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Q06330

- SUH_HUMAN

UniProt

Q06330 - SUH_HUMAN

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
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    4. recombinase activity Source: UniProtKB
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: InterPro
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
    7. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    8. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    9. 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 cardiac muscle cell proliferation Source: BHF-UCL
    35. positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
    36. positive regulation of ephrin receptor signaling pathway Source: BHF-UCL
    37. positive regulation of ERBB signaling pathway Source: BHF-UCL
    38. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    39. positive regulation of transcription of Notch receptor target Source: UniProtKB
    40. regulation of timing of cell differentiation Source: Ensembl
    41. regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
    42. sebaceous gland development Source: Ensembl
    43. somatic stem cell maintenance Source: Ensembl
    44. transcription initiation from RNA polymerase II promoter Source: Reactome
    45. ventricular trabecula myocardium morphogenesis Source: BHF-UCL

    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

    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

    ArrayExpressiQ06330.
    BgeeiQ06330.
    CleanExiHS_RBPJ.
    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. 35 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.
    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

    MDHTEGSPAE EPPAHAPSPG KFGERPPPKR LTREAMRNYL KERGDQTVLI    50
    LHAKVAQKSY GNEKRFFCPP PCVYLMGSGW KKKKEQMERD GCSEQESQPC 100
    AFIGIGNSDQ EMQQLNLEGK NYCTAKTLYI SDSDKRKHFM LSVKMFYGNS 150
    DDIGVFLSKR IKVISKPSKK KQSLKNADLC IASGTKVALF NRLRSQTVST 200
    RYLHVEGGNF HASSQQWGAF FIHLLDDDES EGEEFTVRDG YIHYGQTVKL 250
    VCSVTGMALP RLIIRKVDKQ TALLDADDPV SQLHKCAFYL KDTERMYLCL 300
    SQERIIQFQA TPCPKEPNKE MINDGASWTI ISTDKAEYTF YEGMGPVLAP 350
    VTPVPVVESL QLNGGGDVAM LELTGQNFTP NLRVWFGDVE AETMYRCGES 400
    MLCVVPDISA FREGWRWVRQ PVQVPVTLVR NDGIIYSTSL TFTYTPEPGP 450
    RPHCSAAGAI LRANSSQVPP NESNTNSEGS YTNASTNSTS VTSSTATVVS 500
    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. 35 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.
    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

    ArrayExpressi Q06330.
    Bgeei Q06330.
    CleanExi HS_RBPJ.
    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

    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 1, 2014
    This is version 146 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