RB1 | ENSG00000139687 | NCBI 5925

Details for: RB1

Gene ID: 5925

Symbol: RB1

Ensembl ID: ENSG00000139687

Description: RB transcriptional corepressor 1

Associated with

Aberrant regulation of mitotic cell cycle due to rb1 defects
(R-HSA-9687139)
Aberrant regulation of mitotic exit in cancer due to rb1 defects
(R-HSA-9687136)
Aberrant regulation of mitotic g1/s transition in cancer due to rb1 defects
(R-HSA-9659787)
Apc/c-mediated degradation of cell cycle proteins
(R-HSA-174143)
Apc/c:cdh1 mediated degradation of cdc20 and other apc/c:cdh1 targeted proteins in late mitosis/early g1
(R-HSA-174178)
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)
Condensation of prophase chromosomes
(R-HSA-2299718)
Cyclin a:cdk2-associated events at s phase entry
(R-HSA-69656)
Cyclin d associated events in g1
(R-HSA-69231)
Cyclin e associated events during g1/s transition
(R-HSA-69202)
Defective binding of rb1 mutants to e2f1,(e2f2, e2f3)
(R-HSA-9661069)
Defective translocation of rb1 mutants to the nucleus
(R-HSA-9661070)
Disease
(R-HSA-1643685)
Diseases of mitotic cell cycle
(R-HSA-9675126)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Dna damage/telomere stress induced senescence
(R-HSA-2559586)
E2f mediated regulation of dna replication
(R-HSA-113510)
Early sars-cov-2 infection events
(R-HSA-9772572)
Epigenetic regulation by wdr5-containing histone modifying complexes
(R-HSA-9917777)
Epigenetic regulation of adipogenesis genes by mll3 and mll4 complexes
(R-HSA-9851695)
Epigenetic regulation of gene expression
(R-HSA-212165)
Epigenetic regulation of gene expression by mll3 and mll4 complexes
(R-HSA-9818564)
Formation of senescence-associated heterochromatin foci (sahf)
(R-HSA-2559584)
G1 phase
(R-HSA-69236)
G1/s transition
(R-HSA-69206)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Infectious disease
(R-HSA-5663205)
Inhibition of replication initiation of damaged dna by rb1/e2f1
(R-HSA-113501)
Mitotic g1 phase and g1/s transition
(R-HSA-453279)
Mitotic prophase
(R-HSA-68875)
Mll4 and mll3 complexes regulate expression of pparg target genes in adipogenesis and hepatic steatosis
(R-HSA-9841922)
M phase
(R-HSA-68886)
Nuclear events stimulated by alk signaling in cancer
(R-HSA-9725371)
Oncogene induced senescence
(R-HSA-2559585)
Phosphorylation of proteins involved in g1/s transition by active cyclin e:cdk2 complexes
(R-HSA-69200)
Replication of the sars-cov-1 genome
(R-HSA-9682706)
Replication of the sars-cov-2 genome
(R-HSA-9694686)
Rna polymerase ii transcription
(R-HSA-73857)
Runx2 regulates bone development
(R-HSA-8941326)
Runx2 regulates osteoblast differentiation
(R-HSA-8940973)
Sars-cov-1 genome replication and transcription
(R-HSA-9679514)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-2 genome replication and transcription
(R-HSA-9694682)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov infections
(R-HSA-9679506)
Signaling by alk fusions and activated point mutants
(R-HSA-9725370)
Signaling by alk in cancer
(R-HSA-9700206)
S phase
(R-HSA-69242)
Transcriptional regulation by runx2
(R-HSA-8878166)
Viral infection pathways
(R-HSA-9824446)
Aortic valve morphogenesis
(GO:0003180)
Cell differentiation
(GO:0030154)
Cellular response to insulin stimulus
(GO:0032869)
Chondrocyte differentiation
(GO:0002062)
Chromatin remodeling
(GO:0006338)
Disordered domain specific binding
(GO:0097718)
Dna-binding transcription factor binding
(GO:0140297)
Enucleate erythrocyte differentiation
(GO:0043353)
G1/s transition of mitotic cell cycle
(GO:0000082)
Glial cell apoptotic process
(GO:0034349)
Glial cell proliferation
(GO:0014009)
Heterochromatin formation
(GO:0031507)
Identical protein binding
(GO:0042802)
Importin-alpha family protein binding
(GO:0061676)
Kinase binding
(GO:0019900)
Maintenance of mitotic sister chromatid cohesion
(GO:0034088)
Molecular adaptor activity
(GO:0060090)
Myoblast differentiation
(GO:0045445)
Negative regulation of cell growth
(GO:0030308)
Negative regulation of dna-binding transcription factor activity
(GO:0043433)
Negative regulation of gene expression
(GO:0010629)
Negative regulation of protein kinase activity
(GO:0006469)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Neuron maturation
(GO:0042551)
Neuron projection development
(GO:0031175)
Phosphoprotein binding
(GO:0051219)
Positive regulation of macrophage differentiation
(GO:0045651)
Protein binding
(GO:0005515)
Ras protein signal transduction
(GO:0007265)
Regulation of dna-templated transcription
(GO:0006355)
Regulation of lipid kinase activity
(GO:0043550)
Regulation of mitotic cell cycle
(GO:0007346)
Rna polymerase ii-specific dna-binding transcription factor binding
(GO:0061629)
Rna polymerase ii transcription regulatory region sequence-specific dna binding
(GO:0000977)
Sister chromatid biorientation
(GO:0031134)
Skeletal muscle cell differentiation
(GO:0035914)
Smoothened signaling pathway
(GO:0007224)
Spermatogenesis
(GO:0007283)
Tissue homeostasis
(GO:0001894)
Transcription by rna polymerase ii
(GO:0006366)
Transcription corepressor activity
(GO:0003714)
Ubiquitin protein ligase binding
(GO:0031625)

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: 365.1350
Cell Significance Index: -56.8000
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 236.0795
Cell Significance Index: -59.8800
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 135.0376
Cell Significance Index: -54.8600
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 118.2382
Cell Significance Index: -60.8200
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 95.1682
Cell Significance Index: -63.8600
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 57.6490
Cell Significance Index: -55.0400
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 50.3911
Cell Significance Index: -62.1300
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 22.3080
Cell Significance Index: -59.7600
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 20.1408
Cell Significance Index: -44.0800
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 17.3599
Cell Significance Index: -53.3200
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 15.9400
Cell Significance Index: -62.9000
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: 2.7220
Cell Significance Index: 39.1500
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.1304
Cell Significance Index: 427.3500
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 2.0404
Cell Significance Index: 114.5000
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.8090
Cell Significance Index: 359.0100
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 1.7143
Cell Significance Index: 47.9100
Cell Name: preadipocyte (CL0002334)
Fold Change: 1.6620
Cell Significance Index: 32.4400
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.5852
Cell Significance Index: 1431.3100
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 1.4989
Cell Significance Index: 115.0300
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.3105
Cell Significance Index: 84.5500
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.0057
Cell Significance Index: 360.7300
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.9858
Cell Significance Index: 107.2200
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.9197
Cell Significance Index: 636.1100
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.8703
Cell Significance Index: 141.5500
Cell Name: basal epithelial cell of prostatic duct (CL0002236)
Fold Change: 0.7863
Cell Significance Index: 6.9800
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.7635
Cell Significance Index: 93.8900
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.7183
Cell Significance Index: 129.4800
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.7178
Cell Significance Index: 84.6500
Cell Name: gut absorptive cell (CL0000677)
Fold Change: 0.6183
Cell Significance Index: 37.1200
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.4558
Cell Significance Index: 45.0900
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.4230
Cell Significance Index: 231.0300
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: 0.4100
Cell Significance Index: 25.2000
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.3899
Cell Significance Index: 11.2400
Cell Name: leptomeningeal cell (CL0000708)
Fold Change: 0.3429
Cell Significance Index: 7.3300
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 0.3041
Cell Significance Index: 15.8400
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.2611
Cell Significance Index: 491.5800
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 0.2578
Cell Significance Index: 163.7100
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.2569
Cell Significance Index: 9.7300
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 0.2533
Cell Significance Index: 6.5100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.2378
Cell Significance Index: 15.9900
Cell Name: fibroblast of cardiac tissue (CL0002548)
Fold Change: 0.2096
Cell Significance Index: 3.0100
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.2085
Cell Significance Index: 384.5900
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.1798
Cell Significance Index: 276.8600
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.1772
Cell Significance Index: 4.4300
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: 0.1721
Cell Significance Index: 2.9500
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: 0.1685
Cell Significance Index: 3.6500
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.1530
Cell Significance Index: 69.4200
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.1482
Cell Significance Index: 6.5600
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: 0.1448
Cell Significance Index: 0.8800
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: 0.1335
Cell Significance Index: 6.0500
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.1033
Cell Significance Index: 14.1900
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.1019
Cell Significance Index: 19.4000
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.0948
Cell Significance Index: 41.9200
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0846
Cell Significance Index: 115.0000
Cell Name: corneal epithelial cell (CL0000575)
Fold Change: 0.0330
Cell Significance Index: 0.4700
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.0196
Cell Significance Index: -0.1600
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0406
Cell Significance Index: -5.9000
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0473
Cell Significance Index: -35.0500
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0522
Cell Significance Index: -38.2400
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0578
Cell Significance Index: -36.1100
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0665
Cell Significance Index: -37.5100
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0732
Cell Significance Index: -55.3700
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.0944
Cell Significance Index: -4.4000
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: -0.1047
Cell Significance Index: -2.8000
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.1627
Cell Significance Index: -27.7800
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1666
Cell Significance Index: -17.0200
Cell Name: odontoblast (CL0000060)
Fold Change: -0.1863
Cell Significance Index: -23.8800
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1917
Cell Significance Index: -55.1500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.2093
Cell Significance Index: -44.0800
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2491
Cell Significance Index: -29.0300
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.2564
Cell Significance Index: -12.0500
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.3177
Cell Significance Index: -33.0800
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.3364
Cell Significance Index: -9.6000
Cell Name: lactocyte (CL0002325)
Fold Change: -0.3445
Cell Significance Index: -44.5100
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.3719
Cell Significance Index: -42.6100
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.4219
Cell Significance Index: -14.8300
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.4297
Cell Significance Index: -22.3200
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.4872
Cell Significance Index: -13.2600
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.4904
Cell Significance Index: -55.9800
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.4968
Cell Significance Index: -10.5800
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.4974
Cell Significance Index: -35.1800
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.5342
Cell Significance Index: -33.6700
Cell Name: cortical interneuron (CL0008031)
Fold Change: -0.5416
Cell Significance Index: -12.9900
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.5837
Cell Significance Index: -43.5000
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.6973
Cell Significance Index: -55.2300
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -0.7288
Cell Significance Index: -10.7600
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -0.7331
Cell Significance Index: -13.5500
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.7958
Cell Significance Index: -21.2500
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.8098
Cell Significance Index: -42.5200
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.8210
Cell Significance Index: -21.9600
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.8221
Cell Significance Index: -9.8000
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.8563
Cell Significance Index: -52.5000
Cell Name: pvalb GABAergic cortical interneuron (CL4023018)
Fold Change: -1.0154
Cell Significance Index: -21.5500
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -1.0283
Cell Significance Index: -14.0300
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -1.1107
Cell Significance Index: -31.8400
Cell Name: OFF midget ganglion cell (CL4033047)
Fold Change: -1.1364
Cell Significance Index: -14.1700
Cell Name: type I muscle cell (CL0002211)
Fold Change: -1.1398
Cell Significance Index: -27.8100
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.1600
Cell Significance Index: -37.9800
Cell Name: granulosa cell (CL0000501)
Fold Change: -1.1793
Cell Significance Index: -31.0100
Cell Name: corticothalamic-projecting glutamatergic cortical neuron (CL4023013)
Fold Change: -1.1862
Cell Significance Index: -37.7800

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. **Transcriptional Corepressor**: The RB1 gene acts as a transcriptional corepressor, repressing the expression of genes involved in cell proliferation and DNA replication. 2. **Cell Cycle Regulation**: RB1 regulates the G1/S transition and mitosis, ensuring proper cell cycle progression and preventing uncontrolled cell growth. 3. **DNA Binding**: RB1 binds to specific DNA sequences, regulating gene expression and modulating the cell cycle. 4. **Protein-Protein Interactions**: RB1 interacts with various proteins, including E2F transcription factors, cyclin-dependent kinases, and other cell cycle regulators. 5. **Tumor Suppressor Function**: RB1 acts as a tumor suppressor, preventing the development of cancer by regulating cell proliferation and preventing uncontrolled cell growth. **Pathways and Functions** 1. **Apc/C-Mediated Degradation**: RB1 regulates the degradation of cell cycle proteins by the Apc/C pathway, ensuring proper cell cycle progression. 2. **Cyclin A/CDK2-Associated Events**: RB1 regulates the association of cyclin A with CDK2, ensuring proper S-phase entry and progression. 3. **G1/S Transition**: RB1 regulates the G1/S transition by repressing the expression of genes involved in cell proliferation and DNA replication. 4. **Mitotic Cell Cycle**: RB1 regulates the mitotic cell cycle, ensuring proper chromosome segregation and preventing aneuploidy. 5. **Senescence-Associated Heterochromatin Foci (SAHF)**: RB1 regulates the formation of SAHF, a hallmark of cellular senescence. **Clinical Significance** 1. **Retinoblastoma**: Mutations in the RB1 gene are associated with retinoblastoma, a malignant tumor of the retina. 2. **Other Cancers**: RB1 mutations are also associated with other cancers, including osteosarcoma, breast cancer, and colon cancer. 3. **Neurological Disorders**: RB1 mutations are associated with neurological disorders, including neurofibromatosis type 1 and frontotemporal dementia. 4. **Cardiovascular Disease**: RB1 mutations are associated with cardiovascular disease, including aortic valve morphogenesis and cardiac neuron dysfunction. 5. **Infectious Diseases**: RB1 mutations are associated with infectious diseases, including SARS-CoV-1 and SARS-CoV-2 infections. In conclusion, the RB1 gene plays a critical role in regulating the cell cycle, particularly during the G1/S transition and mitosis. Mutations or alterations in the RB1 gene can lead to aberrant regulation of the cell cycle, resulting in uncontrolled cell growth and tumor formation. Understanding the function and regulation of the RB1 gene is essential for developing effective therapeutic strategies for various diseases.

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.

Retinoblastoma-associated protein

Genular Protein ID: 4096655941

Symbol: RB_HUMAN

Name: Retinoblastoma-associated protein

UniProtKB Accession Codes:

P06400 A8K5E3 P78499 Q5VW46 Q8IZL4

Database IDs:

Citations:

PubMed ID: 3657987

Title: The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNA binding activity.

PubMed ID: 3657987

DOI: 10.1038/329642a0

PubMed ID: 3823889

Title: Human retinoblastoma susceptibility gene: cloning, identification, and sequence.

PubMed ID: 3823889

DOI: 10.1126/science.3823889

PubMed ID: 3480530

Title: Deletions of a DNA sequence in retinoblastomas and mesenchymal tumors: organization of the sequence and its encoded protein.

PubMed ID: 3480530

DOI: 10.1073/pnas.84.24.9059

PubMed ID: 2701949

Title: Structure and partial genomic sequence of the human retinoblastoma susceptibility gene.

PubMed ID: 2701949

DOI: 10.1016/0378-1119(89)90256-4

PubMed ID: 1352398

Title: Detection of heterozygous mutations in the RB1 gene in retinoblastoma patients using single-strand conformation polymorphism analysis and polymerase chain reaction sequencing.

PubMed ID: 1352398

PubMed ID: 7902321

Title: Complete genomic sequence of the human retinoblastoma susceptibility gene.

PubMed ID: 7902321

DOI: 10.1006/geno.1993.1368

PubMed ID: 14702039

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

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057823

Title: The DNA sequence and analysis of human chromosome 13.

PubMed ID: 15057823

DOI: 10.1038/nature02379

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: 2717184

Title: Genomic organization of the human retinoblastoma gene.

PubMed ID: 2717184

PubMed ID: 7881418

Title: Spectrum of small length germline mutations in the RB1 gene.

PubMed ID: 7881418

DOI: 10.1093/hmg/3.12.2187

PubMed ID: 1316611

Title: Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma gene product.

PubMed ID: 1316611

DOI: 10.1073/pnas.89.10.4549

PubMed ID: 8336704

Title: A bipartite nuclear localization signal in the retinoblastoma gene product and its importance for biological activity.

PubMed ID: 8336704

DOI: 10.1128/mcb.13.8.4588-4599.1993

PubMed ID: 8114739

Title: Identification of G1 kinase activity for cdk6, a novel cyclin D partner.

PubMed ID: 8114739

DOI: 10.1128/mcb.14.3.2077-2086.1994

PubMed ID: 2839300

Title: SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene.

PubMed ID: 2839300

DOI: 10.1016/0092-8674(88)90559-4

PubMed ID: 3413073

Title: Molecular mechanism of retinoblastoma gene inactivation in retinoblastoma cell line Y79.

PubMed ID: 3413073

DOI: 10.1073/pnas.85.16.6017

PubMed ID: 1756735

Title: The retinoblastoma protein is phosphorylated on multiple sites by human cdc2.

PubMed ID: 1756735

DOI: 10.1002/j.1460-2075.1991.tb05006.x

PubMed ID: 8414517

Title: Characterization of the retinoblastoma binding proteins RBP1 and RBP2.

PubMed ID: 8414517

PubMed ID: 7525595

Title: The amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing.

PubMed ID: 7525595

DOI: 10.1083/jcb.127.3.609

PubMed ID: 7935440

Title: Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein.

PubMed ID: 7935440

DOI: 10.1128/mcb.14.11.7256-7264.1994

PubMed ID: 8892909

Title: The human cytomegalovirus IE1-72 protein interacts with the cellular p107 protein and relieves p107-mediated transcriptional repression of an E2F-responsive promoter.

PubMed ID: 8892909

DOI: 10.1128/jvi.70.11.7867-7877.1996

PubMed ID: 10446990

Title: Bdp, a new member of a family of DNA-binding proteins, associates with the retinoblastoma gene product.

PubMed ID: 10446990

PubMed ID: 10499802

Title: Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1.

PubMed ID: 10499802

DOI: 10.1016/s0092-8674(00)81519-6

PubMed ID: 10409732

Title: Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins.

PubMed ID: 10409732

DOI: 10.1128/mcb.19.8.5417

PubMed ID: 10779342

Title: Retinoblastoma protein enhances the fidelity of chromosome segregation mediated by hsHec1p.

PubMed ID: 10779342

DOI: 10.1128/mcb.20.10.3529-3537.2000

PubMed ID: 9858607

Title: Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250.

PubMed ID: 9858607

DOI: 10.1128/mcb.19.1.846

PubMed ID: 10197586

Title: The partial homeodomain of the transcription factor Pax-5 (BSAP) is an interaction motif for the retinoblastoma and TATA-binding proteins.

PubMed ID: 10197586

PubMed ID: 10869426

Title: pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F.

PubMed ID: 10869426

DOI: 10.1073/pnas.130198397

PubMed ID: 11223246

Title: Identification and characterization of a novel human cDNA encoding a 21 kDa pRb-associated protein.

PubMed ID: 11223246

DOI: 10.1016/s0378-1119(00)00585-0

PubMed ID: 10888886

Title: DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters.

PubMed ID: 10888886

DOI: 10.1038/77124

PubMed ID: 11484059

Title: Rb targets histone H3 methylation and HP1 to promoters.

PubMed ID: 11484059

DOI: 10.1038/35087620

PubMed ID: 11571652

Title: The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein.

PubMed ID: 11571652

DOI: 10.1038/sj.onc.1204824

PubMed ID: 12450794

Title: Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb.

PubMed ID: 12450794

DOI: 10.1016/s1535-6108(02)00182-4

PubMed ID: 12475961

Title: Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein.

PubMed ID: 12475961

DOI: 10.1091/mbc.e02-07-0450

PubMed ID: 12466551

Title: Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity.

PubMed ID: 12466551

DOI: 10.1093/nar/gkf658

PubMed ID: 12037672

Title: Physical interaction between pRb and cdk9/cyclinT2 complex.

PubMed ID: 12037672

DOI: 10.1038/sj.onc.1205511

PubMed ID: 12682072

Title: Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein.

PubMed ID: 12682072

DOI: 10.1074/jbc.m212822200

PubMed ID: 12626766

Title: Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein.

PubMed ID: 12626766

DOI: 10.1073/pnas.0538058100

PubMed ID: 15084261

Title: Cyclin C/cdk3 promotes Rb-dependent G0 exit.

PubMed ID: 15084261

DOI: 10.1016/s0092-8674(04)00300-9

PubMed ID: 15538385

Title: Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein.

PubMed ID: 15538385

DOI: 10.1038/sj.emboj.7600470

PubMed ID: 15107404

Title: Liver tumors escape negative control of proliferation via PI3K/Akt-mediated block of C/EBP alpha growth inhibitory activity.

PubMed ID: 15107404

DOI: 10.1101/gad.1183304

PubMed ID: 15542589

Title: LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription.

PubMed ID: 15542589

DOI: 10.1073/pnas.0407123101

PubMed ID: 15809340

Title: Preferences for phosphorylation sites in the retinoblastoma protein of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro.

PubMed ID: 15809340

DOI: 10.1093/jb/mvi050

PubMed ID: 15927959

Title: Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein.

PubMed ID: 15927959

DOI: 10.1074/jbc.m413687200

PubMed ID: 15803180

Title: Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas.

PubMed ID: 15803180

DOI: 10.1038/modpathol.3800413

PubMed ID: 15949438

Title: Binding of pRB to the PHD protein RBP2 promotes cellular differentiation.

PubMed ID: 15949438

DOI: 10.1016/j.molcel.2005.05.012

PubMed ID: 16337594

Title: MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein.

PubMed ID: 16337594

DOI: 10.1016/j.molcel.2005.10.017

PubMed ID: 16214886

Title: p600, a unique protein required for membrane morphogenesis and cell survival.

PubMed ID: 16214886

DOI: 10.1073/pnas.0507458102

PubMed ID: 16645588

Title: Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells.

PubMed ID: 16645588

DOI: 10.1038/sj.jid.5700324

PubMed ID: 17380128

Title: Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB and E2F-1 after DNA damage.

PubMed ID: 17380128

DOI: 10.1038/sj.emboj.7601652

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18701596

Title: Targeting the retinoblastoma protein by MC007L, gene product of the molluscum contagiosum virus: detection of a novel virus-cell interaction by a member of the poxviruses.

PubMed ID: 18701596

DOI: 10.1128/jvi.01187-08

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: 20870719

Title: Methylation of the retinoblastoma tumor suppressor by SMYD2.

PubMed ID: 20870719

DOI: 10.1074/jbc.m110.137612

PubMed ID: 20940255

Title: Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation.

PubMed ID: 20940255

DOI: 10.1242/jcs.068924

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: 21952639

Title: NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor.

PubMed ID: 21952639

DOI: 10.4161/cc.10.19.17176

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22787429

Title: RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation.

PubMed ID: 22787429

DOI: 10.1593/neo.12656

PubMed ID: 23186163

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

PubMed ID: 23186163

DOI: 10.1021/pr300630k

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: 26986503

Title: BLCAP arrests G(1)/S checkpoint and induces apoptosis through downregulation of pRb1 in HeLa cells.

PubMed ID: 26986503

DOI: 10.3892/or.2016.4686

PubMed ID: 9145110

Title: Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box.

PubMed ID: 9145110

DOI: 10.1038/nsb0597-390

PubMed ID: 9495340

Title: Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7.

PubMed ID: 9495340

DOI: 10.1038/36038

PubMed ID: 12695505

Title: Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha.

PubMed ID: 12695505

DOI: 10.1074/jbc.m303275200

PubMed ID: 16360038

Title: Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release.

PubMed ID: 16360038

DOI: 10.1016/j.cell.2005.09.044

PubMed ID: 17974914

Title: Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor.

PubMed ID: 17974914

DOI: 10.1101/gad.1590607

PubMed ID: 17996702

Title: Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture.

PubMed ID: 17996702

DOI: 10.1016/j.molcel.2007.08.023

PubMed ID: 2594029

Title: Oncogenic point mutations in the human retinoblastoma gene: their application to genetic counseling.

PubMed ID: 2594029

DOI: 10.1056/nejm198912213212501

PubMed ID: 1352883

Title: Oncogenic point mutations in exon 20 of the RB1 gene in families showing incomplete penetrance and mild expression of the retinoblastoma phenotype.

PubMed ID: 1352883

DOI: 10.1073/pnas.89.13.6177

PubMed ID: 8346255

Title: Molecular mechanisms of oncogenic mutations in tumors from patients with bilateral and unilateral retinoblastoma.

PubMed ID: 8346255

DOI: 10.1073/pnas.90.15.7351

PubMed ID: 7704558

Title: Frequent constitutional C to T mutations in CGA-arginine codons in the RB1 gene produce premature stop codons in patients with bilateral (hereditary) retinoblastoma.

PubMed ID: 7704558

DOI: 10.1159/000472372

PubMed ID: 7927327

Title: Distinct RB1 gene mutations with low penetrance in hereditary retinoblastoma.

PubMed ID: 7927327

DOI: 10.1007/bf00201591

PubMed ID: 8605116

Title: Germline mutations in the RB1 gene in patients with hereditary retinoblastoma.

PubMed ID: 8605116

DOI: 10.1002/gcc.2870140406

PubMed ID: 7795591

Title: Spectrum of germline mutations in the RB1 gene: a study of 232 patients with hereditary and non hereditary retinoblastoma.

PubMed ID: 7795591

DOI: 10.1093/hmg/4.3.383

PubMed ID: 8776589

Title: Mutational scanning of large genes by extensive PCR multiplexing and two-dimensional electrophoresis: application to the RB1 gene.

PubMed ID: 8776589

DOI: 10.1093/hmg/5.6.755

PubMed ID: 9311732

Title: Constitutional RB1-gene mutations in patients with isolated unilateral retinoblastoma.

PubMed ID: 9311732

DOI: 10.1086/514845

PubMed ID: 9140452

Title: Genetics of retinoblastoma: a study.

PubMed ID: 9140452

DOI: 10.1016/s0165-4608(96)00387-1

PubMed ID: 10671068

Title: Twelve novel RB1 gene mutations in patients with hereditary retinoblastoma.

PubMed ID: 10671068

DOI: 10.1002/(sici)1098-1004(1998)12:6<434::aid-humu16>3.0.co;2-7

PubMed ID: 9973307

Title: RB1 gene mutations in peripheral blood DNA of patients with isolated unilateral retinoblastoma.

PubMed ID: 9973307

DOI: 10.1086/302254

PubMed ID: 11524739

Title: Identification of four novel RB1 germline mutations in Korean retinoblastoma patients.

PubMed ID: 11524739

DOI: 10.1002/humu.1184

PubMed ID: 23033978

Title: Diagnostic exome sequencing in persons with severe intellectual disability.

PubMed ID: 23033978

DOI: 10.1056/nejmoa1206524

Sequence Information:

Length: 928
Mass: 106159
Checksum: C8E746111E19CC32
Sequence:

MPPKTPRKTA ATAAAAAAEP PAPPPPPPPE EDPEQDSGPE DLPLVRLEFE ETEEPDFTAL 
CQKLKIPDHV RERAWLTWEK VSSVDGVLGG YIQKKKELWG ICIFIAAVDL DEMSFTFTEL 
QKNIEISVHK FFNLLKEIDT STKVDNAMSR LLKKYDVLFA LFSKLERTCE LIYLTQPSSS 
ISTEINSALV LKVSWITFLL AKGEVLQMED DLVISFQLML CVLDYFIKLS PPMLLKEPYK 
TAVIPINGSP RTPRRGQNRS ARIAKQLEND TRIIEVLCKE HECNIDEVKN VYFKNFIPFM 
NSLGLVTSNG LPEVENLSKR YEEIYLKNKD LDARLFLDHD KTLQTDSIDS FETQRTPRKS 
NLDEEVNVIP PHTPVRTVMN TIQQLMMILN SASDQPSENL ISYFNNCTVN PKESILKRVK 
DIGYIFKEKF AKAVGQGCVE IGSQRYKLGV RLYYRVMESM LKSEEERLSI QNFSKLLNDN 
IFHMSLLACA LEVVMATYSR STSQNLDSGT DLSFPWILNV LNLKAFDFYK VIESFIKAEG 
NLTREMIKHL ERCEHRIMES LAWLSDSPLF DLIKQSKDRE GPTDHLESAC PLNLPLQNNH 
TAADMYLSPV RSPKKKGSTT RVNSTANAET QATSAFQTQK PLKSTSLSLF YKKVYRLAYL 
RLNTLCERLL SEHPELEHII WTLFQHTLQN EYELMRDRHL DQIMMCSMYG ICKVKNIDLK 
FKIIVTAYKD LPHAVQETFK RVLIKEEEYD SIIVFYNSVF MQRLKTNILQ YASTRPPTLS 
PIPHIPRSPY KFPSSPLRIP GGNIYISPLK SPYKISEGLP TPTKMTPRSR ILVSIGESFG 
TSEKFQKINQ MVCNSDRVLK RSAEGSNPPK PLKKLRFDIE GSDEADGSKH LPGESKFQQK 
LAEMTSTRTR MQKQKMNDSM DTSNKEEK

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: RB1

Associated with

Cells (max top 100)

Other Information

The retinoblastoma susceptibility gene encodes a nuclear phosphoprotein associated with DNA binding activity. PubMed ID: 3657987

Human retinoblastoma susceptibility gene: cloning, identification, and sequence. PubMed ID: 3823889

Deletions of a DNA sequence in retinoblastomas and mesenchymal tumors: organization of the sequence and its encoded protein. PubMed ID: 3480530

Structure and partial genomic sequence of the human retinoblastoma susceptibility gene. PubMed ID: 2701949

Detection of heterozygous mutations in the RB1 gene in retinoblastoma patients using single-strand conformation polymorphism analysis and polymerase chain reaction sequencing. PubMed ID: 1352398

Complete genomic sequence of the human retinoblastoma susceptibility gene. PubMed ID: 7902321

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

The DNA sequence and analysis of human chromosome 13. PubMed ID: 15057823

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

Genomic organization of the human retinoblastoma gene. PubMed ID: 2717184

Spectrum of small length germline mutations in the RB1 gene. PubMed ID: 7881418

Adenovirus E1A, simian virus 40 tumor antigen, and human papillomavirus E7 protein share the capacity to disrupt the interaction between transcription factor E2F and the retinoblastoma gene product. PubMed ID: 1316611

A bipartite nuclear localization signal in the retinoblastoma gene product and its importance for biological activity. PubMed ID: 8336704

Identification of G1 kinase activity for cdk6, a novel cyclin D partner. PubMed ID: 8114739

SV40 large tumor antigen forms a specific complex with the product of the retinoblastoma susceptibility gene. PubMed ID: 2839300

Molecular mechanism of retinoblastoma gene inactivation in retinoblastoma cell line Y79. PubMed ID: 3413073

The retinoblastoma protein is phosphorylated on multiple sites by human cdc2. PubMed ID: 1756735

Characterization of the retinoblastoma binding proteins RBP1 and RBP2. PubMed ID: 8414517

The amino-terminal region of the retinoblastoma gene product binds a novel nuclear matrix protein that co-localizes to centers for RNA processing. PubMed ID: 7525595

Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein. PubMed ID: 7935440

The human cytomegalovirus IE1-72 protein interacts with the cellular p107 protein and relieves p107-mediated transcriptional repression of an E2F-responsive promoter. PubMed ID: 8892909

Bdp, a new member of a family of DNA-binding proteins, associates with the retinoblastoma gene product. PubMed ID: 10446990

Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. PubMed ID: 10499802

Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins. PubMed ID: 10409732

Retinoblastoma protein enhances the fidelity of chromosome segregation mediated by hsHec1p. PubMed ID: 10779342

Rb inhibits the intrinsic kinase activity of TATA-binding protein-associated factor TAFII250. PubMed ID: 9858607

The partial homeodomain of the transcription factor Pax-5 (BSAP) is an interaction motif for the retinoblastoma and TATA-binding proteins. PubMed ID: 10197586

pRB binds to and modulates the transrepressing activity of the E1A-regulated transcription factor p120E4F. PubMed ID: 10869426

Identification and characterization of a novel human cDNA encoding a 21 kDa pRb-associated protein. PubMed ID: 11223246

DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses transcription from E2F-responsive promoters. PubMed ID: 10888886

Rb targets histone H3 methylation and HP1 to promoters. PubMed ID: 11484059

The de-ubiquitinating enzyme Unp interacts with the retinoblastoma protein. PubMed ID: 11571652

Che-1 affects cell growth by interfering with the recruitment of HDAC1 by Rb. PubMed ID: 12450794

Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein. PubMed ID: 12475961

Skip interacts with the retinoblastoma tumor suppressor and inhibits its transcriptional repression activity. PubMed ID: 12466551

Physical interaction between pRb and cdk9/cyclinT2 complex. PubMed ID: 12037672

Functional interactions between the estrogen receptor coactivator PELP1/MNAR and retinoblastoma protein. PubMed ID: 12682072

Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. PubMed ID: 12626766

Cyclin C/cdk3 promotes Rb-dependent G0 exit. PubMed ID: 15084261

Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein. PubMed ID: 15538385

Liver tumors escape negative control of proliferation via PI3K/Akt-mediated block of C/EBP alpha growth inhibitory activity. PubMed ID: 15107404

LIM domains-containing protein 1 (LIMD1), a tumor suppressor encoded at chromosome 3p21.3, binds pRB and represses E2F-driven transcription. PubMed ID: 15542589

Preferences for phosphorylation sites in the retinoblastoma protein of D-type cyclin-dependent kinases, Cdk4 and Cdk6, in vitro. PubMed ID: 15809340

Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. PubMed ID: 15927959

Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas. PubMed ID: 15803180

Binding of pRB to the PHD protein RBP2 promotes cellular differentiation. PubMed ID: 15949438

MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein. PubMed ID: 16337594

p600, a unique protein required for membrane morphogenesis and cell survival. PubMed ID: 16214886

Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells. PubMed ID: 16645588

Phosphorylation of pRB at Ser612 by Chk1/2 leads to a complex between pRB and E2F-1 after DNA damage. PubMed ID: 17380128

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Targeting the retinoblastoma protein by MC007L, gene product of the molluscum contagiosum virus: detection of a novel virus-cell interaction by a member of the poxviruses. PubMed ID: 18701596

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

Methylation of the retinoblastoma tumor suppressor by SMYD2. PubMed ID: 20870719

Acetylation of Rb by PCAF is required for nuclear localization and keratinocyte differentiation. PubMed ID: 20940255

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

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

NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor. PubMed ID: 21952639

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

RB1 methylation by SMYD2 enhances cell cycle progression through an increase of RB1 phosphorylation. PubMed ID: 22787429

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

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

BLCAP arrests G(1)/S checkpoint and induces apoptosis through downregulation of pRb1 in HeLa cells. PubMed ID: 26986503

Structural similarity between the pocket region of retinoblastoma tumour suppressor and the cyclin-box. PubMed ID: 9145110

Structure of the retinoblastoma tumour-suppressor pocket domain bound to a peptide from HPV E7. PubMed ID: 9495340

Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-alpha. PubMed ID: 12695505

Structure of the Rb C-terminal domain bound to E2F1-DP1: a mechanism for phosphorylation-induced E2F release. PubMed ID: 16360038

Structure of the retinoblastoma protein bound to adenovirus E1A reveals the molecular basis for viral oncoprotein inactivation of a tumor suppressor. PubMed ID: 17974914

Crystal structure of the retinoblastoma protein N domain provides insight into tumor suppression, ligand interaction, and holoprotein architecture. PubMed ID: 17996702

Oncogenic point mutations in the human retinoblastoma gene: their application to genetic counseling. PubMed ID: 2594029

Oncogenic point mutations in exon 20 of the RB1 gene in families showing incomplete penetrance and mild expression of the retinoblastoma phenotype. PubMed ID: 1352883

Molecular mechanisms of oncogenic mutations in tumors from patients with bilateral and unilateral retinoblastoma. PubMed ID: 8346255

Frequent constitutional C to T mutations in CGA-arginine codons in the RB1 gene produce premature stop codons in patients with bilateral (hereditary) retinoblastoma. PubMed ID: 7704558