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Q09472

- EP300_HUMAN

UniProt

Q09472 - EP300_HUMAN

Protein

Histone acetyltransferase p300

Gene

EP300

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    Functions as histone acetyltransferase and regulates transcription via chromatin remodeling. Acetylates all four core histones in nucleosomes. Histone acetylation gives an epigenetic tag for transcriptional activation. Mediates cAMP-gene regulation by binding specifically to phosphorylated CREB protein. Mediates acetylation of histone H3 at 'Lys-122' (H3K122ac), a modification that localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability. Mediates acetylation of histone H3 at 'Lys-27' (H3K27ac). Also functions as acetyltransferase for nonhistone targets. Acetylates 'Lys-131' of ALX1 and acts as its coactivator in the presence of CREBBP. Acetylates SIRT2 and is proposed to indirectly increase the transcriptional activity of TP53 through acetylation and subsequent attenuation of SIRT2 deacetylase function. Acetylates HDAC1 leading to its inactivation and modulation of transcription. Acts as a TFAP2A-mediated transcriptional coactivator in presence of CITED2. Plays a role as a coactivator of NEUROD1-dependent transcription of the secretin and p21 genes and controls terminal differentiation of cells in the intestinal epithelium. Promotes cardiac myocyte enlargement. Can also mediate transcriptional repression. Binds to and may be involved in the transforming capacity of the adenovirus E1A protein. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Acetylates FOXO1 and enhances its transcriptional activity. Acetylates BCL6 wich disrupts its ability to recruit histone deacetylases and hinders its transcriptional repressor activity. Participates in CLOCK or NPAS2-regulated rhythmic gene transcription; exhibits a circadian association with CLOCK or NPAS2, correlating with increase in PER1/2 mRNA and histone H3 acetylation on the PER1/2 promoter. Acetylates MTA1 at 'Lys-626' which is essential for its transcriptional coactivator activity.15 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei31 – 322Breakpoint for translocation to form KAT6A-EP300 and EP300-KAT6A
    Metal bindingi347 – 3471Zinc 1
    Metal bindingi351 – 3511Zinc 1
    Metal bindingi364 – 3641Zinc 1
    Metal bindingi369 – 3691Zinc 1
    Metal bindingi378 – 3781Zinc 2
    Metal bindingi382 – 3821Zinc 2
    Metal bindingi388 – 3881Zinc 2
    Metal bindingi393 – 3931Zinc 2
    Metal bindingi402 – 4021Zinc 3
    Metal bindingi406 – 4061Zinc 3
    Metal bindingi411 – 4111Zinc 3
    Metal bindingi414 – 4141Zinc 3
    Sitei2088 – 20881Interaction with NCOA2
    Sitei2142 – 21421Interaction with NCOA2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri331 – 41787TAZ-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1664 – 170744ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1728 – 180982TAZ-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. activating transcription factor binding Source: UniProtKB
    3. androgen receptor binding Source: BHF-UCL
    4. antigen binding Source: Ensembl
    5. beta-catenin binding Source: BHF-UCL
    6. chromatin binding Source: UniProtKB
    7. chromatin DNA binding Source: Ensembl
    8. core promoter binding Source: UniProtKB
    9. DNA binding Source: UniProtKB
    10. histone acetyltransferase activity Source: UniProtKB
    11. lysine N-acetyltransferase activity, acting on acetyl phosphate as donor Source: UniProtKB
    12. nuclear hormone receptor binding Source: UniProtKB
    13. protein binding Source: UniProtKB
    14. RNA polymerase II activating transcription factor binding Source: BHF-UCL
    15. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
    16. transcription coactivator activity Source: UniProtKB
    17. transcription factor binding Source: UniProtKB
    18. transferase activity, transferring acyl groups Source: UniProtKB
    19. zinc ion binding Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cellular response to hydrogen peroxide Source: Ensembl
    3. cellular response to hypoxia Source: Reactome
    4. cellular response to organic cyclic compound Source: Ensembl
    5. chromatin organization Source: Reactome
    6. circadian rhythm Source: UniProtKB
    7. digestive tract development Source: Ensembl
    8. G2/M transition of mitotic cell cycle Source: Reactome
    9. heart development Source: Ensembl
    10. histone H2B acetylation Source: UniProtKB
    11. histone H4 acetylation Source: UniProtKB
    12. innate immune response Source: Reactome
    13. internal peptidyl-lysine acetylation Source: UniProtKB
    14. internal protein amino acid acetylation Source: UniProtKB
    15. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
    16. liver development Source: Ensembl
    17. lung development Source: Ensembl
    18. mitotic cell cycle Source: Reactome
    19. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    20. nervous system development Source: ProtInc
    21. Notch signaling pathway Source: Reactome
    22. N-terminal peptidyl-lysine acetylation Source: UniProtKB
    23. organ morphogenesis Source: Ensembl
    24. positive regulation by host of viral transcription Source: BHF-UCL
    25. positive regulation of axon extension Source: Ensembl
    26. positive regulation of cell death Source: Ensembl
    27. positive regulation of cell size Source: Ensembl
    28. positive regulation of collagen biosynthetic process Source: Ensembl
    29. positive regulation of DNA binding Source: Ensembl
    30. positive regulation of glycoprotein biosynthetic process Source: Ensembl
    31. positive regulation of protein binding Source: Ensembl
    32. positive regulation of protein import into nucleus, translocation Source: Ensembl
    33. positive regulation of protein phosphorylation Source: Ensembl
    34. positive regulation of protein secretion Source: Ensembl
    35. positive regulation of proteolysis Source: Ensembl
    36. positive regulation of sarcomere organization Source: Ensembl
    37. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    38. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    39. positive regulation of translation Source: Ensembl
    40. positive regulation of type I interferon production Source: Reactome
    41. protein-DNA complex assembly Source: Ensembl
    42. protein kinase B signaling Source: Ensembl
    43. regulation of androgen receptor signaling pathway Source: BHF-UCL
    44. regulation of angiotensin metabolic process Source: Ensembl
    45. regulation of cell cycle Source: Reactome
    46. regulation of transcription, DNA-templated Source: UniProtKB
    47. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    48. regulation of tubulin deacetylation Source: UniProtKB
    49. response to calcium ion Source: Ensembl
    50. response to cobalt ion Source: Ensembl
    51. response to drug Source: Ensembl
    52. response to estrogen Source: UniProtKB
    53. response to ethanol Source: Ensembl
    54. response to fatty acid Source: Ensembl
    55. response to glucocorticoid Source: Ensembl
    56. response to glucose Source: Ensembl
    57. response to hypoxia Source: UniProtKB
    58. response to retinoic acid Source: Ensembl
    59. response to tumor necrosis factor Source: Ensembl
    60. skeletal muscle tissue development Source: Ensembl
    61. somitogenesis Source: Ensembl
    62. transcription, DNA-templated Source: UniProtKB-KW
    63. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Biological rhythms, Cell cycle, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1006. Polo-like kinase mediated events.
    REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_163910. NOTCH2 intracellular domain regulates transcription.
    REACT_172610. HATs acetylate histones.
    REACT_200624. Attenuation phase.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24941. Circadian Clock.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinkiQ09472.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase p300 (EC:2.3.1.48)
    Short name:
    p300 HAT
    Alternative name(s):
    E1A-associated protein p300
    Gene namesi
    Name:EP300
    Synonyms:P300
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:3373. EP300.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: In the presence of ALX1 relocalizes from the cytoplasm to the nucleus. Colocalizes with ROCK2 in the nucleus.

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. cytoplasm Source: HPA
    3. histone acetyltransferase complex Source: Ensembl
    4. nucleoplasm Source: Reactome
    5. nucleus Source: UniProtKB
    6. protein-DNA complex Source: Ensembl
    7. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in EP300 may play a role in epithelial cancer.
    Chromosomal aberrations involving EP300 may be a cause of acute myeloid leukemias. Translocation t(8;22)(p11;q13) with KAT6A.
    Rubinstein-Taybi syndrome 2 (RSTS2) [MIM:613684]: A disorder characterized by craniofacial abnormalities, postnatal growth deficiency, broad thumbs, broad big toes, mental retardation and a propensity for development of malignancies. Some individuals with RSTS2 have less severe mental impairment, more severe microcephaly, and a greater degree of changes in facial bone structure than RSTS1 patients.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi89 – 891S → A: Abolishes AMPK-mediated phosphorylation. 2 Publications
    Mutagenesisi89 – 891S → D: Phosphomimetic mutant that leads to descreased interaction with nuclear receptors. 2 Publications
    Mutagenesisi344 – 3441L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-345. 2 Publications
    Mutagenesisi345 – 3451L → A: Inhibits interaction with HIF1A and transcription activation; when associated with A-344. 2 Publications
    Mutagenesisi371 – 3766TMKNVL → NAAIRS: Inhibits interaction with HIF1A. Reduces interaction with CITED2. 1 Publication
    Mutagenesisi413 – 4186VCLPLK → NAAIRS: Inhibits interaction with HIF1A. Does not inhibit interaction with CITED2. 1 Publication
    Mutagenesisi1020 – 10201K → A: Abolishes sumoylation and transcriptional repression when associated with A-1024. 3 Publications
    Mutagenesisi1020 – 10201K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1024. 3 Publications
    Mutagenesisi1024 – 10241K → A: Abolishes sumoylation and transcriptional repression; when associated with A-1020. 3 Publications
    Mutagenesisi1024 – 10241K → R: Abolishes sumoylation and transcriptional repression; when associated with R-1020. 3 Publications
    Mutagenesisi1357 – 13571T → L: 40% decrease in activity. 2 Publications
    Mutagenesisi1357 – 13571T → R: 40% decrease in activity. 90% decrease in activity; when associated with R-1505; R-1625 and R-1628. 2 Publications
    Mutagenesisi1396 – 13961S → R: Loss of activity; when associated with R-1397. 2 Publications
    Mutagenesisi1396 – 13961S → W: Loss of activity; when associated with W-1396. 2 Publications
    Mutagenesisi1397 – 13971Y → R: Loss of activity; when associated with R-1396. 2 Publications
    Mutagenesisi1397 – 13971Y → W: Loss of activity; when associated with W-1397. 2 Publications
    Mutagenesisi1399 – 13991D → Y: Does not interact with TFAP2A and inhibits transcriptional coactivation of TFAP2A by CITED2. Does not inhibit interaction with CITED2, DNA-binding of TFAP2A or nuclear localization of TFAP2A or CITED2. No enhancement of FOXO1-mediated transcriptional activity. No inhibition of insulin-mediated translocation to the cytoplasm. 3 Publications
    Mutagenesisi1505 – 15051E → R: 90% decrease in activity; when associated with R-1625 and R-1628. 90% decrease in activity; when associated with R-1357; R-1625 and R-1628. 2 Publications
    Mutagenesisi1625 – 16251D → R: 70% decrease in activity; when associated with R-1628. 90% decrease in activity; when associated with R-1505 and R-1628. 90% decrease in activity; when associated with R-1357; R-1505 and R-1628. 2 Publications
    Mutagenesisi1628 – 16281D → R: 70% decrease in activity; when associated with R-1625. 90% decrease in activity; when associated with E-1505 and R-1625. 90% decrease in activity; when associated with R-1357; R-1505 and R-1625. 2 Publications
    Mutagenesisi2056 – 20561R → K: No effect on interaction with NCOA2. 2 Publications
    Mutagenesisi2088 – 20881R → K: Abolishes interaction with NCOA2. 2 Publications
    Mutagenesisi2142 – 21421R → K: Strongly reduces interaction with NCOA2. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613684. phenotype.
    Orphaneti353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
    PharmGKBiPA27807.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 24142413Histone acetyltransferase p300PRO_0000211193Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei89 – 891Phosphoserine; by AMPK2 Publications
    Modified residuei285 – 2851Phosphoserine
    Modified residuei418 – 4181N6-acetyllysine2 Publications
    Modified residuei423 – 4231N6-acetyllysine2 Publications
    Modified residuei580 – 5801Omega-N-methylated arginine; by CARM11 Publication
    Modified residuei604 – 6041Omega-N-methylated arginine; by CARM11 Publication
    Modified residuei636 – 6361N6-acetyllysine2 Publications
    Modified residuei885 – 8851Phosphothreonine
    Modified residuei887 – 8871Phosphothreonine
    Modified residuei977 – 9771N6-acetyllysine2 Publications
    Modified residuei1020 – 10201N6-acetyllysine; alternate2 Publications
    Cross-linki1020 – 1020Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei1024 – 10241N6-acetyllysine; alternate2 Publications
    Cross-linki1024 – 1024Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
    Modified residuei1038 – 10381Phosphoserine1 Publication
    Modified residuei1180 – 11801N6-acetyllysineBy similarity
    Modified residuei1336 – 13361N6-acetyllysine2 Publications
    Modified residuei1473 – 14731N6-acetyllysine2 Publications
    Modified residuei1499 – 14991N6-acetyllysine; by autocatalysis2 Publications
    Modified residuei1542 – 15421N6-acetyllysine3 Publications
    Modified residuei1546 – 15461N6-acetyllysine3 Publications
    Modified residuei1549 – 15491N6-acetyllysine; by autocatalysis3 Publications
    Modified residuei1554 – 15541N6-acetyllysine; by autocatalysis3 Publications
    Modified residuei1555 – 15551N6-acetyllysine2 Publications
    Modified residuei1558 – 15581N6-acetyllysine3 Publications
    Modified residuei1560 – 15601N6-acetyllysine; by autocatalysis3 Publications
    Modified residuei1583 – 15831N6-acetyllysine2 Publications
    Modified residuei1699 – 16991N6-acetyllysine2 Publications
    Modified residuei1704 – 17041N6-acetyllysine2 Publications
    Modified residuei1707 – 17071N6-acetyllysine2 Publications
    Modified residuei1734 – 17341Phosphoserine
    Modified residuei1857 – 18571Phosphothreonine
    Modified residuei1859 – 18591Phosphothreonine
    Modified residuei2142 – 21421Asymmetric dimethylarginine; by CARM1; alternate1 Publication
    Modified residuei2142 – 21421Citrulline; by PADI4; alternate1 Publication

    Post-translational modificationi

    Acetylated on Lys at up to 17 positions by intermolecular autocatalysis. Deacetylated in the transcriptional repression domain (CRD1) by SIRT1, preferentially at Lys-1020. Deacetylated by SIRT2, preferentially at Lys-418, Lys-423, Lys-1542, Lys-1546, Lys-1549, Lys-1699, Lys-1704 and Lys-1707.8 Publications
    Citrullinated at Arg-2142 by PADI4, which impairs methylation by CARM1 and promotes interaction with NCOA2/GRIP1.2 Publications
    Methylated at Arg-580 and Arg-604 in the KIX domain by CARM1, which blocks association with CREB, inhibits CREB signaling and activates apoptotic response. Also methylated at Arg-2142 by CARM1, which impairs interaction with NCOA2/GRIP1.2 Publications
    Sumoylated; sumoylation in the transcriptional repression domain (CRD1) mediates transcriptional repression. Desumoylated by SENP3 through the removal of SUMO2 and SUMO3.2 Publications
    Probable target of ubiquitination by FBXO3, leading to rapid proteasome-dependent degradation.
    Phosphorylated by HIPK2 in a RUNX1-dependent manner. This phosphorylation that activates EP300 happens when RUNX1 is associated with DNA and CBFB. Phosphorylated by ROCK2 and this enhances its activity. Phosphorylation at Ser-89 by AMPK reduces interaction with nuclear receptors, such as PPARG.5 Publications

    Keywords - PTMi

    Acetylation, Citrullination, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ09472.
    PaxDbiQ09472.
    PRIDEiQ09472.

    PTM databases

    PhosphoSiteiQ09472.

    Expressioni

    Gene expression databases

    ArrayExpressiQ09472.
    BgeeiQ09472.
    CleanExiHS_EP300.
    GenevestigatoriQ09472.

    Organism-specific databases

    HPAiCAB000146.
    HPA003128.
    HPA004112.

    Interactioni

    Subunit structurei

    Interacts with phosphorylated CREB1. Interacts with HIF1A; the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts (via N-terminus) with TFAP2A (via N-terminus); the interaction requires CITED2. Interacts (via CH1 domain) with CITED2 (via C-terminus). Interacts with CITED1 (unphosphorylated form preferentially and via C-terminus). Interacts with ESR1; the interaction is estrogen-dependent and enhanced by CITED1. Interacts with DTX1, EID1, ELF3, FEN1, LEF1, NCOA1, NCOA6, NR3C1, PCAF, PELP1, PRDM6, SP1, SP3, SPIB, SRY, TCF7L2, TP53, DDX5, DDX17, SATB1, SRCAP, TTC5, JMY and TRERF1. The TAZ-type 1 domain interacts with HIF1A. Probably part of a complex with HIF1A and CREBBP. Part of a complex containing CARM1 and NCOA2/GRIP1. Interacts with ING4 and this interaction may be indirect. Interacts with ING5. Interacts with the C-terminal region of CITED4. Non-sumoylated EP300 preferentially interacts with SENP3. Interacts with SS18L1/CREST. Interacts with ALX1 (via homeobox domain). Interacts with NEUROD1; the interaction is inhibited by NR0B2. Interacts with TCF3. Interacts (via CREB-binding domain) with MYOCD (via C-terminus). Binds to HIPK2. Interacts with ROCK2 and PPARG. Forms a complex made of CDK9, CCNT1/cyclin-T1, EP300 and GATA4 that stimulates hypertrophy in cardiomyocytes. Interacts with IRF1 and this interaction enhances acetylation of p53/TP53 and stimulation of its activity. Interacts with FOXO1; the interaction acetylates FOXO1 and enhances its transcriptional activity. Interacts with ALKBH4 and DDIT3/CHOP. Interacts with KLF15. Interacts with CEBPB and RORA. Interacts with HTLV-1 Tax and p30II. Interacts with and acetylates HIV-1 Tat. Interacts with NPAS2, ARNTL/BMAL1 and CLOCK. Interacts with SIRT2 isoform 1, isoform 2 and isoform 5. Interacts with MTA1. Interacts with HDAC4 and HDAC5 in the presence of TFAP2C.57 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P030702EBI-447295,EBI-617698From a different organism.
    P032553EBI-447295,EBI-2603114From a different organism.
    P03255-23EBI-447295,EBI-6859460From a different organism.
    P032593EBI-447295,EBI-6947456From a different organism.
    APEX1P276958EBI-447295,EBI-1048805
    ASH2LQ9UBL35EBI-447295,EBI-540797
    BRD7Q9NPI13EBI-447295,EBI-711221
    CDK2P249415EBI-447295,EBI-375096
    CITED2Q999673EBI-447295,EBI-937732
    COPS2P612012EBI-447295,EBI-1050386
    CREB1P162202EBI-447295,EBI-711855
    Creb1Q011472EBI-447295,EBI-2291098From a different organism.
    DDX5P178444EBI-447295,EBI-351962
    E2P031223EBI-447295,EBI-7028618From a different organism.
    E2P064227EBI-447295,EBI-7136851From a different organism.
    E2P067906EBI-447295,EBI-7010629From a different organism.
    ESR1P033722EBI-447295,EBI-78473
    GTF2BQ004032EBI-447295,EBI-389564
    HIF1AQ1666515EBI-447295,EBI-447269
    Hif1aQ612212EBI-447295,EBI-298954From a different organism.
    HIPK2Q9H2X64EBI-447295,EBI-348345
    JmyQ9QXM116EBI-447295,EBI-866001From a different organism.
    KAT2BQ928312EBI-447295,EBI-477430
    NAP1L1P552093EBI-447295,EBI-356392
    NBNO609345EBI-447295,EBI-494844
    NCOA3Q9Y6Q92EBI-447295,EBI-81196
    POU3F2P202653EBI-447295,EBI-1167176
    PPP1R13BQ96KQ42EBI-447295,EBI-1105153
    PPP1R13LQ8WUF52EBI-447295,EBI-5550163
    RUNX3Q137617EBI-447295,EBI-925990
    SIRT1Q96EB62EBI-447295,EBI-1802965
    SKP2Q133093EBI-447295,EBI-456291
    STAT6P422262EBI-447295,EBI-1186478
    TFAP2AP055497EBI-447295,EBI-347351
    TP53P0463710EBI-447295,EBI-366083
    TP53BP2Q136252EBI-447295,EBI-77642
    VDRP114733EBI-447295,EBI-286357
    YBX1P678092EBI-447295,EBI-354065

    Protein-protein interaction databases

    BioGridi108347. 384 interactions.
    DIPiDIP-257N.
    IntActiQ09472. 170 interactions.
    MINTiMINT-104535.
    STRINGi9606.ENSP00000263253.

    Structurei

    Secondary structure

    1
    2414
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi332 – 3343
    Helixi335 – 35521
    Turni356 – 3583
    Helixi367 – 37913
    Beta strandi386 – 3894
    Helixi391 – 40515
    Beta strandi408 – 4103
    Helixi414 – 4185
    Helixi1051 – 106616
    Turni1069 – 10724
    Helixi1073 – 10753
    Helixi1081 – 10844
    Helixi1089 – 10924
    Helixi1099 – 11079
    Helixi1114 – 113118
    Helixi1137 – 115923
    Beta strandi1178 – 11825
    Beta strandi1190 – 11945
    Turni1195 – 11973
    Beta strandi1198 – 12014
    Helixi1202 – 12065
    Beta strandi1212 – 12143
    Beta strandi1218 – 12214
    Beta strandi1225 – 12273
    Helixi1228 – 12303
    Beta strandi1231 – 12366
    Beta strandi1244 – 12463
    Turni1248 – 12503
    Beta strandi1253 – 12553
    Helixi1256 – 12594
    Turni1263 – 12653
    Helixi1273 – 12775
    Turni1278 – 12803
    Helixi1297 – 131317
    Beta strandi1321 – 133414
    Helixi1339 – 13424
    Turni1343 – 13475
    Beta strandi1351 – 136616
    Beta strandi1369 – 138113
    Beta strandi1392 – 14009
    Helixi1407 – 14093
    Helixi1410 – 142819
    Beta strandi1432 – 14365
    Beta strandi1446 – 14505
    Helixi1460 – 147617
    Beta strandi1482 – 14854
    Helixi1486 – 14938
    Helixi1498 – 15003
    Helixi1508 – 151710
    Helixi1582 – 15909
    Helixi1592 – 15943
    Beta strandi1595 – 16017
    Helixi1603 – 16064
    Helixi1622 – 16243
    Beta strandi1625 – 16273
    Helixi1628 – 16369
    Helixi1644 – 166219
    Helixi1730 – 174718
    Helixi1756 – 177015
    Turni1774 – 17785
    Helixi1780 – 179314
    Helixi1806 – 181813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L3ENMR-B323-423[»]
    1P4QNMR-B323-423[»]
    2K8FNMR-A1723-1812[»]
    3BIYX-ray1.70A1287-1666[»]
    3I3JX-ray2.33A/B/C/D/E/F/G/H/I/J/K/L1040-1161[»]
    3IO2X-ray2.50A1723-1836[»]
    3P57X-ray2.19P1726-1835[»]
    3T92X-ray1.50A1723-1818[»]
    4BHWX-ray2.80A/B1043-1519[»]
    A/B1581-1666[»]
    4PZRX-ray2.10A1287-1664[»]
    4PZSX-ray1.94A1287-1664[»]
    4PZTX-ray2.80A1287-1664[»]
    DisProtiDP00633.
    ProteinModelPortaliQ09472.
    SMRiQ09472. Positions 323-423, 566-646, 1046-1713, 1726-1834, 2050-2092.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ09472.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini566 – 64580KIXPROSITE-ProRule annotationAdd
    BLAST
    Domaini1067 – 113973BromoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 149148Interaction with RORAAdd
    BLAST
    Regioni2 – 139138Interaction with ALX1Add
    BLAST
    Regioni1017 – 102913CRD1; mediates transcriptional repressionAdd
    BLAST
    Regioni1572 – 1818247Binding region for E1A adenovirusAdd
    BLAST
    Regioni2003 – 2212210Interaction with HTLV-1 TaxAdd
    BLAST
    Regioni2041 – 2240200Interaction with NCOA2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi11 – 177Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi797 – 8004Poly-Ser
    Compositional biasi1519 – 15268Poly-Glu
    Compositional biasi2066 – 20694Poly-Gln
    Compositional biasi2190 – 21956Poly-Gln

    Domaini

    The CRD1 domain (cell cycle regulatory domain 1) mediates transcriptional repression of a subset of p300 responsive genes; it can be de-repressed by CDKN1A/p21WAF1 at least at some promoters. It conatins sumoylation and acetylation sites and the same lysine residues may be targeted for the respective modifications. It is proposed that deacetylation by SIRT1 allows sumoylation leading to suppressed activity.

    Sequence similaritiesi

    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 KIX domain.PROSITE-ProRule annotation
    Contains 2 TAZ-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri331 – 41787TAZ-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1664 – 170744ZZ-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1728 – 180982TAZ-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5076.
    HOGENOMiHOG000111353.
    HOVERGENiHBG000185.
    InParanoidiQ09472.
    KOiK04498.
    OMAiPTMIRGS.
    OrthoDBiEOG75B84F.
    PhylomeDBiQ09472.
    TreeFamiTF101097.

    Family and domain databases

    Gene3Di1.10.1630.10. 1 hit.
    1.10.246.20. 1 hit.
    1.20.1020.10. 2 hits.
    1.20.920.10. 1 hit.
    InterProiIPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR010303. DUF902_CREBbp.
    IPR013178. Histone_H3-K56_AcTrfase_RTT109.
    IPR003101. KIX_dom.
    IPR009110. Nuc_rcpt_coact.
    IPR014744. Nuc_rcpt_coact_CREBbp.
    IPR000197. Znf_TAZ.
    IPR000433. Znf_ZZ.
    [Graphical view]
    PfamiPF00439. Bromodomain. 1 hit.
    PF09030. Creb_binding. 1 hit.
    PF06001. DUF902. 1 hit.
    PF08214. KAT11. 1 hit.
    PF02172. KIX. 1 hit.
    PF02135. zf-TAZ. 2 hits.
    PF00569. ZZ. 1 hit.
    [Graphical view]
    PRINTSiPR00503. BROMODOMAIN.
    SMARTiSM00297. BROMO. 1 hit.
    SM00551. ZnF_TAZ. 2 hits.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF47040. SSF47040. 1 hit.
    SSF47370. SSF47370. 1 hit.
    SSF57933. SSF57933. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50952. KIX. 1 hit.
    PS50134. ZF_TAZ. 2 hits.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q09472-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS     50
    TELGLTNGGD INQLQTSLGM VQDAASKHKQ LSELLRSGSS PNLNMGVGGP 100
    GQVMASQAQQ SSPGLGLINS MVKSPMTQAG LTSPNMGMGT SGPNQGPTQS 150
    TGMMNSPVNQ PAMGMNTGMN AGMNPGMLAA GNGQGIMPNQ VMNGSIGAGR 200
    GRQNMQYPNP GMGSAGNLLT EPLQQGSPQM GGQTGLRGPQ PLKMGMMNNP 250
    NPYGSPYTQN PGQQIGASGL GLQIQTKTVL SNNLSPFAMD KKAVPGGGMP 300
    NMGQQPAPQV QQPGLVTPVA QGMGSGAHTA DPEKRKLIQQ QLVLLLHAHK 350
    CQRREQANGE VRQCNLPHCR TMKNVLNHMT HCQSGKSCQV AHCASSRQII 400
    SHWKNCTRHD CPVCLPLKNA GDKRNQQPIL TGAPVGLGNP SSLGVGQQSA 450
    PNLSTVSQID PSSIERAYAA LGLPYQVNQM PTQPQVQAKN QQNQQPGQSP 500
    QGMRPMSNMS ASPMGVNGGV GVQTPSLLSD SMLHSAINSQ NPMMSENASV 550
    PSLGPMPTAA QPSTTGIRKQ WHEDITQDLR NHLVHKLVQA IFPTPDPAAL 600
    KDRRMENLVA YARKVEGDMY ESANNRAEYY HLLAEKIYKI QKELEEKRRT 650
    RLQKQNMLPN AAGMVPVSMN PGPNMGQPQP GMTSNGPLPD PSMIRGSVPN 700
    QMMPRITPQS GLNQFGQMSM AQPPIVPRQT PPLQHHGQLA QPGALNPPMG 750
    YGPRMQQPSN QGQFLPQTQF PSQGMNVTNI PLAPSSGQAP VSQAQMSSSS 800
    CPVNSPIMPP GSQGSHIHCP QLPQPALHQN SPSPVPSRTP TPHHTPPSIG 850
    AQQPPATTIP APVPTPPAMP PGPQSQALHP PPRQTPTPPT TQLPQQVQPS 900
    LPAAPSADQP QQQPRSQQST AASVPTPTAP LLPPQPATPL SQPAVSIEGQ 950
    VSNPPSTSST EVNSQAIAEK QPSQEVKMEA KMEVDQPEPA DTQPEDISES 1000
    KVEDCKMEST ETEERSTELK TEIKEEEDQP STSATQSSPA PGQSKKKIFK 1050
    PEELRQALMP TLEALYRQDP ESLPFRQPVD PQLLGIPDYF DIVKSPMDLS 1100
    TIKRKLDTGQ YQEPWQYVDD IWLMFNNAWL YNRKTSRVYK YCSKLSEVFE 1150
    QEIDPVMQSL GYCCGRKLEF SPQTLCCYGK QLCTIPRDAT YYSYQNRYHF 1200
    CEKCFNEIQG ESVSLGDDPS QPQTTINKEQ FSKRKNDTLD PELFVECTEC 1250
    GRKMHQICVL HHEIIWPAGF VCDGCLKKSA RTRKENKFSA KRLPSTRLGT 1300
    FLENRVNDFL RRQNHPESGE VTVRVVHASD KTVEVKPGMK ARFVDSGEMA 1350
    ESFPYRTKAL FAFEEIDGVD LCFFGMHVQE YGSDCPPPNQ RRVYISYLDS 1400
    VHFFRPKCLR TAVYHEILIG YLEYVKKLGY TTGHIWACPP SEGDDYIFHC 1450
    HPPDQKIPKP KRLQEWYKKM LDKAVSERIV HDYKDIFKQA TEDRLTSAKE 1500
    LPYFEGDFWP NVLEESIKEL EQEEEERKRE ENTSNESTDV TKGDSKNAKK 1550
    KNNKKTSKNK SSLSRGNKKK PGMPNVSNDL SQKLYATMEK HKEVFFVIRL 1600
    IAGPAANSLP PIVDPDPLIP CDLMDGRDAF LTLARDKHLE FSSLRRAQWS 1650
    TMCMLVELHT QSQDRFVYTC NECKHHVETR WHCTVCEDYD LCITCYNTKN 1700
    HDHKMEKLGL GLDDESNNQQ AAATQSPGDS RRLSIQRCIQ SLVHACQCRN 1750
    ANCSLPSCQK MKRVVQHTKG CKRKTNGGCP ICKQLIALCC YHAKHCQENK 1800
    CPVPFCLNIK QKLRQQQLQH RLQQAQMLRR RMASMQRTGV VGQQQGLPSP 1850
    TPATPTTPTG QQPTTPQTPQ PTSQPQPTPP NSMPPYLPRT QAAGPVSQGK 1900
    AAGQVTPPTP PQTAQPPLPG PPPAAVEMAM QIQRAAETQR QMAHVQIFQR 1950
    PIQHQMPPMT PMAPMGMNPP PMTRGPSGHL EPGMGPTGMQ QQPPWSQGGL 2000
    PQPQQLQSGM PRPAMMSVAQ HGQPLNMAPQ PGLGQVGISP LKPGTVSQQA 2050
    LQNLLRTLRS PSSPLQQQQV LSILHANPQL LAAFIKQRAA KYANSNPQPI 2100
    PGQPGMPQGQ PGLQPPTMPG QQGVHSNPAM QNMNPMQAGV QRAGLPQQQP 2150
    QQQLQPPMGG MSPQAQQMNM NHNTMPSQFR DILRRQQMMQ QQQQQGAGPG 2200
    IGPGMANHNQ FQQPQGVGYP PQQQQRMQHH MQQMQQGNMG QIGQLPQALG 2250
    AEAGASLQAY QQRLLQQQMG SPVQPNPMSP QQHMLPNQAQ SPHLQGQQIP 2300
    NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV SPQTSSPHPG 2350
    LVAAQANPME QGHFASPDQN SMLSQLASNP GMANLHGASA TDLGLSTDNS 2400
    DLNSNLSQST LDIH 2414
    Length:2,414
    Mass (Da):264,161
    Last modified:February 10, 2009 - v2
    Checksum:i8E869E1F174A6FEB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti169 – 1691M → T in AAA18639. (PubMed:7523245)Curated
    Sequence conflicti204 – 2041N → D in AAA18639. (PubMed:7523245)Curated
    Sequence conflicti928 – 9281T → N in AAA18639. (PubMed:7523245)Curated
    Sequence conflicti1924 – 19241A → T in AAA18639. (PubMed:7523245)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti289 – 2891M → V.
    Corresponds to variant rs2230111 [ dbSNP | Ensembl ].
    VAR_055554
    Natural varianti827 – 8271L → P in a breast cancer sample. 1 Publication
    VAR_014428
    Natural varianti997 – 9971I → V.
    Corresponds to variant rs20551 [ dbSNP | Ensembl ].
    VAR_020425
    Natural varianti1013 – 10131E → G in a breast cancer sample. 1 Publication
    VAR_014429
    Natural varianti1650 – 16501S → Y in a pancreatic cancer sample. 1 Publication
    VAR_014430
    Natural varianti2174 – 21741T → S.
    Corresponds to variant rs5758252 [ dbSNP | Ensembl ].
    VAR_038376
    Natural varianti2221 – 22211P → Q in a colorectal cancer sample. 1 Publication
    Corresponds to variant rs28937578 [ dbSNP | Ensembl ].
    VAR_014431
    Natural varianti2223 – 22231Q → P.1 Publication
    Corresponds to variant rs1046088 [ dbSNP | Ensembl ].
    VAR_038377

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01877 mRNA. Translation: AAA18639.1.
    AL080243, AL035658, AL096765 Genomic DNA. Translation: CAH70384.1.
    AL096765, AL035658, AL080243 Genomic DNA. Translation: CAH73688.1.
    AL035658, AL080243, AL096765 Genomic DNA. Translation: CAI23037.1.
    CH471095 Genomic DNA. Translation: EAW60408.1.
    CCDSiCCDS14010.1.
    PIRiA54277.
    RefSeqiNP_001420.2. NM_001429.3.
    UniGeneiHs.517517.
    Hs.655211.

    Genome annotation databases

    EnsembliENST00000263253; ENSP00000263253; ENSG00000100393.
    GeneIDi2033.
    KEGGihsa:2033.
    UCSCiuc003azl.4. human.

    Polymorphism databases

    DMDMi223590203.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    P300/CBP entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01877 mRNA. Translation: AAA18639.1 .
    AL080243 , AL035658 , AL096765 Genomic DNA. Translation: CAH70384.1 .
    AL096765 , AL035658 , AL080243 Genomic DNA. Translation: CAH73688.1 .
    AL035658 , AL080243 , AL096765 Genomic DNA. Translation: CAI23037.1 .
    CH471095 Genomic DNA. Translation: EAW60408.1 .
    CCDSi CCDS14010.1.
    PIRi A54277.
    RefSeqi NP_001420.2. NM_001429.3.
    UniGenei Hs.517517.
    Hs.655211.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L3E NMR - B 323-423 [» ]
    1P4Q NMR - B 323-423 [» ]
    2K8F NMR - A 1723-1812 [» ]
    3BIY X-ray 1.70 A 1287-1666 [» ]
    3I3J X-ray 2.33 A/B/C/D/E/F/G/H/I/J/K/L 1040-1161 [» ]
    3IO2 X-ray 2.50 A 1723-1836 [» ]
    3P57 X-ray 2.19 P 1726-1835 [» ]
    3T92 X-ray 1.50 A 1723-1818 [» ]
    4BHW X-ray 2.80 A/B 1043-1519 [» ]
    A/B 1581-1666 [» ]
    4PZR X-ray 2.10 A 1287-1664 [» ]
    4PZS X-ray 1.94 A 1287-1664 [» ]
    4PZT X-ray 2.80 A 1287-1664 [» ]
    DisProti DP00633.
    ProteinModelPortali Q09472.
    SMRi Q09472. Positions 323-423, 566-646, 1046-1713, 1726-1834, 2050-2092.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108347. 384 interactions.
    DIPi DIP-257N.
    IntActi Q09472. 170 interactions.
    MINTi MINT-104535.
    STRINGi 9606.ENSP00000263253.

    Chemistry

    BindingDBi Q09472.
    ChEMBLi CHEMBL3784.
    GuidetoPHARMACOLOGYi 2735.

    PTM databases

    PhosphoSitei Q09472.

    Polymorphism databases

    DMDMi 223590203.

    Proteomic databases

    MaxQBi Q09472.
    PaxDbi Q09472.
    PRIDEi Q09472.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263253 ; ENSP00000263253 ; ENSG00000100393 .
    GeneIDi 2033.
    KEGGi hsa:2033.
    UCSCi uc003azl.4. human.

    Organism-specific databases

    CTDi 2033.
    GeneCardsi GC22P041487.
    GeneReviewsi EP300.
    H-InvDB HIX0203186.
    HGNCi HGNC:3373. EP300.
    HPAi CAB000146.
    HPA003128.
    HPA004112.
    MIMi 602700. gene.
    613684. phenotype.
    neXtProti NX_Q09472.
    Orphaneti 353284. Rubinstein-Taybi syndrome due to EP300 haploinsufficiency.
    PharmGKBi PA27807.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOGENOMi HOG000111353.
    HOVERGENi HBG000185.
    InParanoidi Q09472.
    KOi K04498.
    OMAi PTMIRGS.
    OrthoDBi EOG75B84F.
    PhylomeDBi Q09472.
    TreeFami TF101097.

    Enzyme and pathway databases

    Reactomei REACT_1006. Polo-like kinase mediated events.
    REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118568. Pre-NOTCH Transcription and Translation.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_163743. LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production.
    REACT_163910. NOTCH2 intracellular domain regulates transcription.
    REACT_172610. HATs acetylate histones.
    REACT_200624. Attenuation phase.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.
    REACT_24938. TRAF6 mediated IRF7 activation.
    REACT_24941. Circadian Clock.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    REACT_25026. TRAF3-dependent IRF activation pathway.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.
    SignaLinki Q09472.

    Miscellaneous databases

    ChiTaRSi EP300. human.
    EvolutionaryTracei Q09472.
    GeneWikii EP300.
    GenomeRNAii 2033.
    NextBioi 8251.
    PROi Q09472.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q09472.
    Bgeei Q09472.
    CleanExi HS_EP300.
    Genevestigatori Q09472.

    Family and domain databases

    Gene3Di 1.10.1630.10. 1 hit.
    1.10.246.20. 1 hit.
    1.20.1020.10. 2 hits.
    1.20.920.10. 1 hit.
    InterProi IPR001487. Bromodomain.
    IPR018359. Bromodomain_CS.
    IPR010303. DUF902_CREBbp.
    IPR013178. Histone_H3-K56_AcTrfase_RTT109.
    IPR003101. KIX_dom.
    IPR009110. Nuc_rcpt_coact.
    IPR014744. Nuc_rcpt_coact_CREBbp.
    IPR000197. Znf_TAZ.
    IPR000433. Znf_ZZ.
    [Graphical view ]
    Pfami PF00439. Bromodomain. 1 hit.
    PF09030. Creb_binding. 1 hit.
    PF06001. DUF902. 1 hit.
    PF08214. KAT11. 1 hit.
    PF02172. KIX. 1 hit.
    PF02135. zf-TAZ. 2 hits.
    PF00569. ZZ. 1 hit.
    [Graphical view ]
    PRINTSi PR00503. BROMODOMAIN.
    SMARTi SM00297. BROMO. 1 hit.
    SM00551. ZnF_TAZ. 2 hits.
    SM00291. ZnF_ZZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47040. SSF47040. 1 hit.
    SSF47370. SSF47370. 1 hit.
    SSF57933. SSF57933. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEi PS00633. BROMODOMAIN_1. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50952. KIX. 1 hit.
    PS50134. ZF_TAZ. 2 hits.
    PS01357. ZF_ZZ_1. 1 hit.
    PS50135. ZF_ZZ_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and functional analysis of the adenovirus E1A-associated 300-kD protein (p300) reveals a protein with properties of a transcriptional adaptor."
      Eckner R., Ewen M.E., Newsome D., Gerdes M., Decaprio J.A., Lawrence J.B., Livingston D.M.
      Genes Dev. 8:869-884(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-2223.
    2. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-42, CHROMOSOMAL TRANSLOCATION WITH KAT6A.
    5. "Adenoviral E1A-associated protein p300 as a functional homologue of the transcriptional co-activator CBP."
      Lundblad J.R., Kwok R.P.S., Laurance M.E., Harter M.L., Goodman R.H.
      Nature 374:85-88(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 552-660.
    6. "A transcriptional switch mediated by cofactor methylation."
      Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
      Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH CARM1, METHYLATION AT ARG-580 AND ARG-604, FUNCTION.
    7. "The transcriptional coactivators p300 and CBP are histone acetyltransferases."
      Ogryzko V.V., Schiltz R.L., Russanova V., Howard B.H., Nakatani Y.
      Cell 87:953-959(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY.
    8. "A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A."
      Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.
      Nature 382:319-324(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCAF.
    9. Cited for: INTERACTION WITH HIF1A AND CREBBP.
    10. "Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300."
      Bex F., Yin M.-J., Burny A., Gaynor R.B.
      Mol. Cell. Biol. 18:2392-2405(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX.
    11. "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex."
      Fryer C.J., Archer T.K.
      Nature 393:88-91(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR3C1.
    12. Cited for: INTERACTION WITH HIV-1 TAT.
    13. "Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1."
      Bhattacharya S., Michels C.M., Leung M.K., Arany Z.P., Kung A.L., Livingston D.M.
      Genes Dev. 13:64-75(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED2 AND HIF1A, MUTAGENESIS OF 371-THR--LEU-376 AND 413-VAL--LYS-418.
    14. "Exogenous expression of a dominant negative RORalpha1 vector in muscle cells impairs differentiation: RORalpha1 directly interacts with p300 and myoD."
      Lau P., Bailey P., Dowhan D.H., Muscat G.E.
      Nucleic Acids Res. 27:411-420(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RORA.
    15. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
      Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
      J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED1.
    16. "A novel transcriptional repression domain mediates p21(WAF1/CIP1) induction of p300 transactivation."
      Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.
      Mol. Cell. Biol. 20:2676-2686(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION.
    17. Erratum
      Snowden A.W., Anderson L.A., Webster G.A., Perkins N.D.
      Mol. Cell. Biol. 20:5360-5360(2000)
    18. "Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle."
      Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.
      Mol. Cell. Biol. 20:8889-8902(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EID1.
    19. "A novel Rb- and p300-binding protein inhibits transactivation by MyoD."
      MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.
      Mol. Cell. Biol. 20:8903-8915(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EID1.
    20. "Thyroid hormone receptor-binding protein, an LXXLL motif-containing protein, functions as a general coactivator."
      Ko L., Cardona G.R., Chin W.W.
      Proc. Natl. Acad. Sci. U.S.A. 97:6212-6217(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NCOA6.
    21. "Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones."
      Deng L., de la Fuente C., Fu P., Wang L., Donnelly R., Wade J.D., Lambert P., Li H., Lee C.-G., Kashanchi F.
      Virology 277:278-295(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    22. "Selective coactivation of estrogen-dependent transcription by CITED1 CBP/p300-binding protein."
      Yahata T., Shao W., Endoh H., Hur J., Coser K.R., Sun H., Ueda Y., Kato S., Isselbacher K.J., Brown M., Shioda T.
      Genes Dev. 15:2598-2612(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESR1.
    23. "Regulation of transcription by AMP-activated protein kinase: phosphorylation of p300 blocks its interaction with nuclear receptors."
      Yang W., Hong Y.H., Shen X.Q., Frankowski C., Camp H.S., Leff T.
      J. Biol. Chem. 276:38341-38344(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-89, MUTAGENESIS OF SER-89, INTERACTION WITH PPARG.
    24. "Adenovirus DNA binding protein interacts with the SNF2-related CBP activator protein (SrCap) and inhibits SrCap-mediated transcription."
      Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E., Chrivia J., Yaciuk P.
      J. Virol. 75:10033-10040(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRCAP.
    25. "The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation."
      Scoggin K.E.S., Ulloa A., Nyborg J.K.
      Mol. Cell. Biol. 21:5520-5530(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 TAX.
    26. "Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300."
      Zhang W., Nisbet J.W., Albrecht B., Ding W., Kashanchi F., Bartoe J.T., Lairmore M.D.
      J. Virol. 75:9885-9895(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P30II.
    27. "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression."
      Gizard F., Lavallee B., DeWitte F., Hum D.W.
      J. Biol. Chem. 276:33881-33892(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRERF1.
    28. "Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha."
      Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A., Kumar R.
      J. Biol. Chem. 276:38272-38279(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELP1.
    29. Cited for: INTERACTION WITH DTX1.
    30. "Regulation of human flap endonuclease-1 activity by acetylation through the transcriptional coactivator p300."
      Hasan S., Stucki M., Hassa P.O., Imhof R., Gehrig P., Hunziker P., Hubscher U., Hottiger M.O.
      Mol. Cell 7:1221-1231(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FEN1.
    31. "Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb."
      Yamamoto H., Kihara-Negishi F., Yamada T., Suzuki M., Nakano T., Oikawa T.
      Cell Growth Differ. 13:69-75(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPIB.
    32. "Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2."
      Braganca J., Swingler T., Marques F.I.R., Jones T., Eloranta J.J., Hurst H.C., Shioda T., Bhattacharya S.
      J. Biol. Chem. 277:8559-8565(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED4.
    33. "Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities."
      Lee Y.-H., Koh S.S., Zhang X., Cheng X., Stallcup M.R.
      Mol. Cell. Biol. 22:3621-3632(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CARM1 AND NCOA2.
    34. "Acetylation inactivates the transcriptional repressor BCL6."
      Bereshchenko O.R., Gu W., Dalla-Favera R.
      Nat. Genet. 32:606-613(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BCL6 ACETYLATION.
    35. "p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity."
      Shiseki M., Nagashima M., Pedeux R.M., Kitahama-Shiseki M., Miura K., Okamura S., Onogi H., Higashimoto Y., Appella E., Yokota J., Harris C.C.
      Cancer Res. 63:2373-2378(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ING4 AND ING5.
    36. "Identification of a promoter-specific transcriptional activation domain at the C-terminus of the Wnt effector protein T-cell factor 4."
      Hecht A., Stemmler M.P.
      J. Biol. Chem. 278:3776-3785(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH TCF7L2 AND LEF1.
    37. "Physical and functional interactions among AP-2 transcription factors, p300/CREB-binding protein, and CITED2."
      Braganca J., Eloranta J.J., Bamforth S.D., Ibbitt J.C., Hurst H.C., Bhattacharya S.
      J. Biol. Chem. 278:16021-16029(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CITED2 AND TFAP2A, MUTAGENESIS OF ASP-1399.
    38. Cited for: INTERACTION WITH SP3.
    39. "P300/CBP acts as a coactivator to cartilage homeoprotein-1 (Cart1), paired-like homeoprotein, through acetylation of the conserved lysine residue adjacent to the homeodomain."
      Iioka T., Furukawa K., Yamaguchi A., Shindo H., Yamashita S., Tsukazaki T.
      J. Bone Miner. Res. 18:1419-1429(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ALX1.
    40. "SATB1 makes a complex with p300 and represses gp91(phox) promoter activity."
      Fujii Y., Kumatori A., Nakamura M.
      Microbiol. Immunol. 47:803-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SATB1.
    41. Cited for: SUMOYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
    42. "Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300."
      Rossow K.L., Janknecht R.
      Oncogene 22:151-156(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX5.
    43. "Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53."
      An W., Kim J., Roeder R.G.
      Cell 117:735-748(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TP53, FUNCTION.
    44. "Regulation of human SRY subcellular distribution by its acetylation/deacetylation."
      Thevenet L., Mejean C., Moniot B., Bonneaud N., Galeotti N., Aldrian-Herrada G., Poulat F., Berta P., Benkirane M., Boizet-Bonhoure B.
      EMBO J. 23:3336-3345(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRY.
    45. "Histone acetyltransferase-dependent chromatin remodeling and the vascular clock."
      Curtis A.M., Seo S.B., Westgate E.J., Rudic R.D., Smyth E.M., Chakravarti D., FitzGerald G.A., McNamara P.
      J. Biol. Chem. 279:7091-7097(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPAS2; ARNTL/BMAL1 AND CLOCK.
    46. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
      Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
      J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELF3.
    47. "Interferon regulatory factor 1 binding to p300 stimulates DNA-dependent acetylation of p53."
      Dornan D., Eckert M., Wallace M., Shimizu H., Ramsay E., Hupp T.R., Ball K.L.
      Mol. Cell. Biol. 24:10083-10098(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRF1.
    48. Cited for: ACETYLATION AT LYS-1499; LYS-1549; LYS-1554; LYS-1558 AND LYS-1560.
    49. "Orphan nuclear receptor small heterodimer partner, a novel corepressor for a basic helix-loop-helix transcription factor BETA2/neuroD."
      Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J., Ha H., Shong M., Tsai M.J., Choi H.S.
      Mol. Endocrinol. 18:776-790(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEUROD1 AND TCF3.
    50. "Dendrite development regulated by CREST, a calcium-regulated transcriptional activator."
      Aizawa H., Hu S.-C., Bobb K., Balakrishnan K., Ince G., Gurevich I., Cowan M., Ghosh A.
      Science 303:197-202(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SS18L1/CREST.
    51. "Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease."
      Roelfsema J.H., White S.J., Ariyuerek Y., Bartholdi D., Niedrist D., Papadia F., Bacino C.A., den Dunnen J.T., van Ommen G.-J.B., Breuning M.H., Hennekam R.C., Peters D.J.M.
      Am. J. Hum. Genet. 76:572-580(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RSTS2.
    52. "SIRT1 deacetylation and repression of p300 involves lysine residues 1020/1024 within the cell cycle regulatory domain 1."
      Bouras T., Fu M., Sauve A.A., Wang F., Quong A.A., Perkins N.D., Hay R.T., Gu W., Pestell R.G.
      J. Biol. Chem. 280:10264-10276(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEACETYLATION BY SIRT1, ACETYLATION AT LYS-1020 AND LYS-1024, MUTAGENESIS OF LYS-1020 AND LYS-1024.
    53. "The coactivator p300 directly acetylates the forkhead transcription factor Foxo1 and stimulates Foxo1-induced transcription."
      Perrot V., Rechler M.M.
      Mol. Endocrinol. 19:2283-2298(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXO1, FUNCTION, MUTAGENESIS OF ASP-1399.
    54. "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination."
      Lee Y.-H., Coonrod S.A., Kraus W.L., Jelinek M.A., Stallcup M.R.
      Proc. Natl. Acad. Sci. U.S.A. 102:3611-3616(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-2142, CITRULLINATION AT ARG-2142, INTERACTION WITH NCOA2, MUTAGENESIS OF ARG-2056; ARG-2088 AND ARG-2142.
    55. Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ROCK2, PHOSPHORYLATION AT SER-89.
    56. "The transcriptional activity of CITED1 is regulated by phosphorylation in a cell cycle-dependent manner."
      Shi G., Boyle S.C., Sparrow D.B., Dunwoodie S.L., Shioda T., de Caestecker M.P.
      J. Biol. Chem. 281:27426-27435(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CITED1.
    57. "Kinetic and mass spectrometric analysis of p300 histone acetyltransferase domain autoacetylation."
      Karanam B., Jiang L., Wang L., Kelleher N.L., Cole P.A.
      J. Biol. Chem. 281:40292-40301(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-1336 AND LYS-1473, IDENTIFICATION BY MASS SPECTROMETRY.
    58. "HDAC1 acetylation is linked to progressive modulation of steroid receptor-induced gene transcription."
      Qiu Y., Zhao Y., Becker M., John S., Parekh B.S., Huang S., Hendarwanto A., Martinez E.D., Chen Y., Lu H., Adkins N.L., Stavreva D.A., Wiench M., Georgel P.T., Schiltz R.L., Hager G.L.
      Mol. Cell 22:669-679(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACETYLATION OF HDAC1.
    59. "Sp1 deacetylation induced by phorbol ester recruits p300 to activate 12(S)-lipoxygenase gene transcription."
      Hung J.J., Wang Y.T., Chang W.C.
      Mol. Cell. Biol. 26:1770-1785(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SP1.
    60. Cited for: FUNCTION, INTERACTION WITH MTA1.
    61. Erratum
      Gururaj A.E., Singh R.R., Rayala S.K., Holm C., den Hollander P., Zhang H., Balasenthil S., Talukder A.H., Landberg G., Kumar R.
      Proc. Natl. Acad. Sci. U.S.A. 110:4147-4148(2013)
    62. "Critical and functional regulation of CHOP (C/EBP homologous protein) through the N-terminal portion."
      Ohoka N., Hattori T., Kitagawa M., Onozaki K., Hayashi H.
      J. Biol. Chem. 282:35687-35694(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDIT3.
    63. "Concerted activation of the Mdm2 promoter by p72 RNA helicase and the coactivators p300 and P/CAF."
      Shin S., Janknecht R.
      J. Cell. Biochem. 101:1252-1265(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX17.
    64. Cited for: FUNCTION IN ACETYLATION OF SIRT2.
    65. "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2: implications for leukemogenesis."
      Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.
      Blood 112:3777-3787(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY HIPK2.
    66. "PML activates transcription by protecting HIPK2 and p300 from SCFFbx3-mediated degradation."
      Shima Y., Shima T., Chiba T., Irimura T., Pandolfi P.P., Kitabayashi I.
      Mol. Cell. Biol. 28:7126-7138(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FBXO3-MEDIATED DEGRADATION.
    67. "The SIRT2 deacetylase regulates autoacetylation of p300."
      Black J.C., Mosley A., Kitada T., Washburn M., Carey M.
      Mol. Cell 32:449-455(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-418; LYS-423; LYS-1542; LYS-1546; LYS-1549; LYS-1699; LYS-1704 AND LYS-1707, DEACETYLATION BY SIRT2, FUNCTION IN TRANSCRIPTIONAL REGULATION.
    68. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    69. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    70. "SENP3 is responsible for HIF-1 transactivation under mild oxidative stress via p300 de-SUMOylation."
      Huang C., Han Y., Wang Y., Sun X., Yan S., Yeh E.T.H., Chen Y., Cang H., Li H., Shi G., Cheng J., Tang X., Yi J.
      EMBO J. 28:2748-2762(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SENP3, SUMOYLATION.
    71. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    72. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-977; LYS-1542; LYS-1546; LYS-1554; LYS-1555; LYS-1558; LYS-1560 AND LYS-1583, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    73. "Cyclin-dependent kinase-9 is a component of the p300/GATA4 complex required for phenylephrine-induced hypertrophy in cardiomyocytes."
      Sunagawa Y., Morimoto T., Takaya T., Kaichi S., Wada H., Kawamura T., Fujita M., Shimatsu A., Kita T., Hasegawa K.
      J. Biol. Chem. 285:9556-9568(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN COMPLEX WITH CCNT1; CDK9 AND GATA4.
    74. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    75. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    76. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    77. "Human ALKBH4 interacts with proteins associated with transcription."
      Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
      PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ALKBH4.
    78. "Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer."
      Tropberger P., Pott S., Keller C., Kamieniarz-Gdula K., Caron M., Richter F., Li G., Mittler G., Liu E.T., Buhler M., Margueron R., Schneider R.
      Cell 152:859-872(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    79. Cited for: FUNCTION AS ACETYLTRANSFERASE OF H3K27.
    80. Cited for: INTERACTION WITH KLF15.
    81. "Differential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1."
      Kang H.J., Lee M.H., Kang H.L., Kim S.H., Ahn J.R., Na H., Na T.Y., Kim Y.N., Seong J.K., Lee M.O.
      Cancer Res. 74:1484-1494(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC4 AND HDAC5.
    82. "Constitutive nuclear localization of an alternatively spliced sirtuin-2 isoform."
      Rack J.G., Vanlinden M.R., Lutter T., Aasland R., Ziegler M.
      J. Mol. Biol. 426:1677-1691(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH EP300.
    83. "Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha."
      Freedman S.J., Sun Z.-Y.J., Poy F., Kung A.L., Livingston D.M., Wagner G., Eck M.J.
      Proc. Natl. Acad. Sci. U.S.A. 99:5367-5372(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 302-418 IN COMPLEX WITH 786-826 OF HIF1A.
    84. "Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2."
      Freedman S.J., Sun Z.Y., Kung A.L., France D.S., Wagner G., Eck M.J.
      Nat. Struct. Biol. 10:504-512(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 323-423 IN COMPLEX WITH 216-259 OF CITED2 AND ZINC IONS, INTERACTION WITH CITED2, MUTAGENESIS OF LEU-344 AND LEU-345.
    85. "The structural basis of protein acetylation by the p300/CBP transcriptional coactivator."
      Liu X., Wang L., Zhao K., Thompson P.R., Hwang Y., Marmorstein R., Cole P.A.
      Nature 451:846-850(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1287-1666 IN COMPLEX WITH LYS-COA, MUTAGENESIS OF THR-1357; SER-1396; TYR-1397; GLU-1505; ASP-1625 AND ASP-1628.
    86. "Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation."
      Feng H., Jenkins L.M.M., Durell S.R., Hayashi R., Mazur S.J., Cherry S., Tropea J.E., Miller M., Wlodawer A., Appella E., Bai Y.
      Structure 17:202-210(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1723-1812, INTERACTION WITH TP53.
    87. Cited for: VARIANTS PRO-827; GLY-1013; TYR-1650 AND GLN-2221, POSSIBLE INVOLVEMENT IN CANCER.

    Entry informationi

    Entry nameiEP300_HUMAN
    AccessioniPrimary (citable) accession number: Q09472
    Secondary accession number(s): B1AKC2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 190 of the entry and version 2 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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