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P31266

- SUH_MOUSE

UniProt

P31266 - SUH_MOUSE

Protein

Recombining binding protein suppressor of hairless

Gene

Rbpj

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Jul 1993)
      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 bindingi84 – 918By similarity
    DNA bindingi218 – 22710
    DNA bindingi291 – 32333Add
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. DNA binding Source: MGI
    3. protein binding Source: UniProtKB
    4. protein N-terminus binding Source: MGI
    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: MGI
    8. RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: BHF-UCL
    9. sequence-specific DNA binding Source: MGI
    10. transcription factor binding Source: MGI

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. arterial endothelial cell fate commitment Source: BHF-UCL
    3. atrioventricular canal development Source: BHF-UCL
    4. auditory receptor cell fate commitment Source: MGI
    5. B cell differentiation Source: MGI
    6. blood vessel endothelial cell fate specification Source: BHF-UCL
    7. blood vessel lumenization Source: BHF-UCL
    8. blood vessel remodeling Source: BHF-UCL
    9. cardiac left ventricle morphogenesis Source: BHF-UCL
    10. cell fate commitment Source: MGI
    11. Clara cell differentiation Source: MGI
    12. defense response to bacterium Source: MGI
    13. determination of heart left/right asymmetry Source: BHF-UCL
    14. dorsal aorta morphogenesis Source: BHF-UCL
    15. endocardium development Source: BHF-UCL
    16. endocardium morphogenesis Source: BHF-UCL
    17. epidermal cell fate specification Source: MGI
    18. epithelial to mesenchymal transition Source: MGI
    19. epithelial to mesenchymal transition involved in endocardial cushion formation Source: BHF-UCL
    20. hair follicle maturation Source: MGI
    21. heart development Source: MGI
    22. heart looping Source: BHF-UCL
    23. hemopoiesis Source: MGI
    24. humoral immune response Source: MGI
    25. inflammatory response to antigenic stimulus Source: MGI
    26. interleukin-4 secretion Source: MGI
    27. keratinocyte differentiation Source: MGI
    28. labyrinthine layer blood vessel development Source: BHF-UCL
    29. myeloid dendritic cell differentiation Source: MGI
    30. negative regulation of cell differentiation Source: MGI
    31. negative regulation of cell proliferation Source: MGI
    32. negative regulation of ossification Source: BHF-UCL
    33. negative regulation of transcription, DNA-templated Source: MGI
    34. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    35. neuron differentiation Source: MGI
    36. Notch signaling pathway Source: MGI
    37. Notch signaling pathway involved in arterial endothelial cell fate commitment Source: BHF-UCL
    38. outflow tract morphogenesis Source: BHF-UCL
    39. pituitary gland development Source: MGI
    40. positive regulation of BMP signaling pathway Source: BHF-UCL
    41. positive regulation of canonical Wnt signaling pathway involved in cardiac muscle cell fate commitment Source: MGI
    42. positive regulation of cardiac muscle cell proliferation Source: BHF-UCL
    43. positive regulation of cell proliferation Source: MGI
    44. positive regulation of cell proliferation involved in heart morphogenesis Source: BHF-UCL
    45. positive regulation of ephrin receptor signaling pathway Source: BHF-UCL
    46. positive regulation of ERBB signaling pathway Source: BHF-UCL
    47. positive regulation of gene expression Source: BHF-UCL
    48. positive regulation of Notch signaling pathway involved in heart induction Source: BHF-UCL
    49. positive regulation of transcription, DNA-templated Source: MGI
    50. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    51. positive regulation of transcription of Notch receptor target Source: UniProtKB
    52. regulation of cell adhesion involved in heart morphogenesis Source: BHF-UCL
    53. regulation of gene expression Source: MGI
    54. regulation of timing of cell differentiation Source: MGI
    55. regulation of transcription from RNA polymerase II promoter Source: MGI
    56. regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiation Source: BHF-UCL
    57. sebaceous gland development Source: MGI
    58. secondary heart field specification Source: MGI
    59. somatic stem cell maintenance Source: MGI
    60. somitogenesis Source: BHF-UCL
    61. 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_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196520. Pre-NOTCH Transcription and Translation.
    REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_222486. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
    REACT_223683. Notch-HLH transcription pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Recombining binding protein suppressor of hairless
    Alternative name(s):
    J kappa-recombination signal-binding protein
    RBP-J kappa
    Gene namesi
    Name:Rbpj
    Synonyms:Igkjrb1, Igkrsbp, Rbpsuh
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:96522. Rbpj.

    Subcellular locationi

    Nucleus. Cytoplasm By similarity
    Note: Mainly nuclear, upon interaction with RITA1, translocates to the cytoplasm, down-regulating the Notch signaling pathway.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 526526Recombining binding protein suppressor of hairlessPRO_0000208568Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei201 – 2011N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP31266.
    PaxDbiP31266.
    PRIDEiP31266.

    PTM databases

    PhosphoSiteiP31266.

    Expressioni

    Gene expression databases

    ArrayExpressiP31266.
    BgeeiP31266.
    GenevestigatoriP31266.

    Interactioni

    Subunit structurei

    Interacts with RITA1, leading to nuclear export, prevent the interaction between RBPJ and NICD product and subsequent down-regulation of the Notch signaling pathway By similarity. Interacts with activated NOTCH1, NOTCH2 and 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 SNW1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Notch1Q017056EBI-1392666,EBI-1392707

    Protein-protein interaction databases

    BioGridi202832. 9 interactions.
    DIPiDIP-171N.
    IntActiP31266. 3 interactions.

    Structurei

    Secondary structure

    1
    526
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi59 – 6810
    Beta strandi72 – 8312
    Beta strandi98 – 1036
    Helixi105 – 11511
    Helixi120 – 1234
    Beta strandi124 – 13310
    Beta strandi139 – 1413
    Beta strandi146 – 1505
    Beta strandi163 – 1653
    Beta strandi167 – 1737
    Beta strandi178 – 1836
    Beta strandi187 – 1926
    Helixi200 – 2056
    Beta strandi211 – 2177
    Beta strandi219 – 2213
    Helixi223 – 2253
    Beta strandi227 – 2326
    Beta strandi235 – 2417
    Beta strandi246 – 2505
    Beta strandi257 – 2593
    Beta strandi273 – 2786
    Turni279 – 2813
    Beta strandi288 – 2947
    Beta strandi297 – 3015
    Beta strandi311 – 3166
    Beta strandi319 – 3279
    Beta strandi330 – 3356
    Beta strandi345 – 3473
    Helixi350 – 3523
    Beta strandi354 – 36815
    Beta strandi382 – 3887
    Beta strandi392 – 3943
    Beta strandi396 – 4038
    Beta strandi408 – 4125
    Beta strandi419 – 4235
    Beta strandi426 – 4305
    Helixi434 – 4363
    Beta strandi448 – 4569
    Beta strandi459 – 47012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BRGX-ray2.20C53-474[»]
    3IAGX-ray2.00C53-474[»]
    4J2XX-ray2.85A/C53-474[»]
    ProteinModelPortaliP31266.
    SMRiP31266. Positions 53-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31266.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini381 – 47191IPT/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.
    InParanoidiP31266.
    KOiK06053.
    OMAiMGPVHAP.
    PhylomeDBiP31266.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P31266-1) [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

    MPSGFPQSPR TSPRARPKTR ITGALPMDYS EGLSAEERPA HAPSAGKFGE    50
    RPPPKRLTRE AMRNYLKERG DQTVLILHAK VAQKSYGNEK RFFCPPPCVY 100
    LMGSGWKKKK EQMERDGCSE QESQPCAFIG IGNSDQEMQQ LNLEGKNYCT 150
    AKTLYISDSD KRKHFMLSVK MFYGNSDDIG VFLSKRIKVI SKPSKKKQSL 200
    KNADLCIASG TKVALFNRLR SQTVSTRYLH VEGGNFHASS QQWGAFYIHL 250
    LDDDESEGEE FTVRDGYIHY GQTVKLVCSV TGMALPRLII RKVDKQTALL 300
    DADDPVSQLH KCAFYLKDTE RMYLCLSQER IIQFQATPCP KEQNKEMIND 350
    GASWTIISTD KAEYTFYEGM GPVLAPVTPV PVVESLQLNG GGDVAMLELT 400
    GQNFTPNLRV WFGDVEAETM YRCGESMLCV VPDISAFREG WRWVRQPVQV 450
    PVTLVRNDGV IYSTSLTFTY TPEPGPRPHC SAAGAILRAN SSQVPSNESN 500
    TNSEGNYTNA STNSTSVTSS TATVVS 526
    Length:526
    Mass (Da):58,537
    Last modified:July 1, 1993 - v1
    Checksum:i8BF517CC24099E03
    GO
    Isoform 2 (identifier: P31266-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: Missing.
         40-45: AHAPSA → MAPVVT

    Note: No experimental confirmation available.

    Show »
    Length:487
    Mass (Da):54,347
    Checksum:i88C0D1DCECACC9E2
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3939Missing in isoform 2. 1 PublicationVSP_008392Add
    BLAST
    Alternative sequencei40 – 456AHAPSA → MAPVVT in isoform 2. 1 PublicationVSP_008393

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S63463 mRNA. Translation: AAB20195.1.
    X17459 mRNA. Translation: CAA35501.1.
    X58337 Genomic DNA. No translation available.
    M81867, M81865, M81866 Genomic DNA. Translation: AAA39018.1.
    M81868 Genomic DNA. Translation: AAA39019.1.
    M81870, M81869 Genomic DNA. Translation: AAA39020.1. Sequence problems.
    M81873, M81872 Genomic DNA. Translation: AAA39021.1.
    M81875, M81874 Genomic DNA. Translation: AAA39022.1.
    M81876 Genomic DNA. Translation: AAA39023.1.
    M81877 Genomic DNA. No translation available.
    BC051387 mRNA. Translation: AAH51387.1.
    AK080359 mRNA. Translation: BAC37889.1.
    CCDSiCCDS19292.1. [P31266-1]
    CCDS51504.1. [P31266-2]
    PIRiA42267.
    A43567.
    RefSeqiNP_001074396.1. NM_001080927.2. [P31266-2]
    NP_033061.3. NM_009035.5. [P31266-1]
    UniGeneiMm.209292.
    Mm.488709.

    Genome annotation databases

    EnsembliENSMUST00000037618; ENSMUSP00000040694; ENSMUSG00000039191. [P31266-1]
    ENSMUST00000113865; ENSMUSP00000109496; ENSMUSG00000039191. [P31266-2]
    GeneIDi19664.
    KEGGimmu:19664.
    UCSCiuc008xli.1. mouse. [P31266-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S63463 mRNA. Translation: AAB20195.1 .
    X17459 mRNA. Translation: CAA35501.1 .
    X58337 Genomic DNA. No translation available.
    M81867 , M81865 , M81866 Genomic DNA. Translation: AAA39018.1 .
    M81868 Genomic DNA. Translation: AAA39019.1 .
    M81870 , M81869 Genomic DNA. Translation: AAA39020.1 . Sequence problems.
    M81873 , M81872 Genomic DNA. Translation: AAA39021.1 .
    M81875 , M81874 Genomic DNA. Translation: AAA39022.1 .
    M81876 Genomic DNA. Translation: AAA39023.1 .
    M81877 Genomic DNA. No translation available.
    BC051387 mRNA. Translation: AAH51387.1 .
    AK080359 mRNA. Translation: BAC37889.1 .
    CCDSi CCDS19292.1. [P31266-1 ]
    CCDS51504.1. [P31266-2 ]
    PIRi A42267.
    A43567.
    RefSeqi NP_001074396.1. NM_001080927.2. [P31266-2 ]
    NP_033061.3. NM_009035.5. [P31266-1 ]
    UniGenei Mm.209292.
    Mm.488709.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BRG X-ray 2.20 C 53-474 [» ]
    3IAG X-ray 2.00 C 53-474 [» ]
    4J2X X-ray 2.85 A/C 53-474 [» ]
    ProteinModelPortali P31266.
    SMRi P31266. Positions 53-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202832. 9 interactions.
    DIPi DIP-171N.
    IntActi P31266. 3 interactions.

    PTM databases

    PhosphoSitei P31266.

    Proteomic databases

    MaxQBi P31266.
    PaxDbi P31266.
    PRIDEi P31266.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000037618 ; ENSMUSP00000040694 ; ENSMUSG00000039191 . [P31266-1 ]
    ENSMUST00000113865 ; ENSMUSP00000109496 ; ENSMUSG00000039191 . [P31266-2 ]
    GeneIDi 19664.
    KEGGi mmu:19664.
    UCSCi uc008xli.1. mouse. [P31266-1 ]

    Organism-specific databases

    CTDi 3516.
    MGIi MGI:96522. Rbpj.

    Phylogenomic databases

    eggNOGi NOG295376.
    GeneTreei ENSGT00390000005197.
    HOGENOMi HOG000253907.
    HOVERGENi HBG006618.
    InParanoidi P31266.
    KOi K06053.
    OMAi MGPVHAP.
    PhylomeDBi P31266.
    TreeFami TF314117.

    Enzyme and pathway databases

    Reactomei REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_196520. Pre-NOTCH Transcription and Translation.
    REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_196593. NOTCH2 intracellular domain regulates transcription.
    REACT_222486. Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
    REACT_223683. Notch-HLH transcription pathway.

    Miscellaneous databases

    EvolutionaryTracei P31266.
    NextBioi 296966.
    PROi P31266.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31266.
    Bgeei P31266.
    Genevestigatori P31266.

    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. "A protein binding to the J kappa recombination sequence of immunoglobulin genes contains a sequence related to the integrase motif."
      Matsunami N., Hamaguchi Y., Yamamoto Y., Kuze K., Kangawa K., Matsuo H., Kawaichi M., Honjo T.
      Nature 342:934-937(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Genomic organization of mouse J kappa recombination signal binding protein (RBP-J kappa) gene."
      Kawaichi M., Oka C., Shibayama S., Koromilas A.E., Matsunami N., Hamaguchi Y., Honjo T.
      J. Biol. Chem. 267:4016-4022(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Strain: BALB/c.
      Tissue: Liver.
    3. "Cloning and characterization of a protein binding to the J kappa recombination signal sequence of immunoglobulin genes."
      Hamaguchi Y., Matsunami N., Yamamoto Y., Kuze K., Kangawa K., Matsuo H., Kawaichi M., Honjo T.
      Adv. Exp. Med. Biol. 292:177-186(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary tumor.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Thymus.
    6. "Signalling downstream of activated mammalian Notch."
      Jarriault S., Brou C., Logeat F., Schroeter E.H., Kopan R., Israel A.
      Nature 377:355-358(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NOTCH1.
    7. "LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein."
      Taniguchi Y., Furukawa T., Tun T., Han H., Honjo T.
      Mol. Cell. Biol. 18:644-654(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FHL1.
    8. Cited for: INTERACTION WITH EP300.
    9. "p48 subunit of mouse PTF1 binds to RBP-Jkappa/CBF-1, the intracellular mediator of Notch signalling, and is expressed in the neural tube of early stage embryos."
      Obata J., Yano M., Mimura H., Goto T., Nakayama R., Mibu Y., Oka C., Kawaichi M.
      Genes Cells 6:345-360(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTF1A.
      Strain: ICR.
      Tissue: Embryo.
    10. "Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression."
      Kao H.-Y., Downes M., Ordentlich P., Evans R.M.
      Genes Dev. 14:55-66(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NCOR2 AND HDAC1.
    11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSUH_MOUSE
    AccessioniPrimary (citable) accession number: P31266
    Secondary accession number(s): Q80UN8, Q8C4Z3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3