RB1 and CCNA2

Number of citations of the paper that reports this interaction (PubMedID 9885575)
139

Data Source:
BioGRID (affinity chromatography technology, enzymatic study, enzymatic study, enzymatic study, enzymatic study, enzymatic study, enzymatic study, enzymatic study)

		RB1	CCNA2
Description		RB transcriptional corepressor 1	cyclin A2
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GO Annotations	Cellular Component	Chromatin Nucleus Nucleoplasm Transcription Regulator Complex Spindle Cytosol SWI/SNF Complex PML Body Rb-E2F Complex	Cyclin-dependent Protein Kinase Holoenzyme Complex Female Pronucleus Male Pronucleus Nucleus Nucleoplasm Cytoplasm Cytosol Cyclin A2-CDK2 Complex
	Molecular Function	RNA Polymerase II Transcription Regulatory Region Sequence-specific DNA Binding Transcription Corepressor Activity Protein Binding Transcription Factor Binding Kinase Binding Ubiquitin Protein Ligase Binding Identical Protein Binding Phosphoprotein Binding RNA Polymerase II-specific DNA-binding Transcription Factor Binding Importin-alpha Family Protein Binding Disordered Domain Specific Binding DNA-binding Transcription Factor Binding	Protein Binding Cyclin-dependent Protein Serine/threonine Kinase Regulator Activity Protein Kinase Binding Protein Domain Specific Binding
	Biological Process	Negative Regulation Of Transcription By RNA Polymerase II Tissue Homeostasis Aortic Valve Morphogenesis Chromatin Remodeling Regulation Of Transcription, DNA-templated Negative Regulation Of Protein Kinase Activity Ras Protein Signal Transduction Regulation Of Mitotic Cell Cycle Negative Regulation Of Gene Expression Cell Differentiation Negative Regulation Of Cell Growth Sister Chromatid Biorientation Neuron Projection Development Maintenance Of Mitotic Sister Chromatid Cohesion Glial Cell Apoptotic Process Skeletal Muscle Cell Differentiation Neuron Maturation Enucleate Erythrocyte Differentiation Negative Regulation Of DNA-binding Transcription Factor Activity Regulation Of Lipid Kinase Activity Myoblast Differentiation Positive Regulation Of Macrophage Differentiation Negative Regulation Of Cell Cycle Positive Regulation Of Mitotic Metaphase/anaphase Transition Negative Regulation Of Smoothened Signaling Pathway Negative Regulation Of Transcription, DNA-templated Positive Regulation Of Transcription By RNA Polymerase II Digestive Tract Development Cell Morphogenesis Involved In Neuron Differentiation Negative Regulation Of Epithelial Cell Proliferation Negative Regulation Of Inflammatory Response Striated Muscle Cell Differentiation Cell Division Neuron Apoptotic Process Regulation Of Cell Cycle Protein Localization To Chromosome, Centromeric Region Cellular Response To Xenobiotic Stimulus Negative Regulation Of Protein Serine/threonine Kinase Activity Regulation Of Cohesin Loading Negative Regulation Of Transcription Involved In G1/S Transition Of Mitotic Cell Cycle Regulation Of Centromere Complex Assembly Hepatocyte Apoptotic Process Negative Regulation Of Cold-induced Thermogenesis Negative Regulation Of Tau-protein Kinase Activity Positive Regulation Of Extracellular Matrix Organization Positive Regulation Of Collagen Fibril Organization Negative Regulation Of Myofibroblast Differentiation Negative Regulation Of G1/S Transition Of Mitotic Cell Cycle Positive Regulation Of Transcription Regulatory Region DNA Binding Negative Regulation Of Apoptotic Signaling Pathway	Regulation Of Cyclin-dependent Protein Serine/threonine Kinase Activity G2/M Transition Of Mitotic Cell Cycle Regulation Of DNA Replication Ras Protein Signal Transduction Histone Phosphorylation Animal Organ Regeneration Response To Glucagon Cellular Response To Platelet-derived Growth Factor Stimulus Cellular Response To Leptin Stimulus Mitotic Cell Cycle Phase Transition Cell Cycle G1/S Phase Transition Positive Regulation Of Transcription, DNA-templated Positive Regulation Of Fibroblast Proliferation Cell Division Cellular Response To Cocaine Cellular Response To Luteinizing Hormone Stimulus Cellular Response To Estradiol Stimulus Cellular Response To Hypoxia Cellular Response To Nitric Oxide Cochlea Development Cellular Response To Insulin-like Growth Factor Stimulus
Pathways		Inhibition of replication initiation of damaged DNA by RB1/E2F1 Inhibition of replication initiation of damaged DNA by RB1/E2F1 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 Condensation of Prophase Chromosomes Formation of Senescence-Associated Heterochromatin Foci (SAHF) Oncogene Induced Senescence Phosphorylation of proteins involved in G1/S transition by active Cyclin E:Cdk2 complexes Cyclin E associated events during G1/S transition Cyclin D associated events in G1 Cyclin A:Cdk2-associated events at S phase entry RUNX2 regulates osteoblast differentiation Defective binding of RB1 mutants to E2F1,(E2F2, E2F3) Defective translocation of RB1 mutants to the nucleus Replication of the SARS-CoV-1 genome Aberrant regulation of mitotic exit in cancer due to RB1 defects Replication of the SARS-CoV-2 genome	Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 G0 and Early G1 Phosphorylation of proteins involved in the G2/M transition by Cyclin A:Cdc2 complexes Telomere Extension By Telomerase Cdc20:Phospho-APC/C mediated degradation of Cyclin A Regulation of APC/C activators between G1/S and early anaphase SCF(Skp2)-mediated degradation of p27/p21 Senescence-Associated Secretory Phenotype (SASP) DNA Damage/Telomere Stress Induced Senescence Ub-specific processing proteases Processing of DNA double-strand break ends TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest Regulation of TP53 Activity through Phosphorylation Regulation of TP53 Degradation G2 Phase Orc1 removal from chromatin CDK-mediated phosphorylation and removal of Cdc6 Cyclin A/B1/B2 associated events during G2/M transition Cyclin A/B1/B2 associated events during G2/M transition p53-Dependent G1 DNA Damage Response Cyclin A:Cdk2-associated events at S phase entry
Drugs		Insulin human Insulin pork	4-(2,4-Dimethyl-Thiazol-5-Yl)-Pyrimidin-2-Ylamine 6-O-Cyclohexylmethyl Guanine [4-(2-Amino-4-Methyl-Thiazol-5-Yl)-Pyrimidin-2-Yl]-(3-Nitro-Phenyl)-Amine 4-(2,4-Dimethyl-1,3-thiazol-5-yl)-N-[4-(trifluoromethyl)phenyl]-2-pyrimidinamine 4-[(7-OXO-7H-THIAZOLO[5,4-E]INDOL-8-YLMETHYL)-AMINO]-N-PYRIDIN-2-YL-BENZENESULFONAMIDE N-(3-cyclopropyl-1H-pyrazol-5-yl)-2-(2-naphthyl)acetamide 2-ANILINO-6-CYCLOHEXYLMETHOXYPURINE O6-CYCLOHEXYLMETHOXY-2-(4'-SULPHAMOYLANILINO) PURINE (2S)-N-[(3E)-5-Cyclopropyl-3H-pyrazol-3-ylidene]-2-[4-(2-oxo-1-imidazolidinyl)phenyl]propanamide N-cyclopropyl-4-pyrazolo[1,5-b]pyridazin-3-ylpyrimidin-2-amine 6-CYCLOHEXYLMETHOXY-2-(3'-CHLOROANILINO) PURINE 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]-2-FURYL}-N-METHYLBENZENESULFONAMIDE 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZENESULFONAMIDE 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}-2-(TRIFLUOROMETHYL)BENZENESULFONAMIDE 4-{5-[(Z)-(2-IMINO-4-OXO-1,3-THIAZOLIDIN-5-YLIDENE)METHYL]FURAN-2-YL}BENZOIC ACID N-[4-(2,4-DIMETHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-N',N'-DIMETHYL-BENZENE-1,4-DIAMINE 4-{[5-(CYCLOHEXYLOXY)[1,2,4]TRIAZOLO[1,5-A]PYRIMIDIN-7-YL]AMINO}BENZENESULFONAMIDE 1-(3,5-DICHLOROPHENYL)-5-METHYL-1H-1,2,4-TRIAZOLE-3-CARBOXYLIC ACID 4-(4-methoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine 4-(4-propoxy-1H-pyrrolo[2,3-b]pyridin-3-yl)pyrimidin-2-amine HYDROXY(OXO)(3-{[(2Z)-4-[3-(1H-1,2,4-TRIAZOL-1-YLMETHYL)PHENYL]PYRIMIDIN-2(5H)-YLIDENE]AMINO}PHENYL)AMMONIUM 4-Methyl-5-[(2Z)-2-{[4-(4-morpholinyl)phenyl]imino}-2,5-dihydro-4-pyrimidinyl]-1,3-thiazol-2-amine 6-CYCLOHEXYLMETHYLOXY-2-(4'-HYDROXYANILINO)PURINE 4-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)--BENZAMIDE 3-(6-CYCLOHEXYLMETHOXY-9H-PURIN-2-YLAMINO)-BENZENESULFONAMIDE (2R)-2-{[4-(benzylamino)-8-(1-methylethyl)pyrazolo[1,5-a][1,3,5]triazin-2-yl]amino}butan-1-ol 3-({2-[(4-{[6-(CYCLOHEXYLMETHOXY)-9H-PURIN-2-YL]AMINO}PHENYL)SULFONYL]ETHYL}AMINO)PROPAN-1-OL 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid (2R)-2-({9-(1-methylethyl)-6-[(4-pyridin-2-ylbenzyl)amino]-9H-purin-2-yl}amino)butan-1-ol 1-[4-(AMINOSULFONYL)PHENYL]-1,6-DIHYDROPYRAZOLO[3,4-E]INDAZOLE-3-CARBOXAMIDE 4-{[4-AMINO-6-(CYCLOHEXYLMETHOXY)-5-NITROSOPYRIMIDIN-2-YL]AMINO}BENZAMIDE Variolin B
Diseases
GWAS		Birth weight ( 31043758 27680694) Chronic kidney disease ( 26420894) Diastolic blood pressure ( 34074324) Lymphocyte counts ( 32888494) Offspring birth weight ( 31043758) Post bronchodilator FEV1/FVC ratio ( 26634245)	Mean corpuscular hemoglobin ( 32888494)
Interacting Genes		199 interacting genes: AATF ABL1 AHR ANKS1A AR ARID3B ATF2 BAAT BAG1 BDP1 BNC2 BRCA1 BRF1 CASP10 CASP2 CASP3 CASP6 CASP7 CASP8 CASP9 CBX1 CBX4 CCDC180 CCNA1 CCNA2 CCNB1 CCNC CCND1 CCND2 CCND3 CCNE1 CCNT2 CDADC1 CDC27 CDK1 CDK14 CDK2 CDK3 CDK4 CDK5 CDK6 CDK9 CDKN1A CDKN1C CEBPA CEBPB CEBPD CEBPE CHEK1 CHN2 CLNK CNTN3 CORO2A COX17 CREG1 CRYBA4 CSK CTBP1 CTSV CUX1 DGKZ DNMT1 DVL1 DYRK1A E2F1 E2F2 E2F3 E2F4 E4F1 EID1 ELF1 ENC1 EP300 ESD FANCC FBP1 FBP2 FOS FRK GALNT12 GTF3C2 HBP1 HDAC1 HDAC3 HIF1A HMGA2 HMGB1 HSPA8 ID2 INS IRF3 JUN KAT2B KAT5 KDM4A KDM5A KDM5B KMT5C L3MBTL1 LEF1 LIN54 LIN9 LMNA LRCH1 MAPK1 MAPK14 MAPK3 MAPK9 MCM7 MDM2 MDM4 MNAT1 MNDA MORF4L1 MORF4L2 MRPS18B MTRF1 MYC MYOD1 NCOA6 NDC80 NEFM ORC1 PA2G4 PAX2 PAX5 PAX6 PCDHB5 PELP1 PHB PIK3R1 PIK3R3 PLA2G12A PML POLA1 PPARG PPIA PPP1CA PPP1CB PPP1CC PPP1R26 PRDM2 PRKCB PRKRA PRMT2 PSMD10 PURA RABGAP1L RACK1 RAF1 RASA1 RBAK RBBP4 RBBP5 RBBP6 RBBP7 RBBP8 RBBP9 RING1 RINT1 RNF123 RNF40 RUNX2 SERPINB2 SHC1 SKP2 SMARCA4 SMARCB1 SMYD2 SNAPC1 SNAPC3 SNW1 SP1 SP3 SPI1 SPIB STAT3 STX17 SUV39H1 TAF1 TASOR TBP TFAP2A TGM2 THOC1 TMPO TOP2A TP53 TRAP1 TRIM27 TRIP11 TRMO UBE2I UBTF USP4 USP7 VDR XPA ZBTB16	49 interacting genes: ARID4A BRCA1 BRCA2 BTG1 BUB1B CALM1 CDC20 CDC25C CDC6 CDK1 CDK2 CDK3 CDKN1A CDKN1B CDT1 DRD2 DTNBP1 E2F1 E2F3 FANCC FEN1 H1-1 H1-5 HERC5 HIRA ITGB3BP KAT2B MAD2L1 MAGEA11 MYBL2 NFYA PGR POLA1 PRC1 PSMD4 PTMA RAD23A RB1 RBL1 RBL2 RPA1 SKP1 SKP2 SP1 TAF1 TP53 TRAF3IP1 UBTF USP37
Entrez ID		5925	890
HPRD ID		01574	00453
Ensembl ID		ENSG00000139687	ENSG00000145386
Uniprot IDs		A0A024RDV3 P06400	P20248
PDB IDs		1AD6 1GH6 1GUX 1H25 1N4M 1O9K 1PJM 2AZE 2QDJ 2R7G 3N5U 3POM 4CRI 4ELJ 4ELL	1E9H 1FIN 1FVV 1GY3 1H1P 1H1Q 1H1R 1H1S 1H24 1H25 1H26 1H27 1H28 1JST 1JSU 1OGU 1OI9 1OIU 1OIY 1OKV 1OKW 1OL1 1OL2 1P5E 1PKD 1QMZ 1URC 1VYW 2BKZ 2BPM 2C4G 2C5N 2C5O 2C5V 2C5X 2C6T 2CCH 2CCI 2CJM 2I40 2IW6 2IW8 2IW9 2UUE 2UZB 2UZD 2UZE 2UZL 2V22 2WEV 2WFY 2WHB 2WIH 2WIP 2WMA 2WMB 2WPA 2WXV 2X1N 3EID 3EJ1 3EOC 3F5X 4BCK 4BCM 4BCN 4BCP 4CFM 4CFN 4CFU 4CFV 4CFW 4CFX 4EOI 4EOJ 4EOK 4EOL 4EOM 4EON 4EOO 4EOP 4EOQ 4EOR 4EOS 4FX3 5CYI 5IF1 5LMK 5NEV 6ATH 6GVA 6P3W 6Q6G 6Q6H 6RIJ 6SG4 7B5L 7B5R
Enriched GO Terms of Interacting Partners?
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