.1

Sequence conflict

265

1

R → M in AAA60258. Ref.1

Sequence conflict

270

1

Q → H in AAA60258. Ref.1

Sequence conflict

462

1

R → P in AAA60258. Ref.1

Secondary structure

1

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500

Helix Strand Turn

Details...

Helix

33 – 41

9

Beta strand

50 – 57

8

Beta strand

72 – 74

3

Helix

79 – 88

10

Turn

89 – 91

3

Turn

94 – 96

3

Beta strand

102 – 105

4

Beta strand

118 – 121

4

Beta strand

137 – 139

3

Beta strand

141 – 146

6

Beta strand

152 – 157

6

Beta strand

161 – 166

6

Beta strand

174 – 176

3

Beta strand

178 – 180

3

Beta strand

185 – 191

7

Helix

193 – 195

3

Turn

197 – 199

3

Beta strand

204 – 206

3

Beta strand

209 – 211

3

Beta strand

220 – 225

6

Beta strand

231 – 234

4

Beta strand

246 – 255

10

Beta strand

262 – 268

7

Beta strand

271 – 275

5

Beta strand

284 – 289

6

Beta strand

291 – 295

5

Beta strand

297 – 299

3

Beta strand

302 – 306

5

Beta strand

319 – 321

3

Beta strand

328 – 336

9

Beta strand

343 – 345

3

Beta strand

356 – 362

7

Helix

366 – 368

3

Beta strand

370 – 377

8

Beta strand

382 – 386

5

Beta strand

389 – 391

3

Beta strand

393 – 397

5

Beta strand

400 – 404

5

Helix

408 – 411

4

Beta strand

412 – 414

3

Beta strand

426 – 430

5

Beta strand

431 – 433

3

Beta strand

435 – 437

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform APCR-2 [UniParc]. Last modified June 28, 2011. Version 3. Checksum: 91E50D2DE9087EDA	FASTA	500	55,637
	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
	Isoform APCR-1 [UniParc]. Checksum: 31CC3FCBED8E739E	FASTA	425	47,180
	10 20 30 40 50 60 MGSGWKKKKE QMERDGCSEQ ESQPCAFIGI GNSDQEMQQL NLEGKNYCTA KTLYISDSDK 70 80 90 100 110 120 RKHFMLSVKM FYGNSDDIGV FLSKRIKVIS KPSKKKQSLK NADLCIASGT KVALFNRLRS 130 140 150 160 170 180 QTVSTRYLHV EGGNFHASSQ QWGAFFIHLL DDDESEGEEF TVRDGYIHYG QTVKLVCSVT 190 200 210 220 230 240 GMALPRLIIR KVDKQTALLD ADDPVSQLHK CAFYLKDTER MYLCLSQERI IQFQATPCPK 250 260 270 280 290 300 EPNKEMINDG ASWTIISTDK AEYTFYEGMG PVLAPVTPVP VVESLQLNGG GDVAMLELTG 310 320 330 340 350 360 QNFTPNLRVW FGDVEAETMY RCGESMLCVV PDISAFREGW RWVRQPVQVP VTLVRNDGII 370 380 390 400 410 420 YSTSLTFTYT PEPGPRPHCS AAGAILRANS SQVPPNESNT NSEGSYTNAS TNSTSVTSST ATVVS
	Isoform APCR-3 [UniParc]. Checksum: F213446BAF8AA7BF	FASTA	411	45,642
	10 20 30 40 50 60 MAWIKRESQP CAFIGIGNSD QEMQQLNLEG KNYCTAKTLY ISDSDKRKHF MLSVKMFYGN 70 80 90 100 110 120 SDDIGVFLSK RIKVISKPSK KKQSLKNADL CIASGTKVAL FNRLRSQTVS TRYLHVEGGN 130 140 150 160 170 180 FHASSQQWGA FFIHLLDDDE SEGEEFTVRD GYIHYGQTVK LVCSVTGMAL PRLIIRKVDK 190 200 210 220 230 240 QTALLDADDP VSQLHKCAFY LKDTERMYLC LSQERIIQFQ ATPCPKEPNK EMINDGASWT 250 260 270 280 290 300 IISTDKAEYT FYEGMGPVLA PVTPVPVVES LQLNGGGDVA MLELTGQNFT PNLRVWFGDV 310 320 330 340 350 360 EAETMYRCGE SMLCVVPDIS AFREGWRWVR QPVQVPVTLV RNDGIIYSTS LTFTYTPEPG 370 380 390 400 410 PRPHCSAAGA ILRANSSQVP PNESNTNSEG SYTNASTNST SVTSSTATVV S
	Isoform 4 [UniParc]. Checksum: F0907B0A36490025	FASTA	485	54,146
	10 20 30 40 50 60 MGGCRKFGER PPPKRLTREA MRNYLKERGD QTVLILHAKV AQKSYGNEKR FFCPPPCVYL 70 80 90 100 110 120 MGSGWKKKKE QMERDGCSEQ ESQPCAFIGI GNSDQEMQQL NLEGKNYCTA KTLYISDSDK 130 140 150 160 170 180 RKHFMLSVKM FYGNSDDIGV FLSKRIKVIS KPSKKKQSLK NADLCIASGT KVALFNRLRS 190 200 210 220 230 240 QTVSTRYLHV EGGNFHASSQ QWGAFFIHLL DDDESEGEEF TVRDGYIHYG QTVKLVCSVT 250 260 270 280 290 300 GMALPRLIIR KVDKQTALLD ADDPVSQLHK CAFYLKDTER MYLCLSQERI IQFQATPCPK 310 320 330 340 350 360 EPNKEMINDG ASWTIISTDK AEYTFYEGMG PVLAPVTPVP VVESLQLNGG GDVAMLELTG 370 380 390 400 410 420 QNFTPNLRVW FGDVEAETMY RCGESMLCVV PDISAFREGW RWVRQPVQVP VTLVRNDGII 430 440 450 460 470 480 YSTSLTFTYT PEPGPRPHCS AAGAILRANS SQVPPNESNT NSEGSYTNAS TNSTSVTSST ATVVS
	Isoform 5 [UniParc]. Checksum: 683E1FC7CC0FACC8	FASTA	465	51,877
	10 20 30 40 50 60 MRNYLKERGD QTVLILHAKV AQKSYGNEKR FFCPPPCVYL MGSGWKKKKE QMERDGCSEQ 70 80 90 100 110 120 ESQPCAFIGI GNSDQEMQQL NLEGKNYCTA KTLYISDSDK RKHFMLSVKM FYGNSDDIGV 130 140 150 160 170 180 FLSKRIKVIS KPSKKKQSLK NADLCIASGT KVALFNRLRS QTVSTRYLHV EGGNFHASSQ 190 200 210 220 230 240 QWGAFFIHLL DDDESEGEEF TVRDGYIHYG QTVKLVCSVT GMALPRLIIR KVDKQTALLD 250 260 270 280 290 300 ADDPVSQLHK CAFYLKDTER MYLCLSQERI IQFQATPCPK EPNKEMINDG ASWTIISTDK 310 320 330 340 350 360 AEYTFYEGMG PVLAPVTPVP VVESLQLNGG GDVAMLELTG QNFTPNLRVW FGDVEAETMY 370 380 390 400 410 420 RCGESMLCVV PDISAFREGW RWVRQPVQVP VTLVRNDGII YSTSLTFTYT PEPGPRPHCS 430 440 450 460 AAGAILRANS SQVPPNESNT NSEGSYTNAS TNSTSVTSST ATVVS
	Isoform 6 [UniParc]. Checksum: 31FD3B3D01B13C4C	FASTA	486	54,427
	10 20 30 40 50 60 MAWIKRKFGE RPPPKRLTRE AMRNYLKERG DQTVLILHAK VAQKSYGNEK RFFCPPPCVY 70 80 90 100 110 120 LMGSGWKKKK EQMERDGCSE QESQPCAFIG IGNSDQEMQQ LNLEGKNYCT AKTLYISDSD 130 140 150 160 170 180 KRKHFMLSVK MFYGNSDDIG VFLSKRIKVI SKPSKKKQSL KNADLCIASG TKVALFNRLR 190 200 210 220 230 240 SQTVSTRYLH VEGGNFHASS QQWGAFFIHL LDDDESEGEE FTVRDGYIHY GQTVKLVCSV 250 260 270 280 290 300 TGMALPRLII RKVDKQTALL DADDPVSQLH KCAFYLKDTE RMYLCLSQER IIQFQATPCP 310 320 330 340 350 360 KEPNKEMIND GASWTIISTD KAEYTFYEGM GPVLAPVTPV PVVESLQLNG GGDVAMLELT 370 380 390 400 410 420 GQNFTPNLRV WFGDVEAETM YRCGESMLCV VPDISAFREG WRWVRQPVQV PVTLVRNDGI 430 440 450 460 470 480 IYSTSLTFTY TPEPGPRPHC SAAGAILRAN SSQVPPNESN TNSEGSYTNA STNSTSVTSS TATVVS
	Isoform 7 [UniParc]. Checksum: BF5DE1E391B0E947	FASTA	487	54,297
	10 20 30 40 50 60 MAPVVTGKFG ERPPPKRLTR EAMRNYLKER GDQTVLILHA KVAQKSYGNE KRFFCPPPCV 70 80 90 100 110 120 YLMGSGWKKK KEQMERDGCS EQESQPCAFI GIGNSDQEMQ QLNLEGKNYC TAKTLYISDS 130 140 150 160 170 180 DKRKHFMLSV KMFYGNSDDI GVFLSKRIKV ISKPSKKKQS LKNADLCIAS GTKVALFNRL 190 200 210 220 230 240 RSQTVSTRYL HVEGGNFHAS SQQWGAFFIH LLDDDESEGE EFTVRDGYIH YGQTVKLVCS 250 260 270 280 290 300 VTGMALPRLI IRKVDKQTAL LDADDPVSQL HKCAFYLKDT ERMYLCLSQE RIIQFQATPC 310 320 330 340 350 360 PKEPNKEMIN DGASWTIIST DKAEYTFYEG MGPVLAPVTP VPVVESLQLN GGGDVAMLEL 370 380 390 400 410 420 TGQNFTPNLR VWFGDVEAET MYRCGESMLC VVPDISAFRE GWRWVRQPVQ VPVTLVRNDG 430 440 450 460 470 480 IIYSTSLTFT YTPEPGPRPH CSAAGAILRA NSSQVPPNES NTNSEGSYTN ASTNSTSVTS STATVVS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00030177.
IPI00218576.
IPI00218578.
IPI00402156.
IPI00419892.
IPI00807402.

PIR

A47214.

RefSeq

NP_005340.2. NM_005349.3.
NP_056958.3. NM_015874.4.
NP_976028.1. NM_203283.2.
NP_976029.1. NM_203284.2.

UniGene

Hs.479396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2F8X	X-ray	3.25	C	23-449	[»]
3NBN	X-ray	3.45	A/D	23-448	[»]
3V79	X-ray	3.85	C	23-449	[»]

ProteinModelPortal

Q06330.

SMR

Q06330. Positions 25-448.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33326N.

IntAct

Q06330. 11 interactions.

MINT

MINT-1327001.

STRING

9606.ENSP00000345206.

PTM databases

PhosphoSite

Q06330.

Polymorphism databases

DMDM

118572724.

Proteomic databases

PaxDb

Q06330.

PRIDE

Q06330.

Protocols and materials databases

DNASU

3516.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342295; ENSP00000345206; ENSG00000168214.
ENST00000342320; ENSP00000340124; ENSG00000168214.
ENST00000345843; ENSP00000305815; ENSG00000168214.
ENST00000348160; ENSP00000339699; ENSG00000168214.
ENST00000355476; ENSP00000347659; ENSG00000168214.
ENST00000361572; ENSP00000354528; ENSG00000168214.
ENST00000507561; ENSP00000423907; ENSG00000168214.

GeneID

3516.

KEGG

hsa:3516.

UCSC

uc003grx.2. human.
uc003gry.2. human.
uc003gsa.2. human.

Organism-specific databases

CTD

3516.

GeneCards

GC04P026165.

HGNC

HGNC:5724. RBPJ.

MIM

147183. gene.
614814. phenotype.

neXtProt

NX_Q06330.

PharmGKB

PA34292.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG295376.

HOGENOM

HOG000253907.

HOVERGEN

HBG006618.

InParanoid

Q06330.

KO

K06053.

OMA

MGPVHAP.

PhylomeDB

Q06330.

Enzyme and pathway databases

Pathway_Interaction_DB

ps1pathway. Presenilin action in Notch and Wnt signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q06330.

Bgee

Q06330.

CleanEx

HS_RBPJ.

Genevestigator

Q06330.

GermOnline

ENSG00000168214. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.

InterPro

IPR015350. Beta-trefoil_DNA-bd_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
IPR015351. LAG1_DNA-bd.
IPR008967. p53-like_TF_DNA-bd.
[Graphical view]

Pfam

PF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]

SUPFAM

SSF110217. Beta-trefoil. 1 hit.
SSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

RBPJ. human.

EvolutionaryTrace

Q06330.

GenomeRNAi

3516.

NextBio

13784.

SOURCE

Search...

Entry information

Entry name

SUH_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.