CREBBP | ENSG00000005339 | NCBI 1387

Details for: CREBBP

Gene ID: 1387

Symbol: CREBBP

Ensembl ID: ENSG00000005339

Description: CREB binding protein

Associated with

Activation of anterior hox genes in hindbrain development during early embryogenesis
(R-HSA-5617472)
Activation of gene expression by srebf (srebp)
(R-HSA-2426168)
Activation of hox genes during differentiation
(R-HSA-5619507)
Activation of the tfap2 (ap-2) family of transcription factors
(R-HSA-8866907)
Adipogenesis
(R-HSA-9843745)
Attenuation phase
(R-HSA-3371568)
Bmal1:clock,npas2 activates circadian gene expression
(R-HSA-1368108)
C-type lectin receptors (clrs)
(R-HSA-5621481)
Cd209 (dc-sign) signaling
(R-HSA-5621575)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to chemical stress
(R-HSA-9711123)
Cellular response to heat stress
(R-HSA-3371556)
Cellular response to hypoxia
(R-HSA-1234174)
Chromatin modifying enzymes
(R-HSA-3247509)
Chromatin organization
(R-HSA-4839726)
Circadian clock
(R-HSA-400253)
Constitutive signaling by notch1 hd+pest domain mutants
(R-HSA-2894862)
Constitutive signaling by notch1 pest domain mutants
(R-HSA-2644606)
Cytoprotection by hmox1
(R-HSA-9707564)
Cytosolic sensors of pathogen-associated dna
(R-HSA-1834949)
Ddx58/ifih1-mediated induction of interferon-alpha/beta
(R-HSA-168928)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Epigenetic regulation by wdr5-containing histone modifying complexes
(R-HSA-9917777)
Epigenetic regulation of gene expression
(R-HSA-212165)
Epigenetic regulation of gene expression by mll3 and mll4 complexes
(R-HSA-9818564)
Esr-mediated signaling
(R-HSA-8939211)
Estrogen-dependent gene expression
(R-HSA-9018519)
Formation of paraxial mesoderm
(R-HSA-9793380)
Formation of the beta-catenin:tcf transactivating complex
(R-HSA-201722)
Foxo-mediated transcription
(R-HSA-9614085)
Foxo-mediated transcription of cell death genes
(R-HSA-9614657)
Gastrulation
(R-HSA-9758941)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hats acetylate histones
(R-HSA-3214847)
Heme signaling
(R-HSA-9707616)
Hsf1-dependent transactivation
(R-HSA-3371571)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Innate immune system
(R-HSA-168249)
Keap1-nfe2l2 pathway
(R-HSA-9755511)
Lrr flii-interacting protein 1 (lrrfip1) activates type i ifn production
(R-HSA-3134973)
Maternal to zygotic transition (mzt)
(R-HSA-9816359)
Metabolism
(R-HSA-1430728)
Metabolism of lipids
(R-HSA-556833)
Metabolism of proteins
(R-HSA-392499)
Metabolism of steroids
(R-HSA-8957322)
Mitf-m-regulated melanocyte development
(R-HSA-9730414)
Mitochondrial biogenesis
(R-HSA-1592230)
Notch-hlh transcription pathway
(R-HSA-350054)
Notch1 intracellular domain regulates transcription
(R-HSA-2122947)
Notch3 intracellular domain regulates transcription
(R-HSA-9013508)
Notch4 intracellular domain regulates transcription
(R-HSA-9013695)
Organelle biogenesis and maintenance
(R-HSA-1852241)
Post-translational protein modification
(R-HSA-597592)
Ppara activates gene expression
(R-HSA-1989781)
Pre-notch expression and processing
(R-HSA-1912422)
Pre-notch transcription and translation
(R-HSA-1912408)
Regulation of beta-cell development
(R-HSA-186712)
Regulation of cholesterol biosynthesis by srebp (srebf)
(R-HSA-1655829)
Regulation of foxo transcriptional activity by acetylation
(R-HSA-9617629)
Regulation of gene expression by hypoxia-inducible factor
(R-HSA-1234158)
Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells
(R-HSA-210744)
Regulation of lipid metabolism by pparalpha
(R-HSA-400206)
Respiratory syncytial virus infection pathway
(R-HSA-9820952)
Rna polymerase ii transcription
(R-HSA-73857)
Rora activates gene expression
(R-HSA-1368082)
Runx1 regulates transcription of genes involved in differentiation of myeloid cells
(R-HSA-8939246)
Runx3 regulates notch signaling
(R-HSA-8941856)
Sars-cov infections
(R-HSA-9679506)
Signaling by notch
(R-HSA-157118)
Signaling by notch1
(R-HSA-1980143)
Signaling by notch1 hd+pest domain mutants in cancer
(R-HSA-2894858)
Signaling by notch1 in cancer
(R-HSA-2644603)
Signaling by notch1 pest domain mutants in cancer
(R-HSA-2644602)
Signaling by notch3
(R-HSA-9012852)
Signaling by notch4
(R-HSA-9013694)
Signaling by nuclear receptors
(R-HSA-9006931)
Signaling by wnt
(R-HSA-195721)
Signal transduction
(R-HSA-162582)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of transcription cofactors
(R-HSA-3899300)
Tcf dependent signaling in response to wnt
(R-HSA-201681)
Tp53 regulates transcription of cell death genes
(R-HSA-5633008)
Traf3-dependent irf activation pathway
(R-HSA-918233)
Traf6 mediated irf7 activation
(R-HSA-933541)
Transcriptional activation of mitochondrial biogenesis
(R-HSA-2151201)
Transcriptional and post-translational regulation of mitf-m expression and activity
(R-HSA-9856649)
Transcriptional regulation by npas4
(R-HSA-9634815)
Transcriptional regulation by runx1
(R-HSA-8878171)
Transcriptional regulation by runx3
(R-HSA-8878159)
Transcriptional regulation by the ap-2 (tfap2) family of transcription factors
(R-HSA-8864260)
Transcriptional regulation by tp53
(R-HSA-3700989)
Transcriptional regulation of white adipocyte differentiation
(R-HSA-381340)
Viral infection pathways
(R-HSA-9824446)
Zygotic genome activation (zga)
(R-HSA-9819196)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 427.5927
Cell Significance Index: -66.5100
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 263.7956
Cell Significance Index: -66.9100
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 140.2806
Cell Significance Index: -56.9900
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 128.3474
Cell Significance Index: -66.0200
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 105.4362
Cell Significance Index: -70.7500
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 59.7438
Cell Significance Index: -57.0400
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 55.5332
Cell Significance Index: -68.4700
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 24.9285
Cell Significance Index: -66.7800
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 20.7440
Cell Significance Index: -45.4000
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 20.6515
Cell Significance Index: -63.4300
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 17.6937
Cell Significance Index: -69.8200
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 3.4971
Cell Significance Index: 196.2400
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 2.5439
Cell Significance Index: 65.3900
Cell Name: neoplastic cell (CL0001063)
Fold Change: 2.4365
Cell Significance Index: 483.5400
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: 2.2351
Cell Significance Index: 154.5700
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.1758
Cell Significance Index: 436.4600
Cell Name: preadipocyte (CL0002334)
Fold Change: 1.9275
Cell Significance Index: 37.6200
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.8630
Cell Significance Index: 1682.1200
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.8094
Cell Significance Index: 649.0100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 1.5143
Cell Significance Index: 42.3200
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.5056
Cell Significance Index: 115.5400
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 1.0663
Cell Significance Index: 115.9800
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 1.0184
Cell Significance Index: 704.3700
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.8960
Cell Significance Index: 55.0700
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.7746
Cell Significance Index: 40.3500
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.7724
Cell Significance Index: 46.3700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.7130
Cell Significance Index: 128.5300
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.6686
Cell Significance Index: 29.5800
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.6535
Cell Significance Index: 80.3600
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.6490
Cell Significance Index: 89.1300
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.5945
Cell Significance Index: 12.8800
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.5843
Cell Significance Index: 39.2900
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.5841
Cell Significance Index: 95.0000
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.5440
Cell Significance Index: 20.6000
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.5267
Cell Significance Index: 15.1800
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.4239
Cell Significance Index: 19.2200
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.3330
Cell Significance Index: 181.8700
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.3018
Cell Significance Index: 133.4500
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.2947
Cell Significance Index: 5.0500
Cell Name: cortical interneuron (CL0008031)
Fold Change: 0.2856
Cell Significance Index: 6.8500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2852
Cell Significance Index: 536.9500
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.2751
Cell Significance Index: 5.8800
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.2591
Cell Significance Index: 25.6300
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.2575
Cell Significance Index: 474.8900
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.2177
Cell Significance Index: 335.1000
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.2134
Cell Significance Index: 135.5500
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.1962
Cell Significance Index: 89.0600
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1618
Cell Significance Index: 30.8000
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.1198
Cell Significance Index: 1.7200
Cell Name: early pro-B cell (CL0002046)
Fold Change: 0.0841
Cell Significance Index: 5.4300
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.0583
Cell Significance Index: 9.9500
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0442
Cell Significance Index: 60.1600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.0026
Cell Significance Index: -0.0700
Cell Name: odontoblast (CL0000060)
Fold Change: -0.0166
Cell Significance Index: -2.1300
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0448
Cell Significance Index: -32.8500
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0454
Cell Significance Index: -33.6000
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.0555
Cell Significance Index: -2.6100
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0581
Cell Significance Index: -36.2900
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0628
Cell Significance Index: -2.9300
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0751
Cell Significance Index: -56.8400
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0806
Cell Significance Index: -45.4500
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: -0.0831
Cell Significance Index: -9.8000
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2022
Cell Significance Index: -42.5800
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2128
Cell Significance Index: -30.9400
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.2131
Cell Significance Index: -21.7700
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.2144
Cell Significance Index: -61.6800
Cell Name: lactocyte (CL0002325)
Fold Change: -0.2584
Cell Significance Index: -33.3800
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -0.2976
Cell Significance Index: -4.2800
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.3210
Cell Significance Index: -36.7800
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.3315
Cell Significance Index: -17.2200
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.3404
Cell Significance Index: -38.8600
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.3429
Cell Significance Index: -12.0500
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.3526
Cell Significance Index: -41.0900
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.3541
Cell Significance Index: -10.1500
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.4066
Cell Significance Index: -6.8500
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.4663
Cell Significance Index: -48.5500
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.5073
Cell Significance Index: -37.8100
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.5122
Cell Significance Index: -36.2300
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.5375
Cell Significance Index: -7.9400
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.5519
Cell Significance Index: -7.5300
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.5648
Cell Significance Index: -13.7800
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.6015
Cell Significance Index: -17.1700
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.7029
Cell Significance Index: -18.8400
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.7345
Cell Significance Index: -58.1700
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.7994
Cell Significance Index: -21.0200
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.8002
Cell Significance Index: -21.7800
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.8480
Cell Significance Index: -18.0600
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.8723
Cell Significance Index: -27.9400
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.8750
Cell Significance Index: -45.9400
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.9190
Cell Significance Index: -15.3800
Cell Name: basal epithelial cell of prostatic duct (CL0002236)
Fold Change: -0.9238
Cell Significance Index: -8.2000
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.9291
Cell Significance Index: -58.5600
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.9700
Cell Significance Index: -59.4700
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -1.0179
Cell Significance Index: -8.3000
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -1.0645
Cell Significance Index: -19.6800
Cell Name: periportal region hepatocyte (CL0019026)
Fold Change: -1.1206
Cell Significance Index: -16.5400
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -1.1862
Cell Significance Index: -37.7800
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -1.1869
Cell Significance Index: -10.9300
Cell Name: Purkinje cell (CL0000121)
Fold Change: -1.1906
Cell Significance Index: -26.0700
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.2092
Cell Significance Index: -39.5900

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** 1. **Multifunctional transcriptional coactivator**: CREBBP interacts with various transcription factors and coactivators to regulate gene expression. 2. **Post-translational modifications**: CREBBP is modified by acetylation, phosphorylation, and ubiquitination, which regulate its activity and interactions with other proteins. 3. **Highly expressed in various tissues**: CREBBP is expressed in the brain, immune cells, epithelial tissues, and other cell types. 4. **Involved in numerous signaling pathways**: CREBBP is involved in pathways mediated by Notch, Wnt, nuclear receptors, and other signaling molecules. **Pathways and Functions** 1. **Gene expression**: CREBBP regulates gene expression by interacting with transcription factors and coactivators. 2. **Cell differentiation**: CREBBP plays a role in cell differentiation, particularly in the development of immune cells and epithelial tissues. 3. **Immune responses**: CREBBP is involved in immune responses, including the regulation of cytokine production and the activation of immune cells. 4. **Circadian clock**: CREBBP interacts with the circadian clock to regulate gene expression and cellular responses to light and darkness. 5. **Metabolic regulation**: CREBBP regulates metabolic processes, including lipid metabolism and glucose homeostasis. **Clinical Significance** 1. **Cancer**: CREBBP is often overexpressed in various types of cancer, including leukemia, lymphoma, and breast cancer. 2. **Neurodegenerative disorders**: CREBBP has been implicated in neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. 3. **Metabolic disorders**: CREBBP regulates metabolic processes, and its dysregulation has been implicated in metabolic disorders, including obesity and type 2 diabetes. 4. **Immune system disorders**: CREBBP plays a role in immune responses, and its dysregulation has been implicated in autoimmune disorders, including rheumatoid arthritis and multiple sclerosis. In conclusion, CREBBP is a multifunctional transcriptional coactivator that plays a critical role in various cellular processes, including gene expression, cell differentiation, and immune responses. Its dysregulation has been implicated in various diseases, including cancer, neurodegenerative disorders, and metabolic disorders. Further studies are needed to fully understand the functions and clinical significance of CREBBP.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

CREB-binding protein

Genular Protein ID: 704184725

Symbol: CBP_HUMAN

Name: CREB-binding protein

UniProtKB Accession Codes:

Q92793 D3DUC9 O00147 Q16376 Q4LE28

Database IDs:

Citations:

PubMed ID: 9238046

Title: MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3).

PubMed ID: 9238046

DOI: 10.1073/pnas.94.16.8732

PubMed ID: 9177780

Title: Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3.

PubMed ID: 9177780

DOI: 10.1006/geno.1997.4699

PubMed ID: 8782817

Title: The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein.

PubMed ID: 8782817

DOI: 10.1038/ng0996-33

PubMed ID: 11157802

Title: Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13).

PubMed ID: 11157802

DOI: 10.1093/hmg/10.4.395

PubMed ID: 8684459

Title: A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.

PubMed ID: 8684459

DOI: 10.1038/382319a0

PubMed ID: 8917528

Title: An essential role for p300/CBP in the cellular response to hypoxia.

PubMed ID: 8917528

DOI: 10.1073/pnas.93.23.12969

PubMed ID: 9323138

Title: RNA helicase A mediates association of CBP with RNA polymerase II.

PubMed ID: 9323138

DOI: 10.1016/s0092-8674(00)80376-1

PubMed ID: 9528808

Title: Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300.

PubMed ID: 9528808

DOI: 10.1128/mcb.18.4.2392

PubMed ID: 9707565

Title: Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases.

PubMed ID: 9707565

DOI: 10.1073/pnas.95.17.9855

PubMed ID: 10347196

Title: Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein.

PubMed ID: 10347196

DOI: 10.1074/jbc.274.23.16370

PubMed ID: 10077561

Title: Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling.

PubMed ID: 10077561

DOI: 10.1073/pnas.96.6.2627

PubMed ID: 10490106

Title: Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase.

PubMed ID: 10490106

DOI: 10.1016/s0092-8674(00)80054-9

PubMed ID: 10722728

Title: The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors.

PubMed ID: 10722728

DOI: 10.1074/jbc.275.12.8825

PubMed ID: 10866662

Title: A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP.

PubMed ID: 10866662

DOI: 10.1128/mcb.20.14.5048-5063.2000

PubMed ID: 11154691

Title: Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation.

PubMed ID: 11154691

DOI: 10.1074/jbc.m007846200

PubMed ID: 11514544

Title: Requirement of two NFATc4 transactivation domains for CBP potentiation.

PubMed ID: 11514544

DOI: 10.1074/jbc.m102961200

PubMed ID: 11568182

Title: Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles.

PubMed ID: 11568182

DOI: 10.1074/jbc.m106733200

PubMed ID: 11463834

Title: The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation.

PubMed ID: 11463834

DOI: 10.1128/mcb.21.16.5520-5530.2001

PubMed ID: 11559821

Title: Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300.

PubMed ID: 11559821

DOI: 10.1128/jvi.75.20.9885-9895.2001

PubMed ID: 11349124

Title: A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression.

PubMed ID: 11349124

DOI: 10.1074/jbc.m100113200

PubMed ID: 11481323

Title: Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha.

PubMed ID: 11481323

DOI: 10.1074/jbc.m103783200

PubMed ID: 11314014

Title: HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators.

PubMed ID: 11314014

DOI: 10.1038/sj.onc.1204163

PubMed ID: 11864910

Title: Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb.

PubMed ID: 11864910

PubMed ID: 11744733

Title: 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.

PubMed ID: 11744733

DOI: 10.1074/jbc.m110850200

PubMed ID: 11971985

Title: Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase.

PubMed ID: 11971985

DOI: 10.1128/mcb.22.10.3549-3561.2002

PubMed ID: 12738767

Title: Interferon regulatory factor-2 regulates cell growth through its acetylation.

PubMed ID: 12738767

DOI: 10.1074/jbc.m213037200

PubMed ID: 12730195

Title: Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination.

PubMed ID: 12730195

DOI: 10.1074/jbc.m303518200

PubMed ID: 12929931

Title: 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.

PubMed ID: 12929931

DOI: 10.1359/jbmr.2003.18.8.1419

PubMed ID: 14645221

Title: Histone acetyltransferase-dependent chromatin remodeling and the vascular clock.

PubMed ID: 14645221

DOI: 10.1074/jbc.m311973200

PubMed ID: 15075319

Title: 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.

PubMed ID: 15075319

DOI: 10.1074/jbc.m401356200

PubMed ID: 15126506

Title: FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1).

PubMed ID: 15126506

DOI: 10.1074/jbc.m401138200

PubMed ID: 15488321

Title: The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies.

PubMed ID: 15488321

DOI: 10.1016/j.neulet.2004.08.062

PubMed ID: 15220471

Title: Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity.

PubMed ID: 15220471

DOI: 10.1073/pnas.0400593101

PubMed ID: 14716005

Title: Dendrite development regulated by CREST, a calcium-regulated transcriptional activator.

PubMed ID: 14716005

DOI: 10.1126/science.1089845

PubMed ID: 17434128

Title: Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB.

PubMed ID: 17434128

DOI: 10.1016/j.molcel.2007.02.019

PubMed ID: 17525332

Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.

PubMed ID: 17525332

DOI: 10.1126/science.1140321

PubMed ID: 18316612

Title: Molecular basis of nuclear factor-kappaB activation by astrocyte elevated gene-1.

PubMed ID: 18316612

DOI: 10.1158/0008-5472.can-07-6164

PubMed ID: 18599479

Title: An interaction between the human T cell leukemia virus type 1 basic leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to the down-regulation of tax-dependent viral transcription by HBZ.

PubMed ID: 18599479

DOI: 10.1074/jbc.m803116200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21131905

Title: Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation.

PubMed ID: 21131905

DOI: 10.1038/emboj.2010.318

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24207024

Title: Repression of RNA polymerase I upon stress is caused by inhibition of RNA-dependent deacetylation of PAF53 by SIRT7.

PubMed ID: 24207024

DOI: 10.1016/j.molcel.2013.10.010

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 24939902

Title: CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis.

PubMed ID: 24939902

DOI: 10.1093/nar/gku533

PubMed ID: 25514493

Title: Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced transcriptional responses.

PubMed ID: 25514493

DOI: 10.1016/j.bbagrm.2014.12.008

PubMed ID: 25593309

Title: Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination.

PubMed ID: 25593309

DOI: 10.1101/gad.252189.114

PubMed ID: 26951377

Title: DUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes.

PubMed ID: 26951377

DOI: 10.1093/nar/gkw141

PubMed ID: 28790157

Title: SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic R loops and safeguard genome stability.

PubMed ID: 28790157

DOI: 10.1101/gad.300624.117

PubMed ID: 28128295

Title: RNA helicase DDX3 maintains lipid homeostasis through upregulation of the microsomal triglyceride transfer protein by interacting with HNF4 and SHP.

PubMed ID: 28128295

DOI: 10.1038/srep41452

PubMed ID: 30540930

Title: SIRT7-dependent deacetylation of fibrillarin controls histone H2A methylation and rRNA synthesis during the cell cycle.

PubMed ID: 30540930

DOI: 10.1016/j.celrep.2018.11.051

PubMed ID: 35675826

Title: Deubiquitinase OTUD3 regulates metabolism homeostasis in response to nutritional stresses.

PubMed ID: 35675826

DOI: 10.1016/j.cmet.2022.05.005

PubMed ID: 38128537

Title: Metabolic regulation of homologous recombination repair by MRE11 lactylation.

PubMed ID: 38128537

DOI: 10.1016/j.cell.2023.11.022

PubMed ID: 11959977

Title: Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response.

PubMed ID: 11959977

DOI: 10.1073/pnas.082121399

PubMed ID: 11742995

Title: Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein.

PubMed ID: 11742995

DOI: 10.1093/emboj/20.24.7184

PubMed ID: 14744133

Title: NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP.

PubMed ID: 14744133

DOI: 10.1021/bi035612l

PubMed ID: 22464331

Title: Histone recognition and large-scale structural analysis of the human bromodomain family.

PubMed ID: 22464331

DOI: 10.1016/j.cell.2012.02.013

PubMed ID: 23651431

Title: Allosteric communication in the KIX domain proceeds through dynamic repacking of the hydrophobic core.

PubMed ID: 23651431

DOI: 10.1021/cb4002188

PubMed ID: 24616510

Title: Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.

PubMed ID: 24616510

DOI: 10.1073/pnas.1319122111

PubMed ID: 24361270

Title: Structural insights into acetylated-histone H4 recognition by the bromodomain-PHD finger module of human transcriptional coactivator CBP.

PubMed ID: 24361270

DOI: 10.1016/j.str.2013.10.021

PubMed ID: 27302953

Title: Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins.

PubMed ID: 27302953

DOI: 10.1073/pnas.1603269113

PubMed ID: 11331617

Title: Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome.

PubMed ID: 11331617

DOI: 10.1093/hmg/10.10.1071

PubMed ID: 12114483

Title: Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including a mild variant showing a missense mutation in codon 1175 of CREBBP.

PubMed ID: 12114483

DOI: 10.1136/jmg.39.7.496

PubMed ID: 12566391

Title: Loss of CBP acetyltransferase activity by PHD finger mutations in Rubinstein-Taybi syndrome.

PubMed ID: 12566391

DOI: 10.1093/hmg/ddg039

PubMed ID: 15706485

Title: Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease.

PubMed ID: 15706485

DOI: 10.1086/429130

PubMed ID: 20684013

Title: Inheritance and variable expression in Rubinstein-Taybi syndrome.

PubMed ID: 20684013

DOI: 10.1002/ajmg.a.33598

PubMed ID: 25388907

Title: Insights into genotype-phenotype correlations from CREBBP point mutation screening in a cohort of 46 Rubinstein-Taybi syndrome patients.

PubMed ID: 25388907

DOI: 10.1111/cge.12537

PubMed ID: 27311832

Title: CREBBP mutations in individuals without Rubinstein-Taybi syndrome phenotype.

PubMed ID: 27311832

DOI: 10.1002/ajmg.a.37800

PubMed ID: 29460469

Title: Further delineation of an entity caused by CREBBP and EP300 mutations but not resembling Rubinstein-Taybi syndrome.

PubMed ID: 29460469

DOI: 10.1002/ajmg.a.38626

PubMed ID: 30737887

Title: Confirmation of a new phenotype in an individual with a variant in the last part of exon 30 of CREBBP.

PubMed ID: 30737887

DOI: 10.1002/ajmg.a.61052

Sequence Information:

Length: 2442
Mass: 265351
Checksum: 3BEA9B8558BA1A5E
Sequence:

MAENLLDGPP NPKRAKLSSP GFSANDSTDF GSLFDLENDL PDELIPNGGE LGLLNSGNLV 
PDAASKHKQL SELLRGGSGS SINPGIGNVS ASSPVQQGLG GQAQGQPNSA NMASLSAMGK 
SPLSQGDSSA PSLPKQAAST SGPTPAASQA LNPQAQKQVG LATSSPATSQ TGPGICMNAN 
FNQTHPGLLN SNSGHSLINQ ASQGQAQVMN GSLGAAGRGR GAGMPYPTPA MQGASSSVLA 
ETLTQVSPQM TGHAGLNTAQ AGGMAKMGIT GNTSPFGQPF SQAGGQPMGA TGVNPQLASK 
QSMVNSLPTF PTDIKNTSVT NVPNMSQMQT SVGIVPTQAI ATGPTADPEK RKLIQQQLVL 
LLHAHKCQRR EQANGEVRAC SLPHCRTMKN VLNHMTHCQA GKACQVAHCA SSRQIISHWK 
NCTRHDCPVC LPLKNASDKR NQQTILGSPA SGIQNTIGSV GTGQQNATSL SNPNPIDPSS 
MQRAYAALGL PYMNQPQTQL QPQVPGQQPA QPQTHQQMRT LNPLGNNPMN IPAGGITTDQ 
QPPNLISESA LPTSLGATNP LMNDGSNSGN IGTLSTIPTA APPSSTGVRK GWHEHVTQDL 
RSHLVHKLVQ AIFPTPDPAA LKDRRMENLV AYAKKVEGDM YESANSRDEY YHLLAEKIYK 
IQKELEEKRR SRLHKQGILG NQPALPAPGA QPPVIPQAQP VRPPNGPLSL PVNRMQVSQG 
MNSFNPMSLG NVQLPQAPMG PRAASPMNHS VQMNSMGSVP GMAISPSRMP QPPNMMGAHT 
NNMMAQAPAQ SQFLPQNQFP SSSGAMSVGM GQPPAQTGVS QGQVPGAALP NPLNMLGPQA 
SQLPCPPVTQ SPLHPTPPPA STAAGMPSLQ HTTPPGMTPP QPAAPTQPST PVSSSGQTPT 
PTPGSVPSAT QTQSTPTVQA AAQAQVTPQP QTPVQPPSVA TPQSSQQQPT PVHAQPPGTP 
LSQAAASIDN RVPTPSSVAS AETNSQQPGP DVPVLEMKTE TQAEDTEPDP GESKGEPRSE 
MMEEDLQGAS QVKEETDIAE QKSEPMEVDE KKPEVKVEVK EEEESSSNGT ASQSTSPSQP 
RKKIFKPEEL RQALMPTLEA LYRQDPESLP FRQPVDPQLL GIPDYFDIVK NPMDLSTIKR 
KLDTGQYQEP WQYVDDVWLM FNNAWLYNRK TSRVYKFCSK LAEVFEQEID PVMQSLGYCC 
GRKYEFSPQT LCCYGKQLCT IPRDAAYYSY QNRYHFCEKC FTEIQGENVT LGDDPSQPQT 
TISKDQFEKK KNDTLDPEPF VDCKECGRKM HQICVLHYDI IWPSGFVCDN CLKKTGRPRK 
ENKFSAKRLQ TTRLGNHLED RVNKFLRRQN HPEAGEVFVR VVASSDKTVE VKPGMKSRFV 
DSGEMSESFP YRTKALFAFE EIDGVDVCFF GMHVQEYGSD CPPPNTRRVY ISYLDSIHFF 
RPRCLRTAVY HEILIGYLEY VKKLGYVTGH IWACPPSEGD DYIFHCHPPD QKIPKPKRLQ 
EWYKKMLDKA FAERIIHDYK DIFKQATEDR LTSAKELPYF EGDFWPNVLE ESIKELEQEE 
EERKKEESTA ASETTEGSQG DSKNAKKKNN KKTNKNKSSI SRANKKKPSM PNVSNDLSQK 
LYATMEKHKE VFFVIHLHAG PVINTLPPIV DPDPLLSCDL MDGRDAFLTL ARDKHWEFSS 
LRRSKWSTLC MLVELHTQGQ DRFVYTCNEC KHHVETRWHC TVCEDYDLCI NCYNTKSHAH 
KMVKWGLGLD DEGSSQGEPQ SKSPQESRRL SIQRCIQSLV HACQCRNANC SLPSCQKMKR 
VVQHTKGCKR KTNGGCPVCK QLIALCCYHA KHCQENKCPV PFCLNIKHKL RQQQIQHRLQ 
QAQLMRRRMA TMNTRNVPQQ SLPSPTSAPP GTPTQQPSTP QTPQPPAQPQ PSPVSMSPAG 
FPSVARTQPP TTVSTGKPTS QVPAPPPPAQ PPPAAVEAAR QIEREAQQQQ HLYRVNINNS 
MPPGRTGMGT PGSQMAPVSL NVPRPNQVSG PVMPSMPPGQ WQQAPLPQQQ PMPGLPRPVI 
SMQAQAAVAG PRMPSVQPPR SISPSALQDL LRTLKSPSSP QQQQQVLNIL KSNPQLMAAF 
IKQRTAKYVA NQPGMQPQPG LQSQPGMQPQ PGMHQQPSLQ NLNAMQAGVP RPGVPPQQQA 
MGGLNPQGQA LNIMNPGHNP NMASMNPQYR EMLRRQLLQQ QQQQQQQQQQ QQQQQQGSAG 
MAGGMAGHGQ FQQPQGPGGY PPAMQQQQRM QQHLPLQGSS MGQMAAQMGQ LGQMGQPGLG 
ADSTPNIQQA LQQRILQQQQ MKQQIGSPGQ PNPMSPQQHM LSGQPQASHL PGQQIATSLS 
NQVRSPAPVQ SPRPQSQPPH SSPSPRIQPQ PSPHHVSPQT GSPHPGLAVT MASSIDQGHL 
GNPEQSAMLP QLNTPSRSAL SSELSLVGDT TGDTLEKFVE GL

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: CREBBP

Associated with

Cells (max top 100)

Other Information

MLL is fused to CBP, a histone acetyltransferase, in therapy-related acute myeloid leukemia with a t(11;16)(q23;p13.3). PubMed ID: 9238046

Construction of a 1.2-Mb contig surrounding, and molecular analysis of, the human CREB-binding protein (CBP/CREBBP) gene on chromosome 16p13.3. PubMed ID: 9177780

The translocation t(8;16)(p11;p13) of acute myeloid leukaemia fuses a putative acetyltransferase to the CREB-binding protein. PubMed ID: 8782817

Fusion of the MORF and CBP genes in acute myeloid leukemia with the t(10;16)(q22;p13). PubMed ID: 11157802

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. PubMed ID: 8684459

An essential role for p300/CBP in the cellular response to hypoxia. PubMed ID: 8917528

RNA helicase A mediates association of CBP with RNA polymerase II. PubMed ID: 9323138

Differential transcriptional activation by human T-cell leukemia virus type 1 Tax mutants is mediated by distinct interactions with CREB binding protein and p300. PubMed ID: 9528808

Acetylation and modulation of erythroid Krueppel-like factor (EKLF) activity by interaction with histone acetyltransferases. PubMed ID: 9707565

Identification of a novel SNF2/SWI2 protein family member, SRCAP, which interacts with CREB-binding protein. PubMed ID: 10347196

Modulation of CREB binding protein function by the promyelocytic (PML) oncoprotein suggests a role for nuclear bodies in hormone signaling. PubMed ID: 10077561

Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. PubMed ID: 10490106

The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors. PubMed ID: 10722728

A new family of nuclear receptor coregulators that integrates nuclear receptor signaling through CBP. PubMed ID: 10866662

Stimulation of NF-E2 DNA binding by CREB-binding protein (CBP)-mediated acetylation. PubMed ID: 11154691

Requirement of two NFATc4 transactivation domains for CBP potentiation. PubMed ID: 11514544

Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles. PubMed ID: 11568182

The oncoprotein Tax binds the SRC-1-interacting domain of CBP/p300 to mediate transcriptional activation. PubMed ID: 11463834

Human T-lymphotropic virus type 1 p30(II) regulates gene transcription by binding CREB binding protein/p300. PubMed ID: 11559821

A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate human CYP11A1 gene expression. PubMed ID: 11349124

Molecular cloning and characterization of PELP1, a novel human coregulator of estrogen receptor alpha. PubMed ID: 11481323

HHV-8 encoded vIRF-1 represses the interferon antiviral response by blocking IRF-3 recruitment of the CBP/p300 coactivators. PubMed ID: 11314014

Interaction between the hematopoietic Ets transcription factor Spi-B and the coactivator CREB-binding protein associated with negative cross-talk with c-Myb. PubMed ID: 11864910

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. PubMed ID: 11744733

Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase. PubMed ID: 11971985

Interferon regulatory factor-2 regulates cell growth through its acetylation. PubMed ID: 12738767

Identification and characterization of BCL-3-binding protein: implications for transcription and DNA repair or recombination. PubMed ID: 12730195

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. PubMed ID: 12929931

Histone acetyltransferase-dependent chromatin remodeling and the vascular clock. PubMed ID: 14645221

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. PubMed ID: 15075319

FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1). PubMed ID: 15126506

The calcium-responsive transactivator recruits CREB binding protein to nuclear bodies. PubMed ID: 15488321

Silent information regulator 2 potentiates Foxo1-mediated transcription through its deacetylase activity. PubMed ID: 15220471

Dendrite development regulated by CREST, a calcium-regulated transcriptional activator. PubMed ID: 14716005

Phosphorylation of CBP by IKKalpha promotes cell growth by switching the binding preference of CBP from p53 to NF-kappaB. PubMed ID: 17434128

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. PubMed ID: 17525332

Molecular basis of nuclear factor-kappaB activation by astrocyte elevated gene-1. PubMed ID: 18316612

An interaction between the human T cell leukemia virus type 1 basic leucine zipper factor (HBZ) and the KIX domain of p300/CBP contributes to the down-regulation of tax-dependent viral transcription by HBZ. PubMed ID: 18599479

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Distinct roles of GCN5/PCAF-mediated H3K9ac and CBP/p300-mediated H3K18/27ac in nuclear receptor transactivation. PubMed ID: 21131905

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Repression of RNA polymerase I upon stress is caused by inhibition of RNA-dependent deacetylation of PAF53 by SIRT7. PubMed ID: 24207024

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

CBP and p300 acetylate PCNA to link its degradation with nucleotide excision repair synthesis. PubMed ID: 24939902

Pokemon (FBI-1) interacts with Smad4 to repress TGF-beta-induced transcriptional responses. PubMed ID: 25514493

Screen identifies bromodomain protein ZMYND8 in chromatin recognition of transcription-associated DNA damage that promotes homologous recombination. PubMed ID: 25593309

DUX4 recruits p300/CBP through its C-terminus and induces global H3K27 acetylation changes. PubMed ID: 26951377

SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic R loops and safeguard genome stability. PubMed ID: 28790157

RNA helicase DDX3 maintains lipid homeostasis through upregulation of the microsomal triglyceride transfer protein by interacting with HNF4 and SHP. PubMed ID: 28128295

SIRT7-dependent deacetylation of fibrillarin controls histone H2A methylation and rRNA synthesis during the cell cycle. PubMed ID: 30540930

Deubiquitinase OTUD3 regulates metabolism homeostasis in response to nutritional stresses. PubMed ID: 35675826

Metabolic regulation of homologous recombination repair by MRE11 lactylation. PubMed ID: 38128537

Structural basis for Hif-1 alpha /CBP recognition in the cellular hypoxic response. PubMed ID: 11959977

Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein. PubMed ID: 11742995

NMR mapping of the HIV-1 Tat interaction surface of the KIX domain of the human coactivator CBP. PubMed ID: 14744133

Histone recognition and large-scale structural analysis of the human bromodomain family. PubMed ID: 22464331

Allosteric communication in the KIX domain proceeds through dynamic repacking of the hydrophobic core. PubMed ID: 23651431

Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation. PubMed ID: 24616510

Structural insights into acetylated-histone H4 recognition by the bromodomain-PHD finger module of human transcriptional coactivator CBP. PubMed ID: 24361270

Structural basis for concerted recruitment and activation of IRF-3 by innate immune adaptor proteins. PubMed ID: 27302953

Defect of histone acetyltransferase activity of the nuclear transcriptional coactivator CBP in Rubinstein-Taybi syndrome. PubMed ID: 11331617

Molecular studies in 10 cases of Rubinstein-Taybi syndrome, including a mild variant showing a missense mutation in codon 1175 of CREBBP. PubMed ID: 12114483

Loss of CBP acetyltransferase activity by PHD finger mutations in Rubinstein-Taybi syndrome. PubMed ID: 12566391

Genetic heterogeneity in Rubinstein-Taybi syndrome: mutations in both the CBP and EP300 genes cause disease. PubMed ID: 15706485

Inheritance and variable expression in Rubinstein-Taybi syndrome. PubMed ID: 20684013

Insights into genotype-phenotype correlations from CREBBP point mutation screening in a cohort of 46 Rubinstein-Taybi syndrome patients. PubMed ID: 25388907

CREBBP mutations in individuals without Rubinstein-Taybi syndrome phenotype. PubMed ID: 27311832

Further delineation of an entity caused by CREBBP and EP300 mutations but not resembling Rubinstein-Taybi syndrome. PubMed ID: 29460469

Confirmation of a new phenotype in an individual with a variant in the last part of exon 30 of CREBBP. PubMed ID: 30737887