MGI:Rb1

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Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes
	GO:0000082	G1/S transition of mitotic cell cycle	MGI:MGI:3575978 PMID:15831459^[1]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	MGI:MGI:2386376 PMID:12200151^[2]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	MGI:MGI:3589998 PMID:15870077^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:104813	P	From MGI
	GO:0000122	negative regulation of transcription from RNA polymerase II promoter	MGI:MGI:5285162 PMID:20224733^[4]	IGI: Inferred from Genetic Interaction	UniProtKB:Q01094	P	From MGI
	GO:0001047	core promoter binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	F	From MGI
	GO:0001102	RNA polymerase II activating transcription factor binding	MGI:MGI:5285162 PMID:20224733^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q01094	F	From MGI
	GO:0003677	DNA binding	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0238	F	From MGI
	GO:0005515	protein binding	MGI:MGI:1195383 PMID:9464541^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P24610 UniProtKB:Q61412	F	From MGI
	GO:0005515	protein binding	MGI:MGI:1333653 PMID:10082561^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P53566	F	From MGI
	GO:0005515	protein binding	MGI:MGI:2386376 PMID:12200151^[2]	IPI: Inferred from Physical Interaction	UniProtKB:P32114	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3055264 PMID:15367658^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q9CQL7	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3579756 PMID:15701640^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q60867 UniProtKB:P12813	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3584078 PMID:15983387^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q3TQR0	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3589998 PMID:15870077^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q62315	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3694175 PMID:16286473^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q80UP3	F	From MGI
	GO:0005515	protein binding	MGI:MGI:3843440 PMID:14555653^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q155P7	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4414625 PMID:19640839^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9CS74	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4821084 PMID:11571651^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P35123	F	From MGI
	GO:0005515	protein binding	MGI:MGI:4887349 PMID:7923370^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q3TKT4	F	From MGI
	GO:0005634	nucleus	MGI:MGI:1333653 PMID:10082561^[6]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:3525032 PMID:15616565^[15]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:3579756 PMID:15701640^[8]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:3623720 PMID:16513252^[16]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005634	nucleus	MGI:MGI:4417868	ISO: Inferred from Sequence Orthology	UniProtKB:P33568	C	From MGI
	GO:0005634	nucleus	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	C	From MGI
	GO:0005667	transcription factor complex	MGI:MGI:1333653 PMID:10082561^[6]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0005819	spindle	MGI:MGI:3056244 PMID:15509711^[17]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0006351	transcription, DNA-dependent	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0804	P	From MGI
	GO:0006355	regulation of transcription, DNA-dependent	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0805	P	From MGI
	GO:0006469	negative regulation of protein kinase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0007049	cell cycle	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0131	P	From MGI
	GO:0007050	cell cycle arrest	MGI:MGI:3575978 PMID:15831459^[1]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0007090	regulation of S phase of mitotic cell cycle	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0007346	regulation of mitotic cell cycle	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0007346	regulation of mitotic cell cycle	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0008134	transcription factor binding	MGI:MGI:3687408 PMID:9178770^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q8R316	F	From MGI
	GO:0008134	transcription factor binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	F	From MGI
	GO:0008285	negative regulation of cell proliferation	MGI:MGI:2445783 PMID:11246230^[20]	IGI: Inferred from Genetic Interaction	MGI:MGI:97306	P	From MGI
	GO:0008285	negative regulation of cell proliferation	MGI:MGI:3578603 PMID:15843406^[21]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857242	P	From MGI
	GO:0016568	chromatin modification	MGI:MGI:1354194	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0156	P	From MGI
	GO:0016605	PML body	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	C	From MGI
	GO:0019899	enzyme binding	MGI:MGI:3653799 PMID:16616919^[22]	IPI: Inferred from Physical Interaction	UniProtKB:Q9R144	F	From MGI
	GO:0019900	kinase binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	F	From MGI
	GO:0030182	neuron differentiation	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0031134	sister chromatid biorientation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0031175	neuron projection development	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0031625	ubiquitin protein ligase binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	F	From MGI
	GO:0034088	maintenance of mitotic sister chromatid cohesion	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0035189	Rb-E2F complex	MGI:MGI:5285162 PMID:20224733^[4]	IDA: Inferred from Direct Assay		C	From MGI
	GO:0042551	neuron maturation	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0043353	enucleate erythrocyte differentiation	MGI:MGI:3525032 PMID:15616565^[15]	IGI: Inferred from Genetic Interaction	MGI:MGI:1857242 MGI:MGI:2384134	P	From MGI
	GO:0043550	regulation of lipid kinase activity	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0045445	myoblast differentiation	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0045651	positive regulation of macrophage differentiation	MGI:MGI:3525032 PMID:15616565^[15]	IGI: Inferred from Genetic Interaction	MGI:MGI:1857242 MGI:MGI:2384134	P	From MGI
	GO:0045786	negative regulation of cell cycle	MGI:MGI:2667557 PMID:12853964^[23]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0045842	positive regulation of mitotic metaphase/anaphase transition	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0045879	negative regulation of smoothened signaling pathway	MGI:MGI:3703460 PMID:17257418^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1931018 MGI:MGI:3574761	P	From MGI
	GO:0045892	negative regulation of transcription, DNA-dependent	MGI:MGI:3052717 PMID:11331592^[25]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0045892	negative regulation of transcription, DNA-dependent	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	MGI:MGI:3579756 PMID:15701640^[8]	IDA: Inferred from Direct Assay		P	From MGI
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	MGI:MGI:3579756 PMID:15701640^[8]	IGI: Inferred from Genetic Interaction	MGI:MGI:1339708 MGI:MGI:1352454	P	From MGI
	GO:0045944	positive regulation of transcription from RNA polymerase II promoter	MGI:MGI:3579756 PMID:15701640^[8]	IMP: Inferred from Mutant Phenotype		P	From MGI
	GO:0048565	digestive tract development	MGI:MGI:3703460 PMID:17257418^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1931018 MGI:MGI:3574761	P	From MGI
	GO:0048667	cell morphogenesis involved in neuron differentiation	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0050680	negative regulation of epithelial cell proliferation	MGI:MGI:3703460 PMID:17257418^[24]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1931018 MGI:MGI:3574761	P	From MGI
	GO:0051146	striated muscle cell differentiation	MGI:MGI:3511080 PMID:15542848^[26]	IGI: Inferred from Genetic Interaction	MGI:MGI:96680	P	From MGI
	GO:0051219	phosphoprotein binding	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	F	From MGI
	GO:0051301	cell division	MGI:MGI:3578603 PMID:15843406^[21]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857242	P	From MGI
	GO:0051402	neuron apoptotic process	MGI:MGI:3664376 PMID:7958874^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857339	P	From MGI
	GO:0051726	regulation of cell cycle	MGI:MGI:3583041 PMID:15898111^[27]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1857242	P	From MGI
	GO:0071459	protein localization to chromosome, centromeric region	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0071922	regulation of cohesin localization to chromatin	MGI:MGI:4834177	ISO: Inferred from Sequence Orthology	UniProtKB:P06400	P	From MGI
	GO:0071930	negative regulation of transcription involved in G1/S phase of mitotic cell cycle	MGI:MGI:5285162 PMID:20224733^[4]	IGI: Inferred from Genetic Interaction	UniProtKB:Q01094	P	From MGI
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Chen PL et al. (2005) Inactivation of CtIP leads to early embryonic lethality mediated by G1 restraint and to tumorigenesis by haploid insufficiency. Mol Cell Biol 25: 3535-42 PubMed GONUTS page
↑ ^2.0 ^2.1 Yuan SS et al. (2002) Pax-2 interacts with RB and reverses its repression on the promoter of Rig-1, a Robo member. Biochem Biophys Res Commun 296: 1019-25 PubMed GONUTS page
↑ ^3.0 ^3.1 Jung J et al. (2005) Jumonji regulates cardiomyocyte proliferation via interaction with retinoblastoma protein. J Biol Chem 280: 30916-23 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Sahin F & Sladek TL (2010) E2F-1 has dual roles depending on the cell cycle. Int J Biol Sci 6: 116-28 PubMed GONUTS page
↑ Wiggan O et al. (1998) Interaction of the pRB-family proteins with factors containing paired-like homeodomains. Oncogene 16: 227-36 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Timchenko NA et al. (1999) C/EBPalpha regulates formation of S-phase-specific E2F-p107 complexes in livers of newborn mice. Mol Cell Biol 19: 2936-45 PubMed GONUTS page
↑ Tominaga K et al. (2004) PAM14, a novel MRG- and Rb-associated protein, is not required for development and T-cell function in mice. Mol Cell Biol 24: 8366-73 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 Batsché E et al. (2005) Retinoblastoma and the related pocket protein p107 act as coactivators of NeuroD1 to enhance gene transcription. J Biol Chem 280: 16088-95 PubMed GONUTS page
↑ Ishii H et al. (2005) Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis. Proc Natl Acad Sci U S A 102: 9655-60 PubMed GONUTS page
↑ Los AP et al. (2006) The retinoblastoma family proteins bind to and activate diacylglycerol kinase zeta. J Biol Chem 281: 858-66 PubMed GONUTS page
↑ Ashe M et al. (2004) LEK1 is a potential inhibitor of pocket protein-mediated cellular processes. J Biol Chem 279: 664-76 PubMed GONUTS page
↑ Kim JH et al. (2009) Role of mammalian Ecdysoneless in cell cycle regulation. J Biol Chem 284: 26402-10 PubMed GONUTS page
↑ Blanchette P et al. (2001) Association of UNP, a ubiquitin-specific protease, with the pocket proteins pRb, p107 and p130. Oncogene 20: 5533-7 PubMed GONUTS page
↑ Dunaief JL et al. (1994) The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79: 119-30 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Iavarone A et al. (2004) Retinoblastoma promotes definitive erythropoiesis by repressing Id2 in fetal liver macrophages. Nature 432: 1040-5 PubMed GONUTS page
↑ Konishi M et al. (2006) Role of Fgf10 in cell proliferation in white adipose tissue. Mol Cell Endocrinol 249: 71-7 PubMed GONUTS page
↑ Liu J et al. (2004) Serine-threonine kinases and transcription factors active in signal transduction are detected at high levels of phosphorylation during mitosis in preimplantation embryos and trophoblast stem cells. Reproduction 128: 643-54 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 ^18.6 Lee EY et al. (1994) Dual roles of the retinoblastoma protein in cell cycle regulation and neuron differentiation. Genes Dev 8: 2008-21 PubMed GONUTS page
↑ Lavender P et al. (1997) The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A. Oncogene 14: 2721-8 PubMed GONUTS page
↑ Bajenaru ML et al. (2001) Neurofibromatosis 1 (NF1) heterozygosity results in a cell-autonomous growth advantage for astrocytes. Glia 33: 314-23 PubMed GONUTS page
↑ ^21.0 ^21.1 Mantela J et al. (2005) The retinoblastoma gene pathway regulates the postmitotic state of hair cells of the mouse inner ear. Development 132: 2377-88 PubMed GONUTS page
↑ Yoshimoto T et al. (2006) The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Exp Cell Res 312: 2040-53 PubMed GONUTS page
↑ Sage J et al. (2003) Acute mutation of retinoblastoma gene function is sufficient for cell cycle re-entry. Nature 424: 223-8 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 Yang HS & Hinds PW (2007) pRb-mediated control of epithelial cell proliferation and Indian hedgehog expression in mouse intestinal development. BMC Dev Biol 7: 6 PubMed GONUTS page
↑ Hsu SI et al. (2001) TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting proteins that regulate the transcriptional activity of E2F-1/DP-1. EMBO J 20: 2273-85 PubMed GONUTS page
↑ Takahashi C et al. (2004) Genetic interaction between Rb and K-ras in the control of differentiation and tumor suppression. Mol Cell Biol 24: 10406-15 PubMed GONUTS page
↑ Kalitsis P et al. (2005) Increased chromosome instability but not cancer predisposition in haploinsufficient Bub3 mice. Genes Chromosomes Cancer 44: 29-36 PubMed GONUTS page

[PMID:15831459-0] 1.0 ^1.1 Chen PL et al. (2005) Inactivation of CtIP leads to early embryonic lethality mediated by G1 restraint and to tumorigenesis by haploid insufficiency. Mol Cell Biol 25: 3535-42 PubMed GONUTS page

[PMID:12200151-1] 2.0 ^2.1 Yuan SS et al. (2002) Pax-2 interacts with RB and reverses its repression on the promoter of Rig-1, a Robo member. Biochem Biophys Res Commun 296: 1019-25 PubMed GONUTS page

[PMID:15870077-2] 3.0 ^3.1 Jung J et al. (2005) Jumonji regulates cardiomyocyte proliferation via interaction with retinoblastoma protein. J Biol Chem 280: 30916-23 PubMed GONUTS page

[PMID:20224733-3] 4.0 ^4.1 ^4.2 ^4.3 Sahin F & Sladek TL (2010) E2F-1 has dual roles depending on the cell cycle. Int J Biol Sci 6: 116-28 PubMed GONUTS page

[PMID:9464541-4] Wiggan O et al. (1998) Interaction of the pRB-family proteins with factors containing paired-like homeodomains. Oncogene 16: 227-36 PubMed GONUTS page

[PMID:10082561-5] 6.0 ^6.1 ^6.2 Timchenko NA et al. (1999) C/EBPalpha regulates formation of S-phase-specific E2F-p107 complexes in livers of newborn mice. Mol Cell Biol 19: 2936-45 PubMed GONUTS page

[PMID:15367658-6] Tominaga K et al. (2004) PAM14, a novel MRG- and Rb-associated protein, is not required for development and T-cell function in mice. Mol Cell Biol 24: 8366-73 PubMed GONUTS page

[PMID:15701640-7] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 Batsché E et al. (2005) Retinoblastoma and the related pocket protein p107 act as coactivators of NeuroD1 to enhance gene transcription. J Biol Chem 280: 16088-95 PubMed GONUTS page

[PMID:15983387-8] Ishii H et al. (2005) Frag1, a homolog of alternative replication factor C subunits, links replication stress surveillance with apoptosis. Proc Natl Acad Sci U S A 102: 9655-60 PubMed GONUTS page

[PMID:16286473-9] Los AP et al. (2006) The retinoblastoma family proteins bind to and activate diacylglycerol kinase zeta. J Biol Chem 281: 858-66 PubMed GONUTS page

[PMID:14555653-10] Ashe M et al. (2004) LEK1 is a potential inhibitor of pocket protein-mediated cellular processes. J Biol Chem 279: 664-76 PubMed GONUTS page

[PMID:19640839-11] Kim JH et al. (2009) Role of mammalian Ecdysoneless in cell cycle regulation. J Biol Chem 284: 26402-10 PubMed GONUTS page

[PMID:11571651-12] Blanchette P et al. (2001) Association of UNP, a ubiquitin-specific protease, with the pocket proteins pRb, p107 and p130. Oncogene 20: 5533-7 PubMed GONUTS page

[PMID:7923370-13] Dunaief JL et al. (1994) The retinoblastoma protein and BRG1 form a complex and cooperate to induce cell cycle arrest. Cell 79: 119-30 PubMed GONUTS page

[PMID:15616565-14] 15.0 ^15.1 ^15.2 Iavarone A et al. (2004) Retinoblastoma promotes definitive erythropoiesis by repressing Id2 in fetal liver macrophages. Nature 432: 1040-5 PubMed GONUTS page

[PMID:16513252-15] Konishi M et al. (2006) Role of Fgf10 in cell proliferation in white adipose tissue. Mol Cell Endocrinol 249: 71-7 PubMed GONUTS page

[PMID:15509711-16] Liu J et al. (2004) Serine-threonine kinases and transcription factors active in signal transduction are detected at high levels of phosphorylation during mitosis in preimplantation embryos and trophoblast stem cells. Reproduction 128: 643-54 PubMed GONUTS page

[PMID:7958874-17] 18.0 ^18.1 ^18.2 ^18.3 ^18.4 ^18.5 ^18.6 Lee EY et al. (1994) Dual roles of the retinoblastoma protein in cell cycle regulation and neuron differentiation. Genes Dev 8: 2008-21 PubMed GONUTS page

[PMID:9178770-18] Lavender P et al. (1997) The HMG-box transcription factor HBP1 is targeted by the pocket proteins and E1A. Oncogene 14: 2721-8 PubMed GONUTS page

[PMID:11246230-19] Bajenaru ML et al. (2001) Neurofibromatosis 1 (NF1) heterozygosity results in a cell-autonomous growth advantage for astrocytes. Glia 33: 314-23 PubMed GONUTS page

[PMID:15843406-20] 21.0 ^21.1 Mantela J et al. (2005) The retinoblastoma gene pathway regulates the postmitotic state of hair cells of the mouse inner ear. Development 132: 2377-88 PubMed GONUTS page

[PMID:16616919-21] Yoshimoto T et al. (2006) The arginine methyltransferase PRMT2 binds RB and regulates E2F function. Exp Cell Res 312: 2040-53 PubMed GONUTS page

[PMID:12853964-22] Sage J et al. (2003) Acute mutation of retinoblastoma gene function is sufficient for cell cycle re-entry. Nature 424: 223-8 PubMed GONUTS page

[PMID:17257418-23] 24.0 ^24.1 ^24.2 Yang HS & Hinds PW (2007) pRb-mediated control of epithelial cell proliferation and Indian hedgehog expression in mouse intestinal development. BMC Dev Biol 7: 6 PubMed GONUTS page

[PMID:11331592-24] Hsu SI et al. (2001) TRIP-Br: a novel family of PHD zinc finger- and bromodomain-interacting proteins that regulate the transcriptional activity of E2F-1/DP-1. EMBO J 20: 2273-85 PubMed GONUTS page

[PMID:15542848-25] Takahashi C et al. (2004) Genetic interaction between Rb and K-ras in the control of differentiation and tumor suppression. Mol Cell Biol 24: 10406-15 PubMed GONUTS page

[PMID:15898111-26] Kalitsis P et al. (2005) Increased chromosome instability but not cancer predisposition in haploinsufficient Bub3 mice. Genes Chromosomes Cancer 44: 29-36 PubMed GONUTS page

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Species (Taxon ID)	Mus musculus (house mouse) (taxon:10090)
Gene Name(s)	Rb1 ( synonyms: pRb, Rb, Rb-1 )
Protein Name(s)	retinoblastoma 1,
External Links
MGI	MGI:97874

MGI:Rb1

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