RBBP4 | ENSG00000162521 | NCBI 5928

Details for: RBBP4

Gene ID: 5928

Symbol: RBBP4

Ensembl ID: ENSG00000162521

Description: RB binding protein 4, chromatin remodeling factor

Associated with

Activation of anterior hox genes in hindbrain development during early embryogenesis
(R-HSA-5617472)
Activation of hox genes during differentiation
(R-HSA-5619507)
Adipogenesis
(R-HSA-9843745)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular senescence
(R-HSA-2559583)
Chromatin modifying enzymes
(R-HSA-3247509)
Chromatin organization
(R-HSA-4839726)
Chromosome maintenance
(R-HSA-73886)
Cyclin a:cdk2-associated events at s phase entry
(R-HSA-69656)
Cyclin e associated events during g1/s transition
(R-HSA-69202)
Defective pyroptosis
(R-HSA-9710421)
Deposition of new cenpa-containing nucleosomes at the centromere
(R-HSA-606279)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of programmed cell death
(R-HSA-9645723)
Epigenetic regulation of gene expression
(R-HSA-212165)
Ercc6 (csb) and ehmt2 (g9a) positively regulate rrna expression
(R-HSA-427389)
G0 and early g1
(R-HSA-1538133)
G1/s-specific transcription
(R-HSA-69205)
G1/s transition
(R-HSA-69206)
G2/m transition
(R-HSA-69275)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hdacs deacetylate histones
(R-HSA-3214815)
Infectious disease
(R-HSA-5663205)
Intracellular signaling by second messengers
(R-HSA-9006925)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Mitotic g2-g2/m phases
(R-HSA-453274)
Oxidative stress induced senescence
(R-HSA-2559580)
Pip3 activates akt signaling
(R-HSA-1257604)
Pkmts methylate histone lysines
(R-HSA-3214841)
Polo-like kinase mediated events
(R-HSA-156711)
Positive epigenetic regulation of rrna expression
(R-HSA-5250913)
Potential therapeutics for sars
(R-HSA-9679191)
Prc2 methylates histones and dna
(R-HSA-212300)
Pten regulation
(R-HSA-6807070)
Regulation of endogenous retroelements
(R-HSA-9842860)
Regulation of endogenous retroelements by krab-zfp proteins
(R-HSA-9843940)
Regulation of endogenous retroelements by piwi-interacting rnas (pirnas)
(R-HSA-9845323)
Regulation of pten gene transcription
(R-HSA-8943724)
Regulation of tp53 activity
(R-HSA-5633007)
Regulation of tp53 activity through acetylation
(R-HSA-6804758)
Rna polymerase ii transcription
(R-HSA-73857)
Rna polymerase i promoter clearance
(R-HSA-73854)
Rna polymerase i transcription
(R-HSA-73864)
Rna polymerase i transcription initiation
(R-HSA-73762)
Sars-cov infections
(R-HSA-9679506)
Signal transduction
(R-HSA-162582)
S phase
(R-HSA-69242)
Transcriptional regulation by e2f6
(R-HSA-8953750)
Transcriptional regulation by tp53
(R-HSA-3700989)
Transcriptional regulation of brown and beige adipocyte differentiation
(R-HSA-9843743)
Transcriptional regulation of brown and beige adipocyte differentiation by ebf2
(R-HSA-9844594)
Transcription of e2f targets under negative control by dream complex
(R-HSA-1362277)
Transcription of e2f targets under negative control by p107 (rbl1) and p130 (rbl2) in complex with hdac1
(R-HSA-1362300)
Viral infection pathways
(R-HSA-9824446)
Atp-dependent activity, acting on dna
(GO:0008094)
Brain development
(GO:0007420)
Chromatin
(GO:0000785)
Chromatin remodeling
(GO:0006338)
Chromosome, telomeric region
(GO:0000781)
Cytosol
(GO:0005829)
Dna replication
(GO:0006260)
Dna replication-dependent chromatin assembly
(GO:0006335)
Histone binding
(GO:0042393)
Histone deacetylase binding
(GO:0042826)
Histone deacetylase complex
(GO:0000118)
Negative regulation of cell migration
(GO:0030336)
Negative regulation of cell population proliferation
(GO:0008285)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of stem cell population maintenance
(GO:1902455)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Negative regulation of transforming growth factor beta receptor signaling pathway
(GO:0030512)
Nucleoplasm
(GO:0005654)
Nucleosomal dna binding
(GO:0031492)
Nucleosome assembly
(GO:0006334)
Nucleus
(GO:0005634)
Nurd complex
(GO:0016581)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of stem cell population maintenance
(GO:1902459)
Protein binding
(GO:0005515)
Regulation of cell fate specification
(GO:0042659)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of stem cell differentiation
(GO:2000736)
Rna polymerase ii cis-regulatory region sequence-specific dna binding
(GO:0000978)

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: 342.4085
Cell Significance Index: -53.2600
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 224.9615
Cell Significance Index: -57.0600
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 166.3318
Cell Significance Index: -68.5200
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 155.4469
Cell Significance Index: -73.3900
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 138.0774
Cell Significance Index: -71.0300
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 109.4226
Cell Significance Index: -73.4300
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 56.2388
Cell Significance Index: -69.3400
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 23.1890
Cell Significance Index: -62.1200
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 18.2664
Cell Significance Index: -72.0800
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 17.8873
Cell Significance Index: -54.9400
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 11.6194
Cell Significance Index: -25.4300
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 2.8614
Cell Significance Index: 337.4500
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: 2.7916
Cell Significance Index: 803.2300
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: 1.9994
Cell Significance Index: 69.4800
Cell Name: fibroblast of dermis (CL0002551)
Fold Change: 1.9459
Cell Significance Index: 40.7300
Cell Name: kidney cell (CL1000497)
Fold Change: 1.8173
Cell Significance Index: 14.5100
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 1.7730
Cell Significance Index: 99.4900
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 1.5661
Cell Significance Index: 314.1600
Cell Name: granulosa cell (CL0000501)
Fold Change: 1.5543
Cell Significance Index: 40.8700
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.5468
Cell Significance Index: 278.8400
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.5393
Cell Significance Index: 189.2700
Cell Name: skeletal muscle myoblast (CL0000515)
Fold Change: 1.4975
Cell Significance Index: 16.2800
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 1.4734
Cell Significance Index: 202.3400
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 1.4072
Cell Significance Index: 228.8700
Cell Name: interstitial cell of ovary (CL0002094)
Fold Change: 1.3450
Cell Significance Index: 17.2300
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.2987
Cell Significance Index: 83.7900
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.2780
Cell Significance Index: 253.6300
Cell Name: cell in vitro (CL0001034)
Fold Change: 1.0819
Cell Significance Index: 590.8400
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.9914
Cell Significance Index: 355.5900
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.9229
Cell Significance Index: 408.0300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.8594
Cell Significance Index: 93.4700
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.7829
Cell Significance Index: 21.3100
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: 0.7130
Cell Significance Index: 44.9400
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.7033
Cell Significance Index: 43.2300
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.6910
Cell Significance Index: 19.3100
Cell Name: odontoblast (CL0000060)
Fold Change: 0.6755
Cell Significance Index: 86.5900
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 0.6350
Cell Significance Index: 18.6500
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.6252
Cell Significance Index: 29.1500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.6096
Cell Significance Index: 27.6300
Cell Name: glycinergic neuron (CL1001509)
Fold Change: 0.6036
Cell Significance Index: 31.6900
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.5834
Cell Significance Index: 27.4200
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: 0.5234
Cell Significance Index: 39.0100
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.4453
Cell Significance Index: 31.4900
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.3327
Cell Significance Index: 9.5900
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.3208
Cell Significance Index: 24.6200
Cell Name: lactocyte (CL0002325)
Fold Change: 0.2846
Cell Significance Index: 36.7600
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.2299
Cell Significance Index: 158.9900
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.2278
Cell Significance Index: 205.6900
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.2036
Cell Significance Index: 38.7500
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.1171
Cell Significance Index: 20.0000
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.1014
Cell Significance Index: 190.9100
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: 0.0985
Cell Significance Index: 3.4600
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0435
Cell Significance Index: 80.2300
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.0390
Cell Significance Index: 60.0400
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.0371
Cell Significance Index: 16.8400
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.0251
Cell Significance Index: 0.6700
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.0242
Cell Significance Index: 15.3700
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.0227
Cell Significance Index: 2.2500
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.0083
Cell Significance Index: 0.5000
Cell Name: mesenchymal cell (CL0008019)
Fold Change: 0.0066
Cell Significance Index: 0.1100
Cell Name: secondary lens fiber (CL0002225)
Fold Change: -0.0006
Cell Significance Index: -0.7800
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0220
Cell Significance Index: -16.1200
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0229
Cell Significance Index: -17.3200
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.0239
Cell Significance Index: -0.4100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.0270
Cell Significance Index: -1.4000
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0394
Cell Significance Index: -29.1800
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0534
Cell Significance Index: -33.3600
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0872
Cell Significance Index: -8.9100
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0890
Cell Significance Index: -50.2000
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1967
Cell Significance Index: -41.4300
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.2102
Cell Significance Index: -5.3700
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.2105
Cell Significance Index: -4.5600
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.2618
Cell Significance Index: -38.0500
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.3238
Cell Significance Index: -9.2800
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.3246
Cell Significance Index: -22.4500
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.3480
Cell Significance Index: -40.5500
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.3531
Cell Significance Index: -40.4500
Cell Name: cone retinal bipolar cell (CL0000752)
Fold Change: -0.4229
Cell Significance Index: -3.2600
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.4277
Cell Significance Index: -28.7600
Cell Name: peg cell (CL4033014)
Fold Change: -0.4975
Cell Significance Index: -11.5000
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.5381
Cell Significance Index: -56.0300
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.5447
Cell Significance Index: -24.1000
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: -0.6097
Cell Significance Index: -15.2400
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.6107
Cell Significance Index: -69.7100
Cell Name: germ cell (CL0000586)
Fold Change: -0.6258
Cell Significance Index: -4.7200
Cell Name: cortical interneuron (CL0008031)
Fold Change: -0.6505
Cell Significance Index: -15.6000
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.6882
Cell Significance Index: -26.0600
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.7252
Cell Significance Index: -57.4300
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.7543
Cell Significance Index: -19.3900
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.7554
Cell Significance Index: -13.9600
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.7619
Cell Significance Index: -20.4200
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.8106
Cell Significance Index: -11.0600
Cell Name: intestinal epithelial cell (CL0002563)
Fold Change: -0.8221
Cell Significance Index: -8.5100
Cell Name: umbrella cell of urothelium (CL4030056)
Fold Change: -0.8383
Cell Significance Index: -7.7200
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -1.0305
Cell Significance Index: -27.5700
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: -1.0501
Cell Significance Index: -13.0300
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -1.0907
Cell Significance Index: -34.9400
Cell Name: kidney epithelial cell (CL0002518)
Fold Change: -1.1010
Cell Significance Index: -32.4300
Cell Name: Purkinje cell (CL0000121)
Fold Change: -1.1189
Cell Significance Index: -24.5000
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -1.1757
Cell Significance Index: -72.0800

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:** RBBP4 is a histone-binding protein that interacts with RB1, a tumor suppressor protein, to regulate chromatin remodeling. It is also a component of the NuRD (Nucleosome Remodeling and Deacetylation) complex, which is involved in the removal of histone H3K4me3 and the deposition of new centromeric nucleosomes. RBBP4 is highly expressed in various cell types, including immune cells, and is involved in the regulation of gene expression through its interactions with transcription factors and chromatin-modifying enzymes. **Pathways and Functions:** RBBP4 is involved in a wide range of cellular processes, including: 1. **Chromatin remodeling**: RBBP4 regulates chromatin structure and function through its interactions with NuRD and other chromatin-modifying enzymes. 2. **Cell cycle regulation**: RBBP4 is involved in the regulation of the cell cycle, particularly during the G1/S transition, through its interactions with cyclin-dependent kinases and other cell cycle regulators. 3. **DNA replication**: RBBP4 is involved in the regulation of DNA replication, particularly during the S phase, through its interactions with DNA polymerases and other replication factors. 4. **Gene expression**: RBBP4 regulates gene expression through its interactions with transcription factors and chromatin-modifying enzymes, influencing the expression of genes involved in development, cell cycle regulation, and immune responses. 5. **Immune responses**: RBBP4 is highly expressed in immune cells and is involved in the regulation of immune responses, particularly during the differentiation of T cells and the regulation of cytokine production. **Clinical Significance:** RBBP4 has been implicated in various diseases, including: 1. **Cancer**: RBBP4 is often overexpressed in cancer cells, where it promotes oncogenesis and tumor progression. 2. **Immunodeficiency**: RBBP4 has been linked to immunodeficiency syndromes, such as X-linked lymphoproliferative disease, where it affects the function of immune cells. 3. **Neurological disorders**: RBBP4 has been implicated in neurological disorders, such as Alzheimer's disease, where it regulates the expression of genes involved in neuronal function and survival. In conclusion, RBBP4 is a critical regulator of chromatin remodeling and cellular processes, with significant implications for our understanding of disease. Further research is needed to fully elucidate the mechanisms by which RBBP4 regulates gene expression and cellular processes, and to explore its potential as a therapeutic target for various diseases. **Implications for Immunology:** RBBP4 has significant implications for our understanding of immune cell development and function. Its regulation of gene expression and chromatin remodeling influences the expression of genes involved in immune responses, including cytokine production and T cell differentiation. Further research is needed to fully elucidate the mechanisms by which RBBP4 regulates immune responses and to explore its potential as a therapeutic target for immunological disorders. **Future Directions:** 1. **Investigating the role of RBBP4 in immune cell development and function**: Further research is needed to fully elucidate the mechanisms by which RBBP4 regulates immune cell development and function. 2. **Exploring the therapeutic potential of RBBP4 inhibition**: RBBP4 inhibition has been shown to have potential therapeutic applications in cancer and immunodeficiency disorders. 3. **Investigating the relationship between RBBP4 and other chromatin-modifying enzymes**: Further research is needed to fully elucidate the mechanisms by which RBBP4 regulates chromatin structure and function, and to explore its interactions with other chromatin-modifying enzymes.

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.

Histone-binding protein RBBP4

Genular Protein ID: 919057450

Symbol: RBBP4_HUMAN

Name: Histone-binding protein RBBP4

UniProtKB Accession Codes:

Q09028 B2R6G9 B4DRH0 D3DPQ3 P31149 Q53H02 Q96BV9

Database IDs:

Citations:

PubMed ID: 8350924

Title: A retinoblastoma-binding protein related to a negative regulator of Ras in yeast.

PubMed ID: 8350924

DOI: 10.1038/364648a0

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16710414

Title: The DNA sequence and biological annotation of human chromosome 1.

PubMed ID: 16710414

DOI: 10.1038/nature04727

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 1699755

Title: Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes.

PubMed ID: 1699755

DOI: 10.1002/elps.1150110703

PubMed ID: 1286667

Title: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.

PubMed ID: 1286667

DOI: 10.1002/elps.11501301199

PubMed ID: 8858152

Title: Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4.

PubMed ID: 8858152

DOI: 10.1016/s0092-8674(00)81326-4

PubMed ID: 9150135

Title: Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex.

PubMed ID: 9150135

DOI: 10.1016/s0092-8674(00)80216-0

PubMed ID: 7503932

Title: Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast.

PubMed ID: 7503932

DOI: 10.1074/jbc.270.43.25507

PubMed ID: 8602529

Title: A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p.

PubMed ID: 8602529

DOI: 10.1126/science.272.5260.408

PubMed ID: 9790534

Title: The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities.

PubMed ID: 9790534

DOI: 10.1016/s0092-8674(00)81758-4

PubMed ID: 9427644

Title: Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase.

PubMed ID: 9427644

DOI: 10.1016/s0960-9822(98)70040-5

PubMed ID: 9651585

Title: SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex.

PubMed ID: 9651585

DOI: 10.1016/s1097-2765(00)80102-1

PubMed ID: 9520398

Title: A role for histone deacetylase activity in HDAC1-mediated transcriptional repression.

PubMed ID: 9520398

DOI: 10.1073/pnas.95.7.3519

PubMed ID: 10444591

Title: Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation.

PubMed ID: 10444591

DOI: 10.1101/gad.13.15.1924

PubMed ID: 10220405

Title: BRCA1 interacts with components of the histone deacetylase complex.

PubMed ID: 10220405

DOI: 10.1073/pnas.96.9.4983

PubMed ID: 10734134

Title: RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein.

PubMed ID: 10734134

DOI: 10.1074/jbc.275.13.9797

PubMed ID: 10866654

Title: Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB.

PubMed ID: 10866654

DOI: 10.1128/mcb.20.14.4970-4978.2000

PubMed ID: 11331609

Title: Sharp, an inducible cofactor that integrates nuclear receptor repression and activation.

PubMed ID: 11331609

DOI: 10.1101/gad.871201

PubMed ID: 11102443

Title: Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1.

PubMed ID: 11102443

DOI: 10.1074/jbc.m007372200

PubMed ID: 11118440

Title: Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex.

PubMed ID: 11118440

DOI: 10.1074/jbc.m007664200

PubMed ID: 12435631

Title: Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein.

PubMed ID: 12435631

DOI: 10.1101/gad.1035902

PubMed ID: 11784859

Title: Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1).

PubMed ID: 11784859

DOI: 10.1128/mcb.22.3.835-848.2002

PubMed ID: 12198550

Title: A chromatin remodelling complex that loads cohesin onto human chromosomes.

PubMed ID: 12198550

DOI: 10.1038/nature01024

PubMed ID: 12351676

Title: Role of histone H3 lysine 27 methylation in Polycomb-group silencing.

PubMed ID: 12351676

DOI: 10.1126/science.1076997

PubMed ID: 14609955

Title: Isolation of human NURF: a regulator of Engrailed gene expression.

PubMed ID: 14609955

DOI: 10.1093/emboj/cdg582

PubMed ID: 12920132

Title: The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity.

PubMed ID: 12920132

DOI: 10.1074/jbc.m302955200

PubMed ID: 15310751

Title: A tissue-specific, naturally occurring human SNF2L variant inactivates chromatin remodeling.

PubMed ID: 15310751

DOI: 10.1074/jbc.m406212200

PubMed ID: 15456747

Title: MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex.

PubMed ID: 15456747

DOI: 10.1074/jbc.m409149200

PubMed ID: 15701600

Title: MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing.

PubMed ID: 15701600

DOI: 10.1074/jbc.m413492200

PubMed ID: 16428440

Title: MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties.

PubMed ID: 16428440

DOI: 10.1128/mcb.26.3.843-851.2006

PubMed ID: 17671431

Title: LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes.

PubMed ID: 17671431

DOI: 10.4161/cc.6.15.4512

PubMed ID: 17531812

Title: Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence.

PubMed ID: 17531812

DOI: 10.1016/j.molcel.2007.04.015

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: 20523938

Title: CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex.

PubMed ID: 20523938

DOI: 10.1039/c004108d

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

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: 24554700

Title: Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6.

PubMed ID: 24554700

DOI: 10.1074/jbc.m113.535351

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: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 26030138

Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.

PubMed ID: 26030138

DOI: 10.1371/journal.pone.0128558

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 28977666

Title: CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality.

PubMed ID: 28977666

DOI: 10.1093/nar/gkx711

PubMed ID: 30026490

Title: Armadillo repeat containing 12 promotes neuroblastoma progression through interaction with retinoblastoma binding protein 4.

PubMed ID: 30026490

DOI: 10.1038/s41467-018-05286-2

PubMed ID: 33283408

Title: Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex.

PubMed ID: 33283408

DOI: 10.1111/febs.15650

PubMed ID: 24920672

Title: Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex.

PubMed ID: 24920672

DOI: 10.1074/jbc.m114.558940

PubMed ID: 30045876

Title: Structural and functional characterization of the RBBP4-ZNF827 interaction and its role in NuRD recruitment to telomeres.

PubMed ID: 30045876

DOI: 10.1042/bcj20180310

PubMed ID: 29499137

Title: Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding.

PubMed ID: 29499137

DOI: 10.1016/j.molcel.2018.01.039

PubMed ID: 31959557

Title: A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island Chromatin.

PubMed ID: 31959557

DOI: 10.1016/j.molcel.2019.12.019

Sequence Information:

Length: 425
Mass: 47656
Checksum: B71E2D55A444C360
Sequence:

MADKEAAFDD AVEERVINEE YKIWKKNTPF LYDLVMTHAL EWPSLTAQWL PDVTRPEGKD 
FSIHRLVLGT HTSDEQNHLV IASVQLPNDD AQFDASHYDS EKGEFGGFGS VSGKIEIEIK 
INHEGEVNRA RYMPQNPCII ATKTPSSDVL VFDYTKHPSK PDPSGECNPD LRLRGHQKEG 
YGLSWNPNLS GHLLSASDDH TICLWDISAV PKEGKVVDAK TIFTGHTAVV EDVSWHLLHE 
SLFGSVADDQ KLMIWDTRSN NTSKPSHSVD AHTAEVNCLS FNPYSEFILA TGSADKTVAL 
WDLRNLKLKL HSFESHKDEI FQVQWSPHNE TILASSGTDR RLNVWDLSKI GEEQSPEDAE 
DGPPELLFIH GGHTAKISDF SWNPNEPWVI CSVSEDNIMQ VWQMAENIYN DEDPEGSVDP 
EGQGS

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: RBBP4

Associated with

Cells (max top 100)

Other Information

A retinoblastoma-binding protein related to a negative regulator of Ras in yeast. PubMed ID: 8350924

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and biological annotation of human chromosome 1. PubMed ID: 16710414

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Two-dimensional gel electrophoresis, protein electroblotting and microsequencing: a direct link between proteins and genes. PubMed ID: 1699755

Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. PubMed ID: 1286667

Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. PubMed ID: 8858152

Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. PubMed ID: 9150135

Dual retinoblastoma-binding proteins with properties related to a negative regulator of ras in yeast. PubMed ID: 7503932

A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. PubMed ID: 8602529

The dermatomyositis-specific autoantigen Mi2 is a component of a complex containing histone deacetylase and nucleosome remodeling activities. PubMed ID: 9790534

Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. PubMed ID: 9427644

SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. PubMed ID: 9651585

A role for histone deacetylase activity in HDAC1-mediated transcriptional repression. PubMed ID: 9520398

Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylation. PubMed ID: 10444591

BRCA1 interacts with components of the histone deacetylase complex. PubMed ID: 10220405

RbAp48 belongs to the histone deacetylase complex that associates with the retinoblastoma protein. PubMed ID: 10734134

Histone binding protein RbAp48 interacts with a complex of CREB binding protein and phosphorylated CREB. PubMed ID: 10866654

Sharp, an inducible cofactor that integrates nuclear receptor repression and activation. PubMed ID: 11331609

Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1. PubMed ID: 11102443

Differential association of products of alternative transcripts of the candidate tumor suppressor ING1 with the mSin3/HDAC1 transcriptional corepressor complex. PubMed ID: 11118440

Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. PubMed ID: 12435631

Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). PubMed ID: 11784859

A chromatin remodelling complex that loads cohesin onto human chromosomes. PubMed ID: 12198550

Role of histone H3 lysine 27 methylation in Polycomb-group silencing. PubMed ID: 12351676

Isolation of human NURF: a regulator of Engrailed gene expression. PubMed ID: 14609955

The metastasis-associated proteins 1 and 2 form distinct protein complexes with histone deacetylase activity. PubMed ID: 12920132

A tissue-specific, naturally occurring human SNF2L variant inactivates chromatin remodeling. PubMed ID: 15310751

MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-binding protein 2 (MBD2) and components of the NuRD complex. PubMed ID: 15456747

MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing. PubMed ID: 15701600

MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties. PubMed ID: 16428440

LINC, a human complex that is related to pRB-containing complexes in invertebrates regulates the expression of G2/M genes. PubMed ID: 17671431

Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex represses human cell cycle-dependent genes in quiescence. PubMed ID: 17531812

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

CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex. PubMed ID: 20523938

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

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

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

Structural and functional insights into the human Borjeson-Forssman-Lehmann syndrome-associated protein PHF6. PubMed ID: 24554700

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

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics. PubMed ID: 26030138

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality. PubMed ID: 28977666

Armadillo repeat containing 12 promotes neuroblastoma progression through interaction with retinoblastoma binding protein 4. PubMed ID: 30026490

Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex. PubMed ID: 33283408

Insight into the architecture of the NuRD complex: structure of the RbAp48-MTA1 subcomplex. PubMed ID: 24920672

Structural and functional characterization of the RBBP4-ZNF827 interaction and its role in NuRD recruitment to telomeres. PubMed ID: 30045876

Unique Structural Platforms of Suz12 Dictate Distinct Classes of PRC2 for Chromatin Binding. PubMed ID: 29499137

A Dimeric Structural Scaffold for PRC2-PCL Targeting to CpG Island Chromatin. PubMed ID: 31959557