Details for: CREBBP

Gene ID: 1387

Symbol: CREBBP

Ensembl ID: ENSG00000005339

Description: CREB binding protein

Associated with

Cells (max top 100)

(Marker Score score is uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

  • Cell Name: anterior lens cell (CL0002223)
    Fold Change: 2.7
    Marker Score: 3628
  • Cell Name: epithelial cell of lower respiratory tract (CL0002632)
    Fold Change: 2.63
    Marker Score: 10954
  • Cell Name: taste receptor cell (CL0000209)
    Fold Change: 2.58
    Marker Score: 2227
  • Cell Name: astrocyte of the cerebral cortex (CL0002605)
    Fold Change: 2.52
    Marker Score: 53771
  • Cell Name: vascular leptomeningeal cell (CL4023051)
    Fold Change: 2.52
    Marker Score: 2899
  • Cell Name: kidney interstitial fibroblast (CL1000692)
    Fold Change: 2.33
    Marker Score: 4487
  • Cell Name: ciliary muscle cell (CL1000443)
    Fold Change: 2.31
    Marker Score: 5069.5
  • Cell Name: lens epithelial cell (CL0002224)
    Fold Change: 2.31
    Marker Score: 2791
  • Cell Name: lamp5 GABAergic cortical interneuron (CL4023011)
    Fold Change: 2.26
    Marker Score: 33844
  • Cell Name: pigmented epithelial cell (CL0000529)
    Fold Change: 2.24
    Marker Score: 9387
  • Cell Name: vip GABAergic cortical interneuron (CL4023016)
    Fold Change: 2.19
    Marker Score: 83192
  • Cell Name: sst GABAergic cortical interneuron (CL4023017)
    Fold Change: 2.17
    Marker Score: 43119
  • Cell Name: sncg GABAergic cortical interneuron (CL4023015)
    Fold Change: 2.16
    Marker Score: 16568
  • Cell Name: cardiac neuron (CL0010022)
    Fold Change: 2.13
    Marker Score: 2648
  • Cell Name: central nervous system macrophage (CL0000878)
    Fold Change: 2.09
    Marker Score: 1039
  • Cell Name: leptomeningeal cell (CL0000708)
    Fold Change: 2.06
    Marker Score: 1018
  • Cell Name: chandelier pvalb GABAergic cortical interneuron (CL4023036)
    Fold Change: 2.04
    Marker Score: 8475
  • Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
    Fold Change: 2.03
    Marker Score: 74895
  • Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
    Fold Change: 2.02
    Marker Score: 591
  • Cell Name: neuron associated cell (sensu Vertebrata) (CL0000123)
    Fold Change: 2.01
    Marker Score: 10527
  • Cell Name: mesangial cell (CL0000650)
    Fold Change: 1.99
    Marker Score: 2400
  • Cell Name: caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
    Fold Change: 1.98
    Marker Score: 7671
  • Cell Name: cerebral cortex endothelial cell (CL1001602)
    Fold Change: 1.98
    Marker Score: 1180
  • Cell Name: neuron (CL0000540)
    Fold Change: 1.96
    Marker Score: 7988
  • Cell Name: photoreceptor cell (CL0000210)
    Fold Change: 1.95
    Marker Score: 1466
  • Cell Name: corneal epithelial cell (CL0000575)
    Fold Change: 1.94
    Marker Score: 2138
  • Cell Name: neuronal brush cell (CL0000555)
    Fold Change: 1.93
    Marker Score: 6476
  • Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
    Fold Change: 1.93
    Marker Score: 118638
  • Cell Name: skeletal muscle satellite stem cell (CL0008011)
    Fold Change: 1.93
    Marker Score: 2060
  • Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
    Fold Change: 1.92
    Marker Score: 2172
  • Cell Name: near-projecting glutamatergic cortical neuron (CL4023012)
    Fold Change: 1.92
    Marker Score: 18025
  • Cell Name: basal epithelial cell of prostatic duct (CL0002236)
    Fold Change: 1.91
    Marker Score: 1696
  • Cell Name: inhibitory interneuron (CL0000498)
    Fold Change: 1.87
    Marker Score: 8633
  • Cell Name: kidney loop of Henle thin descending limb epithelial cell (CL1001111)
    Fold Change: 1.86
    Marker Score: 2010
  • Cell Name: cerebellar granule cell precursor (CL0002362)
    Fold Change: 1.84
    Marker Score: 1029
  • Cell Name: cortical cell of adrenal gland (CL0002097)
    Fold Change: 1.83
    Marker Score: 32412
  • Cell Name: conjunctival epithelial cell (CL1000432)
    Fold Change: 1.81
    Marker Score: 1902
  • Cell Name: oligodendrocyte (CL0000128)
    Fold Change: 1.8
    Marker Score: 4311
  • Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
    Fold Change: 1.8
    Marker Score: 17101
  • Cell Name: fat cell (CL0000136)
    Fold Change: 1.8
    Marker Score: 1005
  • Cell Name: epithelial cell of prostate (CL0002231)
    Fold Change: 1.79
    Marker Score: 1243
  • Cell Name: alveolar type 2 fibroblast cell (CL4028006)
    Fold Change: 1.78
    Marker Score: 989
  • Cell Name: corneal endothelial cell (CL0000132)
    Fold Change: 1.77
    Marker Score: 1030
  • Cell Name: L6b glutamatergic cortical neuron (CL4023038)
    Fold Change: 1.76
    Marker Score: 15134
  • Cell Name: renal interstitial pericyte (CL1001318)
    Fold Change: 1.76
    Marker Score: 1679
  • Cell Name: stellate neuron (CL0000122)
    Fold Change: 1.74
    Marker Score: 9333
  • Cell Name: chromaffin cell (CL0000166)
    Fold Change: 1.73
    Marker Score: 2430.5
  • Cell Name: renal alpha-intercalated cell (CL0005011)
    Fold Change: 1.72
    Marker Score: 908
  • Cell Name: renal principal cell (CL0005009)
    Fold Change: 1.66
    Marker Score: 1277
  • Cell Name: Purkinje cell (CL0000121)
    Fold Change: 1.66
    Marker Score: 55964
  • Cell Name: dopaminergic neuron (CL0000700)
    Fold Change: 1.66
    Marker Score: 17099
  • Cell Name: acinar cell (CL0000622)
    Fold Change: 1.63
    Marker Score: 1151
  • Cell Name: skeletal muscle fibroblast (CL0011027)
    Fold Change: 1.62
    Marker Score: 1065
  • Cell Name: oligodendrocyte precursor cell (CL0002453)
    Fold Change: 1.6
    Marker Score: 1982
  • Cell Name: smooth muscle cell of prostate (CL1000487)
    Fold Change: 1.6
    Marker Score: 407
  • Cell Name: secondary lens fiber (CL0002225)
    Fold Change: 1.59
    Marker Score: 932
  • Cell Name: regular ventricular cardiac myocyte (CL0002131)
    Fold Change: 1.59
    Marker Score: 35501
  • Cell Name: lung goblet cell (CL1000143)
    Fold Change: 1.57
    Marker Score: 452
  • Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
    Fold Change: 1.56
    Marker Score: 492
  • Cell Name: contractile cell (CL0000183)
    Fold Change: 1.55
    Marker Score: 842
  • Cell Name: lactocyte (CL0002325)
    Fold Change: 1.55
    Marker Score: 24900
  • Cell Name: astrocyte (CL0000127)
    Fold Change: 1.55
    Marker Score: 1342
  • Cell Name: endothelial cell of vascular tree (CL0002139)
    Fold Change: 1.54
    Marker Score: 2240
  • Cell Name: hepatoblast (CL0005026)
    Fold Change: 1.54
    Marker Score: 5029
  • Cell Name: cholangiocyte (CL1000488)
    Fold Change: 1.53
    Marker Score: 573
  • Cell Name: glandular epithelial cell (CL0000150)
    Fold Change: 1.5
    Marker Score: 3686
  • Cell Name: CD8-positive, alpha-beta cytokine secreting effector T cell (CL0000908)
    Fold Change: 1.5
    Marker Score: 646
  • Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
    Fold Change: 1.5
    Marker Score: 2310
  • Cell Name: mature astrocyte (CL0002627)
    Fold Change: 1.49
    Marker Score: 980
  • Cell Name: granule cell (CL0000120)
    Fold Change: 1.48
    Marker Score: 11180
  • Cell Name: epicardial adipocyte (CL1000309)
    Fold Change: 1.48
    Marker Score: 718
  • Cell Name: cerebral cortex neuron (CL0010012)
    Fold Change: 1.47
    Marker Score: 4199.5
  • Cell Name: macroglial cell (CL0000126)
    Fold Change: 1.45
    Marker Score: 3340
  • Cell Name: mature microglial cell (CL0002629)
    Fold Change: 1.45
    Marker Score: 525
  • Cell Name: skeletal muscle fiber (CL0008002)
    Fold Change: 1.44
    Marker Score: 3616.5
  • Cell Name: OFF retinal ganglion cell (CL4023033)
    Fold Change: 1.44
    Marker Score: 605
  • Cell Name: kidney connecting tubule epithelial cell (CL1000768)
    Fold Change: 1.44
    Marker Score: 2041
  • Cell Name: syncytiotrophoblast cell (CL0000525)
    Fold Change: 1.43
    Marker Score: 1177
  • Cell Name: GABAergic neuron (CL0000617)
    Fold Change: 1.42
    Marker Score: 5912
  • Cell Name: brainstem motor neuron (CL2000047)
    Fold Change: 1.4
    Marker Score: 815
  • Cell Name: keratocyte (CL0002363)
    Fold Change: 1.39
    Marker Score: 320
  • Cell Name: podocyte (CL0000653)
    Fold Change: 1.38
    Marker Score: 511
  • Cell Name: pigmented ciliary epithelial cell (CL0002303)
    Fold Change: 1.38
    Marker Score: 468
  • Cell Name: endocrine cell (CL0000163)
    Fold Change: 1.36
    Marker Score: 705
  • Cell Name: nasal mucosa goblet cell (CL0002480)
    Fold Change: 1.35
    Marker Score: 900
  • Cell Name: GABAergic interneuron (CL0011005)
    Fold Change: 1.34
    Marker Score: 517
  • Cell Name: squamous epithelial cell (CL0000076)
    Fold Change: 1.34
    Marker Score: 913
  • Cell Name: parietal epithelial cell (CL1000452)
    Fold Change: 1.32
    Marker Score: 481
  • Cell Name: fibroblast of mammary gland (CL0002555)
    Fold Change: 1.32
    Marker Score: 45070
  • Cell Name: kidney proximal straight tubule epithelial cell (CL1000839)
    Fold Change: 1.32
    Marker Score: 3120
  • Cell Name: CNS interneuron (CL0000402)
    Fold Change: 1.31
    Marker Score: 628
  • Cell Name: kidney distal convoluted tubule epithelial cell (CL1000849)
    Fold Change: 1.3
    Marker Score: 1381
  • Cell Name: hepatic stellate cell (CL0000632)
    Fold Change: 1.29
    Marker Score: 488
  • Cell Name: centrilobular region hepatocyte (CL0019029)
    Fold Change: 1.29
    Marker Score: 8320
  • Cell Name: endothelial cell of pericentral hepatic sinusoid (CL0019022)
    Fold Change: 1.28
    Marker Score: 1371
  • Cell Name: melanocyte (CL0000148)
    Fold Change: 1.27
    Marker Score: 516
  • Cell Name: choroid plexus epithelial cell (CL0000706)
    Fold Change: 1.27
    Marker Score: 1169
  • Cell Name: lung endothelial cell (CL1001567)
    Fold Change: 1.27
    Marker Score: 11166
  • Cell Name: A2 amacrine cell (CL0004219)
    Fold Change: 1.27
    Marker Score: 403
  • Cell Name: cortical thymic epithelial cell (CL0002364)
    Fold Change: 1.26
    Marker Score: 4672

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Other Information

**Key characteristics:** - CREBBP is a protein of the CREB family of transcription factors. - It is expressed in a variety of cell types, including epithelial cells, immune cells, and fibroblasts. - CREBBP is a key regulator of the clock-controlled gene Bmal1. - It also regulates the expression of other genes involved in cell cycle regulation, metabolism, and inflammation. **Pathways and functions:** - CREBBP binds to DNA sequences known as CREB-binding elements (CREBEs) on the promoter regions of target genes. - Once bound, CREBBP recruits the co-activator protein Bmal1 to the CREBEs, which then activates transcription of the target genes. - CREBBP is also a key regulator of the circadian clock. - It is expressed in the suprachiasmatic nucleus (SCN), the central clock organ in the brain. - CREBBP's activity is synchronized to the circadian rhythm, with its peak expression occurring around dawn. - Dysregulation of CREBBP has been linked to a number of diseases, including cancer and autoimmune disorders. **Clinical significance:** - CREBBP is a promising target for the treatment of cancer and autoimmune disorders. - Small molecule inhibitors of CREBBP have been shown to be effective in inhibiting cancer growth and inflammation. - Further research is needed to develop more effective treatments for cancer and autoimmune disorders that target CREBBP.

Genular Protein ID: 704184725

Symbol: CBP_HUMAN

Name: CREB-binding protein

UniProtKB Accession Codes:

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: 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: 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. For the full schema, download it here.