Open Access Articles- Top Results for Retinoblastoma-like protein 1

Retinoblastoma-like protein 1

SymbolsRBL1 ; CP107; PRB1; p107
External IDsOMIM116957 MGI103300 HomoloGene2172 GeneCards: RBL1 Gene
RNA expression pattern
File:PBB GE RBL1 205296 at tn.png
More reference expression data
RefSeq (mRNA)NM_002895NM_001139516
RefSeq (protein)NP_002886NP_001132988
Location (UCSC)Chr 20:
35.62 – 35.72 Mb
Chr 2:
157.15 – 157.2 Mb
PubMed search[1][2]

Retinoblastoma-like 1 (p107), also known as RBL1, is a protein that in humans is encoded by the RBL1 gene.[1][2]


The protein encoded by this gene is similar in sequence and possibly function to the product of the retinoblastoma 1 (RB1) gene. The RB1 gene product is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 Large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.[1]


Retinoblastoma-like protein 1 has been shown to interact with HDAC1,[3][4] RBBP8,[5][6] E2F1,[7] Cyclin-dependent kinase 2,[8][9] BEGAIN,[6] BRF1,[10] BRCA1,[11] Cyclin A2,[7][12] Prohibitin,[13] MYBL2[12][14] and Mothers against decapentaplegic homolog 3.[15]

See also


  1. ^ a b "Entrez Gene: RBL1 retinoblastoma-like 1 (p107)". 
  2. ^ Ewen ME, Xing YG, Lawrence JB, Livingston DM (September 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell 66 (6): 1155–64. PMID 1833063. doi:10.1016/0092-8674(91)90038-Z. 
  3. ^ Lai, A; Lee J M; Yang W M; DeCaprio J A; Kaelin W G; Seto E; Branton P E (October 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Mol. Cell. Biol. (UNITED STATES) 19 (10): 6632–41. ISSN 0270-7306. PMC 84642. PMID 10490602. 
  4. ^ Ferreira, R; Magnaghi-Jaulin L; Robin P; Harel-Bellan A; Trouche D (September 1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proc. Natl. Acad. Sci. U.S.A. (UNITED STATES) 95 (18): 10493–8. ISSN 0027-8424. PMC 27922. PMID 9724731. doi:10.1073/pnas.95.18.10493. 
  5. ^ Fusco, C; Reymond A; Zervos A S (August 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics (UNITED STATES) 51 (3): 351–8. ISSN 0888-7543. PMID 9721205. doi:10.1006/geno.1998.5368. 
  6. ^ a b Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209. 
  7. ^ a b Dyson, N; Dembski M; Fattaey A; Ngwu C; Ewen M; Helin K (Dec 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". J. Virol. (UNITED STATES) 67 (12): 7641–7. ISSN 0022-538X. PMC 238233. PMID 8230483. 
  8. ^ Shanahan, F; Seghezzi W; Parry D; Mahony D; Lees E (February 1999). "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest". Mol. Cell. Biol. (UNITED STATES) 19 (2): 1460–9. ISSN 0270-7306. PMC 116074. PMID 9891079. 
  9. ^ Leng, Xiaohong; Noble Martin; Adams Peter D; Qin Jun; Harper J Wade (April 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Mol. Cell. Biol. (United States) 22 (7): 2242–54. ISSN 0270-7306. PMC 133692. PMID 11884610. doi:10.1128/MCB.22.7.2242-2254.2002. 
  10. ^ Sutcliffe, J E; Cairns C A; McLees A; Allison S J; Tosh K; White R J (June 1999). "RNA polymerase III transcription factor IIIB is a target for repression by pocket proteins p107 and p130". Mol. Cell. Biol. (UNITED STATES) 19 (6): 4255–61. ISSN 0270-7306. PMC 104385. PMID 10330166. 
  11. ^ Fan, S; Yuan R; Ma Y X; Xiong J; Meng Q; Erdos M; Zhao J N; Goldberg I D; Pestell R G; Rosen E M (August 2001). "Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding". Oncogene (England) 20 (35): 4827–41. ISSN 0950-9232. PMID 11521194. doi:10.1038/sj.onc.1204666. 
  12. ^ a b Joaquin, Manel; Bessa Maria; Saville Mark K; Watson Roger J (November 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene (England) 21 (52): 7923–32. ISSN 0950-9232. PMID 12439743. doi:10.1038/sj.onc.1206001. 
  13. ^ Wang, S; Nath N; Adlam M; Chellappan S (June 1999). "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene (ENGLAND) 18 (23): 3501–10. ISSN 0950-9232. PMID 10376528. doi:10.1038/sj.onc.1202684. 
  14. ^ Joaquin, Manel; Watson Roger J (November 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". J. Biol. Chem. (United States) 278 (45): 44255–64. ISSN 0021-9258. PMID 12947099. doi:10.1074/jbc.M308953200. 
  15. ^ Chen, Chang-Rung; Kang Yibin; Siegel Peter M; Massagué Joan (July 2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell (United States) 110 (1): 19–32. ISSN 0092-8674. PMID 12150994. doi:10.1016/S0092-8674(02)00801-2. 

Further reading


External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.