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Q06330

- SUH_HUMAN

UniProt

Q06330 - SUH_HUMAN

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Protein

Recombining binding protein suppressor of hairless

Gene

RBPJ

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi58 – 658
DNA bindingi192 – 20110
DNA bindingi265 – 29733Add
BLAST

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. DNA binding Source: UniProtKB
  3. recombinase activity Source: UniProtKB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: InterPro
  5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  6. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  7. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  8. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: BHF-UCL
  2. arterial endothelial cell fate commitment Source: Ensembl
  3. atrioventricular canal development Source: BHF-UCL
  4. auditory receptor cell fate commitment Source: Ensembl
  5. B cell differentiation Source: Ensembl
  6. blood vessel endothelial cell fate specification Source: BHF-UCL
  7. blood vessel lumenization Source: BHF-UCL
  8. blood vessel remodeling Source: Ensembl
  9. cardiac left ventricle morphogenesis Source: BHF-UCL
  10. Clara cell differentiation Source: Ensembl
  11. defense response to bacterium Source: Ensembl
  12. DNA recombination Source: UniProtKB
  13. dorsal aorta morphogenesis Source: BHF-UCL
  14. endocardium morphogenesis Source: BHF-UCL
  15. epidermal cell fate specification Source: Ensembl
  16. epithelial to mesenchymal transition Source: BHF-UCL
  17. epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
  18. gene expression Source: Reactome
  19. hair follicle maturation Source: Ensembl
  20. humoral immune response Source: Ensembl
  21. inflammatory response to antigenic stimulus Source: Ensembl
  22. interleukin-4 secretion Source: Ensembl
  23. keratinocyte differentiation Source: Ensembl
  24. labyrinthine layer blood vessel development Source: BHF-UCL
  25. negative regulation of cell proliferation Source: Ensembl
  26. negative regulation of ossification Source: BHF-UCL
  27. negative regulation of transcription, DNA-templated Source: UniProtKB
  28. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  29. Notch signaling involved in heart development Source: BHF-UCL
  30. Notch signaling pathway Source: BHF-UCL
  31. outflow tract morphogenesis Source: BHF-UCL
  32. pituitary gland development Source: Ensembl
  33. positive regulation of BMP signaling pathway Source: BHF-UCL
  34. positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment Source: Ensembl
  35. positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
  36. positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
  37. positive regulation of ephrin receptor signaling pathway Source: BHF-UCL
  38. positive regulation of ERBB signaling pathway Source: BHF-UCL
  39. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  40. positive regulation of transcription of Notch receptor target Source: UniProtKB
  41. regulation of timing of cell differentiation Source: Ensembl
  42. regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
  43. sebaceous gland development Source: Ensembl
  44. secondary heart field specification Source: Ensembl
  45. somatic stem cell maintenance Source: Ensembl
  46. transcription initiation from RNA polymerase II promoter Source: Reactome
  47. ventricular trabecula myocardium morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Notch signaling pathway, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_13673. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinkiQ06330.

Names & Taxonomyi

Protein namesi
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 namesi
Name:RBPJ
Synonyms:IGKJRB, IGKJRB1, RBPJK, RBPSUH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:5724. RBPJ.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. MAML1-RBP-Jkappa- ICN1 complex Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
  6. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631E → G in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. 1 Publication
VAR_068929
Natural varianti169 – 1691K → E in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. 1 Publication
VAR_068930

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614814. phenotype.
Orphaneti974. Adams-Oliver syndrome.
PharmGKBiPA34292.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500Recombining binding protein suppressor of hairlessPRO_0000208567Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ06330.
PaxDbiQ06330.
PRIDEiQ06330.

PTM databases

PhosphoSiteiQ06330.

Expressioni

Gene expression databases

BgeeiQ06330.
CleanExiHS_RBPJ.
ExpressionAtlasiQ06330. baseline and differential.
GenevestigatoriQ06330.

Interactioni

Subunit structurei

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 SNW1.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
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

Protein-protein interaction databases

BioGridi109736. 42 interactions.
DIPiDIP-33326N.
IntActiQ06330. 25 interactions.
MINTiMINT-1327001.
STRINGi9606.ENSP00000345206.

Structurei

Secondary structure

1
500
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 419
Beta strandi50 – 578
Beta strandi72 – 743
Helixi79 – 8810
Turni89 – 913
Turni94 – 963
Beta strandi102 – 1054
Beta strandi118 – 1214
Beta strandi137 – 1393
Beta strandi141 – 1466
Beta strandi152 – 1576
Beta strandi161 – 1666
Beta strandi174 – 1763
Beta strandi178 – 1803
Beta strandi185 – 1917
Helixi193 – 1953
Turni197 – 1993
Beta strandi204 – 2063
Beta strandi209 – 2113
Beta strandi220 – 2256
Beta strandi231 – 2344
Beta strandi246 – 25510
Beta strandi262 – 2687
Beta strandi271 – 2755
Beta strandi284 – 2896
Beta strandi291 – 2955
Beta strandi297 – 2993
Beta strandi302 – 3065
Beta strandi319 – 3213
Beta strandi328 – 3369
Beta strandi343 – 3453
Beta strandi356 – 3627
Helixi366 – 3683
Beta strandi370 – 3778
Beta strandi382 – 3865
Beta strandi389 – 3913
Beta strandi393 – 3975
Beta strandi400 – 4045
Helixi408 – 4114
Beta strandi412 – 4143
Beta strandi426 – 4305
Beta strandi431 – 4333
Beta strandi435 – 4373

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F8XX-ray3.25C23-449[»]
3NBNX-ray3.45A/D23-448[»]
3V79X-ray3.85C23-449[»]
ProteinModelPortaliQ06330.
SMRiQ06330. Positions 25-448.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06330.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini355 – 44591IPT/TIGAdd
BLAST

Sequence similaritiesi

Belongs to the Su(H) family.Curated
Contains 1 IPT/TIG domain.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG295376.
GeneTreeiENSGT00390000005197.
HOGENOMiHOG000253907.
HOVERGENiHBG006618.
InParanoidiQ06330.
KOiK06053.
OMAiMGPVHAP.
PhylomeDBiQ06330.
TreeFamiTF314117.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProiIPR015350. 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]
PfamiPF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
SUPFAMiSSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform APCR-2 (identifier: Q06330-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDHTEGSPAE EPPAHAPSPG KFGERPPPKR LTREAMRNYL KERGDQTVLI
60 70 80 90 100
LHAKVAQKSY GNEKRFFCPP PCVYLMGSGW KKKKEQMERD GCSEQESQPC
110 120 130 140 150
AFIGIGNSDQ EMQQLNLEGK NYCTAKTLYI SDSDKRKHFM LSVKMFYGNS
160 170 180 190 200
DDIGVFLSKR IKVISKPSKK KQSLKNADLC IASGTKVALF NRLRSQTVST
210 220 230 240 250
RYLHVEGGNF HASSQQWGAF FIHLLDDDES EGEEFTVRDG YIHYGQTVKL
260 270 280 290 300
VCSVTGMALP RLIIRKVDKQ TALLDADDPV SQLHKCAFYL KDTERMYLCL
310 320 330 340 350
SQERIIQFQA TPCPKEPNKE MINDGASWTI ISTDKAEYTF YEGMGPVLAP
360 370 380 390 400
VTPVPVVESL QLNGGGDVAM LELTGQNFTP NLRVWFGDVE AETMYRCGES
410 420 430 440 450
MLCVVPDISA FREGWRWVRQ PVQVPVTLVR NDGIIYSTSL TFTYTPEPGP
460 470 480 490 500
RPHCSAAGAI LRANSSQVPP NESNTNSEGS YTNASTNSTS VTSSTATVVS
Length:500
Mass (Da):55,637
Last modified:June 28, 2011 - v3
Checksum:i91E50D2DE9087EDA
GO
Isoform APCR-1 (identifier: Q06330-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-75: Missing.

Show »
Length:425
Mass (Da):47,180
Checksum:i31CC3FCBED8E739E
GO
Isoform APCR-3 (identifier: Q06330-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: Missing.
     90-95: DGCSEQ → MAWIKR

Show »
Length:411
Mass (Da):45,642
Checksum:iF213446BAF8AA7BF
GO
Isoform 4 (identifier: Q06330-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MDHTEGSPAEEPPAHAPSPG → MGGCR

Show »
Length:485
Mass (Da):54,146
Checksum:iF0907B0A36490025
GO
Isoform 5 (identifier: Q06330-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Show »
Length:465
Mass (Da):51,877
Checksum:i683E1FC7CC0FACC8
GO
Isoform 6 (identifier: Q06330-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MDHTEGSPAEEPPAHAPSPG → MAWIKR

Show »
Length:486
Mass (Da):54,427
Checksum:i31FD3B3D01B13C4C
GO
Isoform 7 (identifier: Q06330-7) [UniParc]FASTAAdd to Basket

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

Show »
Length:487
Mass (Da):54,297
Checksum:iBF5DE1E391B0E947
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71S → L in AAA60258. (PubMed:8406481)Curated
Sequence conflicti7 – 71S → L in AAA16253. (PubMed:8406481)Curated
Sequence conflicti7 – 71S → L in AAA16254. (PubMed:8406481)Curated
Sequence conflicti140 – 1412ML → IF in AAA60258. (PubMed:8406481)Curated
Sequence conflicti240 – 2401G → V in AAA60258. (PubMed:8406481)Curated
Sequence conflicti248 – 2481V → C in AAA60258. (PubMed:8406481)Curated
Sequence conflicti265 – 2651R → M in AAA60258. (PubMed:8406481)Curated
Sequence conflicti270 – 2701Q → H in AAA60258. (PubMed:8406481)Curated
Sequence conflicti462 – 4621R → P in AAA60258. (PubMed:8406481)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti63 – 631E → G in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. 1 Publication
VAR_068929
Natural varianti169 – 1691K → E in AOS3; shows decreased binding to the HES1 promoter compared to wild-type. 1 Publication
VAR_068930
Natural varianti291 – 2911K → E.
Corresponds to variant rs1064372 [ dbSNP | Ensembl ].
VAR_028994
Natural varianti296 – 2961M → K.
Corresponds to variant rs5011135 [ dbSNP | Ensembl ].
VAR_057243
Natural varianti334 – 3341D → H.
Corresponds to variant rs1064376 [ dbSNP | Ensembl ].
VAR_028995
Natural varianti408 – 4081I → V.
Corresponds to variant rs1064381 [ dbSNP | Ensembl ].
VAR_057244
Natural varianti419 – 4191R → Q.
Corresponds to variant rs1064384 [ dbSNP | Ensembl ].
VAR_028996
Natural varianti425 – 4251P → S.
Corresponds to variant rs1064387 [ dbSNP | Ensembl ].
VAR_028997
Natural varianti456 – 4561A → V.1 Publication
Corresponds to variant rs1064402 [ dbSNP | Ensembl ].
VAR_028998

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8989Missing in isoform APCR-3. 1 PublicationVSP_002718Add
BLAST
Alternative sequencei1 – 7575Missing in isoform APCR-1. 1 PublicationVSP_002717Add
BLAST
Alternative sequencei1 – 3535Missing in isoform 5. 1 PublicationVSP_021572Add
BLAST
Alternative sequencei1 – 2020MDHTE…APSPG → MGGCR in isoform 4. 1 PublicationVSP_021573Add
BLAST
Alternative sequencei1 – 2020MDHTE…APSPG → MAWIKR in isoform 6. 1 PublicationVSP_021574Add
BLAST
Alternative sequencei1 – 1919MDHTE…HAPSP → MAPVVT in isoform 7. 1 PublicationVSP_042637Add
BLAST
Alternative sequencei90 – 956DGCSEQ → MAWIKR in isoform APCR-3. 1 PublicationVSP_002719

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33969.1. [Q06330-6]
CCDS3436.1. [Q06330-4]
CCDS3437.1. [Q06330-1]
CCDS43219.1. [Q06330-7]
PIRiA47214.
RefSeqiNP_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]
UniGeneiHs.479396.

Genome annotation databases

EnsembliENST00000342295; 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]
GeneIDi3516.
KEGGihsa:3516.
UCSCiuc003grx.2. human. [Q06330-1]
uc003gry.2. human. [Q06330-4]
uc003gsa.2. human. [Q06330-6]
uc003gsb.2. human. [Q06330-7]

Polymorphism databases

DMDMi338817983.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33969.1. [Q06330-6 ]
CCDS3436.1. [Q06330-4 ]
CCDS3437.1. [Q06330-1 ]
CCDS43219.1. [Q06330-7 ]
PIRi A47214.
RefSeqi NP_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 ]
UniGenei Hs.479396.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q06330.
SMRi Q06330. Positions 25-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109736. 42 interactions.
DIPi DIP-33326N.
IntActi Q06330. 25 interactions.
MINTi MINT-1327001.
STRINGi 9606.ENSP00000345206.

PTM databases

PhosphoSitei Q06330.

Polymorphism databases

DMDMi 338817983.

Proteomic databases

MaxQBi Q06330.
PaxDbi Q06330.
PRIDEi Q06330.

Protocols and materials databases

DNASUi 3516.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000342295 ; 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 ]
GeneIDi 3516.
KEGGi hsa:3516.
UCSCi uc003grx.2. human. [Q06330-1 ]
uc003gry.2. human. [Q06330-4 ]
uc003gsa.2. human. [Q06330-6 ]
uc003gsb.2. human. [Q06330-7 ]

Organism-specific databases

CTDi 3516.
GeneCardsi GC04P026165.
HGNCi HGNC:5724. RBPJ.
MIMi 147183. gene.
614814. phenotype.
neXtProti NX_Q06330.
Orphaneti 974. Adams-Oliver syndrome.
PharmGKBi PA34292.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295376.
GeneTreei ENSGT00390000005197.
HOGENOMi HOG000253907.
HOVERGENi HBG006618.
InParanoidi Q06330.
KOi K06053.
OMAi MGPVHAP.
PhylomeDBi Q06330.
TreeFami TF314117.

Enzyme and pathway databases

Reactomei REACT_118568. Pre-NOTCH Transcription and Translation.
REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_13673. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
REACT_14835. Notch-HLH transcription pathway.
REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_163910. NOTCH2 intracellular domain regulates transcription.
SignaLinki Q06330.

Miscellaneous databases

ChiTaRSi RBPJ. human.
EvolutionaryTracei Q06330.
GeneWikii RBPJ.
GenomeRNAii 3516.
NextBioi 13784.
PROi Q06330.
SOURCEi Search...

Gene expression databases

Bgeei Q06330.
CleanExi HS_RBPJ.
ExpressionAtlasi Q06330. baseline and differential.
Genevestigatori Q06330.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.1450. 1 hit.
InterProi IPR015350. 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 ]
Pfami PF09270. BTD. 1 hit.
PF09271. LAG1-DNAbind. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view ]
SUPFAMi SSF110217. SSF110217. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: INTERACTION WITH MINT.
  12. 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. Cited for: VARIANTS AOS3 GLY-63 AND GLU-169, CHARACTERIZATION OF VARIANTS AOS3 GLY-63 AND GLU-169.

Entry informationi

Entry nameiSUH_HUMAN
AccessioniPrimary (citable) accession number: Q06330
Secondary accession number(s): B4DY22, Q5XKH9, Q6P1N3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 28, 2011
Last modified: October 29, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3