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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
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. Ref.4 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Nucleus. Cytoplasm. Note: Mainly nuclear, upon interaction with RITA/C12orf52, translocates to the cytoplasm, down-regulating the Notch signaling pathway. Ref.7 Ref.10
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.

Ontologies

Keywords
Biological process	Notch signaling pathway Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	DNA-binding
Molecular function	Activator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA recombination Non-traceable author statement Ref.1. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB positive regulation of transcription of Notch receptor target Inferred from direct assay Ref.10. Source: UniProtKB
Cellular component	MAML1-RBP-Jkappa- ICN1 complex Inferred from direct assay. Source: UniProtKB cytoplasm Inferred from direct assay Ref.10. Source: UniProtKB nucleolus Inferred from direct assay Ref.7. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular function	DNA binding Traceable author statement Ref.7. Source: UniProtKB RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Inferred from direct assay. Source: MGI protein binding Inferred from physical interaction Ref.11Ref.10Ref.7. Source: UniProtKB 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 6 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

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

DNA binding

192 – 201

10

DNA binding

265 – 297

33

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

90 – 95

6

DGCSEQ → MAWIKR in isoform APCR-3.

VSP_002719

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

Helix

79 – 88

10

Turn

94 – 96

3

Beta strand

102 – 105

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

302 – 306

5

Beta strand

319 – 321

3

Beta strand

328 – 336

9

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

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

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: 8406481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS APCR-1; APCR-2 AND APCR-3), VARIANT VAL-456. Tissue: Placenta.
[2]	"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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6). Tissue: Eye.
[4]	"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: 8016657] [Abstract] Cited for: INTERACTION WITH EBV EBNA2.
[5]	"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: 8627785] [Abstract] Cited for: INTERACTION WITH EBV EBNA3; EBV EBNA4 AND EBV EBNA6.
[6]	"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: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[7]	"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: 9874765] [Abstract] Cited for: INTERACTION WITH CIR1, SUBCELLULAR LOCATION.
[8]	"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: 10637481] [Abstract] Cited for: INTERACTION WITH NOTCH1.
[9]	"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: 12374742] [Abstract] Cited for: INTERACTION WITH MINT.
[10]	"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: 21102556] [Abstract] Cited for: INTERACTION WITH C12ORF52, SUBCELLULAR LOCATION.
[11]	"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: 16530044] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 23-449 IN COMPLEX WITH DNA; MAML1 AND NOTCH1.
+	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.
AC093637 Genomic DNA. No translation available.
AC097109 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	[»]

ProteinModelPortal

Q06330.

SMR

Q06330. Positions 25-448.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33326N.

IntAct

Q06330. 11 interactions.

MINT

MINT-1327001.

STRING

Q06330.

PTM databases

PhosphoSite

Q06330.

Polymorphism databases

DMDM

118572724.

Proteomic databases

PRIDE

Q06330.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342295; ENSP00000345206; ENSG00000168214.
ENST00000361572; ENSP00000354528; ENSG00000168214.

GeneID

3516.

KEGG

hsa:3516.

UCSC

uc003grx.1. human.

Organism-specific databases

CTD

3516.

GeneCards

GC04P026165.

HGNC

HGNC:5724. RBPJ.

MIM

147183. gene.

neXtProt

NX_Q06330.

PharmGKB

PA34292.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09743.

GeneTree

ENSGT00390000005197.

HOGENOM

HBG383440.

HOVERGEN

HBG006618.

InParanoid

Q06330.

PhylomeDB

Q06330.

Enzyme and pathway databases

Pathway_Interaction_DB

ps1pathway. Presenilin action in Notch and Wnt signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q06330.

Bgee

Q06330.

CleanEx

HS_RBPJ.

Genevestigator

Q06330.

GermOnline

ENSG00000168214. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.60.40.1450. LAG1_DNA-bd. 1 hit.

KO

K06053.

Pfam

PF09270. Beta-trefoil. 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

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Other

NextBio

13784.

SOURCE

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Entry information

Entry name

SUH_HUMAN

Accession

Primary (citable) accession number: Q06330
Secondary accession number(s): Q5XKH9, Q6P1N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 28, 2011
Last modified:	January 25, 2012
This is version 117 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.